|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
48-554 |
0e+00 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 1015.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 48 IPEYFNFAKDVLDQWTNMEKAGKRLSNPAFWWIDGNGEELRWSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEW 127
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 128 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMK 207
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 208 YASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWT 287
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 288 QGACVFAHYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRsYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDI 367
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSS-YKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 368 YEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVLPERPFGLFTHYVDNPSKTASTL 447
Cdd:cd05928 320 YEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 448 RGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKS 527
Cdd:cd05928 400 RGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLS 479
|
490 500
....*....|....*....|....*..
gi 1039777677 528 HDQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:cd05928 480 HDPEQLTKELQQHVKSVTAPYKYPRKV 506
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
89-554 |
0e+00 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 588.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 89 WSFEELGLLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITD 168
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLG-LRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 169 DtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTGPPKMIGHTHSsFGL 248
Cdd:cd05972 80 A---------------------------------------------------EDPALIYFTSGTTGLPKGVLHTHS-YPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 249 GLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFESTSILQTLSKFPITVFCSAPTAYRMLV 328
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 329 QNDMSrSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILDEN 408
Cdd:cd05972 188 KQDLS-SYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 409 GATLPPGQEGDIALQVlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEV 488
Cdd:cd05972 267 GRELPPGEEGDIAIKL---PPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEV 343
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039777677 489 ESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:cd05972 344 ESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREI 407
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
45-554 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 570.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 45 KIEIPEYFNFAKDVLDQWtnmekAGKRLSNPAFWWIDGNGEELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKI 124
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRH-----AEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRAL-GVKKGDRVAIYLPNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 125 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD---------TLAPAVDAVAAKCENLHSKLIV---- 191
Cdd:COG0365 75 PEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADgglrggkviDLKEKVDEALEELPSLEHVIVVgrtg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 192 SQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSD 271
Cdd:COG0365 155 ADVPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 272 TGWAKSAWSSVFSPWTQGACVFAhylprFESTS-------ILQTLSKFPITVFCSAPTAYRMLVQ--NDMSRSYKFNSLK 342
Cdd:COG0365 235 IGWATGHSYIVYGPLLNGATVVL-----YEGRPdfpdpgrLWELIEKYGVTVFFTAPTAIRALMKagDEPLKKYDLSSLR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 343 HCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIA 421
Cdd:COG0365 310 LLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 422 LQvlpeRPF-GLFTHYVDNPSKTASTLRGSF---YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPS 497
Cdd:COG0365 390 IK----GPWpGMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPA 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039777677 498 IAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:COG0365 466 VAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSD--ELAKELQAHVREELGPYAYPREI 520
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
37-554 |
0e+00 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 555.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 37 YESMKQDFKIEIPEYFNFAKDVLDQWTNMEKagkrlSNPAFWWIDGNGEELRWSFEELGLLSRKFANILTeACSLQRGDR 116
Cdd:cd05970 1 YEDFHNNFSINVPENFNFAYDVVDAMAKEYP-----DKLALVWCDDAGEERIFTFAELADYSDKTANFFK-AMGIGKGDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 117 VMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITD--DTLAPAVDAVAAKCENLHSKLIVSQH 194
Cdd:cd05970 75 VMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIaeDNIPEEIEKAAPECPSKPKLVWVGDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 195 SREGWGNLKEMMKYASDS----HTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSsFGLGLSVNGRFWLDLIASDVMWNTS 270
Cdd:cd05970 155 VPEGWIDFRKLIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 271 DTGWAKSAWSSVFSPWTQGACVFAHYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRsYKFNSLKHCVSAGEP 350
Cdd:cd05970 234 DTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSR-YDLSSLRYCTTAGEA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 351 INPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVLPERPF 430
Cdd:cd05970 313 LNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 431 GLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPI 510
Cdd:cd05970 393 GLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPI 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1039777677 511 RGEVVKAFIVLNPDYKShdQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:cd05970 473 RGQVVKATIVLAKGYEP--SEELKKELQDHVKKVTAPYKYPRIV 514
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
28-552 |
3.58e-141 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 421.23 E-value: 3.58e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 28 TATPQNFSNYESMKQDFKI-EIPEYF--------NFAKDVLDQWTNMEKAGKrlsnPAFWWIDGNGEElRWSFEELGLLS 98
Cdd:PRK04319 9 IKGEPNLKDYEETYATFSWeEVEKEFswletgkvNIAYEAIDRHADGGRKDK----VALRYLDASRKE-KYTYKELKELS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 99 RKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVdaV 178
Cdd:PRK04319 84 NKFANVLKEL-GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERK--P 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 179 AAKCENLHSKLIVSQHSREGWG--NLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRF 256
Cdd:PRK04319 161 ADDLPSLKHVLLVGEDVEEGPGtlDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAM-LQHYQTGKY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 257 WLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGA--CVFAhylPRFESTSILQTLSKFPITVFCSAPTAYRMLVQ--NDM 332
Cdd:PRK04319 240 VLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGAtnVIDG---GRFSPERWYRILEDYKVTVWYTAPTAIRMLMGagDDL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 333 SRSYKFNSLKHCVSAGEPINPEVMeQWRKKT-GLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSPAFDVKILDENG 409
Cdd:PRK04319 317 VKKYDLSSLRHILSVGEPLNPEVV-RWGMKVfGLPIHDNWWMTETggIMIA-NYPAMDIKPGSMGKPLPGIEAAIVDDQG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 410 ATLPPGQEGDIALQvlPERPfGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVE 489
Cdd:PRK04319 395 NELPPNRMGNLAIK--KGWP-SMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVE 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039777677 490 SALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLKKEIQEHVKKTTAPYKYPR 552
Cdd:PRK04319 472 SKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYE--PSEELKEEIRGFVKKGLGAHAAPR 532
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
90-554 |
3.77e-134 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 398.48 E-value: 3.77e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 90 SFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAkciitdd 169
Cdd:cd05974 2 SFAEMSARSSRVANFL-RSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 170 tlapavdAVAAKCENLHSklivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTGPPKMIGHTHSSFGLG 249
Cdd:cd05974 74 -------VYAAVDENTHA---------------------------------DDPMLLYFTSGTTSKPKLVEHTHRSYPVG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 250 lSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQ 329
Cdd:cd05974 114 -HLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 330 NDMSRSYKfnSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILDENG 409
Cdd:cd05974 193 QDLASFDV--KLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 410 AtlpPGQEGDIALQVLPERPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVE 489
Cdd:cd05974 271 A---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELE 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039777677 490 SALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:cd05974 348 SVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYE--PSPETALEIFRFSRERLAPYKRIRRL 410
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
89-554 |
8.24e-125 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 374.92 E-value: 8.24e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 89 WSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITD 168
Cdd:cd05969 1 YTFAQLKVLSARFANVL-KSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 169 DTLAPAVDAvaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTGPPKMIGHTHSSFgL 248
Cdd:cd05969 80 EELYERTDP-------------------------------------------EDPTLLHYTSGTTGTPKGVLHVHDAM-I 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 249 GLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhYLPRFESTSILQTLSKFPITVFCSAPTAYRMLV 328
Cdd:cd05969 116 FYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVV-YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 329 QND--MSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTET--VLICgNFKGMKIKPGSMGKPSPAFDVKI 404
Cdd:cd05969 195 KEGdeLARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETgsIMIA-NYPCMPIKPGSMGKPLPGVKAAV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 405 LDENGATLPPGQEGDIALQvlPERPfGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIG 484
Cdd:cd05969 274 VDENGNELPPGTKGILALK--PGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVG 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 485 PFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:cd05969 351 PFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEP--SDELKEEIINFVRQKLGAHVAPREI 418
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
88-554 |
8.02e-114 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 346.34 E-value: 8.02e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 88 RWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIT 167
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 168 DDTLAPAVdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhdemmaIYFTSGTTGPPKMIGHTHSsFG 247
Cdd:cd05971 85 DGSDDPAL--------------------------------------------------IIYTSGTTGPPKGALHAHR-VL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 248 LGLSVNGRFWLDLI--ASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFESTSILQTLSKFPITVFCSAPTAYR 325
Cdd:cd05971 114 LGHLPGVQFPFNLFprDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALK 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 326 MLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKG-MKIKPGSMGKPSPAFDVKI 404
Cdd:cd05971 194 MMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIPGHRVAI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 405 LDENGATLPPGQEGDIALqvlpERPFGL-FTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRI 483
Cdd:cd05971 274 VDDNGTPLPPGEVGEIAV----ELPDPVaFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRI 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039777677 484 GPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:cd05971 350 GPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREI 418
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
85-554 |
7.96e-111 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 339.09 E-value: 7.96e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 85 EELRWSFEELGLLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:COG0318 21 GGRRLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 165 IITddtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhdemMAIYFTSGTTGPPKMIGHTHS 244
Cdd:COG0318 100 LVT--------------------------------------------------------ALILYTSGTTGRPKGVMLTHR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 245 SFgLGLSVNGRFWLDLIASDVMWNTS----DTGWaksaWSSVFSPWTQGACVfaHYLPRFESTSILQTLSKFPITVFCSA 320
Cdd:COG0318 124 NL-LANAAAIAAALGLTPGDVVLVALplfhVFGL----TVGLLAPLLAGATL--VLLPRFDPERVLELIERERVTVLFGV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 321 PTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTET-VLICGNFKGMK-IKPGSMGKPSP 398
Cdd:COG0318 197 PTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETsPVVTVNPEDPGeRRPGSVGRPLP 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 399 AFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILS 478
Cdd:COG0318 277 GVEVRIVDEDGRELPPGEVGEIVV-----RGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIIS 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039777677 479 SGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLKKEIQEHVkkttAPYKYPRKV 554
Cdd:COG0318 352 GGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPG-AELDAEELRAFLRERL----ARYKVPRRV 422
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
90-554 |
4.38e-98 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 305.98 E-value: 4.38e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 90 SFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDd 169
Cdd:cd05973 2 TFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 170 tlapavdavAAKCENLHSKLIVsqhsregwgnlkemmkyasdshtcvdtkhdeMMaiyFTSGTTGPPKMIGHTHSSFgLG 249
Cdd:cd05973 80 ---------AANRHKLDSDPFV-------------------------------MM---FTSGTTGLPKGVPVPLRAL-AA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 250 LSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQG-ACVFAHylPRFESTSILQTLSKFPITVFCSAPTAYRMLV 328
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLE--GGFSVESTWRVIERLGVTNLAGSPTAYRLLM 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 329 QNDMSRSYKFN-SLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMK--IKPGSMGKPSPAFDVKIL 405
Cdd:cd05973 194 AAGAEVPARPKgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEhpVHAGSAGRAMPGWRVAVL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 406 DENGATLPPGQEGDIALQVlPERPFGLFTHYVDNPSKTAStlrGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGP 485
Cdd:cd05973 274 DDDGDELGPGEPGRLAIDI-ANSPLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGP 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039777677 486 FEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:cd05973 350 FDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEG--TPALADELQLHVKKRLSAHAYPRTI 416
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
226-554 |
1.53e-96 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 298.04 E-value: 1.53e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 226 IYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAkSAWSSVFSPWTQGACVFAHylPRFESTSI 305
Cdd:cd04433 5 ILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLL--PKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 306 LQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTET--VLICGNF 383
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETggTVATGPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 384 KGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDED 463
Cdd:cd04433 161 DDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVV-----RGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 464 GYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLKKEIQEHVKK 543
Cdd:cd04433 236 GYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRP-----GADLDAEELRAHVRE 310
|
330
....*....|.
gi 1039777677 544 TTAPYKYPRKV 554
Cdd:cd04433 311 RLAPYKVPRRV 321
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
50-554 |
2.50e-95 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 300.82 E-value: 2.50e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 50 EYFNFAKDVLDQwtnmeKAGKRLSNPAFwwIDGNGEelrWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWL 129
Cdd:cd05959 1 EKYNAATLVDLN-----LNEGRGDKTAF--IDDAGS---LTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 130 ANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSQHSRE--GWGNLKEMMK 207
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPeaGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 208 YASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWT 287
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 288 QGACVFahYLP-RFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLD 366
Cdd:cd05959 230 VGATTV--LMPeRPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 367 IYEGYGQTETVLI-CGNFKGmKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDiaLQVlpeRPFGLFTHYVDNPSKTAS 445
Cdd:cd05959 308 ILDGIGSTEMLHIfLSNRPG-RVRYGTTGKPVPGYEVELRDEDGGDVADGEPGE--LYV---RGPSSATMYWNNRDKTRD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 446 TLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDY 525
Cdd:cd05959 382 TFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGY 461
|
490 500
....*....|....*....|....*....
gi 1039777677 526 KshDQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:cd05959 462 E--DSEALEEELKEFVKDRLAPYKYPRWI 488
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
66-554 |
1.48e-94 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 297.55 E-value: 1.48e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 66 EKAGKRLSN-PAFWWIDgngeeLRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 144
Cdd:cd05936 6 EEAARRFPDkTALIFMG-----RKLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 145 TTQLTQKDILYRLQSSKAKCIITDDTLApavdavaakcenlhsKLIVSQHSREGWgnlkemmkyasdshtCVDTKHDeMM 224
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIVAVSFT---------------DLLAAGAPLGER---------------VALTPED-VA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 225 AIYFTSGTTGPPKMIGHTHSSfglgLSVNgrfwldliASDVMWNTSDTGWAKS------------AWS-SVFSPWTQGAC 291
Cdd:cd05936 129 VLQYTSGTTGVPKGAMLTHRN----LVAN--------ALQIKAWLEDLLEGDDvvlaalplfhvfGLTvALLLPLALGAT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 292 VFahYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGY 371
Cdd:cd05936 197 IV--LIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGY 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 372 GQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIAL---QVlperpfglFTHYVDNPSKTASTL 447
Cdd:cd05936 275 GLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVrgpQV--------MKGYWNRPEETAEAF 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 448 RGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyks 527
Cdd:cd05936 347 VDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKE---- 422
|
490 500
....*....|....*....|....*..
gi 1039777677 528 hDQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:cd05936 423 -GASLTEEEIIAFCREQLAGYKVPRQV 448
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
86-554 |
5.35e-86 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 274.36 E-value: 5.35e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 86 ELRWSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQsskaKCI 165
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD----KAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 166 ITDDTLAPAVDAVaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:cd05958 84 ITVALCAHALTAS------------------------------------------DDICILAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 246 FGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhyLPRFESTSILQTLSKFPITVFCSAPTAYR 325
Cdd:cd05958 122 PLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVL--LEEATPDLLLSAIARYKPTVLFTAPTAYR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 326 MLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIL 405
Cdd:cd05958 200 AMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 406 DENGATLPPGQEGDIALQvlpeRPFGLftHYVDNPSKtASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGP 485
Cdd:cd05958 280 DDEGNPVPDGTIGRLAVR----GPTGC--RYLADKRQ-RTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAP 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039777677 486 FEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:cd05958 353 PEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIP--GPVLARELQDHAKAHIAPYKYPRAI 419
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
85-554 |
1.90e-83 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 270.13 E-value: 1.90e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 85 EELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:PRK06187 28 DGRRTTYAELDERVNRLANALRAL-GVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 165 IITDDTLAPAVDAVAAKCENLHSKLIVSQHSREG----WGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIG 240
Cdd:PRK06187 107 VLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 241 HTHSSFgLGLSVNGRFWLDLIASDV------MWNTSDTGWAksawssvFSPWTQGACVFahYLPRFESTSILQTLSKFPI 314
Cdd:PRK06187 187 LSHRNL-FLHSLAVCAWLKLSRDDVylvivpMFHVHAWGLP-------YLALMAGAKQV--IPRRFDPENLLDLIETERV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 315 TVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETV-LICGNF-----KGMKI 388
Cdd:PRK06187 257 TFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLPpedqlPGQWT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 389 KPGSMGKPSPAFDVKILDENGATLPP--GQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYF 466
Cdd:PRK06187 337 KRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIV-----RGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 467 WFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLKKEIQEHVkkttA 546
Cdd:PRK06187 412 YITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPG-ATLDAKELRAFLRGRL----A 486
|
....*...
gi 1039777677 547 PYKYPRKV 554
Cdd:PRK06187 487 KFKLPKRI 494
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-479 |
1.75e-79 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 256.86 E-value: 1.75e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 82 GNGEELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSK 161
Cdd:pfam00501 15 EVGEGRRLTYRELDERANRLAAGLRAL-GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 162 AKCIITDDTL-APAVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSH-TCVDTKHDEMMAIYFTSGTTGPPKMI 239
Cdd:pfam00501 94 AKVLITDDALkLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPpPPPPPDPDDLAYIIYTSGTTGKPKGV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 240 GHTH---SSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAHYLPRFESTSILQTLSKFPIT 315
Cdd:pfam00501 174 MLTHrnlVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGAtVVLPPGFPALDPAALLELIERYKVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 316 VFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTET---VLICGNFKGMKIKPGS 392
Cdd:pfam00501 254 VLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETtgvVTTPLPLDEDLRSLGS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 393 MGKPSPAFDVKILDEN-GATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTL-RGSFYITGDRGYMDEDGYFWFVA 470
Cdd:pfam00501 334 VGRPLPGTEVKIVDDEtGEPVPPGEPGELCV-----RGPGVMKGYLNDPELTAEAFdEDGWYRTGDLGRRDEDGYLEIVG 408
|
....*....
gi 1039777677 471 RSDDIILSS 479
Cdd:pfam00501 409 RKKDQIKLG 417
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
78-554 |
3.24e-79 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 262.18 E-value: 3.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 78 WWIDGNGEELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIPGttqLTQKDIL 154
Cdd:TIGR02188 78 WEGDEPGEVRKITYRELHREVCRFANVLKSL-GVKKGDRVAIYMPMIPEAAIAMLACARIGaihSVVFGG---FSAEALA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 155 YRLQSSKAKCIITDDT---------LAPAVDAVAAKCENLHSKLIVSQH----------SREGWGNlkEMMKYASDSHTC 215
Cdd:TIGR02188 154 DRINDAGAKLVITADEglrggkvipLKAIVDEALEKCPVSVEHVLVVRRtgnpvvpwveGRDVWWH--DLMAKASAYCEP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 216 VDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAH 295
Cdd:TIGR02188 232 EPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMF 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 296 Y-LPRFESTS-ILQTLSKFPITVFCSAPTAYRMLVQ--NDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLD---IY 368
Cdd:TIGR02188 312 EgVPTYPDPGrFWEIIEKHKVTIFYTAPTAIRALMRlgDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKErcpIV 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 369 EGYGQTET--VLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLP-PGQEGDIAL-QVLPERPFGLF---THYVDNPS 441
Cdd:TIGR02188 392 DTWWQTETggIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEgPGEGGYLVIkQPWPGMLRTIYgdhERFVDTYF 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 442 KTAStlrgSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVL 521
Cdd:TIGR02188 472 SPFP----GYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTL 547
|
490 500 510
....*....|....*....|....*....|...
gi 1039777677 522 NPDYKSHDqeQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:TIGR02188 548 KDGYEPDD--ELRKELRKHVRKEIGPIAKPDKI 578
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
53-554 |
5.73e-77 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 255.56 E-value: 5.73e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 53 NFAKDVLDQwtNMEKAGKRlsnPAFWWiDGN--GEELRWSFEELglLSR--KFANILTEAcSLQRGDRVMVILPKIPEWW 128
Cdd:cd05966 53 NISYNCLDR--HLKERGDK---VAIIW-EGDepDQSRTITYREL--LREvcRFANVLKSL-GVKKGDRVAIYMPMIPELV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 129 LANVACLRTG---TVLIPGttqLTQKDILYRLQSSKAKCIITDD---------TLAPAVDAVAAKCENLHsKLIVSQHS- 195
Cdd:cd05966 124 IAMLACARIGavhSVVFAG---FSAESLADRINDAQCKLVITADggyrggkviPLKEIVDEALEKCPSVE-KVLVVKRTg 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 196 --------REGWGNlkEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMW 267
Cdd:cd05966 200 gevpmtegRDLWWH--DLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYW 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 268 NTSDTGWAKSAWSSVFSPWTQGACVFAhylprFEST----------SILQtlsKFPITVFCSAPTAYRMLVQ--NDMSRS 335
Cdd:cd05966 278 CTADIGWITGHSYIVYGPLANGATTVM-----FEGTptypdpgrywDIVE---KHKVTIFYTAPTAIRALMKfgDEWVKK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 336 YKFNSLKHCVSAGEPINPEVMEQWRKKTG---LDIYEGYGQTETVLIC-----GnfkGMKIKPGSMGKPSPAFDVKILDE 407
Cdd:cd05966 350 HDLSSLRVLGSVGEPINPEAWMWYYEVIGkerCPIVDTWWQTETGGIMitplpG---ATPLKPGSATRPFFGIEPAILDE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 408 NGATLPPGQEGDIALqvlpERPFglfthyvdnPSkTASTLRGS--------------FYITGDRGYMDEDGYFWFVARSD 473
Cdd:cd05966 427 EGNEVEGEVEGYLVI----KRPW---------PG-MARTIYGDheryedtyfskfpgYYFTGDGARRDEDGYYWITGRVD 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 474 DIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeQLKKEIQEHVKKTTAPYKYPRK 553
Cdd:cd05966 493 DVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSD--ELRKELRKHVRKEIGPIATPDK 570
|
.
gi 1039777677 554 V 554
Cdd:cd05966 571 I 571
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
90-556 |
3.70e-75 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 246.22 E-value: 3.70e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 90 SFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:cd05919 12 TYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 170 tlapavDAVAakcenlhsklivsqhsregwgnlkemmkYASdshtcvdtkhdemmaiyFTSGTTGPPKMIGHTHSSFGLG 249
Cdd:cd05919 91 ------DDIA----------------------------YLL-----------------YSSGTTGPPKGVMHAHRDPLLF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 250 LSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAHYLPRFEStsILQTLSKFPITVFCSAPTAY-RML 327
Cdd:cd05919 120 ADAMAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGAsAVLNPGWPTAER--VLATLARFRPTVLYGVPTFYaNLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 328 VQNDMSRSyKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILDE 407
Cdd:cd05919 198 DSCAGSPD-ALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 408 NGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFE 487
Cdd:cd05919 277 EGHTIPPGEEGDLLV-----RGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVE 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039777677 488 VESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLKKEIQEHVKKTTAPYKYPRKVGV 556
Cdd:cd05919 352 VESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAP--QESLARDIHRHLLERLSAHKVPRRIAF 418
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
88-554 |
8.26e-75 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 245.21 E-value: 8.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 88 RWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIt 167
Cdd:cd17631 20 SLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 168 ddtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTGPPKMIGHTHSSFg 247
Cdd:cd17631 98 -----------------------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNL- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 248 LGLSVNGRFWLDLIASDV------MWNTSDTGwaksawssVFSPWT--QGACVfaHYLPRFESTSILQTLSKFPITVFCS 319
Cdd:cd17631 124 LWNAVNALAALDLGPDDVllvvapLFHIGGLG--------VFTLPTllRGGTV--VILRKFDPETVLDLIERHRVTSFFL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 320 APTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKtGLDIYEGYGQTETV-LICGNFKGMKI-KPGSMGKPS 397
Cdd:cd17631 194 VPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSpGVTFLSPEDHRrKLGSAGRPV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 398 PAFDVKILDENGATLPPGQEGDIAL---QVLPErpfglfthYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDD 474
Cdd:cd17631 273 FFVEVRIVDPDGREVPPGEVGEIVVrgpHVMAG--------YWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKD 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 475 IILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:cd17631 345 MIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRP-----GAELDEDELIAHCRERLARYKIPKSV 419
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
53-559 |
1.53e-73 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 245.95 E-value: 1.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 53 NFAKDVLDQwtNMEKAGKRLsnpAFWWIDGNGEELR-WSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLAN 131
Cdd:cd17634 53 NLAANALDR--HLRENGDRT---AIIYEGDDTSQSRtISYRELHREVCRFAGTL-LDLGVKKGDRVAIYMPMIPEAAVAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 132 VACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD---------TLAPAVD-AVAAKCENLHSKLIVSqhsREG--- 198
Cdd:cd17634 127 LACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADggvragrsvPLKKNVDdALNPNVTSVEHVIVLK---RTGsdi 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 199 ------WGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDT 272
Cdd:cd17634 204 dwqegrDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 273 GWAKSAWSSVFSPWTQGACVFAHY-LPRFESTSIL-QTLSKFPITVFCSAPTAYRMLVQ--NDMSRSYKFNSLKHCVSAG 348
Cdd:cd17634 284 GWVTGHSYLLYGPLACGATTLLYEgVPNWPTPARMwQVVDKHGVNILYTAPTAIRALMAagDDAIEGTDRSSLRILGSVG 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 349 EPINPEVMEQWRKKTGLD---IYEGYGQTETV-LICGNFKGM-KIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQ 423
Cdd:cd17634 364 EPINPEAYEWYWKKIGKEkcpVVDTWWQTETGgFMITPLPGAiELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVIT 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 424 V-LPERPFGLFThyvDNPSKTASTLR--GSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAE 500
Cdd:cd17634 444 DpWPGQTRTLFG---DHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAE 520
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039777677 501 SAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLKKEIQEHVKKTTAPYKYPRKVGVPGT 559
Cdd:cd17634 521 AAVVGIPHAIKGQAPYAYVVLNHGVE--PSPELYAELRNWVRKEIGPLATPDVVHWVDS 577
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
50-552 |
3.65e-73 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 242.82 E-value: 3.65e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 50 EYFNFAKDVLDqwTNMEKAgkRLSNPAFwwIDGNGeelRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWL 129
Cdd:TIGR02262 1 EKYNAAEDLLD--RNVVEG--RGGKTAF--IDDIS---SLSYGELEAQVRRLAAAL-RRLGVKREERVLLLMLDGVDFPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 130 ANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSkLIVSQHSREGWGNLKEMMKYA 209
Cdd:TIGR02262 71 AFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEH-RVVVGRPEAGEVQLAELLATE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 210 SDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQG 289
Cdd:TIGR02262 150 SEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 290 ACVFAhYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYE 369
Cdd:TIGR02262 230 ATTVL-MGERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 370 GYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVlPERPFGlfthYVDNPSKTASTLRG 449
Cdd:TIGR02262 309 GIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISG-PSSATM----YWNNRAKSRDTFQG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 450 SFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKShd 529
Cdd:TIGR02262 384 EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTA-- 461
|
490 500
....*....|....*....|...
gi 1039777677 530 qeqLKKEIQEHVKKTTAPYKYPR 552
Cdd:TIGR02262 462 ---LETELKEHVKDRLAPYKYPR 481
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
89-549 |
1.02e-69 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 233.26 E-value: 1.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 89 WSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITD 168
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 169 DTLAPAVDAvAAKCENLHSKLIVSQHSREGWGNLKEMMK---YASDSH--TCVDTKHDEMMAIYFTSGTTGPPKMIGHTH 243
Cdd:cd05911 90 PDGLEKVKE-AAKELGPKDKIIVLDDKPDGVLSIEDLLSptlGEEDEDlpPPLKDGKDDTAAILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 244 SSFGLGL-SVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWtQGACVfaHYLPRFESTSILQTLSKFPITVFCSAPT 322
Cdd:cd05911 169 RNLIANLsQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLL-NGATV--IIMPKFDSELFLDLIEKYKITFLYLVPP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 323 AYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGL-DIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFD 401
Cdd:cd05911 246 IAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 402 VKILDENG-ATLPPGQEGDIAL---QVLPErpfglfthYVDNPSKTASTL-RGSFYITGDRGYMDEDGYFWFVARSDDII 476
Cdd:cd05911 326 AKIVDDDGkDSLGPNEPGEICVrgpQVMKG--------YYNNPEATKETFdEDGWLHTGDIGYFDEDGYLYIVDRKKELI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039777677 477 LSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeqlkKEIQEHVKKTTAPYK 549
Cdd:cd05911 398 KYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTE-----KEVKDYVAKKVASYK 465
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
85-554 |
1.76e-69 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 233.26 E-value: 1.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 85 EELRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:PRK07656 27 GDQRLTYAELNARVRRAAAAL-AALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 165 IITDDTLAPAVDAVAAKCENLHSKLIV----SQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPK--M 238
Cdd:PRK07656 106 LFVLGLFLGVDYSATTRLPALEHVVICeteeDDPHTEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKgaM 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 239 IGHTHSsfglgLSvNGRFW---LDLIASD---------------VMWNTsdtgwaksawssvfsPWTQGACVFAHylPRF 300
Cdd:PRK07656 186 LTHRQL-----LS-NAADWaeyLGLTEGDrylaanpffhvfgykAGVNA---------------PLMRGATILPL--PVF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 301 ESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIY-EGYGQTE---T 376
Cdd:PRK07656 243 DPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVlTGYGLSEasgV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 377 VLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLR--GSFYiT 454
Cdd:PRK07656 323 TTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLV-----RGPNVMKGYYDDPEATAAAIDadGWLH-T 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 455 GDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLK 534
Cdd:PRK07656 397 GDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG-AELTEEELI 475
|
490 500
....*....|....*....|
gi 1039777677 535 KEIQEHVkkttAPYKYPRKV 554
Cdd:PRK07656 476 AYCREHL----AKYKVPRSI 491
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
90-554 |
2.54e-67 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 225.05 E-value: 2.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 90 SFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITdd 169
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 170 tlapavdavaakcenlHSKLivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTGPPKMIGHTHSSFgLG 249
Cdd:cd05935 80 ----------------GSEL-------------------------------DDLALIPYTSGTTGLPKGCMHTHFSA-AA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 250 LSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAhyLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQ 329
Cdd:cd05935 112 NALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTMLVDLLA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 330 NDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILD-EN 408
Cdd:cd05935 190 TPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDiET 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 409 GATLPPGQEGDIALQVlPErpfgLFTHYVDNPSKTAS---TLRGS-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIG 484
Cdd:cd05935 270 GRELPPNEVGEIVVRG-PQ----IFKGYWNRPEETEEsfiEIKGRrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVW 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 485 PFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQlkkEIQEHVKKTTAPYKYPRKV 554
Cdd:cd05935 345 PAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTEE---DIIEWAREQMAAYKYPREV 411
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
100-554 |
4.40e-67 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 230.03 E-value: 4.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 100 KFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIPGttqLTQKDILYRLQSSKAKCIITDD------- 169
Cdd:PRK00174 110 RFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGavhSVVFGG---FSAEALADRIIDAGAKLVITADegvrggk 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 170 --TLAPAVDAVAAKCENLHSKLIVS--------QHSREGWGNlkEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMI 239
Cdd:PRK00174 186 piPLKANVDEALANCPSVEKVIVVRrtggdvdwVEGRDLWWH--ELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGV 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 240 GHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHY-LPRFESTS-ILQTLSKFPITVF 317
Cdd:PRK00174 264 LHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEgVPNYPDPGrFWEVIDKHKVTIF 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 318 CSAPTAYRMLVQ--NDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLD---IYEGYGQTET--VLIC---GnfkGMK 387
Cdd:PRK00174 344 YTAPTAIRALMKegDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGErcpIVDTWWQTETggIMITplpG---ATP 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 388 IKPGSMGKPSPAFDVKILDENGATLPPGQEGDIAL------QVL-----PERpfglfthYVdnpsKTA-STLRGSfYITG 455
Cdd:PRK00174 421 LKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIkdpwpgMMRtiygdHER-------FV----KTYfSTFKGM-YFTG 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 456 DRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeQLKK 535
Cdd:PRK00174 489 DGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSD--ELRK 566
|
490
....*....|....*....
gi 1039777677 536 EIQEHVKKTTAPYKYPRKV 554
Cdd:PRK00174 567 ELRNWVRKEIGPIAKPDVI 585
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
84-554 |
7.84e-67 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 228.74 E-value: 7.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 84 GEELRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTV--LIPG---TTQLTQkdilyRLQ 158
Cdd:cd05967 78 GTERTYTYAELLDEVSRLAGVL-RKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsVVFGgfaAKELAS-----RID 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 159 SSKAKCIITDD---------TLAPAVDAVAAKCENLHSKLIVSQHSR--------EGWGNLKEMMKYASdSHTCVDTKHD 221
Cdd:cd05967 152 DAKPKLIVTAScgiepgkvvPYKPLLDKALELSGHKPHHVLVLNRPQvpadltkpGRDLDWSELLAKAE-PVDCVPVAAT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 222 EMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGAcvfahylprfe 301
Cdd:cd05967 231 DPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGA----------- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 302 sTSIL---------------QTLSKFPITVFCSAPTAYRMLVQND----MSRSYKFNSLKHCVSAGEPINPEVMEQWRKK 362
Cdd:cd05967 300 -TTVLyegkpvgtpdpgafwRVIEKYQVNALFTAPTAIRAIRKEDpdgkYIKKYDLSSLRTLFLAGERLDPPTLEWAENT 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 363 TGLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQvLPERPFGLFTHYVD 438
Cdd:cd05967 379 LGVPVIDHWWQTETgwpiTANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIK-LPLPPGCLLTLWKN 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 439 NPSKTASTLRGS--FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVK 516
Cdd:cd05967 458 DERFKKLYLSKFpgYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPL 537
|
490 500 510
....*....|....*....|....*....|....*...
gi 1039777677 517 AFIVLNPDYKShDQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:cd05967 538 GLVVLKEGVKI-TAEELEKELVALVREQIGPVAAFRLV 574
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
62-554 |
1.05e-65 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 224.07 E-value: 1.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 62 WTNMEKAGKRLSNPAFWWIDGNgeelRWSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVL 141
Cdd:PRK08314 13 FHNLEVSARRYPDKTAIVFYGR----AISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 142 IPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAV------------------DAVAAKCENLHSKLIVSQHSRE-----G 198
Cdd:PRK08314 89 VPVNPMNREEELAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaqysDYLPAEPEIAVPAWLRAEPPLQalapgG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 199 WGNLKEMMK--YASDSHTcvdTKHDEMMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSD----T 272
Cdd:PRK08314 169 VVAWKEALAagLAPPPHT---AGPDDLAVLPYTSGTTGVPKGCMHTHRTV-MANAVGSVLWSNSTPESVVLAVLPlfhvT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 273 GWAKSAWSSVFSpwtqGACVFahYLPRFESTSILQTLSKFPITVFCSAPTayrMLVQNDMS---RSYKFNSLKHCVSAGE 349
Cdd:PRK08314 245 GMVHSMNAPIYA----GATVV--LMPRWDREAAARLIERYRVTHWTNIPT---MVVDFLASpglAERDLSSLRYIGGGGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 350 PINPEVMEQWRKKTGLDIYEGYGQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKILD-ENGATLPPGQEGDIAL---QV 424
Cdd:PRK08314 316 AMPEAVAERLKELTGLDYVEGYGLTETMaQTHSNPPD-RPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVhgpQV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 425 lperpfglFTHYVDNPSKTAS---TLRGS-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAE 500
Cdd:PRK08314 395 --------FKGYWNRPEATAEafiEIDGKrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQE 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1039777677 501 SAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQlkkEIQEHVKKTTAPYKYPRKV 554
Cdd:PRK08314 467 ACVIATPDPRRGETVKAVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPRIV 517
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
88-554 |
1.61e-65 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 220.62 E-value: 1.61e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 88 RWSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYrlqsskakcIIT 167
Cdd:cd05941 11 SITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY---------VIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 168 DdtlapavdavaakcenlhsklivsqhsregwgnlkemmkyaSDSHTCVDtkhdeMMAIYFTSGTTGPPKMIGHTHSSfg 247
Cdd:cd05941 82 D-----------------------------------------SEPSLVLD-----PALILYTSGTTGRPKGVVLTHAN-- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 248 lglsvngrfwldlIASDVMWNTSDTGWAKS--------------AWSSVFSP-WTQGACVFahyLPRFESTSILQTLSKF 312
Cdd:cd05941 114 -------------LAANVRALVDAWRWTEDdvllhvlplhhvhgLVNALLCPlFAGASVEF---LPKFDPKEVAISRLMP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 313 PITVFCSAPTAY--------RMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGN-F 383
Cdd:cd05941 178 SITVFMGVPTIYtrllqyyeAHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNpL 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 384 KGmKIKPGSMGKPSPAFDVKILDENGA-TLPPGQEGDIalQVlpeRPFGLFTHYVDNPSKTASTLRG-SFYITGDRGYMD 461
Cdd:cd05941 258 DG-ERRPGTVGMPLPGVQARIVDEETGePLPRGEVGEI--QV---RGPSVFKEYWNKPEATKEEFTDdGWFKTGDLGVVD 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 462 EDGYFWFVAR-SDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQLKkeiqEH 540
Cdd:cd05941 332 EDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEELK----EW 407
|
490
....*....|....
gi 1039777677 541 VKKTTAPYKYPRKV 554
Cdd:cd05941 408 AKQRLAPYKRPRRL 421
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
86-554 |
1.28e-63 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 215.23 E-value: 1.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 86 ELRWSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCI 165
Cdd:cd05934 1 GRRWTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 166 ITDdtlaPAvdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhdemmAIYFTSGTTGPPK--MIGHTH 243
Cdd:cd05934 80 VVD----PA--------------------------------------------------SILYTSGTTGPPKgvVITHAN 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 244 SSFGLGLSVNgrfWLDLIASDVMW--------NTSDTGWAkSAWSSvfspwtQGACVFahyLPRFESTSILQTLSKFPIT 315
Cdd:cd05934 106 LTFAGYYSAR---RFGLGEDDVYLtvlplfhiNAQAVSVL-AALSV------GATLVL---LPRFSASRFWSDVRRYGAT 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 316 VFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAgePINPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGK 395
Cdd:cd05934 173 VTNYLGAMLSYLLAQPPSPDDRAHRLRAAYGA--PNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGR 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 396 PSPAFDVKILDENGATLPPGQEGDIALQvlPERPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDI 475
Cdd:cd05934 251 PAPGYEVRIVDDDGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDM 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 476 ILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYK-SHDqeqlkkEIQEHVKKTTAPYKYPRKV 554
Cdd:cd05934 329 IRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETlDPE------ELFAFCEGQLAYFKVPRYI 402
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
66-554 |
8.75e-62 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 212.48 E-value: 8.75e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 66 EKAGKRLSNPAFwwIDG-NGEELrwSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 144
Cdd:cd05904 13 LFASAHPSRPAL--IDAaTGRAL--TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 145 TTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSQHSREGwgnlkemMKYASDSHTC-VDTKHDEM 223
Cdd:cd05904 88 NPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLALPVVLLDSAEFDSLSFSDL-------LFEADEAEPPvVVIKQDDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 224 MAIYFTSGTTGPPK--MIGH---------THSSFGLGLSVNGRFWLDLIASDVMwntsdtGWAKSAWSSVFSpwtqGACV 292
Cdd:cd05904 161 AALLYSSGTTGRSKgvMLTHrnliamvaqFVAGEGSNSDSEDVFLCVLPMFHIY------GLSSFALGLLRL----GATV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 293 FAhyLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKK-TGLDIYEGY 371
Cdd:cd05904 231 VV--MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVDLGQGY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 372 GQTET---VLICGNFKGMKIKPGSMGKPSPAFDVKILD-ENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTL 447
Cdd:cd05904 309 GMTEStgvVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWI-----RGPSIMKGYLNNPEATAATI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 448 RG-SFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyk 526
Cdd:cd05904 384 DKeGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPG-- 461
|
490 500
....*....|....*....|....*...
gi 1039777677 527 SHDQEQlkkEIQEHVKKTTAPYKYPRKV 554
Cdd:cd05904 462 SSLTED---EIMDFVAKQVAPYKKVRKV 486
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
90-552 |
2.81e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 212.59 E-value: 2.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 90 SFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:PRK06710 51 TFSVFHDKVKRFANYL-QKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 170 TLAPAVDAV--AAKCENL-----------------------HSKLIV---SQHSREGWGNLKEMMKYASDshTCVDTKHD 221
Cdd:PRK06710 130 LVFPRVTNVqsATKIEHVivtriadflpfpknllypfvqkkQSNLVVkvsESETIHLWNSVEKEVNTGVE--VPCDPEND 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 222 eMMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLdliasdvmWNTSDTGWAKSAWSSVFSPWTQGAC----VFAHY- 296
Cdd:PRK06710 208 -LALLQYTGGTTGFPKGVMLTHKNL-VSNTLMGVQWL--------YNCKEGEEVVLGVLPFFHVYGMTAVmnlsIMQGYk 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 297 ---LPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQ 373
Cdd:PRK06710 278 mvlIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 374 TETVLIC-GNFKGMKIKPGSMGKPSPAFDVKILD-ENGATLPPGQEGDIALQVlPErpfgLFTHYVDNPSKTASTLRGSF 451
Cdd:PRK06710 358 TESSPVThSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKG-PQ----IMKGYWNKPEETAAVLQDGW 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 452 YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdyksHDQE 531
Cdd:PRK06710 433 LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLK-----EGTE 507
|
490 500
....*....|....*....|.
gi 1039777677 532 QLKKEIQEHVKKTTAPYKYPR 552
Cdd:PRK06710 508 CSEEELNQFARKYLAAYKVPK 528
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
53-541 |
3.97e-60 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 210.42 E-value: 3.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 53 NFAKDVLDQWTnmekaGKRLSNPAFWWIDGNGEELRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANV 132
Cdd:cd05968 61 NIVEQLLDKWL-----ADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGL-RALGVGKGDRVGIYLPMIPEIVPAFL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 133 ACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD---------TLAPAVDAVAAKCENLhSKLIVSQHSregwGNLK 203
Cdd:cd05968 135 AVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgftrrgrevNLKEEADKACAQCPTV-EKVVVVRHL----GNDF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 204 EMMKYASDSHTCVDTKH----------DEMMAIYfTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTG 273
Cdd:cd05968 210 TPAKGRDLSYDEEKETAgdgaerteseDPLMIIY-TSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 274 WAKSAWSsVFSPWTQGACVFAHY-LPRFESTSIL-QTLSKFPITVFCSAPTAYRMLV--QNDMSRSYKFNSLKHCVSAGE 349
Cdd:cd05968 289 WMMGPWL-IFGGLILGATMVLYDgAPDHPKADRLwRMVEDHEITHLGLSPTLIRALKprGDAPVNAHDLSSLRVLGSTGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 350 PINPEVMeQWRKKTGLD----IYEGYGQTETVL-ICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPgQEGDIALqv 424
Cdd:cd05968 368 PWNPEPW-NWLFETVGKgrnpIINYSGGTEISGgILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVL-- 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 425 lpERPF-GLFTHYVDNPSKTASTLRGSF---YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAE 500
Cdd:cd05968 444 --LAPWpGMTRGFWRDEDRYLETYWSRFdnvWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLE 521
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1039777677 501 SAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLKKEIQEHV 541
Cdd:cd05968 522 SAAIGVPHPVKGEAIVCFVVLKPGVT--PTEALAEELMERV 560
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
84-554 |
2.72e-57 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 200.49 E-value: 2.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 84 GEELRWSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAK 163
Cdd:PRK07514 24 PDGLRYTYGDLDAASARLANLLV-ALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 164 CIITDDTLAPAVDAVAAKCENLHskliVSQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPK--M--- 238
Cdd:PRK07514 103 LVVCDPANFAWLSKIAAAAGAPH----VETLDADGTGSLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKgaMlsh 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 239 ---------------------------IGHTHssfGLGLSVNGRfwldLIAsdvmwntsdtgwaksawssvfspwtqGAC 291
Cdd:PRK07514 179 gnllsnaltlvdywrftpddvlihalpIFHTH---GLFVATNVA----LLA--------------------------GAS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 292 VFahYLPRFESTSILQTLSKfpITVFCSAPTAY-RMLVQNDMSRsykfNSLKH---CVSAGEPINPEVMEQWRKKTGLDI 367
Cdd:PRK07514 226 MI--FLPKFDPDAVLALMPR--ATVMMGVPTFYtRLLQEPRLTR----EAAAHmrlFISGSAPLLAETHREFQERTGHAI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 368 YEGYGQTETVLICGN-FKGMKIkPGSMGKPSPAFDVKILD-ENGATLPPGQEGDIalQVlpeRPFGLFTHYVDNPSKTAS 445
Cdd:PRK07514 298 LERYGMTETNMNTSNpYDGERR-AGTVGFPLPGVSLRVTDpETGAELPPGEIGMI--EV---KGPNVFKGYWRMPEKTAE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 446 TLRG-SFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPD 524
Cdd:PRK07514 372 EFRAdGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPG 451
|
490 500 510
....*....|....*....|....*....|
gi 1039777677 525 yKSHDQEQLKKEIQEHVkkttAPYKYPRKV 554
Cdd:PRK07514 452 -AALDEAAILAALKGRL----ARFKQPKRV 476
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
89-554 |
2.87e-57 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 200.23 E-value: 2.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 89 WSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITD 168
Cdd:cd05926 15 LTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 169 -DTLAPAVDAvAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKH---DEMMAIYFTSGTTGPPKMIGHTHs 244
Cdd:cd05926 94 kGELGPASRA-ASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVplpDDLALILHTSGTTGRPKGVPLTH- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 245 sfgLGLSVNGRFwldlIASDVMWNTSDT-----------GWAKSAWSSVFSpwtQGACVFAhylPRFESTSILQTLSKFP 313
Cdd:cd05926 172 ---RNLAASATN----ITNTYKLTPDDRtlvvmplfhvhGLVASLLSTLAA---GGSVVLP---PRFSASTFWPDVRDYN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 314 ITVFCSAPTAYRMLVQNDMSRSYK-FNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETV--LICGNFKGMKIKP 390
Cdd:cd05926 239 ATWYTAVPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTSNPLPPGPRKP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 391 GSMGKPSPAfDVKILDENGATLPPGQEGDIALQ---VlperpfglfTH-YVDNPSKTA-STLRGSFYITGDRGYMDEDGY 465
Cdd:cd05926 319 GSVGKPVGV-EVRILDEDGEILPPGVVGEICLRgpnV---------TRgYLNNPEANAeAAFKDGWFRTGDLGYLDADGY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 466 FWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKShdqeqLKKEIQEHVKKTT 545
Cdd:cd05926 389 LFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASV-----TEEELRAFCRKHL 463
|
....*....
gi 1039777677 546 APYKYPRKV 554
Cdd:cd05926 464 AAFKVPKKV 472
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
80-554 |
6.92e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 191.27 E-value: 6.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 80 IDGNGEElrWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 159
Cdd:PRK08276 5 MAPSGEV--VTYGELEARSNRLAHGLRAL-GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 160 SKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMaiyFTSGTTGPPKMI 239
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETAGADML---YSSGTTGRPKGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 240 ------GHTHSSFGLGLSVNGRFwldliasdvMWNTSDTGWAKSA--WSSVFSPWTQGACVFAH---YLPRFESTSILQT 308
Cdd:PRK08276 159 krplpgLDPDEAPGMMLALLGFG---------MYGGPDSVYLSPAplYHTAPLRFGMSALALGGtvvVMEKFDAEEALAL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 309 LSKFPITVFCSAPTAY-RMLVQNDMSR-SYKFNSLKHCVSAGEPINPEVMEQ----WrkktGLDIYEGYGQTE----TVL 378
Cdd:PRK08276 230 IERYRVTHSQLVPTMFvRMLKLPEEVRaRYDVSSLRVAIHAAAPCPVEVKRAmidwW----GPIIHEYYASSEgggvTVI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 379 ICGNFKGmkiKPGSMGKPSPAfDVKILDENGATLPPGQEGDIALQvLPERPFglftHYVDNPSKTASTLRGSFYIT-GDR 457
Cdd:PRK08276 306 TSEDWLA---HPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE-MDGYPF----EYHNDPEKTAAARNPHGWVTvGDV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 458 GYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKshDQEQLKKEI 537
Cdd:PRK08276 377 GYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGAD--AGDALAAEL 454
|
490
....*....|....*..
gi 1039777677 538 QEHVKKTTAPYKYPRKV 554
Cdd:PRK08276 455 IAWLRGRLAHYKCPRSI 471
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
85-554 |
3.08e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 189.76 E-value: 3.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 85 EELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:PRK08316 33 GDRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 165 IITDDTLAPAVDAVAAKCENLHSKLIVS---QHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGH 241
Cdd:PRK08316 112 FLVDPALAPTAEAALALLPVDTLILSLVlggREAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 242 THSSFgLGLSVNGRFWLDLIASDVMWNtsdtgwA----KSAWSSVF-SPWTQ-GACVfaHYLPRFESTSILQTLSKFPIT 315
Cdd:PRK08316 192 THRAL-IAEYVSCIVAGDMSADDIPLH------AlplyHCAQLDVFlGPYLYvGATN--VILDAPDPELILRTIEAERIT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 316 VFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSaGEPINP-EVMEQWRKK-TGLDIYEGYGQTE-----TVLicgNFKGMKI 388
Cdd:PRK08316 263 SFFAPPTVWISLLRHPDFDTRDLSSLRKGYY-GASIMPvEVLKELRERlPGLRFYNCYGQTEiaplaTVL---GPEEHLR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 389 KPGSMGKPSPAFDVKILDENGATLPPGQEGDIAlqvlpERPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWF 468
Cdd:PRK08316 339 RPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIV-----HRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 469 VARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLKKEIQEHVKKTTAPY 548
Cdd:PRK08316 414 VDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKA-----GATVTEDELIAHCRARLAGF 488
|
....*.
gi 1039777677 549 KYPRKV 554
Cdd:PRK08316 489 KVPKRV 494
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
90-551 |
4.94e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 187.56 E-value: 4.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 90 SFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:PRK06178 60 TYAELDELSDRFAALL-RQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 170 TLAPAVDAVAAKCEnLHSKLIVSQH--------------------SREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFT 229
Cdd:PRK06178 139 QLAPVVEQVRAETS-LRHVIVTSLAdvlpaeptlplpdslraprlAAAGAIDLLPALRACTAPVPLPPPALDALAALNYT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 230 SGTTGPPKMIGHTHSsfglglsvngrfwlDLIasdvmwntsDTGWAKSAWSSVFSPWTqgacVFAHYLPRF----ESTSI 305
Cdd:PRK06178 218 GGTTGMPKGCEHTQR--------------DMV---------YTAAAAYAVAVVGGEDS----VFLSFLPEFwiagENFGL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 306 LqtlskFPI----TV----------FCSAPTAYR-----MLVQN-----DMSRS--YKFNSLKH--CVSAGEPINPEVME 357
Cdd:PRK06178 271 L-----FPLfsgaTLvllarwdavaFMAAVERYRvtrtvMLVDNavelmDHPRFaeYDLSSLRQvrVVSFVKKLNPDYRQ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 358 QWRKKTGLDIYEG-YGQTETvLICGNF-KGM-------KIKPGSMGKPSPAFDVKILD-ENGATLPPGQEGDIALqvlpe 427
Cdd:PRK06178 346 RWRALTGSVLAEAaWGMTET-HTCDTFtAGFqdddfdlLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVV----- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 428 RPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSP 507
Cdd:PRK06178 420 RTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRP 499
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1039777677 508 DPIRGEVVKAFIVLNPDyksHDQEQlkKEIQEHVKKTTAPYKYP 551
Cdd:PRK06178 500 DPDKGQVPVAFVQLKPG---ADLTA--AALQAWCRENMAVYKVP 538
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
86-523 |
1.90e-51 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 185.35 E-value: 1.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 86 ELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCI 165
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 166 ITDDTLAPAVDAVAAKCENLHSKLIV----SQHSREGWGNLKemMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGH 241
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLdapaSVSVPAGWSTAP--LPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 242 THSSFglglsvngrFW--------LDLIASDVMWNTSDTgWAKSAWSSVFSPWTQGACVfaHYLPRFESTSILQTLSKFP 313
Cdd:PRK06155 201 PHAQF---------YWwgrnsaedLEIGADDVLYTTLPL-FHTNALNAFFQALLAGATY--VLEPRFSASGFWPAVRRHG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 314 ITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPinPEVMEQWRKKTGLDIYEGYGQTETVLICGNFKGMKiKPGSM 393
Cdd:PRK06155 269 ATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSM 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 394 GKPSPAFDVKILDENGATLPPGQEGDIALQVlpERPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSD 473
Cdd:PRK06155 346 GRLAPGFEARVVDEHDQELPDGEPGELLLRA--DEPFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIK 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1039777677 474 DIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNP 523
Cdd:PRK06155 424 DAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRD 473
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
84-554 |
6.74e-50 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 180.06 E-value: 6.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 84 GEELRWSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAK 163
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 164 CIITDDTLAPAVDAVAAKCENLHSKLIVSqhsregwgnLKEMMKYASDShtCVDTKHDEMMAIYFTSGTTGPPKMIGHTH 243
Cdd:PRK06839 103 VLFVEKTFQNMALSMQKVSYVQRVISITS---------LKEIEDRKIDN--FVEKNESASFIICYTSGTTGKPKGAVLTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 244 SSFGLGlSVNGRFWLDLIASDV------MWNTSDTGWAksawssVFSPWTQGACVFahyLP-RFESTSILQTLSKFPITV 316
Cdd:PRK06839 172 ENMFWN-ALNNTFAIDLTMHDRsivllpLFHIGGIGLF------AFPTLFAGGVII---VPrKFEPTKALSMIEKHKVTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 317 FCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKtGLDIYEGYGQTET-----VLICGNFKGmkiKPG 391
Cdd:PRK06839 242 VMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETsptvfMLSEEDARR---KVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 392 SMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVAR 471
Cdd:PRK06839 318 SIGKPVLFCDYELIDENKNKVEVGEVGELLI-----RGPNVMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVGR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 472 SDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLKKEIQEHVKKTTAPYKYP 551
Cdd:PRK06839 393 KKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKS-----SSVLIEKDVIEHCRLFLAKYKIP 467
|
...
gi 1039777677 552 RKV 554
Cdd:PRK06839 468 KEI 470
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
57-554 |
5.01e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 179.43 E-value: 5.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 57 DVLDQwtNMEKAGKRlsnPAFWWIdgnGEELrwSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLR 136
Cdd:PRK05605 36 DLYDN--AVARFGDR---PALDFF---GATT--TYAELGKQVRRAAAGL-RALGVRPGDRVAIVLPNCPQHIVAFYAVLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 137 TGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAP---------------AVD------------------AVAAKCE 183
Cdd:PRK05605 105 LGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPtverlrrttpletivSVNmiaampllqrlalrlpipALRKARA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 184 NLHSKL-------IVSQHSREGWGNLkemmkyasDSHTCVdTKHDEMMaIYFTSGTTGPPKMIGHTHSsfglGLSVN--- 253
Cdd:PRK05605 185 ALTGPApgtvpweTLVDAAIGGDGSD--------VSHPRP-TPDDVAL-ILYTSGTTGKPKGAQLTHR----NLFANaaq 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 254 GRFWLDLIASD----------------VMWNTsdtgwaksawssvFSPWTQGACVFahyLPRFESTSILQTLSKFPITVF 317
Cdd:PRK05605 251 GKAWVPGLGDGpervlaalpmfhayglTLCLT-------------LAVSIGGELVL---LPAPDIDLILDAMKKHPPTWL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 318 CSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKP 396
Cdd:PRK05605 315 PGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 397 SPAFDVKILD-EN-GATLPPGQEGDIAL---QVlperpfglFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVAR 471
Cdd:PRK05605 395 FPDTEVRIVDpEDpDETMPDGEEGELLVrgpQV--------FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 472 SDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLKkeiqEHVKKTTAPYKYP 551
Cdd:PRK05605 467 IKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDPEGLR----AYCREHLTRYKVP 541
|
...
gi 1039777677 552 RKV 554
Cdd:PRK05605 542 RRF 544
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
70-554 |
6.97e-48 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 177.06 E-value: 6.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 70 KRLSNPAFWWIDGN-GEELRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIPG- 144
Cdd:PRK10524 65 KRPEQLALIAVSTEtDEERTYTFRQLHDEVNRMAAML-RSLGVQRGDRVLIYMPMIAEAAFAMLACARIGaihSVVFGGf 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 145 -TTQLTQkdilyRLQSSKAKCIITDDTLA---------PAVDAVAAKCENLHSK-LIVSQhsregwgNLKEMMK------ 207
Cdd:PRK10524 144 aSHSLAA-----RIDDAKPVLIVSADAGSrggkvvpykPLLDEAIALAQHKPRHvLLVDR-------GLAPMARvagrdv 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 208 -YAS------DSHT-CVDTKHDEMMAIYFTSGTTGPPKMI-----GHThssFGLGLSVNGRFwlDLIASDVMWNTSDTGW 274
Cdd:PRK10524 212 dYATlraqhlGARVpVEWLESNEPSYILYTSGTTGKPKGVqrdtgGYA---VALATSMDTIF--GGKAGETFFCASDIGW 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 275 AKSAWSSVFSPWTQG-ACVFAHYLPRFESTSIL-QTLSKFPITVFCSAPTAYRMLVQNDMS--RSYKFNSLKHCVSAGEP 350
Cdd:PRK10524 287 VVGHSYIVYAPLLAGmATIMYEGLPTRPDAGIWwRIVEKYKVNRMFSAPTAIRVLKKQDPAllRKHDLSSLRALFLAGEP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 351 INpEVMEQWRKKT-GLDIYEGYGQTET----VLICGNFKGMKIKPGSMGKPSPAFDVKILDEN-GATLPPGQEGDIALQV 424
Cdd:PRK10524 367 LD-EPTASWISEAlGVPVIDNYWQTETgwpiLAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEG 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 425 -LPerPFGLFTHYVDNpSKTASTLRGSF----YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIA 499
Cdd:PRK10524 446 pLP--PGCMQTVWGDD-DRFVKTYWSLFgrqvYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVA 522
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039777677 500 ESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQ---LKKEIQEHVKKTTAPYKYPRKV 554
Cdd:PRK10524 523 EVAVVGVKDALKGQVAVAFVVPKDSDSLADREArlaLEKEIMALVDSQLGAVARPARV 580
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
65-554 |
7.52e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 175.23 E-value: 7.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 65 MEKAGKRLSN-PAFWWidgnGEElRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIP 143
Cdd:PRK07470 13 LRQAARRFPDrIALVW----GDR-SWTWREIDARVDALAAALAAR-GVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 144 GTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSKL-IVSQHSREGWGNLkeMMKYASDSHTCVDTKHDE 222
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVaIGGARAGLDYEAL--VARHLGARVANAAVDHDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 223 MMAIYFTSGTTGPPKMIGHTHSSfgLGLSVNGRFwldliaSDVMWNTSDTGWaksawSSVFSPWTQGACVfaHYL----- 297
Cdd:PRK07470 165 PCWFFFTSGTTGRPKAAVLTHGQ--MAFVITNHL------ADLMPGTTEQDA-----SLVVAPLSHGAGI--HQLcqvar 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 298 ---------PRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIY 368
Cdd:PRK07470 230 gaatvllpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 369 EGYGQTE-----TVL-ICGNF--KGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVLPerpfgLFTHYVDNP 440
Cdd:PRK07470 310 QYFGLGEvtgniTVLpPALHDaeDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPA-----VFAGYYNNP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 441 SKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIV 520
Cdd:PRK07470 385 EANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCV 464
|
490 500 510
....*....|....*....|....*....|....
gi 1039777677 521 LNpDYKSHDQEqlkkEIQEHVKKTTAPYKYPRKV 554
Cdd:PRK07470 465 AR-DGAPVDEA----ELLAWLDGKVARYKLPKRF 493
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
89-554 |
2.71e-46 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 168.29 E-value: 2.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 89 WSFEEL----GLLSRKFANILTeacslQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:cd05912 2 YTFAELfeevSRLAEHLAALGV-----RKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 165 iitddtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTGPPKMIGHT-- 242
Cdd:cd05912 77 --------------------------------------------------------DDIATIMYTSGTTGKPKGVQQTfg 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 243 -H------SSFGLGLSVNGRfWLDLIAsdvMWNTSdtgwaksAWSSVFSPWTQGACVFAHylPRFESTSILQTLSKFPIT 315
Cdd:cd05912 101 nHwwsaigSALNLGLTEDDN-WLCALP---LFHIS-------GLSILMRSVIYGMTVYLV--DKFDAEQVLHLINSGKVT 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 316 VFCSAPTAYRMLVQnDMSRSYKfNSLKHCVSAGEPINPEVMEQWRKKtGLDIYEGYGQTETV--LICGNFKGMKIKPGSM 393
Cdd:cd05912 168 IISVVPTMLQRLLE-ILGEGYP-NNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETCsqIVTLSPEDALNKIGSA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 394 GKPSPAFDVKILDENGatlPPGQEGDIALQ---VLPErpfglfthYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVA 470
Cdd:cd05912 245 GKPLFPVELKIEDDGQ---PPYEVGEILLKgpnVTKG--------YLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLD 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 471 RSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYkshDQEQLKKEIQEHVKKttapYKY 550
Cdd:cd05912 314 RRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI---SEEELIAYCSEKLAK----YKV 386
|
....
gi 1039777677 551 PRKV 554
Cdd:cd05912 387 PKKI 390
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
84-556 |
2.77e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 171.11 E-value: 2.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 84 GEELRWSfeELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAK 163
Cdd:PRK07786 40 GNTTTWR--ELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 164 CIITDDTLAPAVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTH 243
Cdd:PRK07786 117 VVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 244 SSfglglsVNGRFwLDLIASDVMWNTSDTGWAKS------AWSSVFSPWTQGACVFAHYLPRFESTSILQTLSKFPIT-V 316
Cdd:PRK07786 197 AN------LTGQA-MTCLRTNGADINSDVGFVGVplfhiaGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTgI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 317 FCsAPTAYRMLVQNDMSRSYKFnSLKHCVSAGEPINPEVMEQWRKK-TGLDIYEGYGQTE----TVLICGNFKGMKIkpG 391
Cdd:PRK07786 270 FL-VPAQWQAVCAEQQARPRDL-ALRVLSWGAAPASDTLLRQMAATfPEAQILAAFGQTEmspvTCMLLGEDAIRKL--G 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 392 SMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVAR 471
Cdd:PRK07786 346 SVGKVIPTVAARVVDENMNDVPVGEVGEIVY-----RAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 472 SDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQLKKEIQEHVkkttAPYKYP 551
Cdd:PRK07786 421 KKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDLAEFLTDRL----ARYKHP 496
|
....*
gi 1039777677 552 RKVGV 556
Cdd:PRK07786 497 KALEI 501
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
73-554 |
1.75e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 168.63 E-value: 1.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 73 SNPAFWWIDGngeelRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTG---TVLIP-GTTQl 148
Cdd:PRK06188 27 DRPALVLGDT-----RLTYGQLADRISRYIQAF-EALGLGTGDAVALLSLNRPEVLMAIGAAQLAGlrrTALHPlGSLD- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 149 tqkDILYRLQSSKAKCIITDDtlAPAVD---AVAAKCENLHSKLIVSQhSREGWGNLKEMMKYASDSHTCVDTkHDEMMA 225
Cdd:PRK06188 100 ---DHAYVLEDAGISTLIVDP--APFVEralALLARVPSLKHVLTLGP-VPDGVDLLAAAAKFGPAPLVAAAL-PPDIAG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 226 IYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVF----------AH 295
Cdd:PRK06188 173 LAYTGGTTGKPKGVMGTHRS---------------IATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFflptllrggtVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 296 YLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTE 375
Cdd:PRK06188 238 VLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 376 -----TVLICGNFKGMKIKP-GSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRG 449
Cdd:PRK06188 318 apmviTYLRKRDHDPDDPKRlTSCGRPTPGLRVALLDEDGREVAQGEVGEICV-----RGPLVMDGYWNRPEETAEAFRD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 450 SFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHD 529
Cdd:PRK06188 393 GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPG-AAVD 471
|
490 500
....*....|....*....|....*
gi 1039777677 530 QEqlkkEIQEHVKKTTAPYKYPRKV 554
Cdd:PRK06188 472 AA----ELQAHVKERKGSVHAPKQV 492
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
66-554 |
2.23e-45 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 168.62 E-value: 2.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 66 EKAGKRLSNPAFwwIDG-NGEELrwSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 144
Cdd:PLN02246 31 ERLSEFSDRPCL--IDGaTGRVY--TYADVELLSRRVAAGL-HKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 145 TTQLTQKDILYRLQSSKAKCIITddtLAPAVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHDEMM 224
Cdd:PLN02246 106 NPFYTPAEIAKQAKASGAKLIIT---QSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 225 AIYFTSGTTGPPKMIGHTHSsfGLGLSV---------NgrfwLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAh 295
Cdd:PLN02246 183 ALPYSSGTTGLPKGVMLTHK--GLVTSVaqqvdgenpN----LYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILI- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 296 yLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIY-EGYGQT 374
Cdd:PLN02246 256 -MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 375 E--TVL-ICGNF--KGMKIKPGSMGKPSPAFDVKILD-ENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTL- 447
Cdd:PLN02246 335 EagPVLaMCLAFakEPFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICI-----RGPQIMKGYLNDPEATANTId 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 448 RGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnpdyKS 527
Cdd:PLN02246 410 KDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVV-----RS 484
|
490 500
....*....|....*....|....*..
gi 1039777677 528 HDQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:PLN02246 485 NGSEITEDEIKQFVAKQVVFYKRIHKV 511
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
86-560 |
3.81e-45 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 166.71 E-value: 3.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 86 ELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCI 165
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 166 ITDDTLApavdavaakcenlHSKLIVSQHSREGWgnlkemmKYASDSHtcvdtkhdEMMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:cd12118 106 FVDREFE-------------YEDLLAEGDPDFEW-------IPPADEW--------DPIALNYTSGTTGRPKGVVYHHRG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 246 FglglsvngrfWLDLIASDVMWNTSD-------------TGWAksawssvfSPWTQGACVFAHY-LPRFESTSILQTLSK 311
Cdd:cd12118 158 A----------YLNALANILEWEMKQhpvylwtlpmfhcNGWC--------FPWTVAAVGGTNVcLRKVDAKAIYDLIEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 312 FPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQwRKKTGLDIYEGYGQTET---VLICG------- 381
Cdd:cd12118 220 HKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAK-MEELGFDVTHVYGLTETygpATVCAwkpewde 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 382 ---------------NFKGMK----IKPGSMgKPSPAfdvkildeNGATLppgqeGDIALqvlpeRPFGLFTHYVDNPSK 442
Cdd:cd12118 299 lpteerarlkarqgvRYVGLEevdvLDPETM-KPVPR--------DGKTI-----GEIVF-----RGNIVMKGYLKNPEA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 443 TASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLN 522
Cdd:cd12118 360 TAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELK 439
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1039777677 523 PDYKSHDQeqlkkEIQEHVKKTTAPYKYPRKV---GVPGTS 560
Cdd:cd12118 440 EGAKVTEE-----EIIAFCREHLAGFMVPKTVvfgELPKTS 475
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
90-554 |
1.17e-44 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 166.73 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 90 SFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:PRK07059 50 TYGELDELSRALAAWL-QSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 170 TLAPAVDAVAAKCE--------------------NL---HSKLIVSQHSREGWGNLKEMMKY-ASDSHTCVDTKHDEMMA 225
Cdd:PRK07059 129 NFATTVQQVLAKTAvkhvvvasmgdllgfkghivNFvvrRVKKMVPAWSLPGHVRFNDALAEgARQTFKPVKLGPDDVAF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 226 IYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVMWNTSdtgWAKSAWSSvfsPWTQGACVFAHYLP------- 298
Cdd:PRK07059 209 LQYTGGTTGVSKGATLLHRN---------------IVANVLQMEA---WLQPAFEK---KPRPDQLNFVCALPlyhifal 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 299 --------RFESTSIL-----------QTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQW 359
Cdd:PRK07059 268 tvcgllgmRTGGRNILipnprdipgfiKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERW 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 360 RKKTGLDIYEGYGQTET--VLICGNFKGMKIKpGSMGKPSPAFDVKILDENGATLPPGQEGDIAL---QVLPerpfglft 434
Cdd:PRK07059 348 LEMTGCPITEGYGLSETspVATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIrgpQVMA-------- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 435 HYVDNPSKTASTLRGS-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGE 513
Cdd:PRK07059 419 GYWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGE 498
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1039777677 514 VVKAFIVlnpdykSHDQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:PRK07059 499 AVKLFVV------KKDPALTEEDVKAFCKERLTNYKRPKFV 533
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
66-551 |
1.27e-44 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 166.01 E-value: 1.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 66 EKAGKRLSNPAFWWIDGNGEELRWSFEELGLLSRKFANiLTEACSLQRGDRVMVILPKIPEW---WLAnVACLrtGTVLI 142
Cdd:PRK08008 15 DLADVYGHKTALIFESSGGVVRRYSYLELNEEINRTAN-LFYSLGIRKGDKVALHLDNCPEFifcWFG-LAKI--GAIMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 143 PGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSqhsREGWGNLKEMMKYAS--DSHTCVDTKH 220
Cdd:PRK08008 91 PINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLT---RVALPADDGVSSFTQlkAQQPATLCYA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 221 -----DEMMAIYFTSGTTGPPKMIGHTHSsfglglsvNGRF------W-LDLIASDVMWNTSDTGWAKSAWSSVFSPWTQ 288
Cdd:PRK08008 168 pplstDDTAEILFTSGTTSRPKGVVITHY--------NLRFagyysaWqCALRDDDVYLTVMPAFHIDCQCTAAMAAFSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 289 GACVFAhyLPRFESTSILQTLSKFPITVFCSAPtayrMLVQNDMSRSYKFNSLKHCVSagepinpEVM----------EQ 358
Cdd:PRK08008 240 GATFVL--LEKYSARAFWGQVCKYRATITECIP----MMIRTLMVQPPSANDRQHCLR-------EVMfylnlsdqekDA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 359 WRKKTGLDIYEGYGQTETVL-ICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVLPERPfgLFTHYV 437
Cdd:PRK08008 307 FEERFGVRLLTSYGMTETIVgIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKT--IFKEYY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 438 DNPSKTASTLRGSFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVK 516
Cdd:PRK08008 385 LDPKATAKVLEADGWLhTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIK 464
|
490 500 510
....*....|....*....|....*....|....*.
gi 1039777677 517 AFIVLNPDykshdqEQLKKE-IQEHVKKTTAPYKYP 551
Cdd:PRK08008 465 AFVVLNEG------ETLSEEeFFAFCEQNMAKFKVP 494
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
85-554 |
1.68e-44 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 164.75 E-value: 1.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 85 EELRWSFEELGLLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:PRK03640 24 EEKKVTFMELHEAVVSVAGKLAALG-VKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 165 IITDDTLApavdavaakcenlhSKLIVSQHSRegwgnLKEMMKYASDSHTCVDTKH-DEMMAIYFTSGTTGPPKMI---- 239
Cdd:PRK03640 103 LITDDDFE--------------AKLIPGISVK-----FAELMNGPKEEAEIQEEFDlDEVATIMYTSGTTGKPKGViqty 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 240 -GHTHSSFG----LGLSVNGRfWLdliASDVMWNTSdtgwaksAWSSVFSPWTQGACVFAHylPRFESTSILQTLSKFPI 314
Cdd:PRK03640 164 gNHWWSAVGsalnLGLTEDDC-WL---AAVPIFHIS-------GLSILMRSVIYGMRVVLV--EKFDAEKINKLLQTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 315 TVFCSAPTAYRMLVQNDMSRSYKfNSLKHCVSAGEPINPEVMEQWRKKtGLDIYEGYGQTETV-LICG-NFKGMKIKPGS 392
Cdd:PRK03640 231 TIISVVSTMLQRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETAsQIVTlSPEDALTKLGS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 393 MGKPSPAFDVKILDeNGATLPPGQEGDIALQ---VLPerpfGlfthYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFV 469
Cdd:PRK03640 309 AGKPLFPCELKIEK-DGVVVPPFEEGEIVVKgpnVTK----G----YLNREDATRETFQDGWFKTGDIGYLDEEGFLYVL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 470 ARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdyKSHDQEQLKKEIQEHVkkttAPYK 549
Cdd:PRK03640 380 DRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKS---GEVTEEELRHFCEEKL----AKYK 452
|
....*
gi 1039777677 550 YPRKV 554
Cdd:PRK03640 453 VPKRF 457
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
80-552 |
1.69e-44 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 163.85 E-value: 1.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 80 IDGNGeelRWSFEELGLLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 159
Cdd:cd05930 7 VDGDQ---SLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 160 SKAKCIITDdtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkHDEMMAIYFTSGTTGPPKMI 239
Cdd:cd05930 83 SGAKLVLTD---------------------------------------------------PDDLAYVIYTSGSTGKPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 240 GHTHSSFglglsVNGRFW----LDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLPRFESTS---ILQTLSKF 312
Cdd:cd05930 112 MVEHRGL-----VNLLLWmqeaYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATL--VVLPEEVRKDpeaLADLLAEE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 313 PITVFCSAPTAYRMLVQNDMSRSykFNSLKHCVSAGEPINPEVMEQWRKK-TGLDIYEGYGQTETVLICGNF--KGMKIK 389
Cdd:cd05930 184 GITVLHLTPSLLRLLLQELELAA--LPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATVDATYYrvPPDDEE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 390 PGSM--GKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTAStlrgSF-----------YITGD 456
Cdd:cd05930 262 DGRVpiGRPIPNTRVYVLDENLRPVPPGVPGELYI-----GGAGLARGYLNRPELTAE----RFvpnpfgpgermYRTGD 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 457 RGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLKKE 536
Cdd:cd05930 333 LVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDE-----GGELDEEE 407
|
490
....*....|....*.
gi 1039777677 537 IQEHVKKTTAPYKYPR 552
Cdd:cd05930 408 LRAHLAERLPDYMVPS 423
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
88-523 |
3.18e-44 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 162.94 E-value: 3.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 88 RWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKipeWWLANV---ACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAAL-GVGPGDVVAFQLPN---WWEFAVlylACLRIGAVTNPILPFFREHELAFILRRAKAKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 165 IITDDTlapavdavaakcenlhsklivsqhsregWGNlkemMKYASDShtcvdtkhDEMMAIYFTSGTTGPPKMIGHTHS 244
Cdd:cd05903 77 FVVPER----------------------------FRQ----FDPAAMP--------DAVALLLFTSGTTGEPKGVMHSHN 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 245 SfglgLSVNGRFWLDLIA---SDVMWNTSDTGWAKSAWSSVFSPWTQGACVfaHYLPRFESTSILQTLSKFPITVFCSAP 321
Cdd:cd05903 117 T----LSASIRQYAERLGlgpGDVFLVASPMAHQTGFVYGFTLPLLLGAPV--VLQDIWDPDKALALMREHGVTFMMGAT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 322 TAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLICGNfkgmkIKPG-------SMG 394
Cdd:cd05903 191 PFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTS-----ITPApedrrlyTDG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 395 KPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDD 474
Cdd:cd05903 266 RPLPGVEIKVVDDTGATLAPGVEGELLS-----RGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKD 340
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1039777677 475 IILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNP 523
Cdd:cd05903 341 IIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKS 389
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
297-554 |
7.43e-44 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 159.36 E-value: 7.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 297 LPRFESTSILQTLSKFPITVFCS-APTAYRMLVQNDMSrSYKFNSLKHcVSAGEpiNPEVMEQWRKKTGLDIYEGYGQTE 375
Cdd:cd17637 72 MEKFDPAEALELIEEEKVTLMGSfPPILSNLLDAAEKS-GVDLSSLRH-VLGLD--APETIQRFEETTGATFWSLYGQTE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 376 T---VLICGNFKgmkiKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFY 452
Cdd:cd17637 148 TsglVTLSPYRE----RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVV-----RGPLVFQGYWNLPELTAYTFRNGWH 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 453 ITGDRGYMDEDGYFWFVARS--DDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdykshDQ 530
Cdd:cd17637 219 HTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKP-----GA 293
|
250 260
....*....|....*....|....
gi 1039777677 531 EQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:cd17637 294 TLTADELIEFVGSRIARYKKPRYV 317
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
90-503 |
1.04e-43 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 160.89 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 90 SFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqLtqkDILY---RLQS----SKA 162
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP----L---DPAYpaeRLAFiledAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 163 KCIITDDTLAPAVDAVAAKCENLHSKLIVSQHSRegwgnlkemmkyASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHT 242
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLELAALDDA------------PAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 243 HSSFGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVF----AHYLPRFESTSILqtLSKFPITVFC 318
Cdd:TIGR01733 142 HRSLVNLLAWLARRY-GLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVvppeDEERDDAALLAAL--IAEHPVTVLN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 319 SAPTAYRMLvqnDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTG-LDIYEGYGQTETVLICGnfkgMKIKPGSM---- 393
Cdd:TIGR01733 218 LTPSLLALL---AAALPPALASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWST----ATLVDPDDapre 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 394 -----GKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTA---------STLRGSFYITGDRGY 459
Cdd:TIGR01733 291 spvpiGRPLANTRLYVLDDDLRPVPVGVVGELYI-----GGPGVARGYLNRPELTAerfvpdpfaGGDGARLYRTGDLVR 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1039777677 460 MDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAV 503
Cdd:TIGR01733 366 YLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
85-552 |
2.89e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 163.02 E-value: 2.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 85 EELRWSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:PRK12583 42 QALRYTWRQLADAVDRLARGLL-ALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRW 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 165 IITDD------------TLAPAV---DAVAAKCENL-HSKLIVSQHSRE-----GWGNLKEMMKYASDSHTCVDT---KH 220
Cdd:PRK12583 121 VICADafktsdyhamlqELLPGLaegQPGALACERLpELRGVVSLAPAPppgflAWHELQARGETVSREALAERQaslDR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 221 DEMMAIYFTSGTTGPPKMIGHTHSSfglgLSVNGRF---WLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFahyL 297
Cdd:PRK12583 201 DDPINIQYTSGTTGFPKGATLSHHN----ILNNGYFvaeSLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLV---Y 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 298 PR--FESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGL-DIYEGYGQT 374
Cdd:PRK12583 274 PNeaFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 375 ET---VLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSF 451
Cdd:PRK12583 354 ETspvSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCT-----RGYSVMKGYWNNPEATAESIDEDG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 452 YI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQ 530
Cdd:PRK12583 429 WMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEE 508
|
490 500
....*....|....*....|..
gi 1039777677 531 eqlkkEIQEHVKKTTAPYKYPR 552
Cdd:PRK12583 509 -----ELREFCKARIAHFKVPR 525
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
90-554 |
4.87e-43 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 162.15 E-value: 4.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 90 SFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:PRK08974 50 TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 170 TLAPAVDAVAAKCENLHSKL--IVSQHSReGWGNL--------KEMM-KY---ASDSHTCV------------DTKHDEM 223
Cdd:PRK08974 130 NFAHTLEKVVFKTPVKHVILtrMGDQLST-AKGTLvnfvvkyiKRLVpKYhlpDAISFRSAlhkgrrmqyvkpELVPEDL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 224 MAIYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIASDVMWntsdtgwAKSAWSSVFSPwtqGACVFAHYLPRFE-- 301
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRN---------------MLANLEQ-------AKAAYGPLLHP---GKELVVTALPLYHif 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 302 -------------STSILQT-----------LSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVME 357
Cdd:PRK08974 264 altvncllfielgGQNLLITnprdipgfvkeLKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 358 QWRKKTGLDIYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDiaLQVL-PERPFGlfth 435
Cdd:PRK08974 344 RWVKLTGQYLLEGYGLTEcSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGE--LWVKgPQVMLG---- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 436 YVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVV 515
Cdd:PRK08974 418 YWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAV 497
|
490 500 510
....*....|....*....|....*....|....*....
gi 1039777677 516 KAFIVLNpdykshDQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:PRK08974 498 KIFVVKK------DPSLTEEELITHCRRHLTGYKVPKLV 530
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
75-554 |
8.34e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 160.63 E-value: 8.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 75 PAFWwIDGNGEELrwSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDIL 154
Cdd:PRK13391 14 PAVI-MASTGEVV--TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 155 YRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSQH-SREGWGNLKEMMKYASDSHTCVDTKHDEMMaiyFTSGTT 233
Cdd:PRK13391 90 YIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLDGDgELEGFVGYAEAVAGLPATPIADESLGTDML---YSSGTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 234 GPPKMIGHTHSSFGLGLSVNgrfWLDLIASdvMWN-TSDTGW---------AKSAWSSVfspwTQ--GACVFAhyLPRFE 301
Cdd:PRK13391 167 GRPKGIKRPLPEQPPDTPLP---LTAFLQR--LWGfRSDMVYlspaplyhsAPQRAVML----VIrlGGTVIV--MEHFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 302 STSILQTLSKFPITVFCSAPTAY-RML-VQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLI 379
Cdd:PRK13391 236 AEQYLALIEEYGVTHTQLVPTMFsRMLkLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 380 CG-NFKGMKIKPGSMGKPSPAfDVKILDENGATLPPGQEGDIALQvlPERPFglftHYVDNPSKTASTL--RGSFYITGD 456
Cdd:PRK13391 316 TAcDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFE--GGRPF----EYLNDPAKTAEARhpDGTWSTVGD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 457 RGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeQLKKE 536
Cdd:PRK13391 389 IGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGP--ALAAE 466
|
490
....*....|....*...
gi 1039777677 537 IQEHVKKTTAPYKYPRKV 554
Cdd:PRK13391 467 LIAFCRQRLSRQKCPRSI 484
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
85-541 |
2.37e-42 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 161.28 E-value: 2.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 85 EELRWSFEELglLSR--KFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVlIPGTTQLTQKDILYRLQSSKA 162
Cdd:PRK07529 55 RPETWTYAEL--LADvtRTANLLH-SLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-NPINPLLEPEQIAELLRAAGA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 163 KCIIT-----DDTLAPAVDAVAAKCENLhsKLIVSQHSREGWGNLK--------------------EMMKYASDSHTCVD 217
Cdd:PRK07529 131 KVLVTlgpfpGTDIWQKVAEVLAALPEL--RTVVEVDLARYLPGPKrlavplirrkaharildfdaELARQPGDRLFSGR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 218 TKHDEMMAIYF-TSGTTGPPKMIGHTHSsfglGLSVNGrfWLdlIASDVMWNTSDTGWA-------KSAWSSVFSPWTQG 289
Cdd:PRK07529 209 PIGPDDVAAYFhTGGTTGMPKLAQHTHG----NEVANA--WL--GALLLGLGPGDTVFCglplfhvNALLVTGLAPLARG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 290 A-CVFA--------HYLPRFesTSILQtlsKFPITVFCSAPTAYRMLVQ-----NDMSrsykfnSLKHCVSAGEPINPEV 355
Cdd:PRK07529 281 AhVVLAtpqgyrgpGVIANF--WKIVE---RYRINFLSGVPTVYAALLQvpvdgHDIS------SLRYALCGAAPLPVEV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 356 MEQWRKKTGLDIYEGYGQTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKI--LDENGATL---PPGQEGDIALQvlpeRP 429
Cdd:PRK07529 350 FRRFEAATGVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQRVRVviLDDAGRYLrdcAVDEVGVLCIA----GP 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 430 fGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDP 509
Cdd:PRK07529 426 -NVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDA 504
|
490 500 510
....*....|....*....|....*....|..
gi 1039777677 510 IRGEVVKAFIVLNPDyKSHDQEQLKKEIQEHV 541
Cdd:PRK07529 505 HAGELPVAYVQLKPG-ASATEAELLAFARDHI 535
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
84-554 |
2.17e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 156.71 E-value: 2.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 84 GEELrwSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAK 163
Cdd:PRK13390 22 GEQV--SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 164 CIITddtlAPAVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTcvdtKHDEMMAIYFTSGTTGPPKMI---- 239
Cdd:PRK13390 99 VLVA----SAALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGPRLT----EQPCGAVMLYSSGTTGFPKGIqpdl 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 240 -GHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKS-AWSSVFSPwTQGACVFAHylpRFESTSILQTLSKFPITVF 317
Cdd:PRK13390 171 pGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWCSMVHA-LGGTVVLAK---RFDAQATLGHVERYRITVT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 318 CSAPTAY-RMLVQNDMSRS-YKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTE----TVLICGNFKGmkiKPG 391
Cdd:PRK13390 247 QMVPTMFvRLLKLDADVRTrYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEahgmTFIDSPDWLA---HPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 392 SMGKpSPAFDVKILDENGATLPPGQEGDIALQ--VLPERpfglfthYVDNPSKTASTLRGS--FYIT-GDRGYMDEDGYF 466
Cdd:PRK13390 324 SVGR-SVLGDLHICDDDGNELPAGRIGTVYFErdRLPFR-------YLNDPEKTAAAQHPAhpFWTTvGDLGSVDEDGYL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 467 WFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKShdQEQLKKEIQEHVKKTTA 546
Cdd:PRK13390 396 YLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRG--SDELARELIDYTRSRIA 473
|
....*...
gi 1039777677 547 PYKYPRKV 554
Cdd:PRK13390 474 HYKAPRSV 481
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
90-554 |
4.15e-41 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 156.96 E-value: 4.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 90 SFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 170 TLAPAVDAVAAKCE---------------------NL---HSKLIVSQHSREGWGNLKEMMKYASdSHTC--VDTKHDEM 223
Cdd:PRK08751 132 NFGTTVQQVIADTPvkqvittglgdmlgfpkaalvNFvvkYVKKLVPEYRINGAIRFREALALGR-KHSMptLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 224 MAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRfWLD-----------LIASDVMWNTsdtgWAKSAWSSVFSPWtqGACV 292
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQ-WLAgtgkleegcevVITALPLYHI----FALTANGLVFMKI--GGCN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 293 FAHYLPRfESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYG 372
Cdd:PRK08751 284 HLISNPR-DMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 373 QTETV-LICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIAL---QVLperpfglfTHYVDNPSKTASTLR 448
Cdd:PRK08751 363 LTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIkgpQVM--------KGYWKRPEETAKVMD 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 449 GSFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnpdykS 527
Cdd:PRK08751 435 ADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV------K 508
|
490 500
....*....|....*....|....*..
gi 1039777677 528 HDQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:PRK08751 509 KDPALTAEDVKAHARANLTGYKQPRII 535
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
86-552 |
1.53e-39 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 151.91 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 86 ELRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCI 165
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEAL-KKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 166 ITDDTLAPAVDAVAAKceNLHSKLIVSQHSREGWGNLKEMMKYASD---------SHTCVDTKHDEMMA-IYFTSGTTGP 235
Cdd:cd17642 121 FCSKKGLQKVLNVQKK--LKIIKTIIILDSKEDYKGYQCLYTFITQnlppgfneyDFKPPSFDRDEQVAlIMNSSGSTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 236 PKMIGHTHSSFGLGLSVngrfwldliASDVMWntsdtGWAKSAWSSVFS--PWTQG---------ACVFAH--YLPRFES 302
Cdd:cd17642 199 PKGVQLTHKNIVARFSH---------ARDPIF-----GNQIIPDTAILTviPFHHGfgmfttlgyLICGFRvvLMYKFEE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 303 TSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLD-IYEGYGQTET---VL 378
Cdd:cd17642 265 ELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETtsaIL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 379 ICGNfkgMKIKPGSMGKPSPAFDVKILD-ENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKT-ASTLRGSFYITGD 456
Cdd:cd17642 345 ITPE---GDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCV-----KGPMIMKGYVNNPEATkALIDKDGWLHSGD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 457 RGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLnpdykSHDQEQLKKE 536
Cdd:cd17642 417 IAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVL-----EAGKTMTEKE 491
|
490
....*....|....*.
gi 1039777677 537 IQEHVKKTTAPYKYPR 552
Cdd:cd17642 492 VMDYVASQVSTAKRLR 507
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
81-556 |
1.97e-39 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 151.74 E-value: 1.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 81 DGNGEELRWSFEELGLLSRKFANILTEaCSLQRGDrvmVILPKIPEWWLANV---ACLRTGTVLIPGTTQLTQKDILYRL 157
Cdd:PRK13295 48 LGTGAPRRFTYRELAALVDRVAVGLAR-LGVGRGD---VVSCQLPNWWEFTVlylACSRIGAVLNPLMPIFRERELSFML 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 158 QSSKAKCIItddtlAPAV----DAvAAKCENLHSKLIVSQH----SREGWGNLKEMM-----KYASDSHTCVDTKH---D 221
Cdd:PRK13295 124 KHAESKVLV-----VPKTfrgfDH-AAMARRLRPELPALRHvvvvGGDGADSFEALLitpawEQEPDAPAILARLRpgpD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 222 EMMAIYFTSGTTGPPKMIGHTHSS-FGLGLSVNGRfwLDLIASDVMWNTS----DTGWAKSAwssvFSPWTQGACVFahY 296
Cdd:PRK13295 198 DVTQLIYTSGTTGEPKGVMHTANTlMANIVPYAER--LGLGADDVILMASpmahQTGFMYGL----MMPVMLGATAV--L 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 297 LPRFESTSILQTLSKFPITvFCSAPTAYRM-LVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTE 375
Cdd:PRK13295 270 QDIWDPARAAELIRTEGVT-FTMASTPFLTdLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 376 TVLICGnfkgmkIKPG--------SMGKPSPAFDVKILDENGATLPPGQEGdiALQVlpeRPFGLFTHYVDNPSKTASTL 447
Cdd:PRK13295 349 NGAVTL------TKLDdpderastTDGCPLPGVEVRVVDADGAPLPAGQIG--RLQV---RGCSNFGGYLKRPQLNGTDA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 448 RGSFYiTGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKS 527
Cdd:PRK13295 418 DGWFD-TGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPG-QS 495
|
490 500
....*....|....*....|....*....
gi 1039777677 528 HDQEQLKKEIQEHvkKTTAPYkYPRKVGV 556
Cdd:PRK13295 496 LDFEEMVEFLKAQ--KVAKQY-IPERLVV 521
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
75-553 |
2.78e-39 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 149.70 E-value: 2.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 75 PAFWWidgngEELRWSFEELGLLSRKFANILTEACsLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDIL 154
Cdd:cd05945 8 PAVVE-----GGRTLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 155 YRLQSSKAKCIITDDtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTG 234
Cdd:cd05945 82 EILDAAKPALLIADG---------------------------------------------------DDNAYIIFTSGSTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 235 PPKMIGHTHS---SFGLGLsvNGRFwlDLIASDVMWNTSDtgwaksaWS---SVFS---PWTQGACVFAhyLPRFESTSI 305
Cdd:cd05945 111 RPKGVQISHDnlvSFTNWM--LSDF--PLGPGDVFLNQAP-------FSfdlSVMDlypALASGATLVP--VPRDATADP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 306 LQ---TLSKFPITVFCSAPTAYRMLvqndmSRSYKFN-----SLKHCVSAGEPINPEVMEQWRKKT-GLDIYEGYGQTET 376
Cdd:cd05945 178 KQlfrFLAEHGITVWVSTPSFAAMC-----LLSPTFTpeslpSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 377 VLICgnfKGMKIKPGSM--------GKPSPAFDVKILDENGATLPPGQEGDIAL---QVlperpfglFTHYVDNPSKTAS 445
Cdd:cd05945 253 TVAV---TYIEVTPEVLdgydrlpiGYAKPGAKLVILDEDGRPVPPGEKGELVIsgpSV--------SKGYLNNPEKTAA 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 446 TLRGSF----YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVL 521
Cdd:cd05945 322 AFFPDEgqraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVP 401
|
490 500 510
....*....|....*....|....*....|..
gi 1039777677 522 NPdyksHDQEQLKKEIQEHVKKTTAPYKYPRK 553
Cdd:cd05945 402 KP----GAEAGLTKAIKAELAERLPPYMIPRR 429
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
81-560 |
3.07e-39 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 150.86 E-value: 3.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 81 DGNGEELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILpkipeW--------WLAnVAClrTGTVLIPGTTQLTQKD 152
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRRL-GVKPGDRVATLA-----WnthrhlelYYA-VPG--MGAVLHTINPRLFPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 153 ILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSQHSR------EGWGNLKEMMKYASDSHTCVDTKHDEMMAI 226
Cdd:cd12119 89 IAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAmpepagVGVLAYEELLAAESPEYDWPDFDENTAAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 227 YFTSGTTGPPKMIGHTHSSFGLG-LSVNGRFWLDLIASDV------MWNTSdtgwaksAWSSVFSPWTQGACvfaHYLP- 298
Cdd:cd12119 169 CYTSGTTGNPKGVVYSHRSLVLHaMAALLTDGLGLSESDVvlpvvpMFHVN-------AWGLPYAAAMVGAK---LVLPg 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 299 -RFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKtGLDIYEGYGQTET- 376
Cdd:cd12119 239 pYLDPASLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETs 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 377 -VLICGnfkgmKIKPG--------------SMGKPSPAFDVKILDENGATLP--PGQEGDiaLQVlpeR-PFgLFTHYVD 438
Cdd:cd12119 318 pLGTVA-----RPPSEhsnlsedeqlalraKQGRPVPGVELRIVDDDGRELPwdGKAVGE--LQV---RgPW-VTKSYYK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 439 NPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAF 518
Cdd:cd12119 387 NDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAV 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1039777677 519 IVLNPdykshDQEQLKKEIQEHVKKTTAPYKYPRKV----GVPGTS 560
Cdd:cd12119 467 VVLKE-----GATVTAEELLEFLADKVAKWWLPDDVvfvdEIPKTS 507
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
74-543 |
3.65e-39 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 151.79 E-value: 3.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 74 NPAFWWIDgNGEELRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDI 153
Cdd:COG1022 27 RVALREKE-DGIWQSLTWAEFAERVRALAAGL-LALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 154 LYRLQSSKAKCIIT-DDTLAPAVDAVAAKCENLhsKLIVSQHSREGWG-----NLKEMMKYASDSHT-------CVDTKH 220
Cdd:COG1022 105 AYILNDSGAKVLFVeDQEQLDKLLEVRDELPSL--RHIVVLDPRGLRDdprllSLDELLALGREVADpaelearRAAVKP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 221 DEMMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDV------MWNTSDTGWaksawsSVFSpWTQGACVfa 294
Cdd:COG1022 183 DDLATIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDRtlsflpLAHVFERTV------SYYA-LAAGATV-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 295 HYLPRFEStsILQTLSKFPITVFCSAP------------------------------TAYRMLVQNDMSRS--------Y 336
Cdd:COG1022 253 AFAESPDT--LAEDLREVKPTFMLAVPrvwekvyagiqakaeeagglkrklfrwalaVGRRYARARLAGKSpslllrlkH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 337 KF--------------NSLKHCVSAGEPINPEVMEQWRKkTGLDIYEGYGQTET-VLICGNFKGmKIKPGSMGKPSPAFD 401
Cdd:COG1022 331 ALadklvfsklrealgGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETsPVITVNRPG-DNRIGTVGPPLPGVE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 402 VKIlDENGatlppgqEgdiaLQVlpeR-PfGLFTHYVDNPSKTASTLR--GSFYiTGDRGYMDEDGYFWFVARSDDII-L 477
Cdd:COG1022 409 VKI-AEDG-------E----ILV---RgP-NVMKGYYKNPEATAEAFDadGWLH-TGDIGELDEDGFLRITGRKKDLIvT 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 478 SSGYRIGPFEVESALIEHPSIAESAVVsspdpirGE----VVkAFIVLNPD------------YKSHDQ----EQLKKEI 537
Cdd:COG1022 472 SGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpfLA-ALIVPDFEalgewaeenglpYTSYAElaqdPEVRALI 543
|
....*.
gi 1039777677 538 QEHVKK 543
Cdd:COG1022 544 QEEVDR 549
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
82-559 |
4.59e-39 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 152.36 E-value: 4.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 82 GNGEE--LRWSFEELGL-LSRKFANILTEACSL---------QRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLT 149
Cdd:PLN02654 101 GNGDKiaIYWEGNEPGFdASLTYSELLDRVCQLanylkdvgvKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 150 QKDILYRLQSSKAKCIITDDT---------LAPAVDAVAAKCENLHSKLIV-------SQHSREG--WGNLKEMM----- 206
Cdd:PLN02654 181 AESLAQRIVDCKPKVVITCNAvkrgpktinLKDIVDAALDESAKNGVSVGIcltyenqLAMKREDtkWQEGRDVWwqdvv 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 207 -KYASDSHTCVDTKHDEMMAIYfTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSP 285
Cdd:PLN02654 261 pNYPTKCEVEWVDAEDPLFLLY-TSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 286 WTQGACVFA-HYLPRF-ESTSILQTLSKFPITVFCSAPTAYRMLVQNDMS--RSYKFNSLKHCVSAGEPINPEVmeqWR- 360
Cdd:PLN02654 340 MLNGATVLVfEGAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEyvTRHSRKSLRVLGSVGEPINPSA---WRw 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 361 -----KKTGLDIYEGYGQTETvlicGNFKGMKI------KPGSMGKPSPAFDVKILDENGATLppgqEGDIA--LQVLPE 427
Cdd:PLN02654 417 ffnvvGDSRCPISDTWWQTET----GGFMITPLpgawpqKPGSATFPFFGVQPVIVDEKGKEI----EGECSgyLCVKKS 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 428 RPFGLFTHYVDNPSKTASTLR--GSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVS 505
Cdd:PLN02654 489 WPGAFRTLYGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVG 568
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039777677 506 SPDPIRGEVVKAFIVLNPDYKShdQEQLKKEIQEHVKKTTAPYKYPRKV----GVPGT 559
Cdd:PLN02654 569 IEHEVKGQGIYAFVTLVEGVPY--SEELRKSLILTVRNQIGAFAAPDKIhwapGLPKT 624
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
53-554 |
5.00e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 151.07 E-value: 5.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 53 NFAKDV----------LDQWTNM----EKAGKRLSN-PAFWWIdgnGEELRWSfeELGLLSRKFANILTEACSLQRGDRV 117
Cdd:PRK05677 4 NFWKDKypagiaaeinPDEYPNIqavlKQSCQRFADkPAFSNL---GKTLTYG--ELYKLSGAFAAWLQQHTDLKPGDRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 118 MVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCE----------NLHS 187
Cdd:PRK05677 79 AVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGvkhvivtevaDMLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 188 ---------------KLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSsfglglsv 252
Cdd:PRK05677 159 plkrllinavvkhvkKMVPAYHLPQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHR-------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 253 ngrfwlDLIASDVMWNTSDTGWAKSAWSSVFSP--------WTQGaCVF-----AHYL----PRfESTSILQTLSKFPIT 315
Cdd:PRK05677 231 ------NLVANMLQCRALMGSNLNEGCEILIAPlplyhiyaFTFH-CMAmmligNHNIlisnPR-DLPAMVKELGKWKFS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 316 VFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETV-LICGNFKGmKIKPGSMG 394
Cdd:PRK05677 303 GFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSpVVSVNPSQ-AIQVGTIG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 395 KPSPAFDVKILDENGATLPPGQEGDIAL---QVLperpfglfTHYVDNPSKTASTLRGSFYI-TGDRGYMDEDGYFWFVA 470
Cdd:PRK05677 382 IPVPSTLCKVIDDDGNELPLGEVGELCVkgpQVM--------KGYWQRPEATDEILDSDGWLkTGDIALIQEDGYMRIVD 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 471 RSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDykshdqEQLKKE-IQEHVKKTTAPYK 549
Cdd:PRK05677 454 RKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPG------ETLTKEqVMEHMRANLTGYK 527
|
....*
gi 1039777677 550 YPRKV 554
Cdd:PRK05677 528 VPKAV 532
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
84-556 |
7.05e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 149.27 E-value: 7.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 84 GEELrwSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAK 163
Cdd:PRK06145 25 DQEI--SYAEFHQRILQAAGML-HARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 164 CIITDDTLapavDAVAAKcenLHSKLIVSQHSREGWGNLKEMMKYASDSHTcvdTKHDEMMAIYFTSGTTGPPKMIGHTH 243
Cdd:PRK06145 102 LLLVDEEF----DAIVAL---ETPKIVIDAAAQADSRRLAQGGLEIPPQAA---VAPTDLVRLMYTSGTTDRPKGVMHSY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 244 SSF---------GLGLSVNGRFW----------LDLIASDVMWntsdtgwaksawssvfspwtQGACVFAHYlpRFESTS 304
Cdd:PRK06145 172 GNLhwksidhviALGLTASERLLvvgplyhvgaFDLPGIAVLW--------------------VGGTLRIHR--EFDPEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 305 ILQTLSKFPITVFCSAPTAY-RMLVQNDMSRsYKFNSLKHCVSAGEPiNPE--VMEQWRKKTGLDIYEGYGQTETvliCG 381
Cdd:PRK06145 230 VLAAIERHRLTCAWMAPVMLsRVLTVPDRDR-FDLDSLAWCIGGGEK-TPEsrIRDFTRVFTRARYIDAYGLTET---CS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 382 NFKGMKI-----KPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVlPERPFGlfthYVDNPSKTASTLRGSFYITGD 456
Cdd:PRK06145 305 GDTLMEAgreieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRG-PKVTKG----YWKDPEKTAEAFYGDWFRSGD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 457 RGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdykshDQEQLKKE 536
Cdd:PRK06145 380 VGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNP-----GATLTLEA 454
|
490 500
....*....|....*....|
gi 1039777677 537 IQEHVKKTTAPYKYPRKVGV 556
Cdd:PRK06145 455 LDRHCRQRLASFKVPRQLKV 474
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
225-554 |
1.15e-38 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 148.29 E-value: 1.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 225 AIYFTSGTTGPPKMIGHTHSsFGLGLSVNGRFWLDLIasdvmwntsdtGWakSAWSSVFSPWT------QGACVFAHYL- 297
Cdd:cd05929 129 KMLYSGGTTGRPKGIKRGLP-GGPPDNDTLMAAALGF-----------GP--GADSVYLSPAPlyhaapFRWSMTALFMg 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 298 ------PRFESTSILQTLSKFPITVFCSAPTAY-RMLVQNDMSR-SYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYE 369
Cdd:cd05929 195 gtlvlmEKFDPEEFLRLIERYRVTFAQFVPTMFvRLLKLPEAVRnAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 370 GYGQTETV-LICGNFKGMKIKPGSMGKPSPAfDVKILDENGATLPPGQEGDIALqvlpeRPFGLFThYVDNPSKTA-STL 447
Cdd:cd05929 275 YYGGTEGQgLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYF-----ANGPGFE-YTNDPEKTAaARN 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 448 RGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAfiVLNPDYKS 527
Cdd:cd05929 348 EGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGA 425
|
330 340
....*....|....*....|....*..
gi 1039777677 528 HDQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:cd05929 426 DAGTALAEELIAFLRDRLSRYKCPRSI 452
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
88-551 |
1.20e-38 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 149.51 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 88 RWSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIT 167
Cdd:PRK06087 49 SYTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 168 D-------------------DTLAP--AVDAVAAKcenlHSKLIVSQhsregwgnlkEMMKYASDSHTCvDTKHDEMMAI 226
Cdd:PRK06087 128 PtlfkqtrpvdlilplqnqlPQLQQivGVDKLAPA----TSSLSLSQ----------IIADYEPLTTAI-TTHGDELAAV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 227 YFTSGTTGPPKMIGHTHSSFGLG-LSVNGRfwLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFahYLPRFESTSI 305
Cdd:PRK06087 193 LFTSGTEGLPKGVMLTHNNILASeRAYCAR--LNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSV--LLDIFTPDAC 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 306 LQTLSKFPITVFCSA-PTAYRMLVQNDMSRSYkFNSLKHCVSAGEPInPEVMEQWRKKTGLDIYEGYGQTETV--LICGN 382
Cdd:PRK06087 269 LALLEQQRCTCMLGAtPFIYDLLNLLEKQPAD-LSALRFFLCGGTTI-PKKVARECQQRGIKLLSVYGSTESSphAVVNL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 383 FKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIAlqvlpERPFGLFTHYVDNPSKTASTL--RGSFYiTGDRGYM 460
Cdd:PRK06087 347 DDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEA-----SRGPNVFMGYLDEPELTARALdeEGWYY-SGDLCRM 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 461 DEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEqlkkEIQEH 540
Cdd:PRK06087 421 DEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLE----EVVAF 496
|
490
....*....|..
gi 1039777677 541 V-KKTTAPYKYP 551
Cdd:PRK06087 497 FsRKRVAKYKYP 508
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
226-556 |
2.55e-38 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 148.37 E-value: 2.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 226 IYFTSGTTGPPKmiGHTHSSFGlGLSVngrfwldliASDVMwntSDTGWAKSAWSSVFSP----WTQGACVFAHYLP--- 298
Cdd:PRK13382 201 ILLTSGTTGTPK--GARRSGPG-GIGT---------LKAIL---DRTPWRAEEPTVIVAPmfhaWGFSQLVLAASLActi 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 299 ----RFESTSILQTLSKFPITVFCSAPTAYR--MLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYG 372
Cdd:PRK13382 266 vtrrRFDPEATLDLIDRHRATGLAVVPVMFDriMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYN 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 373 QTETVLIC-GNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVdnPSKTASTLRGsF 451
Cdd:PRK13382 346 ATEAGMIAtATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFV-----RNDTQFDGYT--SGSTKDFHDG-F 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 452 YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQE 531
Cdd:PRK13382 418 MASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG-ASATPE 496
|
330 340
....*....|....*....|....*
gi 1039777677 532 QLKkeiqEHVKKTTAPYKYPRKVGV 556
Cdd:PRK13382 497 TLK----QHVRDNLANYKVPRDIVV 517
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
80-554 |
2.65e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 148.54 E-value: 2.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 80 IDGNGEelrWSFEELGLLSRKFANILTEAcSLQRGDRVMViLPKIPEWW-LANVACLRTGTVLI-----PGTTQLtqKDI 153
Cdd:PRK07788 69 IDERGT---LTYAELDEQSNALARGLLAL-GVRAGDGVAV-LARNHRGFvLALYAAGKVGARIIllntgFSGPQL--AEV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 154 LYRLqssKAKCIITDDTLAPAVDAVAAKCENLHSkLIVS----QHSREGWGNLKEMMKYASDSHTCVDTKHDEMmaIYFT 229
Cdd:PRK07788 142 AARE---GVKALVYDDEFTDLLSALPPDLGRLRA-WGGNpdddEPSGSTDETLDDLIAGSSTAPLPKPPKPGGI--VILT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 230 SGTTGPPKMIGHTHSSfglGLSVNGRFwLDLI---ASDVMWNTS----DTGWAKSAWSsvfspWTQGACVFAHYlpRFES 302
Cdd:PRK07788 216 SGTTGTPKGAPRPEPS---PLAPLAGL-LSRVpfrAGETTLLPApmfhATGWAHLTLA-----MALGSTVVLRR--RFDP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 303 TSILQTLSKFPITVFCSAPTAY-RML-VQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTE----T 376
Cdd:PRK07788 285 EATLEDIAKHKATALVVVPVMLsRILdLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEvafaT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 377 VlicGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKtaSTLRGsFYITGD 456
Cdd:PRK07788 365 I---ATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFV-----GNGFPFEGYTDGRDK--QIIDG-LLSSGD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 457 RGYMDEDGYfWFVA-RSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDykshdqEQL-K 534
Cdd:PRK07788 434 VGYFDEDGL-LFVDgRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPG------AALdE 506
|
490 500
....*....|....*....|
gi 1039777677 535 KEIQEHVKKTTAPYKYPRKV 554
Cdd:PRK07788 507 DAIKDYVRDNLARYKVPRDV 526
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
220-546 |
2.67e-38 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 144.93 E-value: 2.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 220 HDEMMAIYFTSGTTGPPKMIGHTHSSF---GLGLSVNGRFWLDliasDVMWNTSDTGWAKSAWSSVFSPWTQGACVF--- 293
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEvynAWMLALNSLFDPD----DVLLCGLPLFHVNGSVVTLLTPLASGAHVVlag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 294 -AHYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSykFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYG 372
Cdd:cd05944 77 pAGYRNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVNAD--ISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 373 QTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLP-----PGQEGDIALQvlpeRPfGLFTHYVDNPSKTAST 446
Cdd:cd05944 155 LTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRLlrdcaPDEVGEICVA----GP-GVFGGYLYTEGNKNAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 447 LRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYK 526
Cdd:cd05944 230 VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAV 309
|
330 340
....*....|....*....|
gi 1039777677 527 ShDQEQLKKEIQEHVKKTTA 546
Cdd:cd05944 310 V-EEEELLAWARDHVPERAA 328
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
111-554 |
3.76e-38 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 147.54 E-value: 3.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 111 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIT-DDTLAPAVDAVAAKCENLH--- 186
Cdd:PRK12406 33 VRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAhADLLHGLASALPAGVTVLSvpt 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 187 -----SKLIVSQHSR---------EGWgnLKEMMKYASDshtcvdTKHDEMMAIYfTSGTTGPPK--------------- 237
Cdd:PRK12406 113 ppeiaAAYRISPALLtppagaidwEGW--LAQQEPYDGP------PVPQPQSMIY-TSGTTGHPKgvrraaptpeqaaaa 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 238 --MIGHTHssfglGLSVNGRfwldLIASDVMWNTSDTGWAKSAWSsvfspwtqgacvFAHYL---PRFESTSILQTLSKF 312
Cdd:PRK12406 184 eqMRALIY-----GLKPGIR----ALLTGPLYHSAPNAYGLRAGR------------LGGVLvlqPRFDPEELLQLIERH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 313 PITVFCSAPTAY-RML-VQNDMSRSYKFNSLKHCVSAGEPINPEV----MEQWrkktGLDIYEGYGQTET--VLICGNFK 384
Cdd:PRK12406 243 RITHMHMVPTMFiRLLkLPEEVRAKYDVSSLRHVIHAAAPCPADVkramIEWW----GPVIYEYYGSTESgaVTFATSED 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 385 GMKiKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVlPERPfgLFThYVDNPSKTASTLRGSFYITGDRGYMDEDG 464
Cdd:PRK12406 319 ALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRI-AGNP--DFT-YHNKPEKRAEIDRGGFITSGDVGYLDADG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 465 YFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEqlkkEIQEHVKKT 544
Cdd:PRK12406 394 YLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPG-ATLDEA----DIRAQLKAR 468
|
490
....*....|
gi 1039777677 545 TAPYKYPRKV 554
Cdd:PRK12406 469 LAGYKVPKHI 478
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
221-554 |
4.04e-38 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 143.96 E-value: 4.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 221 DEMMAIYFTSGTTGPPKMIGHTHSSFglglsVNGRFwldlIASDVMWNTSDT------------GWAKSAWSSVfspwTQ 288
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNI-----VNNGY----FIGERLGLTEQDrlcipvplfhcfGSVLGVLACL----TH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 289 GA-CVFAHylPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGL-D 366
Cdd:cd05917 69 GAtMVFPS--PSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 367 IYEGYGQTETVLICgnFKGMKIKP-----GSMGKPSPAFDVKILD-ENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNP 440
Cdd:cd05917 147 VTIAYGMTETSPVS--TQTRTDDSiekrvNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCI-----RGYSVMKGYWNDP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 441 SKTASTLRGS-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFI 519
Cdd:cd05917 220 EKTAEAIDGDgWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWI 299
|
330 340 350
....*....|....*....|....*....|....*
gi 1039777677 520 VLNPDYKSHDQeqlkkEIQEHVKKTTAPYKYPRKV 554
Cdd:cd05917 300 RLKEGAELTEE-----DIKAYCKGKIAHYKVPRYV 329
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
111-554 |
2.68e-37 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 144.12 E-value: 2.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 111 LQRGDRVMVILPKIPE--WWLANV--ACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENlh 186
Cdd:cd05922 15 GVRGERVVLILPNRFTyiELSFAVayAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPD-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 187 SKLIVSQhsrEGWgnlkemmKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGL-SVNGRfwLDLIASDV 265
Cdd:cd05922 93 PGTVLDA---DGI-------RAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANArSIAEY--LGITADDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 266 MWNTSDTGWAkSAWSSVFSPWTQGACVFAHYLPRFESTsILQTLSKFPITVFCSAPTAYRMLVQNDMSRSyKFNSLKHCV 345
Cdd:cd05922 161 ALTVLPLSYD-YGLSVLNTHLLRGATLVLTNDGVLDDA-FWEDLREHGATGLAGVPSTYAMLTRLGFDPA-KLPSLRYLT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 346 SAGEPINPEVMEQWRKK-TGLDIYEGYGQTETvlicgnFKGMKI--------KPGSMGKPSPAFDVKILDENGATLPPGQ 416
Cdd:cd05922 238 QAGGRLPQETIARLRELlPGAQVYVMYGQTEA------TRRMTYlpperileKPGSIGLAIPGGEFEILDDDGTPTPPGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 417 EGDIAlqvlPERPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHP 496
Cdd:cd05922 312 PGEIV----HRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIG 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039777677 497 SIAESAVVSSPDPIrGEVVKAFIVLNPDYKSHDqeqlkkeIQEHVKKTTAPYKYPRKV 554
Cdd:cd05922 388 LIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKD-------VLRSLAERLPPYKVPATV 437
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
226-554 |
1.35e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 142.44 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 226 IYFTSGTTGPPKmighthssfGLGLSVNGrfwldlIASDVmwntsdTGWAKsAWSsvfspWTqGACVFAHYLP------- 298
Cdd:PRK07787 133 IVYTSGTTGPPK---------GVVLSRRA------IAADL------DALAE-AWQ-----WT-ADDVLVHGLPlfhvhgl 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 299 ------------------RFESTSILQTLSkFPITVFCSAPTAYRMLVQN-DMSRSykFNSLKHCVSAGEPINPEVMEQW 359
Cdd:PRK07787 185 vlgvlgplrignrfvhtgRPTPEAYAQALS-EGGTLYFGVPTVWSRIAADpEAARA--LRGARLLVSGSAALPVPVFDRL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 360 RKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVlpeRPFGLFTHYVDN 439
Cdd:PRK07787 262 AALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGETVGELQV---RGPTLFDGYLNR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 440 PSKTASTLRG-SFYITGDRGYMDEDGYFWFVAR-SDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKA 517
Cdd:PRK07787 339 PDATAAAFTAdGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVA 418
|
330 340 350
....*....|....*....|....*....|....*..
gi 1039777677 518 FIVLNPDYKShdqeqlkKEIQEHVKKTTAPYKYPRKV 554
Cdd:PRK07787 419 YVVGADDVAA-------DELIDFVAQQLSVHKRPREV 448
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
89-543 |
2.50e-36 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 141.19 E-value: 2.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 89 WSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITD 168
Cdd:cd05907 6 ITWAEFAEEVRALAKGL-IALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 169 DTlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdtkhDEMMAIYFTSGTTGPPKMIGHTHSSFgl 248
Cdd:cd05907 85 DP--------------------------------------------------DDLATIIYTSGTTGRPKGVMLSHRNI-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 249 gLSVngrfwldLIASDVMWNTSDTGW-----------AKSAWSSVfsPWTQGACVFahYLPRFEStsILQTLSKFPITVF 317
Cdd:cd05907 113 -LSN-------ALALAERLPATEGDRhlsflplahvfERRAGLYV--PLLAGARIY--FASSAET--LLDDLSEVRPTVF 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 318 CSAPTAYRML----VQNDMSRSYKF-------NSLKHCVSAGEPINPEVMEQWRKkTGLDIYEGYGQTETV-LICGNFKG 385
Cdd:cd05907 179 LAVPRVWEKVyaaiKVKAVPGLKRKlfdlavgGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSaVVTLNPPG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 386 mKIKPGSMGKPSPAFDVKIldengatlppGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTL--RGSFYiTGDRGYMDED 463
Cdd:cd05907 258 -DNRIGTVGKPLPGVEVRI----------ADDGEILV-----RGPNVMLGYYKNPEATAEALdaDGWLH-TGDLGEIDED 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 464 GYFWFVARSDD-IILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPirgeVVKAFIVLNPDY-----KSHD-------- 529
Cdd:cd05907 321 GFLHITGRKKDlIITSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVPDPEAleawaEEHGiaytdvae 396
|
490
....*....|....*..
gi 1039777677 530 ---QEQLKKEIQEHVKK 543
Cdd:cd05907 397 laaNPAVRAEIEAAVEA 413
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
98-554 |
4.03e-36 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 142.43 E-value: 4.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 98 SRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDA 177
Cdd:PLN02330 65 TRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 178 VAAKCenlhskLIVSQHSREG---WGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTH---------SS 245
Cdd:PLN02330 144 LGLPV------IVLGEEKIEGavnWKELLEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHrnlvanlcsSL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 246 FGLGLSVNGRF-WLDLIASDVMWNTSDTGWAKSAwssvfspwTQGACVFahyLPRFESTSILQTLSKFPITVFCSAPTAY 324
Cdd:PLN02330 218 FSVGPEMIGQVvTLGLIPFFHIYGITGICCATLR--------NKGKVVV---MSRFELRTFLNALITQEVSFAPIVPPII 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 325 RMLVQNDMSRSYKFNSLK--HCVSAGEPINPEVMEQWRKK-TGLDIYEGYGQTETVLICGNF----KGMKI-KPGSMGKP 396
Cdd:PLN02330 287 LNLVKNPIVEEFDLSKLKlqAIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEHSCITLTHgdpeKGHGIaKKNSVGFI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 397 SPAFDVKILD-ENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYI-TGDRGYMDEDGYFWFVARSDD 474
Cdd:PLN02330 367 LPNLEVKFIDpDTGRSLPKNTPGELCV-----RSQCVMQGYYNNKEETDRTIDEDGWLhTGDIGYIDDDGDIFIVDRIKE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 475 IILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQeqlkkEIQEHVKKTTAPYKYPRKV 554
Cdd:PLN02330 442 LIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEE-----DILNFVAANVAHYKKVRVV 516
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
85-560 |
2.14e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 140.08 E-value: 2.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 85 EELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:PRK08162 40 GDRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 165 IITDDTLAPAVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMKYAS-----DSHTCVDTKHDEMMAIY--FTSGTTGPPK 237
Cdd:PRK08162 119 LIVDTEFAEVAREALALLPGPKPLVIDVDDPEYPGGRFIGALDYEAflasgDPDFAWTLPADEWDAIAlnYTSGTTGNPK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 238 MIGHTHSSFGLGLSVNGRFWlDLIASDV-MW-------NtsdtGWAksawssvFsPWT----QGACVFahyLPRFESTSI 305
Cdd:PRK08162 199 GVVYHHRGAYLNALSNILAW-GMPKHPVyLWtlpmfhcN----GWC-------F-PWTvaarAGTNVC---LRKVDPKLI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 306 LQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQwRKKTGLDIYEGYGQTET---VLICGN 382
Cdd:PRK08162 263 FDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIAK-MEEIGFDLTHVYGLTETygpATVCAW 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 383 FKGMKIKP--------GSMGKPSPAFD-VKILD-ENGATLPPGQE--GDIALqvlpeRPFGLFTHYVDNPSKTASTLRGS 450
Cdd:PRK08162 342 QPEWDALPlderaqlkARQGVRYPLQEgVTVLDpDTMQPVPADGEtiGEIMF-----RGNIVMKGYLKNPKATEEAFAGG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 451 FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdykshDQ 530
Cdd:PRK08162 417 WFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKD-----GA 491
|
490 500 510
....*....|....*....|....*....|...
gi 1039777677 531 EQLKKEIQEHVKKTTAPYKYPRKV---GVPGTS 560
Cdd:PRK08162 492 SATEEEIIAHCREHLAGFKVPKAVvfgELPKTS 524
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
66-565 |
1.21e-34 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 138.03 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 66 EKAGKRLSN-PAFwwiDGNGEELrwSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 144
Cdd:PRK12492 31 ERSCKKFADrPAF---SNLGVTL--SYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 145 TTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLH---SKLIVSQHSREGW------GNLKEMMKY------- 208
Cdd:PRK12492 106 NPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYlieAKMGDLLPAAKGWlvntvvDKVKKMVPAyhlpqav 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 209 ---------ASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSsfglglsvngrfwlDLIAS--DVMWNTSDTGwaks 277
Cdd:PRK12492 186 pfkqalrqgRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHG--------------NLVANmlQVRACLSQLG---- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 278 awSSVFSPWTQGACVFAHYLPRFE---------------STSILQT-----------LSKFPITVFCSAPTAYRMLVQND 331
Cdd:PRK12492 248 --PDGQPLMKEGQEVMIAPLPLYHiyaftancmcmmvsgNHNVLITnprdipgfikeLGKWRFSALLGLNTLFVALMDHP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 332 MSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETV-LICGNFKGMKIKPGSMGKPSPAFDVKILDENGA 410
Cdd:PRK12492 326 GFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 411 TLPPGQEGDIALQVlPERPFGlfthYVDNPSKTASTLRGS-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVE 489
Cdd:PRK12492 406 ELPLGERGELCIKG-PQVMKG----YWQQPEATAEALDAEgWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIE 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039777677 490 SALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnPDYKSHDQEQLKKeiqeHVKKTTAPYKYPRKVGVPGTSDVSPV 565
Cdd:PRK12492 481 DVVMAHPKVANCAAIGVPDERSGEAVKLFVV--ARDPGLSVEELKA----YCKENFTGYKVPKHIVLRDSLPMTPV 550
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
215-535 |
1.20e-33 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 134.38 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 215 CVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGL-SVNGRFwlDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVF 293
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVeQITAIF--DPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 294 AHYLPrFESTSILQTLSKFPITVFCSAPTAYRMLVQNdmSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQ 373
Cdd:cd05909 219 FHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARA--AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGT 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 374 TETV-LICGNFKGMKIKPGSMGKPSPAFDVKILDENGAT-LPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSF 451
Cdd:cd05909 296 TECSpVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLV-----RGPNVMLGYLNEPELTSFAFGDGW 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 452 YITGDRGYMDEDGYFWFVARsddiiLSSGYRIG----PFE-VESALIEH-PSIAESAVVSSPDPIRGEVVKAFIVLNPDY 525
Cdd:cd05909 371 YDTGDIGKIDGEGFLTITGR-----LSRFAKIAgemvSLEaIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTDTD 445
|
330
....*....|
gi 1039777677 526 KSHDQEQLKK 535
Cdd:cd05909 446 PSSLNDILKN 455
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
111-556 |
2.23e-32 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 132.46 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 111 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITD----DTLAPAVDAVAAKcenlh 186
Cdd:PRK06060 52 LSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSdalrDRFQPSRVAEAAE----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 187 sklIVSQHSREGWGNLKEMMKYASDSHTcvdtkhdemmaiyFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVM 266
Cdd:PRK06060 127 ---LMSEAARVAPGGYEPMGGDALAYAT-------------YTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 267 WNTSDTGWAKSAWSSVFSPWTQGACVFAHYLP-RFESTSILQTlsKFPITVFCSAPTAYRMLVqnDMSRSYKFNSLKHCV 345
Cdd:PRK06060 191 LCSARMYFAYGLGNSVWFPLATGGSAVINSAPvTPEAAAILSA--RFGPSVLYGVPNFFARVI--DSCSPDSFRSLRCVV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 346 SAGEPINPEVMEQWRKK-TGLDIYEGYGQTEtvlICGNFKGMKI---KPGSMGKPSPAFDVKILDENGATLPPGQEGDIA 421
Cdd:PRK06060 267 SAGEALELGLAERLMEFfGGIPILDGIGSTE---VGQTFVSNRVdewRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLW 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 422 LqvlpeRPFGLFTHYVDNPSKTASTlrGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAES 501
Cdd:PRK06060 344 V-----RGPAIAKGYWNRPDSPVAN--EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEA 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1039777677 502 AVVSSPDPIRGEVVKAFIVlnPDYKSHDQEQLKKEIQEHVKKTTAPYKYPRKVGV 556
Cdd:PRK06060 417 AVVAVRESTGASTLQAFLV--ATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAV 469
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
289-554 |
5.98e-32 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 126.26 E-value: 5.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 289 GACVFahyLPRFESTSILQTLSKFPIT-VFCSAPTAYRMLVQNDMSRsYKFNSLKHCVSAGE--PINPEVMEQWRKKTGl 365
Cdd:cd17636 67 GTNVF---VRRVDAEEVLELIEAERCThAFLLPPTIDQIVELNADGL-YDLSSLRSSPAAPEwnDMATVDTSPWGRKPG- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 366 diyeGYGQTETV-LICGNFKGMKIKpGSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTA 444
Cdd:cd17636 142 ----GYGQTEVMgLATFAALGGGAI-GGAGRPSPLVQVRILDEDGREVPDGEVGEIVA-----RGPTVMAGYWNRPEVNA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 445 STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPD 524
Cdd:cd17636 212 RRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPG 291
|
250 260 270
....*....|....*....|....*....|
gi 1039777677 525 ykSHDQEQlkkEIQEHVKKTTAPYKYPRKV 554
Cdd:cd17636 292 --ASVTEA---ELIEHCRARIASYKKPKSV 316
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
225-554 |
1.02e-31 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 125.84 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 225 AIYFTSGTTGPPKMIGHTHSSFGLGLSVngrfwldLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYL-----PR 299
Cdd:cd17635 5 AVIFTSGTTGEPKAVLLANKTFFAVPDI-------LQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLcvtggEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 300 FESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGE-PINPEV-MEQWRKKTglDIYEGYGQTET- 376
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSrAIAADVrFIEATGLT--NTAQVYGLSETg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 377 VLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVlPERPFGlfthYVDNPSKTASTLRGSFYITGD 456
Cdd:cd17635 156 TALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKS-PANMLG----YWNNPERTAEVLIDGWVNTGD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 457 RGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdykSHDQEQLKKE 536
Cdd:cd17635 231 LGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS----AELDENAIRA 306
|
330
....*....|....*...
gi 1039777677 537 IQEHVKKTTAPYKYPRKV 554
Cdd:cd17635 307 LKHTIRRELEPYARPSTI 324
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
87-554 |
1.23e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 128.39 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 87 LRWSFEEL-GLLSRKFANILTEACSlqRGDRVMViLPKIPEWWLA-NVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:PRK09088 21 RRWTYAELdALVGRLAAVLRRRGCV--DGERLAV-LARNSVWLVAlHFACARVGAIYVPLNWRLSASELDALLQDAEPRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 165 IITDDTLApavdavAAKCENLHSKLIVSQhsregwgnlkemmkyaSDSHTCVDTKH---DEMMAIYFTSGTTGPPK--MI 239
Cdd:PRK09088 98 LLGDDAVA------AGRTDVEDLAAFIAS----------------ADALEPADTPSippERVSLILFTSGTSGQPKgvML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 240 G-----HTHSSFGLGLSVNGR--FWLDLiasdVMWNTsdTGWAksawSSVFSPWTQGACVFAHylPRFESTSILQTLS-- 310
Cdd:PRK09088 156 SernlqQTAHNFGVLGRVDAHssFLCDA----PMFHI--IGLI----TSVRPVLAVGGSILVS--NGFEPKRTLGRLGdp 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 311 KFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPiNPEVMEQWRKKTGLDIYEGYGQTE--TVLicgnfkGMKI 388
Cdd:PRK09088 224 ALGITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAP-HAAEDILGWLDDGIPMVDGFGMSEagTVF------GMSV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 389 -------KPGSMGKPSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGS-FYITGDRGYM 460
Cdd:PRK09088 297 dcdviraKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLL-----RGPNLSPGYWRRPQATARAFTGDgWFRTGDIARR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 461 DEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEqlkkEIQEH 540
Cdd:PRK09088 372 DADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG-APLDLE----RIRSH 446
|
490
....*....|....
gi 1039777677 541 VKKTTAPYKYPRKV 554
Cdd:PRK09088 447 LSTRLAKYKVPKHL 460
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
84-541 |
1.44e-31 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 128.23 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 84 GEELRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAK 163
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRL-RARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 164 CIITDDTLAPAVDAVAAkcenlhsklIVSQHSREGWGNLkemmkyASDSHTcVDTKHDEMMAIYFTSGTTGPPKmighth 243
Cdd:cd17651 95 LVLTHPALAGELAVELV---------AVTLLDQPGAAAG------ADAEPD-PALDADDLAYVIYTSGSTGRPK------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 244 ssfglGLSVNGRFWLDLIAsdvmWNT----SDTGWAKSAWSS---------VFSPWTQGACVfaHYLP---RFESTSILQ 307
Cdd:cd17651 153 -----GVVMPHRSLANLVA----WQArassLGPGARTLQFAGlgfdvsvqeIFSTLCAGATL--VLPPeevRTDPPALAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 308 TLSKFPITVfCSAPTAYRMLVQNDMSRSYKFN-SLKHCVSAGEP--INPEVMEQWRKKTGLDIYEGYGQTE----TVLIC 380
Cdd:cd17651 222 WLDEQRISR-VFLPTVALRALAEHGRPLGVRLaALRYLLTGGEQlvLTEDLREFCAGLPGLRLHNHYGPTEthvvTALSL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 381 GNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQvlperPFGLFTHYVDNPSKTASTL-------RGSFYI 453
Cdd:cd17651 301 PGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIG-----GAGLARGYLNRPELTAERFvpdpfvpGARMYR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 454 TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQL 533
Cdd:cd17651 376 TGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPE-APVDAAEL 454
|
....*...
gi 1039777677 534 KKEIQEHV 541
Cdd:cd17651 455 RAALATHL 462
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
90-551 |
2.60e-31 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 127.39 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 90 SFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:cd17646 25 TYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 170 TLAPAVDAVAAKCENLHSKLIVSQHSREGwgnlkemmkyasdshtcVDTKHDEMMAIYFTSGTTGPPK--MIGHThssfg 247
Cdd:cd17646 104 DLAARLPAGGDVALLGDEALAAPPATPPL-----------------VPPRPDNLAYVIYTSGSTGRPKgvMVTHA----- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 248 lGLsVNGRFWL----DLIASDVMWNTSDTGWAKSAWSsVFSPWTQGAC-VFA--------HYLPRFestsilqtLSKFPI 314
Cdd:cd17646 162 -GI-VNRLLWMqdeyPLGPGDRVLQKTPLSFDVSVWE-LFWPLVAGARlVVArpgghrdpAYLAAL--------IREHGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 315 TVFCSAPTAYRMLVQNDMSRSYKfnSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTET---VLICGNFKGMKIKPG 391
Cdd:cd17646 231 TTCHFVPSMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAaidVTHWPVRGPAETPSV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 392 SMGKPSPAFDVKILDENGATLPPGQEGDIALQvlperPFGLFTHYVDNPSKTASTL------RGS-FYITGDRGYMDEDG 464
Cdd:cd17646 309 PIGRPVPNTRLYVLDDALRPVPVGVPGELYLG-----GVQLARGYLGRPALTAERFvpdpfgPGSrMYRTGDLARWRPDG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 465 YFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQLkkeiQEHVKKT 544
Cdd:cd17646 384 ALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAAL----RAHLAER 459
|
....*..
gi 1039777677 545 TAPYKYP 551
Cdd:cd17646 460 LPEYMVP 466
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
80-554 |
5.31e-31 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 126.29 E-value: 5.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 80 IDGNGeelRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQS 159
Cdd:cd05920 35 VDGDR---RLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 160 SKAKCIITDDTLAPaVDAVAAKCENLHSklivsqhsregwgnlkemmkyasdshtcvdtkHDEMMAIYFTSGTTGPPKMI 239
Cdd:cd05920 111 AEAVAYIVPDRHAG-FDHRALARELAES--------------------------------IPEVALFLLSGGTTGTPKLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 240 GHTHSSFGLGLSVngrfwldliASDVMWNTSDT----------GWAKSAWSSVFSPWTQGACVFAhylPRFESTSILQTL 309
Cdd:cd05920 158 PRTHNDYAYNVRA---------SAEVCGLDQDTvylavlpaahNFPLACPGVLGTLLAGGRVVLA---PDPSPDAAFPLI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 310 SKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVLicgNFKGM--- 386
Cdd:cd05920 226 EREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLL---NYTRLddp 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 387 -KIKPGSMGKP-SPAFDVKILDENGATLPPGQEGdialQVLPERPFgLFTHYVDNPSKTAS--TLRGsFYITGDRGYMDE 462
Cdd:cd05920 303 dEVIIHTQGRPmSPDDEIRVVDEEGNPVPPGEEG----ELLTRGPY-TIRGYYRAPEHNARafTPDG-FYRTGDLVRRTP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 463 DGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdyKSHDQEQLKKEIQEhvk 542
Cdd:cd05920 377 DGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD--PPPSAAQLRRFLRE--- 451
|
490
....*....|..
gi 1039777677 543 KTTAPYKYPRKV 554
Cdd:cd05920 452 RGLAAYKLPDRI 463
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
226-554 |
1.00e-30 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 122.61 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 226 IYFTSGTTGPPK--MIGHTHSsfgLGLSVNgrfWldliaSDVMWNTSDTGWA-----------KSAWSSVFspwTQGACV 292
Cdd:cd17638 5 IMFTSGTTGRSKgvMCAHRQT---LRAAAA---W-----ADCADLTEDDRYLiinpffhtfgyKAGIVACL---LTGATV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 293 FAHYLprFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLD-IYEGY 371
Cdd:cd17638 71 VPVAV--FDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 372 GQTE--TVLICGNFKGMKIKPGSMGKPSPAFDVKILDEngatlppgqeGDIALqvlpeRPFGLFTHYVDNPSKTASTLRG 449
Cdd:cd17638 149 GLTEagVATMCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLV-----RGYNVMQGYLDDPEATAEAIDA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 450 SFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSH 528
Cdd:cd17638 214 DGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG-VTL 292
|
330 340
....*....|....*....|....*.
gi 1039777677 529 DQEQLKKEIQEHVkkttAPYKYPRKV 554
Cdd:cd17638 293 TEEDVIAWCRERL----ANYKVPRFV 314
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
216-554 |
1.09e-30 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 127.17 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 216 VDTKHDemMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNTSDTGWAKsawssvFSPWTQGACVFAH 295
Cdd:PTZ00237 251 VESSHP--LYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVS------FHGFLYGSLSLGN 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 296 YLPRFES---------TSILQTLSKFPITVFCSAPTAYRMLVQND-----MSRSYKFNSLKHCVSAGEPINPEVMEQWRK 361
Cdd:PTZ00237 323 TFVMFEGgiiknkhieDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiIRSKYDLSNLKEIWCGGEVIEESIPEYIEN 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 362 KTGLDIYEGYGQTE---TVLICgnFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQvLPERPFGLFTHYV- 437
Cdd:PTZ00237 403 KLKIKSSRGYGQTEigiTYLYC--YGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFK-LPMPPSFATTFYKn 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 438 DNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKA 517
Cdd:PTZ00237 480 DEKFKQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIG 559
|
330 340 350
....*....|....*....|....*....|....*....
gi 1039777677 518 FIVLNPDYKSH--DQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:PTZ00237 560 LLVLKQDQSNQsiDLNKLKNEINNIITQDIESLAVLRKI 598
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
84-554 |
4.92e-30 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 123.32 E-value: 4.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 84 GEELRWSFEELGLLSRKFANiLTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAK 163
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFAL-LLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 164 CIITddtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcvdTKHDEMMAIYFTSGTTGPPKMIGHTH 243
Cdd:cd05914 82 AIFV--------------------------------------------------SDEDDVALINYTSGTTGNSKGVMLTY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 244 SSfgLGLSVNGRFWLDLI-ASDVMWNTSDTGWAKSAWSSVFSPWTQGACVfaHYLPRFeSTSILQTLSKFPITVFCSAPT 322
Cdd:cd05914 112 RN--IVSNVDGVKEVVLLgKGDKILSILPLHHIYPLTFTLLLPLLNGAHV--VFLDKI-PSAKIIALAFAQVTPTLGVPV 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 323 AYRML-----------------------VQNDMSRSYKFNSL--------KHCVSAGEPINPEVmEQWRKKTGLDIYEGY 371
Cdd:cd05914 187 PLVIEkifkmdiipkltlkkfkfklakkINNRKIRKLAFKKVheafggniKEFVIGGAKINPDV-EEFLRTIGFPYTIGY 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 372 GQTETV-LICGNFKGmKIKPGSMGKPSPAFDVKILDENgatlPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTAS--TLR 448
Cdd:cd05914 266 GMTETApIISYSPPN-RIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIV-----RGPNVMKGYYKNPEATAEafDKD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 449 GSFYiTGDRGYMDEDGYFWFVARSDD-IILSSGYRIGPFEVESALIEHPSIAESAVVsspdpIRGEVVKAFIVLNPDY-- 525
Cdd:cd05914 336 GWFH-TGDLGKIDAEGYLYIRGRKKEmIVLSSGKNIYPEEIEAKINNMPFVLESLVV-----VQEKKLVALAYIDPDFld 409
|
490 500 510
....*....|....*....|....*....|....
gi 1039777677 526 -----KSHDQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:cd05914 410 vkalkQRNIIDAIKWEVRDKVNQKVPNYKKISKV 443
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
111-530 |
6.10e-30 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 123.39 E-value: 6.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 111 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqltqkdILYRLQSSKAKCIITDDTLAPAVDAVAAKcenlhskli 190
Cdd:cd05923 50 LRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL---------INPRLKAAELAELIERGEMTAAVIAVDAQ--------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 191 VSQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMA--------IYFTSGTTGPPKMIGHTHSSfglglsvngrfwldlIA 262
Cdd:cd05923 112 VMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPrepeqpafVFYTSGTTGLPKGAVIPQRA---------------AE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 263 SDVMWNTSDTGWAKSAWSSVFS--PWTQGACVFA-----------HYLPR-FESTSILQTLSKFPITVFCSAPTAYRMLV 328
Cdd:cd05923 177 SRVLFMSTQAGLRHGRHNVVLGlmPLYHVIGFFAvlvaalaldgtYVVVEeFDPADALKLIEQERVTSLFATPTHLDALA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 329 QNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETVlicgNFKGMK-IKPGSMGKPSPAFDVKILDE 407
Cdd:cd05923 257 AAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAM----NSLYMRdARTGTEMRPGFFSEVRIVRI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 408 NGAT---LPPGQEGDIALQVLPERPFglfTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIG 484
Cdd:cd05923 333 GGSPdeaLANGEEGELIVAAAADAAF---TGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIH 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1039777677 485 PFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQ 530
Cdd:cd05923 410 PSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADE 455
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
211-551 |
3.94e-29 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 120.55 E-value: 3.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 211 DS-HTCVDTKHDEMMA-IYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFwLDLIASDVMWNTSDTGWaKSAWSSVFSPWTQ 288
Cdd:cd17649 82 DSgAGLLLTHHPRQLAyVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNF-DGAHEQLLPPLIC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 289 GACVFAHYLPRFESTSILQTL-SKFPITVFcSAPTAY-RMLVQ---NDMSRSYKfnSLKHCVSAGEPINPEVMEQWRKkT 363
Cdd:cd17649 160 GACVVLRPDELWASADELAEMvRELGVTVL-DLPPAYlQQLAEeadRTGDGRPP--SLRLYIFGGEALSPELLRRWLK-A 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 364 GLDIYEGYGQTETVLICGNFK---GMKIKPGSM--GKPSPAFDVKILDENGATLPPGQEGD--IALQVLP----ERPfGL 432
Cdd:cd17649 236 PVRLFNAYGPTEATVTPLVWKceaGAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGElyIGGEGLArgylGRP-EL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 433 fTH--YVDNPSKTAStlrGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPI 510
Cdd:cd17649 315 -TAerFVPDPFGAPG---SRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG 390
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1039777677 511 RGEVVkAFIVLNPDYKshdQEQLKKEIQEHVKKTTAPYKYP 551
Cdd:cd17649 391 GKQLV-AYVVLRAAAA---QPELRAQLRTALRASLPDYMVP 427
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
90-554 |
5.97e-29 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 121.10 E-value: 5.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 90 SFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLipgttqlTQKDILYRLQSSKAKCIITDD 169
Cdd:PLN02574 68 SYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIV-------TTMNPSSSLGEIKKRVVDCSV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 170 TLAPAVDAVAAKCENLHSKLIVSQHS------REGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTH 243
Cdd:PLN02574 141 GLAFTSPENVEKLSPLGVPVIGVPENydfdskRIEFPKFYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTH 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 244 SSFGLGLSVNGRFWldliASDVMWNTSDTGWAksAWSSVFSPWtqGACVFAHYL----------PRFESTSILQTLSKFP 313
Cdd:PLN02574 221 RNLIAMVELFVRFE----ASQYEYPGSDNVYL--AALPMFHIY--GLSLFVVGLlslgstivvmRRFDASDMVKVIDRFK 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 314 ITVFCSAPTAYRMLVQNDMSRSYK-FNSLKHCVSAGEPINPEVMEQWRKK-TGLDIYEGYGQTETVLICG---NFKGMKi 388
Cdd:PLN02574 293 VTHFPVVPPILMALTKKAKGVCGEvLKSLKQVSCGAAPLSGKFIQDFVQTlPHVDFIQGYGMTESTAVGTrgfNTEKLS- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 389 KPGSMGKPSPAFDVKILD-ENGATLPPGQEGDIALQvlpeRPfGLFTHYVDNPSKTASTL-RGSFYITGDRGYMDEDGYF 466
Cdd:PLN02574 372 KYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQ----GP-GVMKGYLNNPKATQSTIdKDGWLRTGDIAYFDEDGYL 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 467 WFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQlkkeIQEHVKKTTA 546
Cdd:PLN02574 447 YIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG-STLSQEA----VINYVAKQVA 521
|
....*...
gi 1039777677 547 PYKYPRKV 554
Cdd:PLN02574 522 PYKKVRKV 529
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
99-554 |
9.27e-29 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 120.72 E-value: 9.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 99 RKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD---TLAP-A 174
Cdd:PLN02479 56 RRLASALAKR-SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQeffTLAEeA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 175 VDAVAAKCENLHSK--LIVSQHSREGWGNLK--------EMMKYASDSHTCVDTK--HDEM--MAIYFTSGTTGPPK-MI 239
Cdd:PLN02479 135 LKILAEKKKSSFKPplLIVIGDPTCDPKSLQyalgkgaiEYEKFLETGDPEFAWKppADEWqsIALGYTSGTTASPKgVV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 240 GHTHSSFGLGLSvNGRFWLDLIASDVMWNTSD---TGWAksawssvfSPWTQGA-CVFAHYLPRFESTSILQTLSKFPIT 315
Cdd:PLN02479 215 LHHRGAYLMALS-NALIWGMNEGAVYLWTLPMfhcNGWC--------FTWTLAAlCGTNICLRQVTAKAIYSAIANYGVT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 316 VFCSAPTAYRMLVqnDMSRSYKFNSLKHCV---SAGEPINPEVMEQWRKKtGLDIYEGYGQTETV---LICG-------- 381
Cdd:PLN02479 286 HFCAAPVVLNTIV--NAPKSETILPLPRVVhvmTAGAAPPPSVLFAMSEK-GFRVTHTYGLSETYgpsTVCAwkpewdsl 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 382 --------------NFKGMK----IKPGSMgKPSPAfdvkildeNGATLppgqeGDIALqvlpeRPFGLFTHYVDNPSKT 443
Cdd:PLN02479 363 ppeeqarlnarqgvRYIGLEgldvVDTKTM-KPVPA--------DGKTM-----GEIVM-----RGNMVMKGYLKNPKAN 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 444 ASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNP 523
Cdd:PLN02479 424 EEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKP 503
|
490 500 510
....*....|....*....|....*....|.
gi 1039777677 524 DYKSHDQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:PLN02479 504 GVDKSDEAALAEDIMKFCRERLPAYWVPKSV 534
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
84-551 |
1.24e-28 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 119.87 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 84 GEELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGtvLIPGTT--QLTQKDILYRLQSSK 161
Cdd:COG1021 46 DGERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFRAG--AIPVFAlpAHRRAEISHFAEQSE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 162 AKCIITDDT-----LAPAVDAVAAKCENLHSKLIVsqHSREGWGNLKEMmkYASDSHTCVDTKHDEMMAIYFTS-GTTGP 235
Cdd:COG1021 123 AVAYIIPDRhrgfdYRALARELQAEVPSLRHVLVV--GDAGEFTSLDAL--LAAPADLSEPRPDPDDVAFFQLSgGTTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 236 PKMIGHTH---------SSFGLGLSVNGRFwldLIASDVMWNtsdtgwakSAWSS--VFSPWTQGAC-VFAhylPRFEST 303
Cdd:COG1021 199 PKLIPRTHddylysvraSAEICGLDADTVY---LAALPAAHN--------FPLSSpgVLGVLYAGGTvVLA---PDPSPD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 304 SILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYG-------QT-- 374
Cdd:COG1021 265 TAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGmaeglvnYTrl 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 375 ----ETVLicgnfkgmkikpGSMGKP-SPAFDVKILDENGATLPPGQEGdiALQVlpeRPFGLFTHYVDNPSKTAS--TL 447
Cdd:COG1021 345 ddpeEVIL------------TTQGRPiSPDDEVRIVDEDGNPVPPGEVG--ELLT---RGPYTIRGYYRAPEHNARafTP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 448 RGsFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLnpdyks 527
Cdd:COG1021 408 DG-FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVP------ 480
|
490 500
....*....|....*....|....*.
gi 1039777677 528 hDQEQLK-KEIQEHVK-KTTAPYKYP 551
Cdd:COG1021 481 -RGEPLTlAELRRFLReRGLAAFKLP 505
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
88-551 |
2.00e-28 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 118.84 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 88 RWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIT 167
Cdd:cd12117 22 SLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 168 DDTLAPAVDAVAAKcenlhskLIVSQHSREGwgnlkemmkYASDSHTCVDTkhDEMMAIYFTSGTTGPPKMIGHTHSSFg 247
Cdd:cd12117 101 DRSLAGRAGGLEVA-------VVIDEALDAG---------PAGNPAVPVSP--DDLAYVMYTSGSTGRPKGVAVTHRGV- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 248 LGLsVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLPR---FESTSILQTLSKFPITV-FCSAPTa 323
Cdd:cd12117 162 VRL-VKNTNYVTLGPDDRVLQTSPLAFDASTFE-IWGALLNGARL--VLAPKgtlLDPDALGALIAEEGVTVlWLTAAL- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 324 YRMLVQNDMSRsykFNSLKHCVSAGEPINPEVMEQWRKKT-GLDIYEGYGQTE--TVLICGNFKGMKIKPGS--MGKPSP 398
Cdd:cd12117 237 FNQLADEDPEC---FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTEntTFTTSHVVTELDEVAGSipIGRPIA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 399 AFDVKILDENGATLPPGQEGDiaLQVLPErpfGLFTHYVDNPSKTA------STLRGS-FYITGDRGYMDEDGYFWFVAR 471
Cdd:cd12117 314 NTRVYVLDEDGRPVPPGVPGE--LYVGGD---GLALGYLNRPALTAerfvadPFGPGErLYRTGDLARWLPDGRLEFLGR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 472 SDDIILSSGYRIGPFEVESALIEHPSIAESAV-VSSPDPIRGEVVkAFIVLNPDyKSHDqeqlkkEIQEHVKKTTAPYKY 550
Cdd:cd12117 389 IDDQVKIRGFRIELGEIEAALRAHPGVREAVVvVREDAGGDKRLV-AYVVAEGA-LDAA------ELRAFLRERLPAYMV 460
|
.
gi 1039777677 551 P 551
Cdd:cd12117 461 P 461
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
87-554 |
2.25e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 119.53 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 87 LRWSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCII 166
Cdd:PRK08315 42 LRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 167 TDD------------TLAP------AVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHtcvDTKHDEMMA--- 225
Cdd:PRK08315 121 AADgfkdsdyvamlyELAPelatcePGQLQSARLPELRRVIFLGDEKHPGMLNFDELLALGRAVD---DAELAARQAtld 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 226 ------IYFTSGTTGPPKmiGHTHSSFGLGLsvNGRF---WLDLIASD--------------VMWNTSDTgwaksawssv 282
Cdd:PRK08315 198 pddpinIQYTSGTTGFPK--GATLTHRNILN--NGYFigeAMKLTEEDrlcipvplyhcfgmVLGNLACV---------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 283 fspwTQGAC-VFAhyLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRK 361
Cdd:PRK08315 264 ----THGATmVYP--GEGFDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLRTGIMAGSPCPIEVMKRVID 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 362 KTGL-DIYEGYGQTETvlicgnfkgmkiKPGSM---------------GKPSPAFDVKILD-ENGATLPPGQEGDIAlqv 424
Cdd:PRK08315 338 KMHMsEVTIAYGMTET------------SPVSTqtrtddplekrvttvGRALPHLEVKIVDpETGETVPRGEQGELC--- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 425 lpERPFGLFTHYVDNPSKTASTL-RGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAV 503
Cdd:PRK08315 403 --TRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1039777677 504 VSSPDPIRGEVVKAFIVLNPDYKSHDQeqlkkEIQEHVKKTTAPYKYPRKV 554
Cdd:PRK08315 481 VGVPDEKYGEEVCAWIILRPGATLTEE-----DVRDFCRGKIAHYKIPRYI 526
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
88-554 |
3.48e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 118.83 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 88 RWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIT 167
Cdd:PRK07798 28 RLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 168 DDTLAPAVDAVAAKCENLHSKLIV----SQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYfTSGTTGPPK--MIGH 241
Cdd:PRK07798 107 EREFAPRVAEVLPRLPKLRTLVVVedgsGNDLLPGAVDYEDALAAGSPERDFGERSPDDLYLLY-TGGTTGMPKgvMWRQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 242 T---HSSFGLGLSVNGRFWLD----------------LIASDVMWNTSDtgWAksAWSSVFSpwtqGACVFAHYLPRFES 302
Cdd:PRK07798 186 EdifRVLLGGRDFATGEPIEDeeelakraaagpgmrrFPAPPLMHGAGQ--WA--AFAALFS----GQTVVLLPDVRFDA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 303 TSILQTLSKFPITVFCSAPTAY-RMLVQN-DMSRSYKFNSLKHCVSAGEPINPEVMEQWRK-KTGLDIYEGYGQTETvli 379
Cdd:PRK07798 258 DEVWRTIEREKVNVITIVGDAMaRPLLDAlEARGPYDLSSLFAIASGGALFSPSVKEALLElLPNVVLTDSIGSSET--- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 380 cgNFKGMKI-KPGSMGKPSPAF----DVKILDENGATLPPGQE--GDIALQvlPERPFGlfthYVDNPSKTASTLR---G 449
Cdd:PRK07798 335 --GFGGSGTvAKGAVHTGGPRFtigpRTVVLDEDGNPVEPGSGeiGWIARR--GHIPLG----YYKDPEKTAETFPtidG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 450 SFY-ITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDyKSH 528
Cdd:PRK07798 407 VRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREG-ARP 485
|
490 500
....*....|....*....|....*.
gi 1039777677 529 DQEqlkkEIQEHVKKTTAPYKYPRKV 554
Cdd:PRK07798 486 DLA----ELRAHCRSSLAGYKVPRAI 507
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
90-540 |
3.60e-28 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 118.20 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 90 SFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:cd17655 24 TYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 170 TLAPAVdAVAAKCENLHSKLIVSQHSRegwgNLKemmkyasdshtcVDTKHDEMMAIYFTSGTTGPPK--MIGHtHSSFG 247
Cdd:cd17655 103 HLQPPI-AFIGLIDLLDEDTIYHEESE----NLE------------PVSKSDDLAYVIYTSGSTGKPKgvMIEH-RGVVN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 248 LGLSVNGRFWLDliASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfahYLPRFES----TSILQTLSKFPITVFCSAPTA 323
Cdd:cd17655 165 LVEWANKVIYQG--EHLRVALFASISFDASVTE-IFASLLSGNTL---YIVRKETvldgQALTQYIRQNRITIIDLTPAH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 324 YRMLVQNDMSrsyKFNSLKHCVSAGEPINPEVMEQWRKKTGL--DIYEGYGQTETVLIC--GNFKGMKIKPGS--MGKPS 397
Cdd:cd17655 239 LKLLDAADDS---EGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETTVDAsiYQYEPETDQQVSvpIGKPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 398 PAFDVKILDENGATLPPGQEGDiaLQVLPErpfGLFTHYVDNPSKTASTL-------RGSFYITGDRGYMDEDGYFWFVA 470
Cdd:cd17655 316 GNTRIYILDQYGRPQPVGVAGE--LYIGGE---GVARGYLNRPELTAEKFvddpfvpGERMYRTGDLARWLPDGNIEFLG 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 471 RSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKshdQEQLKKEIQEH 540
Cdd:cd17655 391 RIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELP---VAQLREFLARE 457
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
85-524 |
4.65e-28 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 119.96 E-value: 4.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 85 EELRWSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:COG1020 498 GDQSLTYAELNARANRLAHHLR-ALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 165 IITDDTLAPAVDAVAAKCENLhSKLIVSQHSregwgnlkemmkyASDSHTCVDTKHdemMA-IYFTSGTTGPPK--MIgh 241
Cdd:COG1020 577 VLTQSALAARLPELGVPVLAL-DALALAAEP-------------ATNPPVPVTPDD---LAyVIYTSGSTGRPKgvMV-- 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 242 THSSFG-LGLSVNGRFWLDliASDVM-WNTS---DTgwakSAWSsVFSPWTQGAC-VFAHYLPRFESTSILQTLSKFPIT 315
Cdd:COG1020 638 EHRALVnLLAWMQRRYGLG--PGDRVlQFASlsfDA----SVWE-IFGALLSGATlVLAPPEARRDPAALAELLARHRVT 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 316 VFCSAPTAYRMLVQNDMSRsykFNSLKHCVSAGEPINPEVMEQWRKKT-GLDIYEGYGQTETVL--ICGNFKGMKIKPGS 392
Cdd:COG1020 711 VLNLTPSLLRALLDAAPEA---LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVdsTYYEVTPPDADGGS 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 393 M--GKPSPAFDVKILDENGATLPPGQEGDI-------ALqvlperpfGlfthYVDNPSKTAS-------TLRGS-FYITG 455
Cdd:COG1020 788 VpiGRPIANTRVYVLDAHLQPVPVGVPGELyiggaglAR--------G----YLNRPELTAErfvadpfGFPGArLYRTG 855
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039777677 456 DRGYMDEDGYFWFVARSDD---IilsSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPD 524
Cdd:COG1020 856 DLARWLPDGNLEFLGRADDqvkI---RGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG 924
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
226-554 |
4.99e-28 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 114.81 E-value: 4.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 226 IYFTSGTTGPPKMIGHTHSSfglglsvngrfWldlIASDVMwntSDTGWAKSAWSSVFSPWTQG------ACVFAHYLPR 299
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERS-----------W---IESFVC---NEDLFNISGEDAILAPGPLShslflyGAISALYLGG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 300 -------FESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSykfnSLKHCVSAGEPINPEVMEQWRKKT-GLDIYEGY 371
Cdd:cd17633 68 tfigqrkFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPES----KIKSIFSSGQKLFESTKKKLKNIFpKANLIEFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 372 GQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILDENGatlppGQEGDIALQvlpeRPFgLFTHYVDNPSKTAstlrGSF 451
Cdd:cd17633 144 GTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVK----SEM-VFSGYVRGGFSNP----DGW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 452 YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdykshdqE 531
Cdd:cd17633 210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD--------K 281
|
330 340
....*....|....*....|...
gi 1039777677 532 QLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:cd17633 282 LTYKQLKRFLKQKLSRYEIPKKI 304
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
74-524 |
9.31e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 117.47 E-value: 9.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 74 NPAFWWidgngEELRWSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIpGTTQLTQKDI 153
Cdd:PRK07867 19 DRGLYF-----EDSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPV-GLNPTRRGAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 154 LYR-LQSSKAKCIITDDTLAPAVDAVAAKCEnlhsklIVSQHSREgWGNlkEMMKYASDSHTCVDTKHDEMMAIYFTSGT 232
Cdd:PRK07867 93 LARdIAHADCQLVLTESAHAELLDGLDPGVR------VINVDSPA-WAD--ELAAHRDAEPPFRVADPDDLFMLIFTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 233 TGPPKMIGHTHSSF-GLGLSVNGRFwlDLIASDVMWntsdtgwaksawssVFSPWTQGACVFAHYLP------------R 299
Cdd:PRK07867 164 SGDPKAVRCTHRKVaSAGVMLAQRF--GLGPDDVCY--------------VSMPLFHSNAVMAGWAValaagasialrrK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 300 FESTSILQTLSKFPITVF--CSAPTAYRMLVQ---NDMSrsykfNSLKhcVSAGEPINPEVMEQWRKKTGLDIYEGYGQT 374
Cdd:PRK07867 228 FSASGFLPDVRRYGATYAnyVGKPLSYVLATPerpDDAD-----NPLR--IVYGNEGAPGDIARFARRFGCVVVDGFGST 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 375 ETvlicgnfkGMKIK------PGSMGKPSPafDVKILD-ENGATLPPGQEGDIALQ---------VLPERPfGLFTHYVD 438
Cdd:PRK07867 301 EG--------GVAITrtpdtpPGALGPLPP--GVAIVDpDTGTECPPAEDADGRLLnadeaigelVNTAGP-GGFEGYYN 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 439 NPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAF 518
Cdd:PRK07867 370 DPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAA 449
|
....*.
gi 1039777677 519 IVLNPD 524
Cdd:PRK07867 450 LVLAPG 455
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
217-547 |
2.65e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 117.72 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 217 DTKHDEMMAIYFTSGTTGPPK--MIGHT----------------------------HSsfgLGLSVNgrFWLDLIasdvm 266
Cdd:PRK08633 778 TFKPDDTATIIFSSGSEGEPKgvMLSHHnilsnieqisdvfnlrnddvilsslpffHS---FGLTVT--LWLPLL----- 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 267 wntsdtgwaksawssvfspwtQGACVFAHYLPrFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVS 346
Cdd:PRK08633 848 ---------------------EGIKVVYHPDP-TDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVA 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 347 AGEPINPEVMEQWRKKTGLDIYEGYGQTET----------VLICGNFKGMKIKPGSMGKPSPAFDVKILD-ENGATLPPG 415
Cdd:PRK08633 906 GAEKLKPEVADAFEEKFGIRILEGYGATETspvasvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPG 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 416 QEGDIAL---QVLperpfglfTHYVDNPSKTASTLR----GSFYITGDRGYMDEDGYFWFVARsddiiLSSGYRIG---- 484
Cdd:PRK08633 986 EDGLILIggpQVM--------KGYLGDPEKTAEVIKdidgIGWYVTGDKGHLDEDGFLTITDR-----YSRFAKIGgemv 1052
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039777677 485 PF-EVESALIE--HPSIAESAVVSSPDPIRGEVVkafIVLnpdyksHDQEQLKKE-IQEHVKKTTAP 547
Cdd:PRK08633 1053 PLgAVEEELAKalGGEEVVFAVTAVPDEKKGEKL---VVL------HTCGAEDVEeLKRAIKESGLP 1110
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
226-558 |
3.49e-27 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 114.71 E-value: 3.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 226 IYfTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFAHYLPRFESTS 304
Cdd:cd17643 99 IY-TSGSTGRPKGVVVSHANV-LALFAATQRWFGFNEDDVWTLFHSYAFDFSVWE-IWGALLHGGrLVVVPYEVARSPED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 305 ILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGL---DIYEGYGQTET-VLIc 380
Cdd:cd17643 176 FARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETtVHV- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 381 gNFKGMK---IKPGSM---GKPSPAFDVKILDENGATLPPGQEGDIAL---QVLP---ERPFGLFTHYVDNPsKTASTLR 448
Cdd:cd17643 255 -TFRPLDaadLPAAAAspiGRPLPGLRVYVLDADGRPVPPGVVGELYVsgaGVARgylGRPELTAERFVANP-FGGPGSR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 449 GsfYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNpdyksH 528
Cdd:cd17643 333 M--YRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVAD-----D 405
|
330 340 350
....*....|....*....|....*....|.
gi 1039777677 529 DQEQLKKEIQEHVKKTTAPYKYP-RKVGVPG 558
Cdd:cd17643 406 GAAADIAELRALLKELLPDYMVPaRYVPLDA 436
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
90-551 |
4.13e-27 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 115.37 E-value: 4.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 90 SFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 170 TLAPAVDAVAAKCENLhsKLIVSQHSREGWGNLKEMMKYASDSHTCVDT----KHDEMMaIYFTSGTTGPPKMIGHTHSS 245
Cdd:PRK05852 124 DGPHDRAEPTTRWWPL--TVNVGGDSGPSGGTLSVHLDAATEPTPATSTpeglRPDDAM-IMFTGGTTGLPKMVPWTHAN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 246 fgLGLSVNGrfwldLIAS----------DVMWNTSDTGWAKSAWSSVFSpwtqGACVFAHYLPRFESTSILQTLSKFPIT 315
Cdd:PRK05852 201 --IASSVRA-----IITGyrlsprdatvAVMPLYHGHGLIAALLATLAS----GGAVLLPARGRFSAHTFWDDIKAVGAT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 316 VFCSAPTAYRMLVQNDMSRSY--KFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTET--------VLICGNFKG 385
Cdd:PRK05852 270 WYTAVPTIHQILLERAATEPSgrKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAthqvtttqIEGIGQTEN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 386 MKIKPGSMGKpSPAFDVKILDENGATLPPGQEGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGY 465
Cdd:PRK05852 350 PVVSTGLVGR-STGAQIRIVGSDGLPLPAGAVGEVWL-----RGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 466 FWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnPDYKSHDQEQlkkEIQEHVKKTT 545
Cdd:PRK05852 424 LSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--PRESAPPTAE---ELVQFCRERL 498
|
....*.
gi 1039777677 546 APYKYP 551
Cdd:PRK05852 499 AAFEIP 504
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
100-553 |
7.60e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 114.11 E-value: 7.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 100 KFANILTEACSLQRgdRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVA 179
Cdd:PRK07638 38 KVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERYKLNDLPDEE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 180 AKcenlhsklIVSqhsregWGNLKEMM-KYASDSHTCVDTKHDEM-MAiyFTSGTTGPPKMIGHTHSSFGLGLSVNGR-F 256
Cdd:PRK07638 116 GR--------VIE------IDEWKRMIeKYLPTYAPIENVQNAPFyMG--FTSGSTGKPKAFLRAQQSWLHSFDCNVHdF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 257 WLD-----LIASDVMwntsdtgwaksawSSVF-----SPWTQGACVfaHYLPRFESTSILQTLSKFPITVFCSAPTAYRM 326
Cdd:PRK07638 180 HMKredsvLIAGTLV-------------HSLFlygaiSTLYVGQTV--HLMRKFIPNQVLDKLETENISVMYTVPTMLES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 327 LVQNDMSRSykfNSLKhCVSAGEPINPEVMEQWRKK-TGLDIYEGYGQTE----TVLICGNFKgmkIKPGSMGKPSPAFD 401
Cdd:PRK07638 245 LYKENRVIE---NKMK-IISSGAKWEAEAKEKIKNIfPYAKLYEFYGASElsfvTALVDEESE---RRPNSVGRPFHNVQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 402 VKILDENGATLPPGQEGDIALQvlpeRPFgLFTHYVdNPSKTASTLRGSFYIT-GDRGYMDEDGYFWFVARSDDIILSSG 480
Cdd:PRK07638 318 VRICNEAGEEVQKGEIGTVYVK----SPQ-FFMGYI-IGGVLARELNADGWMTvRDVGYEDEEGFIYIVGREKNMILFGG 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039777677 481 YRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIvlnpdykshDQEQLKKEIQEHVKKTTAPYKYPRK 553
Cdd:PRK07638 392 INIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKIPKE 455
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
228-552 |
9.66e-27 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 110.88 E-value: 9.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 228 FTSGTTGPPKMIGHT-----HSSFG----LGLSVNGRFWLDLIASDV-----MWNtsdtgWAKSAWSSVFSPWTQGAcvf 293
Cdd:cd17630 7 LTSGSTGTPKAVVHTaanllASAAGlhsrLGFGGGDSWLLSLPLYHVgglaiLVR-----SLLAGAELVLLERNQAL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 294 ahylprfestsiLQTLSKFPITVFCSAPTAYRMLVQNDMSRSyKFNSLKHCVSAGEPINPEVMEQWRKKtGLDIYEGYGQ 373
Cdd:cd17630 79 ------------AEDLAPPGVTHVSLVPTQLQRLLDSGQGPA-ALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 374 TETV-LICGNFKGMKiKPGSMGKPSPAFDVKILDEngatlppgqeGDIALqvlpeRPFGLFTHYVDNPSKTASTLRGSFY 452
Cdd:cd17630 145 TETAsQVATKRPDGF-GRGGVGVLLPGRELRIVED----------GEIWV-----GGASLAMGYLRGQLVPEFNEDGWFT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 453 iTGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPdykSHDQEq 532
Cdd:cd17630 209 -TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRG---PADPA- 283
|
330 340
....*....|....*....|
gi 1039777677 533 lkkEIQEHVKKTTAPYKYPR 552
Cdd:cd17630 284 ---ELRAWLKDKLARFKLPK 300
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
90-540 |
1.77e-26 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 113.84 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 90 SFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTG--TVLI-PGttqLTQKDILYRLQSSKAKCII 166
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGavPVLVdPG---MGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 167 TddtlAPAvdAVAAKC------ENLHSKLIVSQhsREGWGN--LKEMM-KYASDSHTCVDTKHDEMMAIYFTSGTTGPPK 237
Cdd:PRK09274 119 G----IPK--AHLARRlfgwgkPSVRRLVTVGG--RLLWGGttLATLLrDGAAAPFPMADLAPDDMAAILFTSGSTGTPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 238 MIGHTHSSF---------GLGLSVNGRfwlDLIASDVMwntsdtgwaksawsSVFSPwtqgACVFAHYLPRFEST----- 303
Cdd:PRK09274 191 GVVYTHGMFeaqiealreDYGIEPGEI---DLPTFPLF--------------ALFGP----ALGMTSVIPDMDPTrpatv 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 304 ---SILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRK--KTGLDIYEGYGQTETVL 378
Cdd:PRK09274 250 dpaKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPYGATEALP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 379 ICgnfkgmKIkpGS------------------MGKPSPAFDVKIL---DENGAT------LPPGQEGDIALQ---VLPEr 428
Cdd:PRK09274 330 IS------SI--ESreilfatraatdngagicVGRPVDGVEVRIIaisDAPIPEwddalrLATGEIGEIVVAgpmVTRS- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 429 pfglfthYVDNPSKTA-----STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAV 503
Cdd:PRK09274 401 -------YYNRPEATRlakipDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSAL 473
|
490 500 510
....*....|....*....|....*....|....*...
gi 1039777677 504 VSSPDPirGEVVKAFIV-LNPDyKSHDQEQLKKEIQEH 540
Cdd:PRK09274 474 VGVGVP--GAQRPVLCVeLEPG-VACSKSALYQELRAL 508
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
80-541 |
2.77e-26 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 111.63 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 80 IDGNGEELrwSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqltqkdilyrlqs 159
Cdd:cd17653 16 VESLGGSL--TYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP---------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 160 skakciitDDTLAPAvDAVAAKCENLHSKLIVsqhsregwgnlkemmkyasdshtCVDTKHDEMMAIyFTSGTTGPPKMI 239
Cdd:cd17653 77 --------LDAKLPS-ARIQAILRTSGATLLL-----------------------TTDSPDDLAYII-FTSGSTGIPKGV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 240 GHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWsSVFSPWTQGAC-VFAHYLPRFesTSILQTLSKFPITvfc 318
Cdd:cd17653 124 MVPHRGV-LNYVSQPPARLDVGPGSRVAQVLSIAFDACIG-EIFSTLCNGGTlVLADPSDPF--AHVARTVDALMST--- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 319 saPTAYRMLVQNDmsrsykFNSLKHCVSAGEPINPEVMEQWRKktGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSP 398
Cdd:cd17653 197 --PSILSTLSPQD------FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 399 AFDVKILDENGATLPPGQEGDIALQVLperpfGLFTHYVDNPSKTASTLR------GS-FYITGDRGYMDEDGYFWFVAR 471
Cdd:cd17653 267 NSTCYILDADLQPVPEGVVGEICISGV-----QVARGYLGNPALTASKFVpdpfwpGSrMYRTGDYGRWTEDGGLEFLGR 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 472 SDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSpdpIRGEVVkAFIVlnPDykSHDQEQLKKEIQEHV 541
Cdd:cd17653 342 EDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIV---VNGRLV-AFVT--PE--TVDVDGLRSELAKHL 403
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
110-554 |
9.31e-26 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 111.65 E-value: 9.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 110 SLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAV----AAKCENL 185
Cdd:PLN03102 60 NITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVlhllSSEDSNL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 186 HSKLIV------------SQHSREGWGNLKEMMKYASDSHTCVDTKHDEMmAIYFTSGTTGPPK--MIGHTHSSFGLGLS 251
Cdd:PLN03102 140 NLPVIFiheidfpkrpssEELDYECLIQRGEPTPSLVARMFRIQDEHDPI-SLNYTSGTTADPKgvVISHRGAYLSTLSA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 252 VNGrfWLDLIASDVMWNTSD---TGWAKSaWSSVFSPWTQgACVFAHYLPRfestsILQTLSKFPITVFCSAPTAYRMLV 328
Cdd:PLN03102 219 IIG--WEMGTCPVYLWTLPMfhcNGWTFT-WGTAARGGTS-VCMRHVTAPE-----IYKNIEMHNVTHMCCVPTVFNILL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 329 QNDMSRSYKFNSLKHCVSAGEPiNPEVMEQWRKKTGLDIYEGYGQTET---VLICG---------NFKGMKIKPGSMGKP 396
Cdd:PLN03102 290 KGNSLDLSPRSGPVHVLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEAtgpVLFCEwqdewnrlpENQQMELKARQGVSI 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 397 SPAFDVKIldENGATLPPGQEGDIALQVLPERPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDII 476
Cdd:PLN03102 369 LGLADVDV--KNKETQESVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDII 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 477 LSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQLK-----KEIQEHVKKTTAPYKYP 551
Cdd:PLN03102 447 ISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKlvtreRDLIEYCRENLPHFMCP 526
|
...
gi 1039777677 552 RKV 554
Cdd:PLN03102 527 RKV 529
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
81-542 |
2.12e-25 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 109.87 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 81 DGNGEELRWSfeELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS 160
Cdd:cd05932 1 GGQVVEFTWG--EVADKARRLAAAL-RALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 161 KAKCIIT---DD--TLAPAV-DAVAAKCENLHSKLivsqHSREGWGNLKEMMKYASDSHTcvdTKHDEMMAIYFTSGTTG 234
Cdd:cd05932 78 ESKALFVgklDDwkAMAPGVpEGLISISLPPPSAA----NCQYQWDDLIAQHPPLEERPT---RFPEQLATLIYTSGTTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 235 PPKMIGHTHSSFG---------LGLSVNGRF--WLDL--IASDVMwntsdtgwaksawssVFSPWTQGACV--FAHYLPR 299
Cdd:cd05932 151 QPKGVMLTFGSFAwaaqagiehIGTEENDRMlsYLPLahVTERVF---------------VEGGSLYGGVLvaFAESLDT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 300 FestsiLQTLSKFPITVFCSAP---TAYRMLVQNDMSRSyKFNSL----------KHCVSAG-------------EPINP 353
Cdd:cd05932 216 F-----VEDVQRARPTLFFSVPrlwTKFQQGVQDKIPQQ-KLNLLlkipvvnslvKRKVLKGlgldqcrlagcgsAPVPP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 354 EVMEqWRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIldengatlppGQEGDIALqvlpeRPFGLF 433
Cdd:cd05932 290 ALLE-WYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRI----------SEDGEILV-----RSPALM 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 434 THYVDNPSKTASTLRGS-FYITGDRGYMDEDGYFWFVARSDDIILSS-GYRIGPFEVESALIEHPSIAESAVVSS--PDP 509
Cdd:cd05932 354 MGYYKDPEATAEAFTADgFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAP 433
|
490 500 510
....*....|....*....|....*....|...
gi 1039777677 510 IRGEVVKAFIVLNPDykSHDQEQLKKEIQEHVK 542
Cdd:cd05932 434 LALVVLSEEARLRAD--AFARAELEASLRAHLA 464
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
213-524 |
2.30e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 110.12 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 213 HTCVDTKHDEMMaiYFTSGTTGPPKMIGHTHSSFG-LGLSVNGRFwlDLIASDVMW--------NTSDTGWAKSAwssvf 283
Cdd:PRK13388 144 HREVDAMDPFML--IFTSGTTGAPKAVRCSHGRLAfAGRALTERF--GLTRDDVCYvsmplfhsNAVMAGWAPAV----- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 284 spwTQGACVFAHylPRFESTSILQTLSKFPITVF--CSAPTAYRMLV--QNDMSRsykfNSLKhcVSAGEPINPEVMEQW 359
Cdd:PRK13388 215 ---ASGAAVALP--AKFSASGFLDDVRRYGATYFnyVGKPLAYILATpeRPDDAD----NPLR--VAFGNEASPRDIAEF 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 360 RKKTGLDIYEGYGQTETVLICGNFKGMKikPGSMGKPSPafDVKI-------------LDENGATLPPgqegDIAL-QVL 425
Cdd:PRK13388 284 SRRFGCQVEDGYGSSEGAVIVVREPGTP--PGSIGRGAP--GVAIynpetltecavarFDAHGALLNA----DEAIgELV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 426 PERPFGLFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVS 505
Cdd:PRK13388 356 NTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYA 435
|
330
....*....|....*....
gi 1039777677 506 SPDPIRGEVVKAFIVLNPD 524
Cdd:PRK13388 436 VPDERVGDQVMAALVLRDG 454
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
85-540 |
2.32e-25 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 109.30 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 85 EELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 165 IITDDTLA-------PAVDAVAAKCENLHSKLIVSQHSregwGNLKEMMkyasdshtcvdtkhdemmaiyFTSGTTGPPK 237
Cdd:cd12116 88 VLTDDALPdrlpaglPVLLLALAAAAAAPAAPRTPVSP----DDLAYVI---------------------YTSGSTGRPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 238 MIGHTHSSF-GLGLSVNGRfwLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFAHYLPRFESTSILQTLSKFPIT 315
Cdd:cd12116 143 GVVVSHRNLvNFLHSMRER--LGLGPGDRLLAVTTYAFDISLLE-LLLPLLAGArVVIAPRETQRDPEALARLIEAHSIT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 316 VFCSAPTAYRMLVQNDMSRSYKFNSLkhCvsAGEPINPEVMEQWRKKTGlDIYEGYGQTETVL------ICGNFKGMKIk 389
Cdd:cd12116 220 VMQATPATWRMLLDAGWQGRAGLTAL--C--GGEALPPDLAARLLSRVG-SLWNLYGPTETTIwstaarVTAAAGPIPI- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 390 pgsmGKPSPAFDVKILDENGATLPPGQEGDIAL---QVLP---ERPFGLFTHYVDNPSKTAstlRGSFYITGDRGYMDED 463
Cdd:cd12116 294 ----GRPLANTQVYVLDAALRPVPPGVPGELYIggdGVAQgylGRPALTAERFVPDPFAGP---GSRLYRTGDLVRRRAD 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039777677 464 GYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVkAFIVLnPDYKSHDQEQLKKEIQEH 540
Cdd:cd12116 367 GRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVL-KAGAAPDAAALRAHLRAT 441
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
226-552 |
3.71e-25 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 109.89 E-value: 3.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 226 IYFTSGTTGPPKMIGHTHSSfglgLSVNGrfwLDLIA------SDVMWNTS---DTGWAKSAWSSVFSpwtqGAC-VFah 295
Cdd:PLN02860 177 ICFTSGTTGRPKGVTISHSA----LIVQS---LAKIAivgygeDDVYLHTAplcHIGGLSSALAMLMV----GAChVL-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 296 yLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQ-NDMSRSYK-FNSLKHCVSAGEPINPEVMEQWRKK-TGLDIYEGYG 372
Cdd:PLN02860 244 -LPKFDAKAALQAIKQHNVTSMITVPAMMADLISlTRKSMTWKvFPSVRKILNGGGSLSSRLLPDAKKLfPNAKLFSAYG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 373 QTET----------VLICGNFK-----GMKIKPGS--------MGKPSPAFDVKI-LDEngatlpPGQEGDIAlqvlpER 428
Cdd:PLN02860 323 MTEAcssltfmtlhDPTLESPKqtlqtVNQTKSSSvhqpqgvcVGKPAPHVELKIgLDE------SSRVGRIL-----TR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 429 PFGLFTHYVDNPSKTASTLRGSFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSP 507
Cdd:PLN02860 392 GPHVMLGYWGQNSETASVLSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVP 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1039777677 508 DPIRGEVVKAFIVLNPDYK-SHDQEQLKK--------EIQEHV-KKTTAPYKYPR 552
Cdd:PLN02860 472 DSRLTEMVVACVRLRDGWIwSDNEKENAKknltlsseTLRHHCrEKNLSRFKIPK 526
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
113-554 |
7.82e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 105.60 E-value: 7.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 113 RGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCII----------------TDDTLAPAVD 176
Cdd:PRK06164 59 RGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVvwpgfkgidfaailaaVPPDALPPLR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 177 AVAAKCENLHSkliVSQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIYFT-SGTTGPPKMIGHTHSSF--------- 246
Cdd:PRK06164 139 AIAVVDDAADA---TPAPAPGARVQLFALPDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLlrharaiar 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 247 GLGLSVNGRFWLDLIASDVMwntsdtgwaksAWSSVFSPWTQGACVfaHYLPRFESTSILQTLSKFPIT-VFCSAPTAYR 325
Cdd:PRK06164 216 AYGYDPGAVLLAALPFCGVF-----------GFSTLLGALAGGAPL--VCEPVFDAARTARALRRHRVThTFGNDEMLRR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 326 MLVQNDMSRSykFNSLKHC-VSAGEPINPEVMeQWRKKTGLDIYEGYGQTE--TVLICGNFK---GMKIKPGsmGKP-SP 398
Cdd:PRK06164 283 ILDTAGERAD--FPSARLFgFASFAPALGELA-ALARARGVPLTGLYGSSEvqALVALQPATdpvSVRIEGG--GRPaSP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 399 AFDVKILD-ENGATLPPGQEGDIALQVlperPfGLFTHYVDNPSKTASTLRGS-FYITGDRGYMDEDGYFWFVARSDDII 476
Cdd:PRK06164 358 EARVRARDpQDGALLPDGESGEIEIRA----P-SLMRGYLDNPDATARALTDDgYFRTGDLGYTRGDGQFVYQTRMGDSL 432
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039777677 477 LSSGYRIGPFEVESALIEHPSIAESAVVSSpdPIRGEVVKAFIVLNPDYKSHDQEQLKKeiqeHVKKTTAPYKYPRKV 554
Cdd:PRK06164 433 RLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKTVPVAFVIPTDGASPDEAGLMA----ACREALAGFKVPARV 504
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
88-591 |
1.17e-23 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 104.36 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 88 RWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIt 167
Cdd:cd17640 5 RITYKDLYQEILDFAAGL-RSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 168 ddtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshtcVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFG 247
Cdd:cd17640 83 ------------------------------------------------VENDSDDLATIIYTSGTTGNPKGVMLTHANLL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 248 LGLSvngRFW--LDLIASDVMWntsdtgwaksawsSVFSPW--TQGAC---VFA-----HYlprfesTSI---LQTLSKF 312
Cdd:cd17640 115 HQIR---SLSdiVPPQPGDRFL-------------SILPIWhsYERSAeyfIFAcgcsqAY------TSIrtlKDDLKRV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 313 PITVFCSAPTAYRMLVQN------DMSRSYKF--------NSLKHCVSAGEPINPEVmEQWRKKTGLDIYEGYGQTET-- 376
Cdd:cd17640 173 KPHYIVSVPRLWESLYSGiqkqvsKSSPIKQFlflfflsgGIFKFGISGGGALPPHV-DTFFEAIGIEVLNGYGLTETsp 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 377 VLICGNFKGMKIkpGSMGKPSPAFDVKILDENG-ATLPPGQEGdIALQVLPERPFGlfthYVDNPSKTASTLRGS-FYIT 454
Cdd:cd17640 252 VVSARRLKCNVR--GSVGRPLPGTEIKIVDPEGnVVLPPGEKG-IVWVRGPQVMKG----YYKNPEATSKVLDSDgWFNT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 455 GDRGYMDEDGYFWFVARSDD-IILSSGYRIGPFEVESALIEHPSIaESAVVSSPDPIRgevVKAFIVlnPDYkshdqEQL 533
Cdd:cd17640 325 GDLGWLTCGGELVLTGRAKDtIVLSNGENVEPQPIEEALMRSPFI-EQIMVVGQDQKR---LGALIV--PNF-----EEL 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039777677 534 KKEIQEhvkkttapykyprkVGVPGTSDVSPVLwtvfSSDILCERFQTELMTIVNQKL 591
Cdd:cd17640 394 EKWAKE--------------SGVKLANDRSQLL----ASKKVLKLYKNEIKDEISNRP 433
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
65-554 |
1.21e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 105.09 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 65 MEKAGKRLSNPAFWWIDGNGEelrWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPG 144
Cdd:PRK05857 21 FEQARQQPEAIALRRCDGTSA---LRYRELVAEVGGLAADL-RAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 145 TTQLTQKDIlyrlqssKAKCIITDdtlaPAVDAVAAKC--------ENLHSKLIVSQHSREGWGNLKEMMKYASDShTCV 216
Cdd:PRK05857 97 DGNLPIAAI-------ERFCQITD----PAAALVAPGSkmassavpEALHSIPVIAVDIAAVTRESEHSLDAASLA-GNA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 217 DTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLG---LSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVF 293
Cdd:PRK05857 165 DQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAVpdiLQKEGLNWVTWVVGETTYSPLPATHIGGLWWILTCLMHGGLCVT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 294 AHYlprfESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAG-EPINPEVmeQWRKKTGLDIYEGYG 372
Cdd:PRK05857 245 GGE----NTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGsRAIAADV--RFIEATGVRTAQVYG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 373 QTET-----VLICGNFKGMKIKPGSMGKPSPAFDVKILDENGA--TLPPGQEGDIALQVLPERPFGLFThYVDNPSKTAS 445
Cdd:PRK05857 319 LSETgctalCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGIgpTAPGAGPSASFGTLWIKSPANMLG-YWNNPERTAE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 446 TLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDY 525
Cdd:PRK05857 398 VLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAEL 477
|
490 500
....*....|....*....|....*....
gi 1039777677 526 KSHDQEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:PRK05857 478 DESAARALKHTIAARFRRESEPMARPSTI 506
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
221-564 |
3.56e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 101.30 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 221 DEMMAIYfTSGTTGPPKMIGHTHSSFGLGLS-----VNGRFWLDLIASDVMWNTSDTGW--------AKSAWSSVFSPWT 287
Cdd:cd05924 4 DDLYILY-TGGTTGMPKGVMWRQEDIFRMLMggadfGTGEFTPSEDAHKAAAAAAGTVMfpapplmhGTGSWTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 288 QGACVFAHylPRFESTSILQTLSKFPITVFCSAPTAY-RMLVQN-DMSRSYKFNSLKHCVSAGEPINPEVMEQW-RKKTG 364
Cdd:cd05924 83 GQTVVLPD--DRFDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDAlRDAGPYDLSSLFAISSGGALLSPEVKQGLlELVPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 365 LDIYEGYGQTET-VLICGNFKGMKIKPGSMGKPSPafDVKILDENGATLPPGQEGdiaLQVLPER---PFGlfthYVDNP 440
Cdd:cd05924 161 ITLVDAFGSSETgFTGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGG---VGWIARRghiPLG----YYGDE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 441 SKTASTLR---GSFY-ITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVK 516
Cdd:cd05924 232 AKTAETFPevdGVRYaVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVV 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1039777677 517 AFIVLNPDYKSHDQeqlkkEIQEHVKKTTAPYKYPRKVGVPGTSDVSP 564
Cdd:cd05924 312 AVVQLREGAGVDLE-----ELREHCRTRIARYKLPKQVVFVDEIERSP 354
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
85-551 |
7.54e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 104.27 E-value: 7.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 85 EELRWSFEELGLLSRKFANILTEacslqRG----DRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSS 160
Cdd:PRK12316 4573 DEEKLTYAELNRRANRLAHALIA-----RGvgpeVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDS 4647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 161 KAKCIITDDTLAPAVDAVAAkcenLHSKLIVSQHSREGWgnlkemmkyaSDSHTCVDTKHDEMMAIYFTSGTTGPPKMIG 240
Cdd:PRK12316 4648 GAALLLTQSHLLQRLPIPDG----LASLALDRDEDWEGF----------PAHDPAVRLHPDNLAYVIYTSGSTGRPKGVA 4713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 241 HTHSSFGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHYLPRFESTSILQTLSKFPITVFCSA 320
Cdd:PRK12316 4714 VSHGSLVNHLHATGERY-ELTPDDRVLQFMSFSFDGSHEG-LYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFP 4791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 321 PTAYRMLVQNDmSRSYKFNSLKHCVSAGEPINPEVMEQ-WRKKTGLDIYEGYGQTETVLICGNFKGMK-IKPGS----MG 394
Cdd:PRK12316 4792 PVYLQQLAEHA-ERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVLLWKARDgDACGAaympIG 4870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 395 KPSPAFDVKILDENGATLPPGQEGDIALQvlperPFGLFTHYVDNPSKTASTL--------RGSFYITGDRGYMDEDGYF 466
Cdd:PRK12316 4871 TPLGNRSGYVLDGQLNPLPVGVAGELYLG-----GEGVARGYLERPALTAERFvpdpfgapGGRLYRTGDLARYRADGVI 4945
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 467 WFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQ--LKKEIQEHVKKT 544
Cdd:PRK12316 4946 DYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQaeLRDELKAALRER 5025
|
....*..
gi 1039777677 545 TAPYKYP 551
Cdd:PRK12316 5026 LPEYMVP 5032
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
341-556 |
3.53e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 100.07 E-value: 3.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 341 LKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTET-VLICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGD 419
Cdd:PRK13383 294 LRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVgIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 420 IALQvlperpfGLF--THYVDNPSKTASTLRGSfyiTGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPS 497
Cdd:PRK13383 374 IFVG-------GELagTRYTDGGGKAVVDGMTS---TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPA 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039777677 498 IAESAVVSSPDPIRGEVVKAFIVLNPDyKSHDQEQLKKEIQEHVKKttapYKYPRKVGV 556
Cdd:PRK13383 444 VADNAVIGVPDERFGHRLAAFVVLHPG-SGVDAAQLRDYLKDRVSR----FEQPRDINI 497
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
218-520 |
3.81e-22 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 99.82 E-value: 3.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 218 TKHDEMMAIYFTSGTTGPPK--MIGHtHSSFGLGLSVNGRFwlDLIASDVMWNTSDTGWAKSAwSSVFSPWTQGAC-VFA 294
Cdd:cd17644 103 TQPENLAYVIYTSGSTGKPKgvMIEH-QSLVNLSHGLIKEY--GITSSDRVLQFASIAFDVAA-EEIYVTLLSGATlVLR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 295 HYLPRFESTSILQTLSKFPITVFcSAPTAYRMLVQNDMSRSYK--FNSLKHCVSAGEPINPEVMEQWRKKTGLDI--YEG 370
Cdd:cd17644 179 PEEMRSSLEDFVQYIQQWQLTVL-SLPPAYWHLLVLELLLSTIdlPSSLRLVIVGGEAVQPELVRQWQKNVGNFIqlINV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 371 YGQTETVL--ICGNFK---GMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVLperpfGLFTHYVDNPSKTA- 444
Cdd:cd17644 258 YGPTEATIaaTVCRLTqltERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGV-----GLARGYLNRPELTAe 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 445 --------STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVK 516
Cdd:cd17644 333 kfishpfnSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLV 412
|
....
gi 1039777677 517 AFIV 520
Cdd:cd17644 413 AYIV 416
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
85-551 |
1.68e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 99.85 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 85 EELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:PRK12467 534 GEQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRL 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 165 IITDDTLA---PAVDAVAAKCENLHSKLIvsQHSregwgnlkemmkyaSDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGH 241
Cdd:PRK12467 613 LLTQSHLLaqlPVPAGLRSLCLDEPADLL--CGY--------------SGHNPEVALDPDNLAYVIYTSGSTGQPKGVAI 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 242 THSSFGLGLSVNGRfWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLPR---FESTSILQTLSKFPITVFC 318
Cdd:PRK12467 677 SHGALANYVCVIAE-RLQLAADDSMLMVSTFAFDLGVTE-LFGALASGATL--HLLPPdcaRDAEAFAALMADQGVTVLK 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 319 SAPTAYRMLVQNdmSRSYKFNSLKHCVSAGEPINPEVMEQWRKKT-GLDIYEGYGQTETVLICGNFK----GMKIKPGSM 393
Cdd:PRK12467 753 IVPSHLQALLQA--SRVALPRPQRALVCGGEALQVDLLARVRALGpGARLINHYGPTETTVGVSTYElsdeERDFGNVPI 830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 394 GKPSPAFDVKILDENGATLPPGQEGD--IALQVLPE----RPFGLFTHYVDNPSKTAStlrGSFYITGDRGYMDEDGYFW 467
Cdd:PRK12467 831 GQPLANLGLYILDHYLNPVPVGVVGElyIGGAGLARgyhrRPALTAERFVPDPFGADG---GRLYRTGDLARYRADGVIE 907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 468 FVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVkAFIVLNPDYKSHDQEQLKKEIQEHVKKTTAP 547
Cdd:PRK12467 908 YLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLVPAAVADGAEHQATRDELKAQLRQVLPD 986
|
....
gi 1039777677 548 YKYP 551
Cdd:PRK12467 987 YMVP 990
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
214-551 |
1.38e-20 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 94.63 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 214 TCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGlGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVf 293
Cdd:cd17652 86 ALLLTTPDNLAYVIYTSGSTGRPKGVVVTHRGLA-NLAAAQIAAFDVGPGSRVLQFASPSFDASVWE-LLMALLAGATL- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 294 aHYLPRFESTS---ILQTLSKFPITVFCSAPTAYRMLVQNDMSrsykfnSLKHCVSAGEPINPEVMEQWrkKTGLDIYEG 370
Cdd:cd17652 163 -VLAPAEELLPgepLADLLREHRITHVTLPPAALAALPPDDLP------DLRTLVVAGEACPAELVDRW--APGRRMINA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 371 YGQTETVL---ICGNFKGMKIKPgsMGKPSPAFDVKILDENGATLPPGQEGDIALQvlperPFGLFTHYVDNPSKTA--- 444
Cdd:cd17652 234 YGPTETTVcatMAGPLPGGGVPP--IGRPVPGTRVYVLDARLRPVPPGVPGELYIA-----GAGLARGYLNRPGLTAerf 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 445 -----STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFI 519
Cdd:cd17652 307 vadpfGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYV 386
|
330 340 350
....*....|....*....|....*....|..
gi 1039777677 520 VLNPDyKSHDQEQLKkeiqEHVKKTTAPYKYP 551
Cdd:cd17652 387 VPAPG-AAPTAAELR----AHLAERLPGYMVP 413
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
84-547 |
1.83e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.56 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 84 GEElRWSFEELGLLSRKFANILTEaCSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAK 163
Cdd:PRK12316 533 GEE-TLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQ 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 164 CIITDDTLAPAVDaVAAKCENL---HSKLIVSQHSREgwgNLKemmkyasdshTCVDTKHdeMMAIYFTSGTTGPPKMIG 240
Cdd:PRK12316 611 LLLSQSHLGRKLP-LAAGVQVLdldRPAAWLEGYSEE---NPG----------TELNPEN--LAYVIYTSGSTGKPKGAG 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 241 HTHSSFglglsVNGRFW----LDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGA-CVFAHYLPRFESTSILQTLSKFPIT 315
Cdd:PRK12316 675 NRHRAL-----SNRLCWmqqaYGLGVGDTVLQKTPFSFDVSVWE-FFWPLMSGArLVVAAPGDHRDPAKLVELINREGVD 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 316 VFCSAPTAYRMLVQNDMSRSykFNSLKHCVSAGEPINPEVMEQ-WRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGS-- 392
Cdd:PRK12316 749 TLHFVPSMLQAFLQDEDVAS--CTSLRRIVCSGEALPADAQEQvFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSvp 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 393 MGKPSPAFDVKILDENGATLPPGQEGDIALQvlperPFGLFTHYVDNPSKTASTLRGS-------FYITGDRGYMDEDGY 465
Cdd:PRK12316 827 IGRPIANLACYILDANLEPVPVGVLGELYLA-----GRGLARGYHGRPGLTAERFVPSpfvagerMYRTGDLARYRADGV 901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 466 FWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSspdpIRGEVVKAFIVLNpDYKSHDQEQLKKEIQEHVKKTT 545
Cdd:PRK12316 902 IEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLE-SEGGDWREALKAHLAASLPEYM 976
|
..
gi 1039777677 546 AP 547
Cdd:PRK12316 977 VP 978
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
86-551 |
2.18e-20 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 94.26 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 86 ELRWSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCI 165
Cdd:cd12114 10 DGTLTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 166 ITDDTLAPAVDAVAAkcenLHSKLIVSQHsregwgnlkemmkyASDSHTCVDTKHDEMMAIYFTSGTTGPPK--MIGHTH 243
Cdd:cd12114 89 LTDGPDAQLDVAVFD----VLILDLDALA--------------APAPPPPVDVAPDDLAYVIFTSGSTGTPKgvMISHRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 244 SSFGLgLSVNGRFWLDliASDVMWNTSDTGWAKSAWSsVFSPWTQGAC-VFAHYLPRFESTSILQTLSKFPITVFCSAPT 322
Cdd:cd12114 151 ALNTI-LDINRRFAVG--PDDRVLALSSLSFDLSVYD-IFGALSAGATlVLPDEARRRDPAHWAELIERHGVTLWNSVPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 323 AYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKT-GLDIYEGYGQTETVlICGNFkgMKIKPGSM-------G 394
Cdd:cd12114 227 LLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEAS-IWSIY--HPIDEVPPdwrsipyG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 395 KPSPAFDVKILDENGATLPPGQEGDIalqvlperpF----GLFTHYVDNPSKTAS-----TLRGSFYITGDRGYMDEDGY 465
Cdd:cd12114 304 RPLANQRYRVLDPRGRDCPDWVPGEL---------WiggrGVALGYLGDPELTAArfvthPDGERLYRTGDLGRYRPDGT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 466 FWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPiRGEVVKAFIVLNPDYKSHDQEQLKKEIQEHVKKTT 545
Cdd:cd12114 375 LEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYM 453
|
....*.
gi 1039777677 546 APYKYP 551
Cdd:cd12114 454 IPSRVI 459
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-551 |
2.20e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.18 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 86 ELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCI 165
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIER-GVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL 3158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 166 ITDDTLA-PAVDAVAAKCenlhsklivsqhsregwgnLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHS 244
Cdd:PRK12316 3159 LSQSHLRlPLAQGVQVLD-------------------LDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHS 3219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 245 SFGLGLSVNGRFwLDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFAHYLPRFES-TSILQTLSKFPITVFCSAPTA 323
Cdd:PRK12316 3220 ALSNHLCWMQQA-YGLGVGDRVLQFTTFSFDVFVEE-LFWPLMSGARVVLAGPEDWRDpALLVELINSEGVDVLHAYPSM 3297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 324 YRMLVQNDMSRSYKfnSLKHCVSAGEPINPEVMEQWrkKTGLDIYEGYGQTETVLICGNFKGMKIKPGS--MGKPSPAFD 401
Cdd:PRK12316 3298 LQAFLEEEDAHRCT--SLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRA 3373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 402 VKILDENGATLPPGQEGDIALQvlperPFGLFTHYVDNPSKTASTLR-------GSFYITGDRGYMDEDGYFWFVARSDD 474
Cdd:PRK12316 3374 CYILDGSLEPVPVGALGELYLG-----GEGLARGYHNRPGLTAERFVpdpfvpgERLYRTGDLARYRADGVIEYIGRVDH 3448
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039777677 475 IILSSGYRIGPFEVESALIEHPSIAESAVVSspdpIRGEVVKAFIVLnpdykSHDQEQLKKEIQEHVKKTTAPYKYP 551
Cdd:PRK12316 3449 QVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVP-----EDEAGDLREALKAHLKASLPEYMVP 3516
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
117-551 |
3.44e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 95.61 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 117 VMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTL-----APAVDAVaakcenlhskLIV 191
Cdd:PRK12467 3148 VGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLleqlpAPAGDTA----------LTL 3217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 192 SQHSREGWgnlkemmkyaSDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWlDLIASDVMWNTSD 271
Cdd:PRK12467 3218 DRLDLNGY----------SENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAY-ELDANDRVLLFMS 3286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 272 TGWAKSAWSsVFSPWTQGACVFAHYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYkfNSLKHCVSAGEPI 351
Cdd:PRK12467 3287 FSFDGAQER-FLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADC--ASLDIYVFGGEAV 3363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 352 NPEVMEQWRKKTG-LDIYEGYGQTETVLI-----CGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQVL 425
Cdd:PRK12467 3364 PPAAFEQVKRKLKpRGLTNGYGPTEAVVTvtlwkCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGV 3443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 426 perpfGLFTHYVDNPSKTA--------STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPS 497
Cdd:PRK12467 3444 -----GLARGYHQRPSLTAerfvadpfSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPS 3518
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1039777677 498 IAESAVVSSpDPIRGEVVKAFIVLNPdykshDQEQLKKEIQEHVKKTTAPYKYP 551
Cdd:PRK12467 3519 VREAVVLAR-DGAGGKQLVAYVVPAD-----PQGDWRETLRDHLAASLPDYMVP 3566
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
79-547 |
3.70e-20 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 94.46 E-value: 3.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 79 WIDGNGEELrwSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEWW--LANVACLrtGTVLIPGTTQLTQKDILYR 156
Cdd:PRK05620 31 WGGAEQEQT--TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 157 LQSSKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSQHS-REGWGNLKEMMKYAS-----DSHTCV----DTKHDEMMAI 226
Cdd:PRK05620 107 INHAEDEVIVADPRLAEQLGEILKECPCVRAVVFIGPSDaDSAAAHMPEGIKVYSyeallDGRSTVydwpELDETTAAAI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 227 YFTSGTTGPPKMIGHTHSSFGLGLsvngrfwLDLIASDVMWNTSDTGWAKS-------AWSSVFSPWTQGA-CVFAhylp 298
Cdd:PRK05620 187 CYSTGTTGAPKGVVYSHRSLYLQS-------LSLRTTDSLAVTHGESFLCCvpiyhvlSWGVPLAAFMSGTpLVFP---- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 299 rfESTSILQTLSKFPIT----VFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQT 374
Cdd:PRK05620 256 --GPDLSAPTLAKIIATamprVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 375 ETVLIcgnfkGMKIKPG-------------SMGKPSPAFDVKILDEnGATLPPGQEGDIALQVlpeRPFGLFTHYVDNPS 441
Cdd:PRK05620 334 ETSPV-----GTVARPPsgvsgearwayrvSQGRFPASLEYRIVND-GQVMESTDRNEGEIQV---RGNWVTASYYHSPT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 442 KT----ASTLRGS-------------FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVV 504
Cdd:PRK05620 405 EEgggaASTFRGEdvedandrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVI 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1039777677 505 SSPDPIRGEVVKAFIVLNPDYKSHDQ--EQLKKEIQEHVKKTTAP 547
Cdd:PRK05620 485 GYPDDKWGERPLAVTVLAPGIEPTREtaERLRDQLRDRLPNWMLP 529
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
88-551 |
4.12e-20 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 93.39 E-value: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 88 RWSFEELGLLSRKFANILTEaCSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIT 167
Cdd:cd17645 23 SLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 168 DDtlapavdavaakcenlhsklivsqhsregwGNLKEMMkyasdshtcvdtkhdemmaiyFTSGTTGPPKMIGHTHSSFg 247
Cdd:cd17645 102 NP------------------------------DDLAYVI---------------------YTSGSTGLPKGVMIEHHNL- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 248 lglsVNGRFW----LDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVfaHYLP---RFESTSILQTLSKFPITV-FCS 319
Cdd:cd17645 130 ----VNLCEWhrpyFGVTPADKSLVYASFSFDASAWE-IFPHLTAGAAL--HVVPserRLDLDALNDYFNQEGITIsFLP 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 320 APTAYR-MLVQNdmsrsykfNSLKHCVSAGEPINPEvmeqwrKKTGLDIYEGYGQTETVLICGNFKGMKIKPG-SMGKPS 397
Cdd:cd17645 203 TGAAEQfMQLDN--------QSLRVLLTGGDKLKKI------ERKGYKLVNNYGPTENTVVATSFEIDKPYANiPIGKPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 398 PAFDVKILDENGATLPPGQEGDiaLQVLPErpfGLFTHYVDNPSKTASTLRGS-------FYITGDRGYMDEDGYFWFVA 470
Cdd:cd17645 269 DNTRVYILDEALQLQPIGVAGE--LCIAGE---GLARGYLNRPELTAEKFIVHpfvpgerMYRTGDLAKFLPDGNIEFLG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 471 RSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLnpdykshDQEQLKKEIQEHVKKTTAPYKY 550
Cdd:cd17645 344 RLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTA-------PEEIPHEELREWLKNDLPDYMI 416
|
.
gi 1039777677 551 P 551
Cdd:cd17645 417 P 417
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
487-554 |
4.14e-20 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 84.52 E-value: 4.14e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039777677 487 EVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYkshdqEQLKKEIQEHVKKTTAPYKYPRKV 554
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGV-----ELLEEELVAHVREELGPYAVPKEV 63
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
88-509 |
4.39e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 94.00 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 88 RWSFEELGLLSRKFANILTeACSLQRGDRVMVIlpkipEW-----WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKA 162
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALA-ALGVEPGDRVGTL-----AWngyrhLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 163 KCIITDDTLAPAVDAVAAKCENLhsklivsqhsrEGWGNLKEMMKYASDS--HTCVDT------------KHDEMMAIY- 227
Cdd:PRK07008 113 RYVLFDLTFLPLVDALAPQCPNV-----------KGWVAMTDAAHLPAGStpLLCYETlvgaqdgdydwpRFDENQASSl 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 228 -FTSGTTGPPKMIGHTHSS-----FGLGLSVNgrfwLDLIASDV------MWNTSdtgwaksAWSSVFS-PWTQGACVFA 294
Cdd:PRK07008 182 cYTSGTTGNPKGALYSHRStvlhaYGAALPDA----MGLSARDAvlpvvpMFHVN-------AWGLPYSaPLTGAKLVLP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 295 HylPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQT 374
Cdd:PRK07008 251 G--PDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 375 ETVLIcGNFKGMKIKPGSM------------GKPSPAFDVKILDENGATLP-PGQE-GDiaLQVlpeRPFGLFTHYVDNp 440
Cdd:PRK07008 329 EMSPL-GTLCKLKWKHSQLpldeqrkllekqGRVIYGVDMKIVGDDGRELPwDGKAfGD--LQV---RGPWVIDRYFRG- 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039777677 441 skTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDP 509
Cdd:PRK07008 402 --DASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHP 468
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
68-541 |
5.78e-20 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 93.46 E-value: 5.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 68 AGKRLSNPAF-WWIDGNGEELRWSFEELGLLSRKFANILTEACslQRGDRVMVILPKIPEWWLANVACLRTGTV---LIP 143
Cdd:cd05931 3 AAARPDRPAYtFLDDEGGREETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPGLDFVAAFLGCLYAGAIavpLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 144 GTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAK-CENLHSKLIVSQHSREGwgnlkemmkyASDSHTCVDTKHDE 222
Cdd:cd05931 81 PTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAASrPAAGTPRLLVVDLLPDT----------SAADWPPPSPDPDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 223 MMAIYFTSGTTGPPK--MIGHthssfgLGLSVNgrfwLDLIASDVMWNTSDTGwakSAW----------SSVFSPWTQGA 290
Cdd:cd05931 151 IAYLQYTSGSTGTPKgvVVTH------RNLLAN----VRQIRRAYGLDPGDVV---VSWlplyhdmgliGGLLTPLYSGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 291 -CVF---AHYL--P-RFestsiLQTLSKFPITvFCSAPT-AYRMLVQN---------DMSrsykfnSLKHCVSAGEPINP 353
Cdd:cd05931 218 pSVLmspAAFLrrPlRW-----LRLISRYRAT-ISAAPNfAYDLCVRRvrdedleglDLS------SWRVALNGAEPVRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 354 EVMEQWRKK---TGLD---IYEGYGQTE-TVLICGNFKG------------------MKIKPG-------SMGKPSPAFD 401
Cdd:cd05931 286 ATLRRFAEAfapFGFRpeaFRPSYGLAEaTLFVSGGPPGtgpvvlrvdrdalagravAVAADDpaarelvSCGRPLPDQE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 402 VKILDENGAT-LPPGQEGDIALQ---VLPerpfGlfthYVDNPSKTASTLR-------GSFYITGDRGYMDeDGYFWFVA 470
Cdd:cd05931 366 VRIVDPETGReLPDGEVGEIWVRgpsVAS----G----YWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITG 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039777677 471 RSDDIILSSGYRIGPFEVESALIE-HPSIAES--AVVSSPDPIRGEVVkAFIVLNPDYKSHDQEQLKKEIQEHV 541
Cdd:cd05931 437 RLKDLIIVRGRNHYPQDIEATAEEaHPALRPGcvAAFSVPDDGEERLV-VVAEVERGADPADLAAIAAAIRAAV 509
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
80-541 |
1.13e-19 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 92.73 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 80 IDGNGEELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPK----IPEWWlanvACLRTGTVLIPGTTQLTqkdilY 155
Cdd:cd05906 31 IDADGSEEFQSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLTVPPT-----Y 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 156 RLQSSKAK------------CIITDDTLAPAVDAVAAKCENLHSKLIVSQhsregwgnlkEMMKYASDSHTcVDTKHDEM 223
Cdd:cd05906 101 DEPNARLRklrhiwqllgspVVLTDAELVAEFAGLETLSGLPGIRVLSIE----------ELLDTAADHDL-PQSRPDDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 224 MAIYFTSGTTGPPKMIGHTHSSF---GLGLSVNGRF--------W--LDLIASDVMWNTSDtgwaksawssVFSPWTQGA 290
Cdd:cd05906 170 ALLMLTSGSTGFPKAVPLTHRNIlarSAGKIQHNGLtpqdvflnWvpLDHVGGLVELHLRA----------VYLGCQQVH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 291 CVFAHYLPrfESTSILQTLSKFPITV-FcsAPT-AYRMLVQ---NDMSRSYKFNSLKHCVSAGEPINPEVMEQWR---KK 362
Cdd:cd05906 240 VPTEEILA--DPLRWLDLIDRYRVTItW--APNfAFALLNDlleEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLrllEP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 363 TGLD---IYEGYGQTET---VLICGNFKGMKIKPG----SMGKPSPAFDVKILDENGATLPPGQEGDiaLQVlpeRPFGL 432
Cdd:cd05906 316 YGLPpdaIRPAFGMTETcsgVIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDEGQLLPEGEVGR--LQV---RGPVV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 433 FTHYVDNPSKTASTLR-GSFYITGDRGYMDeDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAES--AVVSSPDP 509
Cdd:cd05906 391 TKGYYNNPEANAEAFTeDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVRDP 469
|
490 500 510
....*....|....*....|....*....|...
gi 1039777677 510 IRGEVVKAfIVLNPDYKSHDQ-EQLKKEIQEHV 541
Cdd:cd05906 470 GAETEELA-IFFVPEYDLQDAlSETLRAIRSVV 501
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
80-554 |
1.40e-19 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 92.36 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 80 IDGngeELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTV------------LIPGTTQ 147
Cdd:PRK10946 43 ICG---ERQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLGNVAEFYITFFALLKLGVApvnalfshqrseLNAYASQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 148 LTQKdilyRLQSSKAKCIITDDTLapaVDAVAAKCENLhskLIVSQHSREGWGNLKEMMKYASDSHTCVDTKHDEMMAIY 227
Cdd:PRK10946 119 IEPA----LLIADRQHALFSDDDF---LNTLVAEHSSL---RVVLLLNDDGEHSLDDAINHPAEDFTATPSPADEVAFFQ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 228 FTSGTTGPPKMIGHTHSSFGL---------GLSVNGRFWLDLIASDvmwntsdtgwaKSAWSS-----VFspWTQGACVF 293
Cdd:PRK10946 189 LSGGSTGTPKLIPRTHNDYYYsvrrsveicGFTPQTRYLCALPAAH-----------NYPMSSpgalgVF--LAGGTVVL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 294 AhylPRFESTSILQTLSKFPITVFCSAPTAYRMLVQ--NDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLDIYEGY 371
Cdd:PRK10946 256 A---PDPSATLCFPLIEKHQVNVTALVPPAVSLWLQaiAEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQVF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 372 GQTETVLicgNFKGMKIKP----GSMGKP-SPAFDVKILDENGATLPPGQEGdialqVLPER-PFgLFTHYVDNPSKTAS 445
Cdd:PRK10946 333 GMAEGLV---NYTRLDDSDerifTTQGRPmSPDDEVWVADADGNPLPQGEVG-----RLMTRgPY-TFRGYYKSPQHNAS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 446 TLRGS-FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPD 524
Cdd:PRK10946 404 AFDANgFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEP 483
|
490 500 510
....*....|....*....|....*....|
gi 1039777677 525 YKShdqEQLKKEIQEHvkkTTAPYKYPRKV 554
Cdd:PRK10946 484 LKA---VQLRRFLREQ---GIAEFKLPDRV 507
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
226-524 |
3.20e-19 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 90.45 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 226 IYFTSGTTGPPKMIGHTHSSfglglSVNGRFWldliasdvmwntSDTGWAKSAWSSV---------------FSPWTQGA 290
Cdd:cd12115 110 VIYTSGSTGRPKGVAIEHRN-----AAAFLQW------------AAAAFSAEELAGVlastsicfdlsvfelFGPLATGG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 291 CVF----AHYL---PRFESTSILQTLskfpitvfcsaPTAYRMLV-QNDMSRSYKFNSLkhcvsAGEPINPEVMEQWRKK 362
Cdd:cd12115 173 KVVladnVLALpdlPAAAEVTLINTV-----------PSAAAELLrHDALPASVRVVNL-----AGEPLPRDLVQRLYAR 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 363 TGLD-IYEGYGQTE-----TVLICGnfKGMKIKPgSMGKPSPAFDVKILDENGATLPPGQEGDIALQvlperPFGLFTHY 436
Cdd:cd12115 237 LQVErVVNLYGPSEdttysTVAPVP--PGASGEV-SIGRPLANTQAYVLDRALQPVPLGVPGELYIG-----GAGVARGY 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 437 VDNPSKTASTLR-------GSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDP 509
Cdd:cd12115 309 LGRPGLTAERFLpdpfgpgARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDA 388
|
330
....*....|....*
gi 1039777677 510 IRGEVVKAFIVLNPD 524
Cdd:cd12115 389 AGERRLVAYIVAEPG 403
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
89-523 |
1.57e-18 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 89.02 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 89 WSFEELGLLSRKFANILTeACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITD 168
Cdd:cd17641 12 FTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 169 DTlaPAVDAVAAKCENLHS--KLIVS--------QHSREGW-GNLKEMMKYASDSHTCV------DTKHDEMMAIYFTSG 231
Cdd:cd17641 91 DE--EQVDKLLEIADRIPSvrYVIYCdprgmrkyDDPRLISfEDVVALGRALDRRDPGLyerevaAGKGEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 232 TTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACV-FAHylprfESTSILQTLS 310
Cdd:cd17641 169 TTGKPKLAMLSHGNF-LGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVnFPE-----EPETMMEDLR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 311 KFPITVFCSAP------------------------------TAYRMLVQNDMSRSYK----------------------- 337
Cdd:cd17641 243 EIGPTFVLLPPrvwegiaadvrarmmdatpfkrfmfelgmkLGLRALDRGKRGRPVSlwlrlaswladallfrplrdrlg 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 338 FNSLKHCVSAGEPINPEVMEQWRKkTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKIlDENGatlppgqe 417
Cdd:cd17641 323 FSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI-DEVG-------- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 418 gdialQVLPERPfGLFTHYVDNPSKTASTL-RGSFYITGDRGYMDEDGYFWFVARSDDI-ILSSGYRIGPFEVESALIEH 495
Cdd:cd17641 393 -----EILVRSP-GVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKLKFS 466
|
490 500
....*....|....*....|....*...
gi 1039777677 496 PSIAESAVVSSPDPIrgevVKAFIVLNP 523
Cdd:cd17641 467 PYIAEAVVLGAGRPY----LTAFICIDY 490
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
163-534 |
4.41e-18 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 87.50 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 163 KCIITDDTLAPAVDAVAAKCENLHSKLIVSQHSREGWGNLKEMMKY----ASDSHTCVDTKHDEMMA--IYFTSGTTGPP 236
Cdd:PRK06018 113 RVVITDLTFVPILEKIADKLPSVERYVVLTDAAHMPQTTLKNAVAYeewiAEADGDFAWKTFDENTAagMCYTSGTTGDP 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 237 KMIGHTHSSFGL-GLSVNGRFWLDLIASDVMWNTSDTGWAkSAWSSVFSPWTQGACVFahyLP--RFESTSILQTLSKFP 313
Cdd:PRK06018 193 KGVLYSHRSNVLhALMANNGDALGTSAADTMLPVVPLFHA-NSWGIAFSAPSMGTKLV---MPgaKLDGASVYELLDTEK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 314 ITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPInPEVMEQWRKKTGLDIYEGYGQTETVLI--CGNFKG------ 385
Cdd:PRK06018 269 VTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEMSPLgtLAALKPpfsklp 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 386 ----MKIKPgSMGKPSPAFDVKILDENGATLPpgQEGdialqvlpeRPFGLFThyVDNPSKTASTLRGS--------FYI 453
Cdd:PRK06018 348 gdarLDVLQ-KQGYPPFGVEMKITDDAGKELP--WDG---------KTFGRLK--VRGPAVAAAYYRVDgeildddgFFD 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 454 TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQEQL 533
Cdd:PRK06018 414 TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEIL 493
|
.
gi 1039777677 534 K 534
Cdd:PRK06018 494 K 494
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
88-524 |
4.53e-18 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 87.21 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 88 RWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIP-GTTQLTQkdilyRLQSskakciI 166
Cdd:cd05918 24 SLTYAELDRLSSRLAHHLRSL-GVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPlDPSHPLQ-----RLQE------I 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 167 TDDTLAPAVdavaakcenlhsklIVSQHSRegwgnlkemmkyasdshtcvdtkhdemmAIY--FTSGTTGPPKMIGHTHS 244
Cdd:cd05918 92 LQDTGAKVV--------------LTSSPSD----------------------------AAYviFTSGSTGKPKGVVIEHR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 245 SF---------GLGLSVNGRfWLDL--IASDVMWNtsdtgwaksawsSVFSPWTQGACV-----------FAHYLPRFES 302
Cdd:cd05918 130 ALstsalahgrALGLTSESR-VLQFasYTFDVSIL------------EIFTTLAAGGCLcipseedrlndLAGFINRLRV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 303 TSILQTlskfpitvfcsaPTAYRMLVQNDmsrsykFNSLKHCVSAGEPINPEVMEQWRKKTGLdiYEGYGQTE-TVLICG 381
Cdd:cd05918 197 TWAFLT------------PSVARLLDPED------VPSLRTLVLGGEALTQSDVDTWADRVRL--INAYGPAEcTIAATV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 382 NFKGMKIKPGSMGKPSPAFdVKILDENGAT--LPPGQEGDIAL---QVLPErpfglfthYVDNPSKTA------------ 444
Cdd:cd05918 257 SPVVPSTDPRNIGRPLGAT-CWVVDPDNHDrlVPIGAVGELLIegpILARG--------YLNDPEKTAaafiedpawlkq 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 445 --STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVK---AFI 519
Cdd:cd05918 328 egSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPqlvAFV 407
|
....*
gi 1039777677 520 VLNPD 524
Cdd:cd05918 408 VLDGS 412
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
85-561 |
6.60e-18 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 86.76 E-value: 6.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 85 EELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKC 164
Cdd:cd17656 10 ENQKLTYRELNERSNQLARFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 165 IITDDTLApavdaVAAKCENLHSKLIVSQHSREgwgnlkemmkyaSDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHS 244
Cdd:cd17656 89 VLTQRHLK-----SKLSFNKSTILLEDPSISQE------------DTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 245 SFGLGLSVNGRFWLDLIASDVMWNTSDTgwAKSAWSSVFSPWTQGACVfahYLPRFESTSILQTLSKF----PITVFcSA 320
Cdd:cd17656 152 NMVNLLHFEREKTNINFSDKVLQFATCS--FDVCYQEIFSTLLSGGTL---YIIREETKRDVEQLFDLvkrhNIEVV-FL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 321 PTAYRMLVQNDmsRSYK---FNSLKHCVSAGEP--INPEVMEQWRKKtGLDIYEGYGQTETVLIcgnfKGMKIKPGS--- 392
Cdd:cd17656 226 PVAFLKFIFSE--REFInrfPTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGPSETHVV----TTYTINPEAeip 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 393 ----MGKPSPAFDVKILDENGATLPPGQEGDIALQVLperpfGLFTHYVDNPSKTASTLRGS-------FYITGDRGYMD 461
Cdd:cd17656 299 elppIGKPISNTWIYILDQEQQLQPQGIVGELYISGA-----SVARGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 462 EDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnPDYKSHDqEQLKKEIQEHV 541
Cdd:cd17656 374 PDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV--MEQELNI-SQLREYLAKQL 450
|
490 500
....*....|....*....|
gi 1039777677 542 KKTTAPYKYPRKVGVPGTSD 561
Cdd:cd17656 451 PEYMIPSFFVPLDQLPLTPN 470
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
111-574 |
7.48e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 86.72 E-value: 7.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 111 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLApavdAVAAKCENLHSKLI 190
Cdd:cd05915 46 VGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLL----PLVEAIRGELKTVQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 191 VSQHSREGWGNLKEMMKYASDSHTCVDTKHD-EMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLIASDVMWNT 269
Cdd:cd05915 122 HFVVMDEKAPEGYLAYEEALGEEADPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVLP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 270 SDTGWAKSAWSSVFSPWTQGACVFAhYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGE 349
Cdd:cd05915 202 VVPMFHVNAWCLPYAATLVGAKQVL-PGPRLDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGS 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 350 PiNPEVMEQWRKKTGLDIYEGYGQTETVLI---CGNFKGMKIKPGSMGKPSPAFD--------VKILDENGATLPpgQEG 418
Cdd:cd05915 281 A-APRSLIARFERMGVEVRQGYGLTETSPVvvqNFVKSHLESLSEEEKLTLKAKTglpiplvrLRVADEEGRPVP--KDG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 419 DiALQVLPERPFGLFTHYV-DNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPS 497
Cdd:cd05915 358 K-ALGEVQLKGPWITGGYYgNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPK 436
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039777677 498 IAESAVVSSPDPIRGEVVKAFIVLNpdykshDQEQLKKEIQEHVKKTTAPYKYprkvgVPGTsdvspvlwTVFSSDI 574
Cdd:cd05915 437 VKEAAVVAIPHPKWQERPLAVVVPR------GEKPTPEELNEHLLKAGFAKWQ-----LPDA--------YVFAEEI 494
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
57-508 |
8.13e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 86.85 E-value: 8.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 57 DVLDQWtnmekAGKRLSNPAFwwIDGNGeelRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLR 136
Cdd:PRK08279 41 DVFEEA-----AARHPDRPAL--LFEDQ---SISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 137 TGTV--LIpgTTQLTQKDILYRLQSSKAKCIITDDTLAPAVDAVAAKCENLHSKLIVSQ---HSREGWGNLKEMMKYASD 211
Cdd:PRK08279 110 LGAVvaLL--NTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGdtlDDPEGYEDLAAAAAGAPT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 212 ---SHTCVDTKHDEmmAIY-FTSGTTGPPKMIGHTH-----SSFGLGLSvngrfwLDLIASDVMWNT----SDTGwAKSA 278
Cdd:PRK08279 188 tnpASRSGVTAKDT--AFYiYTSGTTGLPKAAVMSHmrwlkAMGGFGGL------LRLTPDDVLYCClplyHNTG-GTVA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 279 WSSVFSPwtqGACVFAHylPRFESTSILQTLSKFPITVFCsaptaY-----RMLVQNDMSRSYKFNSLKHCVSAGepINP 353
Cdd:PRK08279 259 WSSVLAA---GATLALR--RKFSASRFWDDVRRYRATAFQ-----YigelcRYLLNQPPKPTDRDHRLRLMIGNG--LRP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 354 EVMEQWRKKTGLD-IYEGYGQTE--TVLIcgNFKGmkiKPGSMGKpSPAFD------VKILDENGATL----------PP 414
Cdd:PRK08279 327 DIWDEFQQRFGIPrILEFYAASEgnVGFI--NVFN---FDGTVGR-VPLWLahpyaiVKYDVDTGEPVrdadgrcikvKP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 415 GQEGDIALQVLPERPfglFTHYVDnPSKT-ASTLRGSF------YITGDRGYMDEDGYFWFVARSDDIilssgYR----- 482
Cdd:PRK08279 401 GEVGLLIGRITDRGP---FDGYTD-PEASeKKILRDVFkkgdawFNTGDLMRDDGFGHAQFVDRLGDT-----FRwkgen 471
|
490 500
....*....|....*....|....*...
gi 1039777677 483 IGPFEVESALIEHPSIAESAV--VSSPD 508
Cdd:PRK08279 472 VATTEVENALSGFPGVEEAVVygVEVPG 499
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
116-551 |
1.19e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.52 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 116 RVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLA---PAVDAVAAkcenlhskLIVS 192
Cdd:PRK12467 1626 LVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQarlPLPDGLRS--------LVLD 1697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 193 QhsregwgnLKEMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDT 272
Cdd:PRK12467 1698 Q--------EDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGAL-VNRLCATQEAYQLSAADVVLQFTSF 1768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 273 GWAKSAWSsVFSPWTQGA-CVFAHYLPRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDmSRSYKFNSLKHCVSAGEPI 351
Cdd:PRK12467 1769 AFDVSVWE-LFWPLINGArLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD-EQVEHPLSLRRVVCGGEAL 1846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 352 NPEVMEQWRKKTG-LDIYEGYGQTETVL-----IC--GNFKGMKIKPgsMGKPSPAFDVKILDENGATLPPGQEGDIALQ 423
Cdd:PRK12467 1847 EVEALRPWLERLPdTGLFNLYGPTETAVdvthwTCrrKDLEGRDSVP--IGQPIANLSTYILDASLNPVPIGVAGELYLG 1924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 424 VLperpfGLFTHYVDNPSKTA--------STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEH 495
Cdd:PRK12467 1925 GV-----GLARGYLNRPALTAerfvadpfGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQ 1999
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039777677 496 PSIAESAVVSSpDPIRGEVVKAFIV-LNPDYKSHDQEQ--LKKEIQEHVKKTTAPYKYP 551
Cdd:PRK12467 2000 GGVREAVVIAQ-DGANGKQLVAYVVpTDPGLVDDDEAQvaLRAILKNHLKASLPEYMVP 2057
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-551 |
2.52e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 86.55 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 86 ELRWSFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCI 165
Cdd:PRK12316 2026 DQHLSYAELDSRANRLAHRLRAR-GVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALL 2104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 166 ITDDTLAPAVdAVAAKCENLhsklivsQHSREGWgnlkemMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSS 245
Cdd:PRK12316 2105 LTQRHLLERL-PLPAGVARL-------PLDRDAE------WADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGA 2170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 246 FGLGLSVNGRFWlDLIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVFA----HYLPRfestSILQTLSKFPITVFcSAP 321
Cdd:PRK12316 2171 LVAHCQAAGERY-ELSPADCELQFMSFSFDGAHEQ-WFHPLLNGARVLIrddeLWDPE----QLYDEMERHGVTIL-DFP 2243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 322 TAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLD-IYEGYGQTETVLICGNFKGMKIKPGS-----MGK 395
Cdd:PRK12316 2244 PVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVTPLLWKCRPQDPCGaayvpIGR 2323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 396 PSPAFDVKILDENGATLPPGQEGDIALQVLperpfGLFTHYVDNPSKTA--------STLRGSFYITGDRGYMDEDGYFW 467
Cdd:PRK12316 2324 ALGNRRAYILDADLNLLAPGMAGELYLGGE-----GLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVVE 2398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 468 FVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSpDPIRGEVVKAFIVlnPDyksHDQEQLKKEIQEHVKKTTAP 547
Cdd:PRK12316 2399 YLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV--PD---DAAEDLLAELRAWLAARLPA 2472
|
....
gi 1039777677 548 YKYP 551
Cdd:PRK12316 2473 YMVP 2476
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
90-504 |
2.99e-17 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 85.87 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 90 SFEELGLLSRKFANILTEAcSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDD 169
Cdd:PRK10252 485 SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 170 TLAPAVDAVaakcenlhSKLIVSQHSREGWgnlkemmkyASDSHTCVDTKHDEMMAIYFTSGTTGPPK--MIGHThssfg 247
Cdd:PRK10252 564 DQLPRFADV--------PDLTSLCYNAPLA---------PQGAAPLQLSQPHHTAYIIFTSGSTGRPKgvMVGQT----- 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 248 lgLSVNGRFWLD----LIASDVMWNTSDTGWAKSAWSsVFSPWTQGACVF-----AHYLPrfesTSILQTLSKFPITVFC 318
Cdd:PRK10252 622 --AIVNRLLWMQnhypLTADDVVLQKTPCSFDVSVWE-FFWPFIAGAKLVmaepeAHRDP----LAMQQFFAEYGVTTTH 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 319 SAPTAYRMLVQNDMSRSYKFN--SLKHCVSAGEPINPEVMEQWRKKTGLDIYEGYGQTET-VLICGNFKGMKIKPGSMGK 395
Cdd:PRK10252 695 FVPSMLAAFVASLTPEGARQScaSLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAaVDVSWYPAFGEELAAVRGS 774
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 396 PSP-AFDV-----KILDENGATLPPGQEGDIAL---QvlperpfgLFTHYVDNPSKTAST-LRGSF------YITGDRGY 459
Cdd:PRK10252 775 SVPiGYPVwntglRILDARMRPVPPGVAGDLYLtgiQ--------LAQGYLGRPDLTASRfIADPFapgermYRTGDVAR 846
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1039777677 460 MDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVV 504
Cdd:PRK10252 847 WLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTH 891
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
218-504 |
1.50e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 82.51 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 218 TKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLsvngrfwlDLIASDVMWNTSDTGWAKSAWSSVFSPwtqgACVFAHYL 297
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQI--------DALRQLYGIRPGEVDLATFPLFALFGP----ALGLTSVI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 298 PRFESTS--------ILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRK--KTGLDI 367
Cdd:cd05910 150 PDMDPTRparadpqkLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKmlSDEAEI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 368 YEGYGQTETVLICG-------NFKGMKIKPGS---MGKPSPAFDVKILD---------ENGATLPPGQEGDIAL---QVL 425
Cdd:cd05910 230 LTPYGATEALPVSSigsrellATTTAATSGGAgtcVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVtgpTVT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 426 PErpfglfthYVDNPSKTA----STLRGSF-YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAE 500
Cdd:cd05910 310 PT--------YVNRPVATAlakiDDNSEGFwHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRR 381
|
....
gi 1039777677 501 SAVV 504
Cdd:cd05910 382 SALV 385
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
284-553 |
1.55e-16 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 82.35 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 284 SPWTQGACVFAHYlPRFESTsilQTLSKFPITVFCS-APTAYRMLVQNDMSRSYKFNSLkhcVSAGEPINPEVMEQWRKK 362
Cdd:PRK07445 181 SFLTGGKLVILPY-KRLKSG---QELPPNPSDFFLSlVPTQLQRLLQLRPQWLAQFRTI---LLGGAPAWPSLLEQARQL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 363 tGLDIYEGYGQTETV-LICgnfkgmKIKPG-------SMGKPSPafDVKIldengaTLPPGQEGDIALQVlPERPFGLFT 434
Cdd:PRK07445 254 -QLRLAPTYGMTETAsQIA------TLKPDdflagnnSSGQVLP--HAQI------TIPANQTGNITIQA-QSLALGYYP 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 435 HYVDNPSktastlrgsFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEV 514
Cdd:PRK07445 318 QILDSQG---------IFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEV 388
|
250 260 270
....*....|....*....|....*....|....*....
gi 1039777677 515 VKAFIVlnPDYKSHDQEqlkkEIQEHVKKTTAPYKYPRK 553
Cdd:PRK07445 389 VTAIYV--PKDPSISLE----ELKTAIKDQLSPFKQPKH 421
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
219-553 |
2.21e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 79.17 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 219 KHDEMMAIYFTSGTTGPPKMIGHTHSS-----------FGLGlsvNGRFWL-------DLiasDVMwntsdtgwaksaws 280
Cdd:PRK04813 141 KGDDNYYIIFTSGTTGKPKGVQISHDNlvsftnwmledFALP---EGPQFLnqapysfDL---SVM-------------- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 281 SVFSPWTQGACVFAhyLPRfESTS----ILQTLSKFPITVFCSAPTAYRMLVqndMSRSY---KFNSLKHCVSAGEPINP 353
Cdd:PRK04813 201 DLYPTLASGGTLVA--LPK-DMTAnfkqLFETLPQLPINVWVSTPSFADMCL---LDPSFneeHLPNLTHFLFCGEELPH 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 354 EVMEQWRKK-TGLDIYEGYGQTE-TVLIcgnfKGMKI--------KPGSMGKPSPAFDVKILDENGATLPPGQEGDIALq 423
Cdd:PRK04813 275 KTAKKLLERfPSATIYNTYGPTEaTVAV----TSIEItdemldqyKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVI- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 424 VLPERPFGlfthYVDNPSKTAS---TLRGS-FYITGDRGYMDeDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIA 499
Cdd:PRK04813 350 SGPSVSKG----YLNNPEKTAEaffTFDGQpAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVE 424
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039777677 500 ESAVVsspdPI-RGEVVK---AFIVLNPdyksHDQE---QLKKEIQEHVKKTTAPYKYPRK 553
Cdd:PRK04813 425 SAVVV----PYnKDHKVQyliAYVVPKE----EDFErefELTKAIKKELKERLMEYMIPRK 477
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
121-558 |
1.06e-14 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 76.78 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 121 LPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLAPA----------VDAVAAKCENL-HSKL 189
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGgralplyskvVEAAPAKAIVLpAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 190 IVSQHSREGWGNLKEMMKYASDSHtCVDTKH--------DEMMAIYFTSGTTGPPKMIGHTHSSfGLGLSVNGRFWLDLI 261
Cdd:PLN03051 81 PVAVPLREQDLSWCDFLGVAAAQG-SVGGNEyspvyapvESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 262 ASDVM-WNTSdTGWAKSAWsSVFSPWTQGACVfAHYLPRFESTSILQTLSKFPITVFCSAPT---AYRMLVQNDMSRsYK 337
Cdd:PLN03051 159 PGDVVcWPTN-LGWMMGPW-LLYSAFLNGATL-ALYGGAPLGRGFGKFVQDAGVTVLGLVPSivkAWRHTGAFAMEG-LD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 338 FNSLKHCVSAGEPINPE------VMEQWRKKT-----GLDIYEGYGQTETVLICGnfkgmkikPGSMGKPSPAFDVKILD 406
Cdd:PLN03051 235 WSKLRVFASTGEASAVDdvlwlsSVRGYYKPVieycgGTELASGYISSTLLQPQA--------PGAFSTASLGTRFVLLN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 407 ENGATLPPGQE--GDIALQVlperPFGLFTHYVDNPSKTASTLRG-SFYIT--------GDRGYMDEDGYFWFVARSDDI 475
Cdd:PLN03051 307 DNGVPYPDDQPcvGEVALAP----PMLGASDRLLNADHDKVYYKGmPMYGSkgmplrrhGDIMKRTPGGYFCVQGRADDT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 476 ILSSGYRIGPFEVESALIE-HPSIAESAVVSSPDPIRGE----VVKAFIVLNPDYKSHDQEQLKKEIQEHVKKTTAP-YK 549
Cdd:PLN03051 383 MNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTNLNPlFK 462
|
....*....
gi 1039777677 550 YPRKVGVPG 558
Cdd:PLN03051 463 VSRVKIVPE 471
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
125-545 |
1.45e-14 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 76.49 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 125 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTLApavdavaakcenlhsklIVSqhsregwgnLKE 204
Cdd:cd05927 43 PEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDAGVK-----------------VYS---------LEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 205 MMK-YASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFGLGLSVNGRFWLDLiasdVMWNTSDTGWAksawssvF 283
Cdd:cd05927 97 FEKlGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEIL----NKINPTDVYIS-------Y 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 284 SPwtqgacvFAHYLPRF-ESTSI-------------------LQTLSkfPiTVFCSAPTAY-RML--VQNDMSRS----- 335
Cdd:cd05927 166 LP-------LAHIFERVvEALFLyhgakigfysgdirlllddIKALK--P-TVFPGVPRVLnRIYdkIFNKVQAKgplkr 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 336 --------YKFNSLKH---------------------------CVSAGEPINPEVMEQWRKKTGLDIYEGYGQTETV-LI 379
Cdd:cd05927 236 klfnfalnYKLAELRSgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTaGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 380 CGNFKGMKIkPGSMGKPSPAFDVKILD--ENG--ATLPPGqEGDIALqvlpeRPFGLFTHYVDNPSKTASTLR--GsFYI 453
Cdd:cd05927 316 TLTLPGDTS-VGHVGGPLPCAEVKLVDvpEMNydAKDPNP-RGEVCI-----RGPNVFSGYYKDPEKTAEALDedG-WLH 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 454 TGDRGYMDEDGYFWFVARSDDII-LSSGYRIGPFEVESALIEHPSIAESAVvsspdpiRGEVVKAF----IVLNPDY--- 525
Cdd:cd05927 388 TGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFVAQIFV-------YGDSLKSFlvaiVVPDPDVlke 460
|
490 500 510
....*....|....*....|....*....|...
gi 1039777677 526 ---------KSHDQ----EQLKKEIQEHVKKTT 545
Cdd:cd05927 461 waaskgggtGSFEElcknPEVKKAILEDLVRLG 493
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
226-551 |
3.61e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 74.69 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 226 IYFTSGTTGPPKMIGHTHSSFGLGL-SVNGRFWLD-----LIASDVmwnTSDTGWAksawSSVFSPWTQGA--CVFAHYL 297
Cdd:PRK08308 106 LQYSSGTTGEPKLIRRSWTEIDREIeAYNEALNCEqdetpIVACPV---THSYGLI----CGVLAALTRGSkpVIITNKN 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 298 PRFestsILQTLSKFPITVFCSAPTAYRMlvqndMSR----SYKFNSLkhcVSAGEPINPEVMEQWRKKTgLDIYEGYGQ 373
Cdd:PRK08308 179 PKF----ALNILRNTPQHILYAVPLMLHI-----LGRllpgTFQFHAV---MTSGTPLPEAWFYKLRERT-TYMMQQYGC 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 374 TET--VLICGNFKgmkiKPGSMGKPSPAFDVKIldenGATlpPGQEGDIALQVLPERPFglfthyvdnpsktastlrgsf 451
Cdd:PRK08308 246 SEAgcVSICPDMK----SHLDLGNPLPHVSVSA----GSD--ENAPEEIVVKMGDKEIF--------------------- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 452 yiTGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVlnpdykSH--- 528
Cdd:PRK08308 295 --TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI------SHeei 366
|
330 340
....*....|....*....|...
gi 1039777677 529 DQEQLKKEIQEHVkkttAPYKYP 551
Cdd:PRK08308 367 DPVQLREWCIQHL----APYQVP 385
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
85-552 |
6.28e-14 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 74.64 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 85 EELRWSFEELGLLSRKFANILTEACSLQRGDRVMVILPKIPEW---WLAnVACLRTGTVLIPgtTQLTQKDILYRLQSSK 161
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWLG-LAKLGCPVAFLN--TNIRSKSLLHCFRCCG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 162 AKCIITDDTLAPAVDAV--AAKCENLHSKLIVSQHSREGWGNLKEMMKYASDSHTCVDTK-HDEMM--AIY-FTSGTTGP 235
Cdd:cd05938 79 AKVLVVAPELQEAVEEVlpALRADGVSVWYLSHTSNTEGVISLLDKVDAASDEPVPASLRaHVTIKspALYiYTSGTTGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 236 PK--MIGHTHSSFGLG-LSVNGrfwldLIASDVMWNTSDTGWAKSAWSSVFSPWTQGA-CVFAhylPRFESTSILQTLSK 311
Cdd:cd05938 159 PKaaRISHLRVLQCSGfLSLCG-----VTADDVIYITLPLYHSSGFLLGIGGCIELGAtCVLK---PKFSASQFWDDCRK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 312 FPITVFCSAPTAYRMLV---QNDMSRSYKFNslkhcVSAGEPINPEVMEQWRKKTG-LDIYEGYGQTETVLICGNFKGmk 387
Cdd:cd05938 231 HNVTVIQYIGELLRYLCnqpQSPNDRDHKVR-----LAIGNGLRADVWREFLRRFGpIRIREFYGSTEGNIGFFNYTG-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 388 iKPGSMGKPS-------P----AFDVK----ILDENG--ATLPPGQEGDIALQVLPERPfglFTHYVDNPSKTASTL--- 447
Cdd:cd05938 304 -KIGAVGRVSylykllfPfeliKFDVEkeepVRDAQGfcIPVAKGEPGLLVAKITQQSP---FLGYAGDKEQTEKKLlrd 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 448 ---RGSFYI-TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAV--VSSPDpIRGEVVKAFIVL 521
Cdd:cd05938 380 vfkKGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVTVPG-HEGRIGMAAVKL 458
|
490 500 510
....*....|....*....|....*....|.
gi 1039777677 522 NPDYkSHDQEQLkkeiQEHVKKTTAPYKYPR 552
Cdd:cd05938 459 KPGH-EFDGKKL----YQHVREYLPAYARPR 484
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
226-554 |
7.89e-14 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 73.97 E-value: 7.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 226 IYFTSGTTGPPK--MIGHtHSSFGLGLSVNGRFWLDLIASDVMwntsdtgwaksawsSVFSPWtqgacVFAHYLPRFeST 303
Cdd:cd17648 99 AIYTSGTTGKPKgvLVEH-GSVVNLRTSLSERYFGRDNGDEAV--------------LFFSNY-----VFDFFVEQM-TL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 304 SIL--QTLSKFPITVFCSAPTAYR---------------MLVQNDMSRsykFNSLKHCVSAGEPINPEVMEQWRKKTGLD 366
Cdd:cd17648 158 ALLngQKLVVPPDEMRFDPDRFYAyinrekvtylsgtpsVLQQYDLAR---LPHLKRVDAAGEEFTAPVFEKLRSRFAGL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 367 IYEGYGQTETVL--ICGNFKGMKIKPGSMGKPSPAFDVKILDENGATLPPGQEGDIALQ---VLP---ERPFGLFTHYVD 438
Cdd:cd17648 235 IINAYGPTETTVtnHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGgdgVARgylNRPELTAERFLP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 439 NPSKTAS-TLRGSF---YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDP-IRGE 513
Cdd:cd17648 315 NPFQTEQeRARGRNarlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDAsQAQS 394
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1039777677 514 VVKAFIVlnpDYKSHDQEQL-KKEIQEHVKKTTAPYKYPRKV 554
Cdd:cd17648 395 RIQKYLV---GYYLPEPGHVpESDLLSFLRAKLPRYMVPARL 433
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
116-504 |
1.19e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 74.82 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 116 RVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTL---APAVDAVAAKC-ENLHSkliv 191
Cdd:PRK05691 1183 CVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLlerLPQAEGVSAIAlDSLHL---- 1258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 192 sqhsrEGWgnlkemmkyasDSHTCVDTKHDEMMA-IYFTSGTTGPPKMIGHTHSSFGLGLSvngrfWLD----LIASDVM 266
Cdd:PRK05691 1259 -----DSW-----------PSQAPGLHLHGDNLAyVIYTSGSTGQPKGVGNTHAALAERLQ-----WMQatyaLDDSDVL 1317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 267 WNTSDTGWAKSAWSsVFSPWTQGA-CVFA----HYLPRfestSILQTLSKFPITVFCSAPTAYRMLVqnDMSRSYKFNSL 341
Cdd:PRK05691 1318 MQKAPISFDVSVWE-CFWPLITGCrLVLAgpgeHRDPQ----RIAELVQQYGVTTLHFVPPLLQLFI--DEPLAAACTSL 1390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 342 KHCVSAGEPINPEVMEQWRKK-TGLDIYEGYGQTETVL-----ICGNFKGMKikpGSMGKPSPAFDVKILDENGATLPPG 415
Cdd:PRK05691 1391 RRLFSGGEALPAELRNRVLQRlPQVQLHNRYGPTETAInvthwQCQAEDGER---SPIGRPLGNVLCRVLDAELNLLPPG 1467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 416 QEGDIALQVLperpfGLFTHYVDNPSKTA--------STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFE 487
Cdd:PRK05691 1468 VAGELCIGGA-----GLARGYLGRPALTAerfvpdplGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEE 1542
|
410
....*....|....*..
gi 1039777677 488 VESALIEHPSIAESAVV 504
Cdd:PRK05691 1543 IQARLLAQPGVAQAAVL 1559
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
218-508 |
3.69e-13 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 71.73 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 218 TKHDEMMAIYFTSGTTGPPK--MIGH---THSSFGL-------GLSVN----GRFWLDLIASDvmwntsdtgWAKSAWS- 280
Cdd:cd17650 90 TQPEDLAYVIYTSGTTGKPKgvMVEHrnvAHAAHAWrreyeldSFPVRllqmASFSFDVFAGD---------FARSLLNg 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 281 SVFSPWTQGAcvfahylpRFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCV--SAGEPINPEVMEQ 358
Cdd:cd17650 161 GTLVICPDEV--------KLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIvgSDGCKAQDFKTLA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 359 WRKKTGLDIYEGYGQTETVLICGNFK-GMKIKPGS----MGKPSPAFDVKILDENGATLPPGQEGDIALQvlperPFGLF 433
Cdd:cd17650 233 ARFGQGMRIINSYGVTEATIDSTYYEeGRDPLGDSanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIG-----GAGVA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 434 THYVDNPSKTASTLR-------GSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSS 506
Cdd:cd17650 308 RGYLNRPELTAERFVenpfapgERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVR 387
|
..
gi 1039777677 507 PD 508
Cdd:cd17650 388 ED 389
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
88-492 |
5.24e-13 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 71.30 E-value: 5.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 88 RWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEW---WLAnVACLRTGTVLIpgTTQLTQKDILYRLQSSKAKC 164
Cdd:cd05939 3 HWTFRELNEYSNKVANFF-QAQGYRSGDVVALFMENRLEFvalWLG-LAKIGVETALI--NSNLRLESLLHCITVSKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 165 IITDdtlapavdavaakcenlHSKLIVSQHSREgwgnlkemmkyasdSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHS 244
Cdd:cd05939 79 LIFN-----------------LLDPLLTQSSTE--------------PPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 245 SFgLGLSVNGRFWLDLIASDVMWNTsdtgwaKSAWSSVFSPWTQGACVFahylprFESTSILQtlSKFPITVFCSAPTAY 324
Cdd:cd05939 128 RY-YRIAAGAYYAFGMRPEDVVYDC------LPLYHSAGGIMGVGQALL------HGSTVVIR--KKFSASNFWDDCVKY 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 325 RMLVQN---DMSR-----SYKFNSLKHCV--SAGEPINPEVMEQWRKKTGL-DIYEGYGQTETVLICGNFKG-------- 385
Cdd:cd05939 193 NCTIVQyigEICRyllaqPPSEEEQKHNVrlAVGNGLRPQIWEQFVRRFGIpQIGEFYGATEGNSSLVNIDNhvgacgfn 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 386 ----MKIKPGSMGKPSPAFDVKILDENGATLP--PGQEGDIALQVLPERPFGLFTHYVDNPSKTASTLRG------SFYI 453
Cdd:cd05939 273 srilPSVYPIRLIKVDEDTGELIRDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIARDvfkkgdSAFL 352
|
410 420 430
....*....|....*....|....*....|....*....
gi 1039777677 454 TGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESAL 492
Cdd:cd05939 353 SGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGIL 391
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
51-557 |
6.40e-13 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 71.65 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 51 YFNFAKDVLdqwtnMEKAGKRLSNPAFWWIDGNGEEL---RWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEW 127
Cdd:PLN03052 173 VLNVAECCL-----TPKPSKTDDSIAIIWRDEGSDDLpvnRMTLSELRSQVSRVANAL-DALGFEKGDAIAIDMPMNVHA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 128 WLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDTL-----------------APAVDAVAAKCENLHSKLi 190
Cdd:PLN03052 247 VIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIvrggksiplysrvveakAPKAIVLPADGKSVRVKL- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 191 vsqhsREGWGNLKEMMKYAS-----DSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHSSfGLGLSVNGRFWLDLIASDV 265
Cdd:PLN03052 326 -----REGDMSWDDFLARANglrrpDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQLT-PLRAAADAWAHLDIRKGDI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 266 M-WNTsDTGWAKSAWSsVFSPWTQGACvfahyLPRFESTSILQTLSKF----PITVFCSAPTAYRMLVQNDMSRSYKFNS 340
Cdd:PLN03052 400 VcWPT-NLGWMMGPWL-VYASLLNGAT-----LALYNGSPLGRGFAKFvqdaKVTMLGTVPSIVKTWKNTNCMAGLDWSS 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 341 LKHCVSAGEPINPE----VMEQWRKKTgldIYEGYGQTEtvlICGNF-KGMKIKPGSMGK---PSPAFDVKILDENGATL 412
Cdd:PLN03052 473 IRCFGSTGEASSVDdylwLMSRAGYKP---IIEYCGGTE---LGGGFvTGSLLQPQAFAAfstPAMGCKLFILDDSGNPY 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 413 PPGQE--GDIALQVLperPFGLFT----------HYVDNPSKTASTLRGSfyitGDRGYMDEDGYFWFVARSDDIIlssg 480
Cdd:PLN03052 547 PDDAPctGELALFPL---MFGASStllnadhykvYFKGMPVFNGKILRRH----GDIFERTSGGYYRAHGRADDTM---- 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 481 yRIGPFEVESALIE------HPSIAESAVVSSPDPIRG--EVVKAFIVLNPDYKSHDQEQLKKEIQEHVKKTTAP-YKYP 551
Cdd:PLN03052 616 -NLGGIKVSSVEIErvcnaaDESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPlFKVS 694
|
....*.
gi 1039777677 552 RKVGVP 557
Cdd:PLN03052 695 AVVIVP 700
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
226-551 |
4.72e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 66.35 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 226 IYfTSGTTGPPKMIGHTHSSFGLGL-SVNGRFwlDLIASDVMWNTSDTGWaKSAWSSVFSPWTQGACVFAHYLPRFESTS 304
Cdd:PRK05691 2339 IY-TSGSTGKPKGVVVSHGEIAMHCqAVIERF--GMRADDCELHFYSINF-DAASERLLVPLLCGARVVLRAQGQWGAEE 2414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 305 ILQTLSKFPITVFCSAPTAYRMLVQNdMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKTGLD-IYEGYGQTETV---LIC 380
Cdd:PRK05691 2415 ICQLIREQQVSILGFTPSYGSQLAQW-LAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTETVvmpLAC 2493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 381 GNFKGMKIKPGS--MGKPSPAFDVKILDENGATLPPGQEGDIALQVLperpfGLFTHYVDNPSKTA--------STLRGS 450
Cdd:PRK05691 2494 LAPEQLEEGAASvpIGRVVGARVAYILDADLALVPQGATGELYVGGA-----GLAQGYHDRPGLTAerfvadpfAADGGR 2568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 451 FYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDQ 530
Cdd:PRK05691 2569 LYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDEAQ 2648
|
330 340
....*....|....*....|.
gi 1039777677 531 EQLKKEIQEHVKKTTAPYKYP 551
Cdd:PRK05691 2649 AALREALKAHLKQQLPDYMVP 2669
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
225-547 |
5.25e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 65.76 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 225 AIYFTSGTTGPPKMIGHTHSSFglgLS----VNGRfwLDLIASDVMWNTsdtgwaksawssvfspwtqgacvfahyLPRF 300
Cdd:PRK06814 797 VILFTSGSEGTPKGVVLSHRNL---LAnraqVAAR--IDFSPEDKVFNA---------------------------LPVF 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 301 ES---TS--ILQTLSKFPITVFCSaPTAYR------------MLVQND--------MSRSYKFNSLKHCVSAGEPINPEV 355
Cdd:PRK06814 845 HSfglTGglVLPLLSGVKVFLYPS-PLHYRiipeliydtnatILFGTDtflngyarYAHPYDFRSLRYVFAGAEKVKEET 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 356 MEQWRKKTGLDIYEGYGQTET--VLICGNfkGMKIKPGSMGKPSPAFDVKI-----LDENGATLPPGQegDIALQVL-PE 427
Cdd:PRK06814 924 RQTWMEKFGIRILEGYGVTETapVIALNT--PMHNKAGTVGRLLPGIEYRLepvpgIDEGGRLFVRGP--NVMLGYLrAE 999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 428 RPfglfthYVDNPsktastLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSP 507
Cdd:PRK06814 1000 NP------GVLEP------PADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIP 1067
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1039777677 508 DPIRGEVvkafIVLNPDYKSHDQEqlkkEIQEHVKKTTAP 547
Cdd:PRK06814 1068 DARKGER----IILLTTASDATRA----AFLAHAKAAGAS 1099
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
207-546 |
1.40e-10 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 63.65 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 207 KYASDSHTCVDTKHDEMMA-IYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAwSSVFSP 285
Cdd:cd17654 103 LSFTPEHRHFNIRTDECLAyVIHTSGTTGTPKIVAVPHKCI-LPNIQHFRSLFNITSEDILFLTSPLTFDPSV-VEIFLS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 286 WTQGACVFAHYLPRFESTSILQTL--SKFPITVFCSAPTAYRMLVQND-----MSRSykfNSLKHCVSAGEPInPE--VM 356
Cdd:cd17654 181 LSSGATLLIVPTSVKVLPSKLADIlfKRHRITVLQATPTLFRRFGSQSikstvLSAT---SSLRVLALGGEPF-PSlvIL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 357 EQWRKK-TGLDIYEGYGQTETVlICGNFKGMKIKPGSMGKPSPAFDVKI--LDENGATlppgQEGDIALQVLPERpfGLF 433
Cdd:cd17654 257 SSWRGKgNRTRIFNIYGITEVS-CWALAYKVPEEDSPVQLGSPLLGTVIevRDQNGSE----GTGQVFLGGLNRV--CIL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 434 THYVDNPsktastlRGSFYITGDRGYMdEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDpirgE 513
Cdd:cd17654 330 DDEVTVP-------KGTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----Q 397
|
330 340 350
....*....|....*....|....*....|...
gi 1039777677 514 VVKAFIVLNPDYKShdqeqLKKEIQEHVKKTTA 546
Cdd:cd17654 398 RLIAFIVGESSSSR-----IHKELQLTLLSSHA 425
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
88-552 |
2.64e-10 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 62.76 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 88 RWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIIT 167
Cdd:cd05940 3 ALTYAELDAMANRYARWL-KSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 168 DdtlapavdavaakcenlhsklivsqhsregwgnlkemmkyasdshTCvdtkhdemMAIYfTSGTTGPPKMIGHTHSSFG 247
Cdd:cd05940 82 D---------------------------------------------AA--------LYIY-TSGTTGLPKAAIISHRRAW 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 248 LGLSVNGrFWLDLIASDVMWNTsdtgwaksawssvfspwtqgacvfahyLPRFESTSILQTLS-------------KFPI 314
Cdd:cd05940 108 RGGAFFA-GSGGALPSDVLYTC---------------------------LPLYHSTALIVGWSaclasgatlvirkKFSA 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 315 TVFCSAPTAYR-MLVQ--NDMSRsYKFNS------LKHCVSA--GEPINPEVMEQWRKKTGL-DIYEGYGQTETVLICGN 382
Cdd:cd05940 160 SNFWDDIRKYQaTIFQyiGELCR-YLLNQppkpteRKHKVRMifGNGLRPDIWEEFKERFGVpRIAEFYAATEGNSGFIN 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 383 FKGmkiKPGSMG-------KPSPAFDVKILDENGATL----------PPGQEGDIALQVLPERPFglfTHYVDNPSKTAS 445
Cdd:cd05940 239 FFG---KPGAIGrnpsllrKVAPLALVKYDLESGEPIrdaegrcikvPRGEPGLLISRINPLEPF---DGYTDPAATEKK 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 446 TLRGSF------YITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAV--VSSPDpIRGEVVKA 517
Cdd:cd05940 313 ILRDVFkkgdawFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPG-TDGRAGMA 391
|
490 500 510
....*....|....*....|....*....|....*
gi 1039777677 518 FIVLNPDYkshdQEQLKKeIQEHVKKTTAPYKYPR 552
Cdd:cd05940 392 AIVLQPNE----EFDLSA-LAAHLEKNLPGYARPL 421
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
125-504 |
4.14e-10 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 62.37 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 125 PEWWLANVACLRTGTVLIPGTTQLTQKDILYRLQSSKAKCIITDDtlAPAVDAVAAKCENL-HSKLIVsQHSRE------ 197
Cdd:cd05933 44 PEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEN--QKQLQKILQIQDKLpHLKAII-QYKEPlkekep 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 198 ---GWGNLKEMMKYASDS--HTCVDT-KHDEMMAIYFTSGTTGPPK--MIGHTHSSF-GLGLSVNGRF------------ 256
Cdd:cd05933 121 nlySWDEFMELGRSIPDEqlDAIISSqKPNQCCTLIYTSGTTGMPKgvMLSHDNITWtAKAASQHMDLrpatvgqesvvs 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 257 WLDL--IASDVMwntsdtgwaksawsSVFSPWTQGACV-FAHylPRFESTSILQTLSKFPITVFCSAP------------ 321
Cdd:cd05933 201 YLPLshIAAQIL--------------DIWLPIKVGGQVyFAQ--PDALKGTLVKTLREVRPTAFMGVPrvwekiqekmka 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 322 -----TAYRMLV------------QNDMSRSYK---------------------FNSLKHCVSAGEPINPEVMEQWrkkT 363
Cdd:cd05933 265 vgaksGTLKRKIaswakgvgletnLKLMGGESPsplfyrlakklvfkkvrkalgLDRCQKFFTGAAPISRETLEFF---L 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 364 GLDI--YEGYGQTE-----TVLICGNFKgmkikPGSMGKPSPAFDVKIL--DENGatlppgqEGDIALqvlpeRPFGLFT 434
Cdd:cd05933 342 SLNIpiMELYGMSEtsgphTISNPQAYR-----LLSCGKALPGCKTKIHnpDADG-------IGEICF-----WGRHVFM 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039777677 435 HYVDNPSKTASTLRGSFYI-TGDRGYMDEDGYFWFVARSDD-IILSSGYRIGPFEVESALIEHPSIAESAVV 504
Cdd:cd05933 405 GYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKElIITAGGENVPPVPIEDAVKKELPIISNAML 476
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
209-491 |
5.35e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 61.94 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 209 ASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHssfglglsvnGRFWLDL----------IASDVMwntsdtgwakSA 278
Cdd:PRK07768 140 AADPIDPVETGEDDLALMQLTSGSTGSPKAVQITH----------GNLYANAeamfvaaefdVETDVM----------VS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 279 WSSVF----------SPWTQGACVfAHYLP-RFESTSIL--QTLSKFPITVFCSAPTAY----RMLVQNDMSRSYKFNSL 341
Cdd:PRK07768 200 WLPLFhdmgmvgfltVPMYFGAEL-VKVTPmDFLRDPLLwaELISKYRGTMTAAPNFAYallaRRLRRQAKPGAFDLSSL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 342 KHCVSAGEPINPEVMEQWR---KKTGLD---IYEGYGQTETVLI-----CGNfkGMKI------------------KPG- 391
Cdd:PRK07768 279 RFALNGAEPIDPADVEDLLdagARFGLRpeaILPAYGMAEATLAvsfspCGA--GLVVdevdadllaalrravpatKGNt 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 392 ----SMGKPSPAFDVKILDENGATLPPGQEGDIALQ---VLPerpfglftHYVDNPSKTASTLRGSFYITGDRGYMDEDG 464
Cdd:PRK07768 357 rrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRgesVTP--------GYLTMDGFIPAQDADGWLDTGDLGYLTEEG 428
|
330 340
....*....|....*....|....*..
gi 1039777677 465 YFWFVARSDDIILSSGYRIGPFEVESA 491
Cdd:PRK07768 429 EVVVCGRVKDVIIMAGRNIYPTDIERA 455
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
221-551 |
6.12e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.49 E-value: 6.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 221 DEMMAIYFTSGTTGPPKmighthssfglGLSVNGRF----------WLDLIASDVMWNTSDTGWAKSAWSSVFSPWTqGA 290
Cdd:PRK05691 3869 DNLAYVIYTSGSTGLPK-----------GVMVEQRGmlnnqlskvpYLALSEADVIAQTASQSFDISVWQFLAAPLF-GA 3936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 291 CV------FAHylprfESTSILQTLSKFPITVFCSAPT-AYRMLVQNDMSrsykFNSLKHCVSAGEPINPEVMEQWRKK- 362
Cdd:PRK05691 3937 RVeivpnaIAH-----DPQGLLAHVQAQGITVLESVPSlIQGMLAEDRQA----LDGLRWMLPTGEAMPPELARQWLQRy 4007
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 363 TGLDIYEGYGQTETVLICGNFK-GMKIKPGS---MGKPSPAFDVKILDENGATLPPGQEGDIALQvlperPFGLFTHYVD 438
Cdd:PRK05691 4008 PQIGLVNAYGPAECSDDVAFFRvDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVA-----GTGVGRGYVG 4082
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 439 NPSKTA--------STLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPi 510
Cdd:PRK05691 4083 DPLRTAlafvphpfGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGV- 4161
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1039777677 511 RGEVVKAFIVlnPDYKSHDQEQLKKEIQEHVKKTTAPYKYP 551
Cdd:PRK05691 4162 NGKHLVGYLV--PHQTVLAQGALLERIKQRLRAELPDYMVP 4200
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
217-495 |
1.73e-09 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 60.60 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 217 DTKHDEMMAIYFTSGTTGPPKMIGHTHSSfglgLSVNGRFWLDLIA---SDVMWNTSDTGWAKSAWSSVFSPWTQGACVF 293
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHAN----LLANQRACLKFFSpkeDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 294 AHYLPrFESTSILQTLSKFPITVFCSAPTAYRMLVQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKK-TGLDIYEGYG 372
Cdd:PRK06334 255 FAYNP-LYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTfPHIQLRQGYG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 373 QTE-TVLICGNFKGMKIKPGSMGKPSPAFDVKILDENgaTLPPGQEGDIALQVLpeRPFGLFTHYVDN-PSKTASTLRG- 449
Cdd:PRK06334 334 TTEcSPVITINTVNSPKHESCVGMPIRGMDVLIVSEE--TKVPVSSGETGLVLT--RGTSLFSGYLGEdFGQGFVELGGe 409
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1039777677 450 SFYITGDRGYMDEDGYFWFVARsddiiLSSGYRIGPFEV-----ESALIEH 495
Cdd:PRK06334 410 TWYVTGDLGYVDRHGELFLKGR-----LSRFVKIGAEMVslealESILMEG 455
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
111-517 |
2.66e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 56.65 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 111 LQRGDRVMVILPKIPEWWLANVACLRTGTVLIPgttqltqkdiLY-RLQSSKAKCIITDDTLApAVDAVAAKCENLHS-- 187
Cdd:PLN02736 100 IPKGACVGLYFINRPEWLIVDHACSAYSYVSVP----------LYdTLGPDAVKFIVNHAEVA-AIFCVPQTLNTLLScl 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 188 ------KLIV----------SQHSREGwgnlKEMMKYA-------SDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHs 244
Cdd:PLN02736 169 seipsvRLIVvvggadeplpSLPSGTG----VEIVTYSkllaqgrSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTH- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 245 sfglglsvngrfwLDLIAS------DVMWNTSDTGWAKSAWSSVFSPWTQGACVFAHYLPRFESTSILQTLSKFPI---T 315
Cdd:PLN02736 244 -------------GNLIANvagsslSTKFYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAAlrpT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 316 VFCSAP--------------------------TAY---RMLVQNDMSRS-----YKFNSLK--------HCVSAGEPINP 353
Cdd:PLN02736 311 IFCSVPrlynriydgitnavkesgglkerlfnAAYnakKQALENGKNPSpmwdrLVFNKIKaklggrvrFMSSGASPLSP 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 354 EVMEQWRKKTGLDIYEGYGQTET-VLICGNFKGMKIKpGSMGKPSPAFDVKILD--ENGATL--PPGQEGDIALqvlpeR 428
Cdd:PLN02736 391 DVMEFLRICFGGRVLEGYGMTETsCVISGMDEGDNLS-GHVGSPNPACEVKLVDvpEMNYTSedQPYPRGEICV-----R 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 429 PFGLFTHYVDNPSKTASTLRGSFYI-TGDRGYMDEDGYFWFVARSDDII-LSSGYRIGPFEVESALIEHPSIAESAV--- 503
Cdd:PLN02736 465 GPIIFKGYYKDEVQTREVIDEDGWLhTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQCFVygd 544
|
490 500
....*....|....*....|..
gi 1039777677 504 --------VSSPDPirgEVVKA 517
Cdd:PLN02736 545 slnsslvaVVVVDP---EVLKA 563
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
348-554 |
5.79e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 55.05 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 348 GEPINPEVMEQwRKKTGLDIYEGYGQTETvliCGnfkgmkikpGSM--GKPSPAFDVKILDEN----GATLPPGQEGdia 421
Cdd:PRK07824 160 GGPAPAPVLDA-AAAAGINVVRTYGMSET---SG---------GCVydGVPLDGVRVRVEDGRialgGPTLAKGYRN--- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 422 lqvLPERPFglFThyvdNPSktastlrgsFYITGDRGYMDeDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAES 501
Cdd:PRK07824 224 ---PVDPDP--FA----EPG---------WFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADC 284
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1039777677 502 AVVSSPDPIRGEVVKAFIVLNPdyksHDQEQLkKEIQEHVKKTTAPYKYPRKV 554
Cdd:PRK07824 285 AVFGLPDDRLGQRVVAAVVGDG----GPAPTL-EALRAHVARTLDRTAAPREL 332
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
216-540 |
1.06e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 55.10 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 216 VDTKHDEMMAIYFTSGTTGPPKMIGHTHSSFgLGLSVNGRFWLDLIASDVMWNTSDTGWAKSAWSSVFSPWTQGACVFA- 294
Cdd:PRK08043 360 VKQQPEDAALILFTSGSEGHPKGVVHSHKSL-LANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLy 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 295 ----HY--LPR----------FESTSILQTLSKFpitvfcsaptayrmlvqndmSRSYKFNSLKHCVSAGEPINPEVMEQ 358
Cdd:PRK08043 439 psplHYriVPElvydrnctvlFGTSTFLGNYARF--------------------ANPYDFARLRYVVAGAEKLQESTKQL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 359 WRKKTGLDIYEGYGQTETVLICGNFKGMKIKPGSMGKPSPAFDVKILD----ENGATL----PPGQEGdiALQVlpERPF 430
Cdd:PRK08043 499 WQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSvpgiEQGGRLqlkgPNIMNG--YLRV--EKPG 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 431 GLFTHYVDNPsktASTLRGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVES-ALIEHPSiAESAVVSSPDP 509
Cdd:PRK08043 575 VLEVPTAENA---RGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPD-KQHATAIKSDA 650
|
330 340 350
....*....|....*....|....*....|.
gi 1039777677 510 IRGEvvkAFIVLNPDyKSHDQEQLKKEIQEH 540
Cdd:PRK08043 651 SKGE---ALVLFTTD-SELTREKLQQYAREH 677
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
217-544 |
8.53e-07 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 51.83 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 217 DTKHDEMMAIYFTSGTTGPPKMIGHTHSSF-----GLGLSVNGRFW--------------LDLIASDV--MWNT------ 269
Cdd:cd17639 84 DGKPDDLACIMYTSGSTGNPKGVMLTHGNLvagiaGLGDRVPELLGpddrylaylplahiFELAAENVclYRGGtigygs 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 270 ----SDTGWAKSAWS-SVFSPwTQGACVfahylPR-FEST-----SILQTLSKFPITVFCSAPTAYRMLVQNDMSRSY-- 336
Cdd:cd17639 164 prtlTDKSKRGCKGDlTEFKP-TLMVGV-----PAiWDTIrkgvlAKLNPMGGLKRTLFWTAYQSKLKALKEGPGTPLld 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 337 --KFNS--------LKHCVSAGEPINPEVMEqWRKKTGLDIYEGYGQTETvliCGNfkGMKIKPGSM-----GKPSPAFD 401
Cdd:cd17639 238 elVFKKvraalggrLRYMLSGGAPLSADTQE-FLNIVLCPVIQGYGLTET---CAG--GTVQDPGDLetgrvGPPLPCCE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 402 VKILD--ENG--ATLPPGQeGDIALQvlpeRPFgLFTHYVDNPSKT--ASTLRGSFYiTGDRGYMDEDGYFWFVARSDDI 475
Cdd:cd17639 312 IKLVDweEGGysTDKPPPR-GEILIR----GPN-VFKGYYKNPEKTkeAFDGDGWFH-TGDIGEFHPDGTLKIIDRKKDL 384
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 476 I-LSSGYRIGPFEVESALIEHPSIAESAVVSspDPIRGEVVkAFIVLNpdykshdQEQLKKEIQEHVKKT 544
Cdd:cd17639 385 VkLQNGEYIALEKLESIYRSNPLVNNICVYA--DPDKSYPV-AIVVPN-------EKHLTKLAEKHGVIN 444
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
53-559 |
1.10e-06 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 51.72 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 53 NFAKDVLDQwtnmekagKRLSNPAFWWIDGNGEELRWSFEELGLLSRKFANILtEACSLQRGDRVMVILPKIPEwwlANV 132
Cdd:PRK03584 87 NYAENLLRH--------RRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAAL-RALGVGPGDRVAAYLPNIPE---TVV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 133 ACLRT---GTVLIPGTTQLTQKDILYRLQSSKAKCIITDD---------TLAPAVDAVAAKCENLHSKLIVSQHSREG-- 198
Cdd:PRK03584 155 AMLATaslGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDgyryggkafDRRAKVAELRAALPSLEHVVVVPYLGPAAaa 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 199 --------WGNLkeMMKYASDSHTCVDTKHDEMMAIYFTSGTTGPPKMIGHTHssfG---------LGLSvngrfwLDLI 261
Cdd:PRK03584 235 aalpgallWEDF--LAPAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGH---GgillehlkeLGLH------CDLG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 262 ASD-VMWNTSdTGWAksAWSSVFSPWTQGACVfahYL----PRFESTSIL-QTLSKFPITVFCSAPTAYRMLVQNDMS-- 333
Cdd:PRK03584 304 PGDrFFWYTT-CGWM--MWNWLVSGLLVGATL---VLydgsPFYPDPNVLwDLAAEEGVTVFGTSAKYLDACEKAGLVpg 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 334 RSYKFNSLKHCVSAGEPINPEVMEqWrkktgldIYEGYGQ----------TEtvlICGNFKG----MKIKPGSMGKPSPA 399
Cdd:PRK03584 378 ETHDLSALRTIGSTGSPLPPEGFD-W-------VYEHVKAdvwlasisggTD---ICSCFVGgnplLPVYRGEIQCRGLG 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 400 FDVKILDENGATLpPGQEGD-IALQVLPERPFGlFTHYVDNpsktaSTLRGSFYIT-------GDRGYMDEDGYFWFVAR 471
Cdd:PRK03584 447 MAVEAWDEDGRPV-VGEVGElVCTKPFPSMPLG-FWNDPDG-----SRYRDAYFDTfpgvwrhGDWIEITEHGGVVIYGR 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 472 SDDIILSSGYRIGPFEVESALIEHPSIAESAVVSSPDPIRGEVVKAFIVLNPDYKSHDqeQLKKEIQEHVKKTTAPYKYP 551
Cdd:PRK03584 520 SDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDD--ALRARIRTTIRTNLSPRHVP 597
|
570
....*....|..
gi 1039777677 552 RKV----GVPGT 559
Cdd:PRK03584 598 DKIiavpDIPRT 609
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
345-524 |
2.72e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 50.20 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 345 VSAGEPINPEVMEQWRKKTGLDIYEGYGQTETvliCGnfkgmkikPGSMGKPSpafDVKILDENGAtlpPGQEGDIALQV 424
Cdd:PLN02430 389 ISGGAPLSTEIEEFLRVTSCAFVVQGYGLTET---LG--------PTTLGFPD---EMCMLGTVGA---PAVYNELRLEE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 425 LPE---RPFG-------------LFTHYVDNPSKTASTLRGSFYITGDRGYMDEDGYFWFVARSDDII-LSSGYRIGPFE 487
Cdd:PLN02430 452 VPEmgyDPLGepprgeicvrgkcLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQGEYVALEY 531
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039777677 488 VESALIEHPSIAESAVVSspDPIRGEVVkAFIVLNPD 524
Cdd:PLN02430 532 LENVYGQNPIVEDIWVYG--DSFKSMLV-AVVVPNEE 565
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
342-504 |
1.19e-05 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 48.20 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 342 KHCVSA--GEPINPEVMEQWRKKTGL-DIYEGYGQTETVLICGNFKGMKIKPGSMGKPSP---------AFDVKILDENG 409
Cdd:cd05937 201 DHKVRVawGNGLRPDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLirrwkfenqVVLVKMDPETD 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 410 ATL-----------PPGQEGDIaLQVLPERPFGLFTHYVDNPSKTASTL------RGS-FYITGDRGYMDEDGYFWFVAR 471
Cdd:cd05937 281 DPIrdpktgfcvraPVGEPGEM-LGRVPFKNREAFQGYLHNEDATESKLvrdvfrKGDiYFRTGDLLRQDADGRWYFLDR 359
|
170 180 190
....*....|....*....|....*....|...
gi 1039777677 472 SDDIILSSGYRIGPFEVESALIEHPSIAESAVV 504
Cdd:cd05937 360 LGDTFRWKSENVSTTEVADVLGAHPDIAEANVY 392
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
394-542 |
1.40e-05 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 48.08 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 394 GKPSPAFDVKILDENGatlppgqegdialQVLPERPFG--------LFTHYVDNPSKTASTLRGSFYITGDRGYMdEDGY 465
Cdd:PRK09192 388 GKALPGHEIEIRNEAG-------------MPLPERVVGhicvrgpsLMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGY 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 466 FWFVARSDDIILSSGYRIGPFEVESALIEHPSI--AESAVVSSPDPiRGEVVKAFI---VLNPDykshDQEQLKKEIQEH 540
Cdd:PRK09192 454 LYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQE-NGEKIVLLVqcrISDEE----RRGQLIHALAAL 528
|
..
gi 1039777677 541 VK 542
Cdd:PRK09192 529 VR 530
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
172-524 |
1.55e-05 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 47.81 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 172 APAVDAVAAkCENLHSKLIVSQHSREGWGNLKemmkYASDSHTCVDTKHDEMMA---------IYFTSGTTGPPKMIGHT 242
Cdd:cd05921 112 APFARALAA-IFPLGTPLVVSRNAVAGRGAIS----FAELAATPPTAAVDAAFAavgpdtvakFLFTSGSTGLPKAVINT 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 243 HSSFGLGLSVNGRFWLDLIASD-VMWNtsdtgWAksAWSSVFSpwtqGACVF--------AHYL----P---RFESTsiL 306
Cdd:cd05921 187 QRMLCANQAMLEQTYPFFGEEPpVLVD-----WL--PWNHTFG----GNHNFnlvlynggTLYIddgkPmpgGFEET--L 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 307 QTLSKFPITVFCSAPTAYRMLVQ---ND--MSRSYkFNSLKHCVSAGEPINPEVMEQWR----KKTGLDI--YEGYGQTE 375
Cdd:cd05921 254 RNLREISPTVYFNVPAGWEMLVAaleKDeaLRRRF-FKRLKLMFYAGAGLSQDVWDRLQalavATVGERIpmMAGLGATE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 376 TVLICGNFKGMKIKPGSMGKPSPAFDVKIldengatLPPGQEGDIAL---QVLPerpfglftHYVDNPSKTASTL-RGSF 451
Cdd:cd05921 333 TAPTATFTHWPTERSGLIGLPAPGTELKL-------VPSGGKYEVRVkgpNVTP--------GYWRQPELTAQAFdEEGF 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 452 YITGDRGYM----DEDGYFWFVAR-SDDIILSSG--YRIGPFEVEsALIEHPSIAESAVVSSPDpirGEVVKAFIVLNPD 524
Cdd:cd05921 398 YCLGDAAKLadpdDPAKGLVFDGRvAEDFKLASGtwVSVGPLRAR-AVAACAPLVHDAVVAGED---RAEVGALVFPDLL 473
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
220-496 |
5.60e-05 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 45.69 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 220 HDEMMAIYFTSGTTGPPKMIGHTHSSFglglsvngRFWLDLIA----------SDVMWNTSDTGWAKSAWSSVFSPWTQG 289
Cdd:cd05913 77 REKVVRIHASSGTTGKPTVVGYTKNDL--------DVWAELVArcldaagvtpGDRVQNAYGYGLFTGGLGFHYGAERLG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 290 ACVFAhylprfESTSI----LQTLSKFPITVFCSAPTAYRML--VQNDMSRSYKFNSLKHCVSAGEPINPEVMEQWRKKT 363
Cdd:cd05913 149 ALVIP------AGGGNterqLQLIKDFGPTVLCCTPSYALYLaeEAEEEGIDPRELSLKVGIFGAEPWTEEMRKRIERRL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 364 GLDIYEGYGQTE-----TVLICGNFKGMKIKpgsmgkpSPAFDVKILD-ENGATLPPGQEGDIalqvlperpfgLFTHYv 437
Cdd:cd05913 223 GIKAYDIYGLTEiigpgVAFECEEKDGLHIW-------EDHFIPEIIDpETGEPVPPGEVGEL-----------VFTTL- 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039777677 438 dnpSKTASTLRgsFYITGD------------RGYMDEDGyfwFVARSDDIILSSGYRIGPFEVESALIEHP 496
Cdd:cd05913 284 ---TKEAMPLI--RYRTRDitrllpgpcpcgRTHRRIDR---ITGRSDDMLIIRGVNVFPSQIEDVLLKIP 346
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
165-261 |
1.57e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 41.50 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 165 IITDDTLAPAVDAvaakcenlHSKLIVSqhsregWGNLKEMMKYASDSHTC-VDTKHDEMMAIYFTSGTTGPPKMIGHTH 243
Cdd:PTZ00216 221 IIYLDSLPASVDT--------EGCRLVA------WTDVVAKGHSAGSHHPLnIPENNDDLALIMYTSGTTGDPKGVMHTH 286
|
90
....*....|....*....
gi 1039777677 244 SSFGLG-LSVNGRFwLDLI 261
Cdd:PTZ00216 287 GSLTAGiLALEDRL-NDLI 304
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
448-551 |
5.78e-03 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 39.42 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777677 448 RGSFYITGDRGYMDEDGYFWFVARSDDIILSSGYRIGPFEVESALIEHPSIAES------------AVVS--SPDPIRGE 513
Cdd:cd17647 370 RDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSyiVPRFDKPD 449
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1039777677 514 VVKAFIVLNPDYKSHDQ--------EQLKKEIQEHVKKTTAPYKYP 551
Cdd:cd17647 450 DESFAQEDVPKEVSTDPivkgligyRKLIKDIREFLKKRLASYAIP 495
|
|
| |
