|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
45-430 |
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: 531.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 45 VSQNFNFAKDVLDQWSQLEKDGLRGPYPALWKVSAKGEEDKWSFERMTQLSKKAASILSDTCALSHGDRLMIILPPTPEA 124
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 125 YWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSDCPTLKTKLLVSDKSYDGWLDFKKLIQ 204
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 205 VAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLGMGFSQASRRWMDLQPTDVLWSLGDAFGGSLSLSAVLGTWF 284
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 285 QGACVFLCHMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKcFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDI 364
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQD-LSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDI 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217275610 365 YEGYGQTETGLLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIRIKLNQPASLY 430
Cdd:cd05928 320 YEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLF 385
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
86-430 |
1.27e-82 |
|
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: 263.04 E-value: 1.27e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 86 WSFERMTQLSKKAASILSDtCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVAN 165
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 166 EamapvvnsavsdcptlktkllvsdksydgwldfkkliqvappkqtymrtksQDPMAIFFTKGTTGAPKMVEYSqYGLGM 245
Cdd:cd05972 80 A---------------------------------------------------EDPALIYFTSGTTGLPKGVLHT-HSYPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 246 GFSQASRRWMDLQPTDVLWSLGDAFGGSLSLSAVLGTWFQGACVFLCHMPTFCPETVLNVLSRFPITTLSANPEMYQELL 325
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 326 QHKcFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGLLCATSKTIKLKPSSLGKPLPPYIVQIVDEN 405
Cdd:cd05972 188 KQD-LSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDD 266
|
330 340
....*....|....*....|....*
gi 2217275610 406 SNLLPPGEEGNIAIRIKLNQPASLY 430
Cdd:cd05972 267 GRELPPGEEGDIAIKLPPPGLFLGY 291
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
45-430 |
5.47e-77 |
|
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: 251.65 E-value: 5.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 45 VSQNFNFAKDVLDQWSQLEKDGLrgpypALWKVSAKGEEDKWSFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEA 124
Cdd:cd05970 12 VPENFNFAYDVVDAMAKEYPDKL-----ALVWCDDAGEERIFTFAELADYSDKTANFFKAM-GIGKGDTVMLTLKRRYEF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 125 YWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVA-NEAMAP-VVNSAVSDCPTLKTKLLVSDKSYDGWLDFKKL 202
Cdd:cd05970 86 WYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAiAEDNIPeEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 203 IQVAPP----KQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQ-YGLGMGFSqaSRRWMDLQPTDVLWSLGDAFGGSLSLS 277
Cdd:cd05970 166 IKNASPdferPTANSYPCGEDILLVYFSSGTTGMPKMVEHDFtYPLGHIVT--AKYWQNVREGGLHLTVADTGWGKAVWG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 278 AVLGTWFQGACVFLCHMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKcFTSYRFKSLKQCVAAGGPISPGVIEDWK 357
Cdd:cd05970 244 KIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIRED-LSRYDLSSLRYCTTAGEALNPEVFNTFK 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217275610 358 RITKLDIYEGYGQTETGLLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIRIKLNQPASLY 430
Cdd:cd05970 323 EKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVGLF 395
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
49-420 |
5.95e-77 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 252.34 E-value: 5.95e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 49 FNFAKDVLDQWSQLEKDGlrgpyPALWKVSAKGEEDKWSFERMTQLSKKAASILSDtCALSHGDRLMIILPPTPEAYWIC 128
Cdd:COG0365 8 LNIAYNCLDRHAEGRGDK-----VALIWEGEDGEERTLTYAELRREVNRFANALRA-LGVKKGDRVAIYLPNIPEAVIAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 129 LACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEA---------MAPVVNSAVSDCPTLKTKLLV----SDKSYDG 195
Cdd:COG0365 82 LACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGglrggkvidLKEKVDEALEELPSLEHVIVVgrtgADVPMEG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 196 WLDFKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLGMGFSQASRRWMDLQPTDVLWSLGD---AFGG 272
Cdd:COG0365 162 DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADigwATGH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 273 SlslSAVLGTWFQGACVFLCH-MPTFC-PETVLNVLSRFPITTLSANPEMYQELLQH--KCFTSYRFKSLKQCVAAGGPI 348
Cdd:COG0365 242 S---YIVYGPLLNGATVVLYEgRPDFPdPGRLWELIEKYGVTVFFTAPTAIRALMKAgdEPLKKYDLSSLRLLGSAGEPL 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217275610 349 SPGVIEDWKRITKLDIYEGYGQTETG-LLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:COG0365 319 NPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK 391
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
82-420 |
1.49e-54 |
|
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: 190.02 E-value: 1.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 82 EEDKWSFERMTQLSKKAASILSDtCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQC 161
Cdd:COG0318 21 GGRRLTYAELDARARRLAAALRA-LGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 162 IVAneamapvvnsavsdcptlktkllvsdksydgwldfkkliqvappkqtymrtksqdpMAIFFTKGTTGAPKMVEYSQY 241
Cdd:COG0318 100 LVT--------------------------------------------------------ALILYTSGTTGRPKGVMLTHR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 242 GLgMGFSQASRRWMDLQPTDV-LWSLGDAFGGSLSLsAVLGTWFQGACVFLchMPTFCPETVLNVLSRFPITTLSANPEM 320
Cdd:COG0318 124 NL-LANAAAIAAALGLTPGDVvLVALPLFHVFGLTV-GLLAPLLAGATLVL--LPRFDPERVLELIERERVTVLFGVPTM 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 321 YQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGLLCATS--KTIKLKPSSLGKPLPPYI 398
Cdd:COG0318 200 LARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNpeDPGERRPGSVGRPLPGVE 279
|
330 340
....*....|....*....|..
gi 2217275610 399 VQIVDENSNLLPPGEEGNIAIR 420
Cdd:COG0318 280 VRIVDEDGRELPPGEVGEIVVR 301
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
68-420 |
6.30e-50 |
|
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: 177.76 E-value: 6.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 68 RGPYPALWkvsakGEEDKWSFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEaYWICL-ACVRLGITFVPGSPQLT 146
Cdd:cd05936 12 FPDKTALI-----FMGRKLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQ-FPIAYfGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 147 AKKIRYQLRMSKAQCIVANEAmapvvnsavsdcptlktkllvsdksydgwldFKKLIQVAPPKQTYMRTKSQDPMAIFFT 226
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVS-------------------------------FTDLLAAGAPLGERVALTPEDVAVLQYT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 227 KGTTGAPKMVEYSQYGLGMGFSQAsRRWM--DLQPTDVLwsLG-----DAFGgsLSLSAVLGtWFQGACVFLchMPTFCP 299
Cdd:cd05936 134 SGTTGVPKGAMLTHRNLVANALQI-KAWLedLLEGDDVV--LAalplfHVFG--LTVALLLP-LALGATIVL--IPRFRP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 300 ETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETG-LLCA 378
Cdd:cd05936 206 IGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAV 285
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2217275610 379 TSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:cd05936 286 NPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVR 327
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
81-420 |
3.88e-49 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 174.42 E-value: 3.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 81 GEEDKWSFERMTQLSKKAASILSDtCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQ 160
Cdd:pfam00501 17 GEGRRLTYRELDERANRLAAGLRA-LGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 161 CIVANEAM-APVVNSAVSDCPTLKTKLLVS-DKSYDGWLDFKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEY 238
Cdd:pfam00501 96 VLITDDALkLEELLEALGKLEVVKLVLVLDrDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVML 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 239 SQYGL---GMGFSQASRRWMDLQPTDVLWSLGD-AFGGSLSLsAVLGTWFQGA-CVFLCHMPTFCPETVLNVLSRFPITT 313
Cdd:pfam00501 176 THRNLvanVLSIKRVRPRGFGLGPDDRVLSTLPlFHDFGLSL-GLLGPLLAGAtVVLPPGFPALDPAALLELIERYKVTV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 314 LSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGLLCATS---KTIKLKPSSL 390
Cdd:pfam00501 255 LYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPlplDEDLRSLGSV 334
|
330 340 350
....*....|....*....|....*....|.
gi 2217275610 391 GKPLPPYIVQIVDENS-NLLPPGEEGNIAIR 420
Cdd:pfam00501 335 GRPLPGTEVKIVDDETgEPVPPGEPGELCVR 365
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
87-429 |
6.98e-47 |
|
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: 168.90 E-value: 6.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 87 SFERMTQLSKKAASILSdTCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANE 166
Cdd:cd05974 2 SFAEMSARSSRVANFLR-SIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 167 AmapvvnsavsdcptlktkllvsdksydgwldfkkliqvappkqtymrTKSQDPMAIFFTKGTTGAPKMVEYSQYGLGMG 246
Cdd:cd05974 81 N-----------------------------------------------THADDPMLLYFTSGTTSKPKLVEHTHRSYPVG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 247 fSQASRRWMDLQPTDVLWSLGDAFGGSLSLSAVLGTWFQGACVFLCHMPTFCPETVLNVLSRFPITTLSANPEMYQELLQ 326
Cdd:cd05974 114 -HLSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 327 HKcFTSYRFKsLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGLLCATSKTIKLKPSSLGKPLPPYIVQIVDENS 406
Cdd:cd05974 193 QD-LASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDG 270
|
330 340
....*....|....*....|...
gi 2217275610 407 NllpPGEEGNIAIRIKLNQPASL 429
Cdd:cd05974 271 A---PATEGEVALDLGDTRPVGL 290
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
219-420 |
8.60e-42 |
|
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: 152.44 E-value: 8.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 219 DPMAIFFTKGTTGAPKMVEYSQYGLgMGFSQASRRWMDLQPTDVLWSLGDAFGGSLsLSAVLGTWFQGACVFLchMPTFC 298
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHIGG-LFGLLGALLAGGTVVL--LPKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 299 PETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGLLCA 378
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217275610 379 TSK--TIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:cd04433 157 TGPpdDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVR 200
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
82-420 |
1.30e-37 |
|
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: 144.28 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 82 EEDKWSFERMTQLSKKAASILsDTCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQC 161
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGL-RKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 162 IVANEAMAPVVNSAVSDCPTlKTKLLVSDKSYDGWLDFKKLIQVAPPKQTYMR-----TKSQDPMAIFFTKGTTGAPKMV 236
Cdd:cd05911 86 IFTDPDGLEKVKEAAKELGP-KDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLppplkDGKDDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 237 EYSQYGLGMGFSQASRRW-MDLQPTDVLWS---LGDAFGgslsLSAVLGTWFQGACVFLchMPTFCPETVLNVLSRFPIT 312
Cdd:cd05911 165 CLSHRNLIANLSQVQTFLyGNDGSNDVILGflpLYHIYG----LFTTLASLLNGATVII--MPKFDSELFLDLIEKYKIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 313 TLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDW-KRITKLDIYEGYGQTETGLLCATSKTIKLKPSSLG 391
Cdd:cd05911 239 FLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLaKRFPNATIKQGYGMTETGGILTVNPDGDDKPGSVG 318
|
330 340 350
....*....|....*....|....*....|
gi 2217275610 392 KPLPPYIVQIVDENSN-LLPPGEEGNIAIR 420
Cdd:cd05911 319 RLLPNVEAKIVDDDGKdSLGPNEPGEICVR 348
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
65-420 |
3.18e-36 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 141.57 E-value: 3.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 65 DGLRGPYPALWKVSAKGEEDkWSFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQ 144
Cdd:PRK04319 54 DGGRKDKVALRYLDASRKEK-YTYKELKELSNKFANVLKEL-GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 145 LTAKKIRYQLRMSKAQCIVANEAMAPVVnsAVSDCPTLKTKLLVSD--KSYDGWLDFKKLIQVAPPKQTYMRTKSQDPMA 222
Cdd:PRK04319 132 FMEEAVRDRLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEdvEEGPGTLDFNALMEQASDEFDIEWTDREDGAI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 223 IFFTKGTTGAPKMVEYSQYGLGMGFsqASRRW-MDLQPTDVLWSLGD-------AFGgslslsaVLGTWFQGAcvflchm 294
Cdd:PRK04319 210 LHYTSGSTGKPKGVLHVHNAMLQHY--QTGKYvLDLHEDDVYWCTADpgwvtgtSYG-------IFAPWLNGA------- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 295 pT-------FCPETVLNVLSRFPITT-----------LSANPEMyqellqhkcFTSYRFKSLKQCVAAGGPISPGVIEdW 356
Cdd:PRK04319 274 -TnvidggrFSPERWYRILEDYKVTVwytaptairmlMGAGDDL---------VKKYDLSSLRHILSVGEPLNPEVVR-W 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217275610 357 -KRITKLDIYEGYGQTETG-LLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK04319 343 gMKVFGLPIHDNWWMTETGgIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIK 408
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
86-420 |
3.07e-34 |
|
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: 134.17 E-value: 3.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 86 WSFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVAN 165
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSL-GVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 166 EAMapvvnsavsdcptlktkllvsdksydgwldfkkliqvappkqtYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGlgM 245
Cdd:cd05969 80 EEL-------------------------------------------YERTDPEDPTLLHYTSGTTGTPKGVLHVHDA--M 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 246 GFSQASRRW-MDLQPTDVLWSLGDAFGGSLSLSAVLGTWFQGACVFLcHMPTFCPETVLNVLSRFPITTLSANPEMYQEL 324
Cdd:cd05969 115 IFYYFTGKYvLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVV-YEGRFDAESWYGIIERVKVTVWYTAPTAIRML 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 325 LQH--KCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETG-LLCATSKTIKLKPSSLGKPLPPYIVQI 401
Cdd:cd05969 194 MKEgdELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGsIMIANYPCMPIKPGSMGKPLPGVKAAV 273
|
330
....*....|....*....
gi 2217275610 402 VDENSNLLPPGEEGNIAIR 420
Cdd:cd05969 274 VDENGNELPPGTKGILALK 292
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
49-420 |
6.19e-34 |
|
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: 134.42 E-value: 6.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 49 FNFAKDVLDQwsqleKDGLRGPYPALWkvsakGEEDKWSFERMTQLSKKAASILSdTCALSHGDRLMIILPPTPEAYWIC 128
Cdd:cd05959 3 YNAATLVDLN-----LNEGRGDKTAFI-----DDAGSLTYAELEAEARRVAGALR-ALGVKREERVLLIMLDTVDFPTAF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 129 LACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSDCPTLKTKLLVSD--KSYDGWLDFKKLIQVA 206
Cdd:cd05959 72 LGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGgaGPEAGALLLAELVAAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 207 PPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLGMGFSQASRRWMDLQPTDVLWS---LGDAFGgsLSLSAVLGTW 283
Cdd:cd05959 152 AEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSaakLFFAYG--LGNSLTFPLS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 284 FQGACVFLCHMPTfcPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLD 363
Cdd:cd05959 230 VGATTVLMPERPT--PAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLD 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217275610 364 IYEGYGQTETGLLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:cd05959 308 ILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVR 364
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
87-421 |
4.00e-32 |
|
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: 128.02 E-value: 4.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 87 SFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANE 166
Cdd:cd05973 2 TFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 167 AMapvvnsavsdcptlKTKLlvsdksydgwldfkkliqvappkqtymrtkSQDPMAIFFTKGTTGAPKMVEYSQYGLgMG 246
Cdd:cd05973 81 AN--------------RHKL------------------------------DSDPFVMMFTSGTTGLPKGVPVPLRAL-AA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 247 FSQASRRWMDLQPTDVLWSLGD---AFGgslSLSAVLGTWFQGACVFLCHMPtFCPETVLNVLSRFPITTLSANPEMYQE 323
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWNAADpgwAYG---LYYAITGPLALGHPTILLEGG-FSVESTWRVIERLGVTNLAGSPTAYRL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 324 LLQHKCFTSYRFK-SLKQCVAAGGPISPGVIeDWKRIT-KLDIYEGYGQTETGLLCATSKTIK--LKPSSLGKPLPPYIV 399
Cdd:cd05973 192 LMAAGAEVPARPKgRLRRVSSAGEPLTPEVI-RWFDAAlGVPIHDHYGQTELGMVLANHHALEhpVHAGSAGRAMPGWRV 270
|
330 340
....*....|....*....|..
gi 2217275610 400 QIVDENSNLLPPGEEGNIAIRI 421
Cdd:cd05973 271 AVLDDDGDELGPGEPGRLAIDI 292
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
86-420 |
1.18e-31 |
|
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: 126.57 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 86 WSFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAqcivan 165
Cdd:cd17631 21 LTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGA------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 166 eamapvvnsavsdcptlktKLLVSDksydgwldfkkliqvappkqtymrtksqdPMAIFFTKGTTGAPKMVEYSQYGL-G 244
Cdd:cd17631 94 -------------------KVLFDD-----------------------------LALLMYTSGTTGRPKGAMLTHRNLlW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 245 MGFSQASRRwmDLQPTDVLWSLGDAFGGSLSLSAVLGTWFQGACVFLchMPTFCPETVLNVLSRFPITTLSANPEMYQEL 324
Cdd:cd17631 126 NAVNALAAL--DLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVI--LRKFDPETVLDLIERHRVTSFFLVPTMIQAL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 325 LQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRItKLDIYEGYGQTETG-LLCATSKTIKL-KPSSLGKPLPPYIVQIV 402
Cdd:cd17631 202 LQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSpGVTFLSPEDHRrKLGSAGRPVFFVEVRIV 280
|
330
....*....|....*...
gi 2217275610 403 DENSNLLPPGEEGNIAIR 420
Cdd:cd17631 281 DPDGREVPPGEVGEIVVR 298
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
82-420 |
1.09e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 125.30 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 82 EEDKWSFERMTQLSKKAASILSDtCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQC 161
Cdd:PRK06187 28 DGRRTTYAELDERVNRLANALRA-LGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 162 IVANEAMAPVVNSAVSDCPTLKTKLLVSDKSYDG----WLDFKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVE 237
Cdd:PRK06187 107 VLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 238 YSQYGLGMGfSQASRRWMDLQPTDVlwslgdafggslSLSAV----LGTWfqGacvfLCHMPT-----------FCPETV 302
Cdd:PRK06187 187 LSHRNLFLH-SLAVCAWLKLSRDDV------------YLVIVpmfhVHAW--G----LPYLALmagakqviprrFDPENL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 303 LNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETG-LLCA--- 378
Cdd:PRK06187 248 LDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVlpp 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2217275610 379 ---TSKTIKlKPSSLGKPLPPYIVQIVDENSNLLPP--GEEGNIAIR 420
Cdd:PRK06187 328 edqLPGQWT-KRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVR 373
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
111-420 |
2.43e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 123.86 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 111 GDRLMIILPPTPEayWI--CLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSDCPTLKTKLLV 188
Cdd:PRK07656 55 GDRVAIWAPNSPH--WViaALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVIC 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 189 ----SDKSYDGWLDFKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLgmgFSqASRRW---MDLQPTD 261
Cdd:PRK07656 133 eteeDDPHTEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQL---LS-NAADWaeyLGLTEGD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 262 -VLWSLG--DAFGGSLSLSAVLGTwfqGACVFLchMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSL 338
Cdd:PRK07656 209 rYLAANPffHVFGYKAGVNAPLMR---GATILP--LPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 339 KQCVAAGGPISPGVIEDWKRitKLDIY---EGYGQTE---TGLLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPG 412
Cdd:PRK07656 284 RLAVTGAASMPVALLERFES--ELGVDivlTGYGLSEasgVTTFNRLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVG 361
|
....*...
gi 2217275610 413 EEGNIAIR 420
Cdd:PRK07656 362 EVGELLVR 369
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
108-420 |
6.72e-30 |
|
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: 121.80 E-value: 6.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 108 LSHGDRLMIILPPTPEayWIC--LACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAmapvvnsavsdcptlktk 185
Cdd:cd05919 32 VSSGDRVLLLMLDSPE--LVQlfLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSAD------------------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 186 llvsDKSYdgWLdfkkliqvappkqtymrtksqdpmaifFTKGTTGAPKMVEYSQYGLgMGFSQA-SRRWMDLQPTDVLW 264
Cdd:cd05919 92 ----DIAY--LL---------------------------YSSGTTGPPKGVMHAHRDP-LLFADAmAREALGLTPGDRVF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 265 SLGDAF-----GGSLslsavLGTWFQGACVFLchMPTF-CPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSL 338
Cdd:cd05919 138 SSAKMFfgyglGNSL-----WFPLAVGASAVL--NPGWpTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 339 KQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGLLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIA 418
Cdd:cd05919 211 RLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLL 290
|
..
gi 2217275610 419 IR 420
Cdd:cd05919 291 VR 292
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
86-419 |
1.17e-29 |
|
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: 122.69 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 86 WSFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVAN 165
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDL-GVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 166 EA---------MAPVVNSAVSDCPTLKTKLLVSDKS---YDG----WLDFKKLIQVAPPKQTYMRTKSQDPMAIFFTKGT 229
Cdd:cd17634 164 DGgvragrsvpLKKNVDDALNPNVTSVEHVIVLKRTgsdIDWqegrDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 230 TGAPKMVEYSQYGLGMGFSQASRRWMDLQPTDVLWSLGD---AFGGSLslsAVLGTWFQGACVFLCH----MPTfcPETV 302
Cdd:cd17634 244 TGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADvgwVTGHSY---LLYGPLACGATTLLYEgvpnWPT--PARM 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 303 LNVLSRFPITTLSANPEMYQELLQH--KCFTSYRFKSLKQCVAAGGPISPgviEDWKRITKLDIYEG------YGQTETG 374
Cdd:cd17634 319 WQVVDKHGVNILYTAPTAIRALMAAgdDAIEGTDRSSLRILGSVGEPINP---EAYEWYWKKIGKEKcpvvdtWWQTETG 395
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2217275610 375 LLCATSKTIK--LKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAI 419
Cdd:cd17634 396 GFMITPLPGAieLKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVI 442
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
80-420 |
1.13e-28 |
|
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: 118.30 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 80 KGEEDKWSFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKA 159
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 160 QCIVANEamapvvnsavsdcptlktkllvsdksydgwldfkkliqvappkqtymrtkSQDPMAIFFTKGTTGAPKMVEYS 239
Cdd:cd05971 80 SALVTDG--------------------------------------------------SDDPALIIYTSGTTGPPKGALHA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 240 QY-------GLGMGFSQASRrwmdlqPTDVLWSLGD-AFGGSLsLSAVLGTWFQGACVFLCHMPTFCPETVLNVLSRFPI 311
Cdd:cd05971 110 HRvllghlpGVQFPFNLFPR------DGDLYWTPADwAWIGGL-LDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 312 TTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISpGVIEDWKRIT-KLDIYEGYGQTETGLLCATSKTI-KLKPSS 389
Cdd:cd05971 183 TTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLG-EELLGWAREQfGVEVNEFYGQTECNLVIGNCSALfPIKPGS 261
|
330 340 350
....*....|....*....|....*....|.
gi 2217275610 390 LGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:cd05971 262 MGKPIPGHRVAIVDDNGTPLPPGEVGEIAVE 292
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
89-420 |
4.36e-28 |
|
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: 115.83 E-value: 4.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 89 ERMTQLskkaASILSDTCALSHGDRLMIILPPTPEAY-WIcLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEA 167
Cdd:TIGR01733 7 ERANRL----ARHLRAAGGVGPGDRVAVLLERSAELVvAI-LAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 168 MAPVVnsavsDCPTLKTKLLVSDksydgwlDFKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLGMGF 247
Cdd:TIGR01733 82 LASRL-----AGLVLPVILLDPL-------ELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 248 SQASRRWmDLQPTDVlWSLGDAFGGSLSLSAVLGTWFQGACVFLC--HMPTFCPETVLNVLSRFPITTLSANPEMYQELL 325
Cdd:TIGR01733 150 AWLARRY-GLDPDDR-VLQFASLSFDASVEEIFGALLAGATLVVPpeDEERDDAALLAALIAEHPVTVLNLTPSLLALLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 326 QHKCFtsyRFKSLKQCVAAGGPISPGVIEDWK-RITKLDIYEGYGQTE-----TGLLCATSKTIKLKPSSLGKPLPPYIV 399
Cdd:TIGR01733 228 AALPP---ALASLRLVILGGEALTPALVDRWRaRGPGARLINLYGPTEttvwsTATLVDPDDAPRESPVPIGRPLANTRL 304
|
330 340
....*....|....*....|.
gi 2217275610 400 QIVDENSNLLPPGEEGNIAIR 420
Cdd:TIGR01733 305 YVLDDDLRPVPVGVVGELYIG 325
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
108-417 |
3.70e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 114.62 E-value: 3.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 108 LSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSDCPTLKTKLL 187
Cdd:PRK08276 33 LREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSAALADTAAELAAELPAGVPLLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 188 VSDKSYDGWLDFKKLIQVAPPKQTYMRTKSQDpMAifFTKGTTGAPKMVEYSQYGLGmgfsqasrrwMDLQPTDVLWSLG 267
Cdd:PRK08276 113 VVAGPVPGFRSYEEALAAQPDTPIADETAGAD-ML--YSSGTTGRPKGIKRPLPGLD----------PDEAPGMMLALLG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 268 ---DAFGGSLSLS-------AVLGtwFQGACVFLCH----MPTFCPETVLNVLSRFPITTLSANPEMYQELLQ--HKCFT 331
Cdd:PRK08276 180 fgmYGGPDSVYLSpaplyhtAPLR--FGMSALALGGtvvvMEKFDAEEALALIERYRVTHSQLVPTMFVRMLKlpEEVRA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 332 SYRFKSLKQCVAAGGPISPGV----IEDWKRItkldIYEGYGQTETGLLC-ATSKTIKLKPSSLGKPLPPyIVQIVDENS 406
Cdd:PRK08276 258 RYDVSSLRVAIHAAAPCPVEVkramIDWWGPI----IHEYYASSEGGGVTvITSEDWLAHPGSVGKAVLG-EVRILDEDG 332
|
330
....*....|.
gi 2217275610 407 NLLPPGEEGNI 417
Cdd:PRK08276 333 NELPPGEIGTV 343
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
86-420 |
1.56e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 106.94 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 86 WSFERMTQLSKKAASILSDTcALSHGDRLmIILPPTPEAYWIC-LACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVA 164
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDL-GLKKGDRV-AALGHNSDAYALLwLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 165 NEAMAPVVNSAVSDCPTLKTKLLVS---DKSYDGWLDFKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQY 241
Cdd:PRK08316 115 DPALAPTAEAALALLPVDTLILSLVlggREAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 242 GLgMGFSQASRRWMDLQPTDV-LWSLG-------DAFggslslsavLGTWFQ-GACVFLCHMPTfcPETVLNVLSRFPIT 312
Cdd:PRK08316 195 AL-IAEYVSCIVAGDMSADDIpLHALPlyhcaqlDVF---------LGPYLYvGATNVILDAPD--PELILRTIEAERIT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 313 TLSANPEMYQELLQHKCFTSYRFKSLKQCVaAGGPISPG-VIEDWK-RITKLDIYEGYGQTETGLLcATS---KTIKLKP 387
Cdd:PRK08316 263 SFFAPPTVWISLLRHPDFDTRDLSSLRKGY-YGASIMPVeVLKELReRLPGLRFYNCYGQTEIAPL-ATVlgpEEHLRRP 340
|
330 340 350
....*....|....*....|....*....|...
gi 2217275610 388 SSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK08316 341 GSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHR 373
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
83-420 |
2.69e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 101.98 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 83 EDKWSFERMTQLSKKAASILSDtCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCI 162
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAA-LGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 163 VAneamapvvnsavsdcptlktkllvsdksydgwldfkkliqvappkqtymrtksqDPMAIFFTKGTTGAPKMVEYSQYG 242
Cdd:cd05934 80 VV------------------------------------------------------DPASILYTSGTTGPPKGVVITHAN 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 243 LGMgFSQASRRWMDLQPTDVLWSLGDAFGGSLSLSAVLGTWFQGACVFLchMPTFCPE-----------TVLNVLSrFPI 311
Cdd:cd05934 106 LTF-AGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVL--LPRFSASrfwsdvrrygaTVTNYLG-AML 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 312 TTLSANPEMYQELlQHKcftsYRfkslkqcVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGLLCATSKTIKLKPSSLG 391
Cdd:cd05934 182 SYLLAQPPSPDDR-AHR----LR-------AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIG 249
|
330 340
....*....|....*....|....*....
gi 2217275610 392 KPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:cd05934 250 RPAPGYEVRIVDDDGQELPAGEPGELVIR 278
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
83-420 |
3.87e-23 |
|
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: 101.79 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 83 EDKWSFERMTQLSKKAASILSDTCALSHGDRLMIILPPTPE--AYWicLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQ 160
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPElvACW--FGIQKAGAIAVATMPLLRPKELAYILDKARIT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 161 CIVANEAMapvvnsavsdcptlktkllvsdksydgwldfkkliqvappkqtymrTKSQDPMAIFFTKGTTGAPKMVEYSQ 240
Cdd:cd05958 86 VALCAHAL----------------------------------------------TASDDICILAFTSGTTGAPKATMHFH 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 241 YGLGMGFSQASRRWMDLQPTDVLWSLGD-AFGGSLSLSAVLgTWFQGACVFLchMPTFCPETVLNVLSRFPITTLSANPE 319
Cdd:cd05958 120 RDPLASADRYAVNVLRLREDDRFVGSPPlAFTFGLGGVLLF-PFGVGASGVL--LEEATPDLLLSAIARYKPTVLFTAPT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 320 MYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGLLCATSKTIKLKPSSLGKPLPPYIV 399
Cdd:cd05958 197 AYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEA 276
|
330 340
....*....|....*....|.
gi 2217275610 400 QIVDENSNLLPPGEEGNIAIR 420
Cdd:cd05958 277 KVVDDEGNPVPDGTIGRLAVR 297
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
87-420 |
4.62e-23 |
|
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: 102.31 E-value: 4.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 87 SFERMTQLSKKAASILSdTCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANE 166
Cdd:cd05904 34 TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 167 AMAPVVNSAVSdcptlktKLLVSDKSYDGWLDFKKLIQVAPPKQT-YMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLgM 245
Cdd:cd05904 113 ELAEKLASLAL-------PVVLLDSAEFDSLSFSDLLFEADEAEPpVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNL-I 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 246 GFSQASRRWMDLQPtdvlwSLGDAFGGSLSLSAVLG-TWF------QGACVFLchMPTFCPETVLNVLSRFPITTLSANP 318
Cdd:cd05904 185 AMVAQFVAGEGSNS-----DSEDVFLCVLPMFHIYGlSSFalgllrLGATVVV--MPRFDLEELLAAIERYKVTHLPVVP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 319 EMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWK-RITKLDIYEGYGQTETG---LLCATSKTIKLKPSSLGKPL 394
Cdd:cd05904 258 PIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRaKFPNVDLGQGYGMTESTgvvAMCFAPEKDRAKYGSVGRLV 337
|
330 340
....*....|....*....|....*..
gi 2217275610 395 PPYIVQIVDENSNL-LPPGEEGNIAIR 420
Cdd:cd05904 338 PNVEAKIVDPETGEsLPPNQTGELWIR 364
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
76-419 |
4.68e-22 |
|
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: 98.75 E-value: 4.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 76 KVSAKGEEDKWSFERMTQLSKKAASILSDTCAlSHGDRLMIILPPTPEAYwIC-LACVRLGITFVPGSPQLTAKKIRYQL 154
Cdd:cd05930 3 AVAVVDGDQSLTYAELDARANRLARYLRERGV-GPGDLVAVLLERSLEMV-VAiLAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 155 RMSKAQCIVaneamapvvnsavsdcptlktkllvsdksydgwldfkkliqvappkqtymrTKSQDPMAIFFTKGTTGAPK 234
Cdd:cd05930 81 EDSGAKLVL---------------------------------------------------TDPDDLAYVIYTSGSTGKPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 235 --MVEYSqyGLgMGFSQASRRWMDLQPTD-VLWSLGDAFggSLSLSAVLGTWFQGACVFLC-HMPTFCPETVLNVLSRFP 310
Cdd:cd05930 110 gvMVEHR--GL-VNLLLWMQEAYPLTPGDrVLQFTSFSF--DVSVWEIFGALLAGATLVVLpEEVRKDPEALADLLAEEG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 311 ITTLSANPEMYQELLQHKCFTsyRFKSLKQCVAAGGPISPGVIEDWKRI-TKLDIYEGYGQTETGLlCATSKTIKLK--- 386
Cdd:cd05930 185 ITVLHLTPSLLRLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATV-DATYYRVPPDdee 261
|
330 340 350
....*....|....*....|....*....|....*
gi 2217275610 387 --PSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAI 419
Cdd:cd05930 262 dgRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYI 296
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
108-420 |
2.30e-21 |
|
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: 96.74 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 108 LSHGDRLMIILPPTPEAYW----ICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSDCPTLK 183
Cdd:cd05922 15 GVRGERVVLILPNRFTYIElsfaVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPDPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 184 TKLLVsdksyDGWLDFKKLIQVAPPKQtymrtksQDPMAIFFTKGTTGAPKMVEYSQYGLgMGFSQASRRWMDLQPTDVL 263
Cdd:cd05922 95 TVLDA-----DGIRAARASAPAHEVSH-------EDLALLLYTSGSTGSPKLVRLSHQNL-LANARSIAEYLGITADDRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 264 WS---LGDAFGGSLSLSAVLgtwfQGACVFLcHMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKcFTSYRFKSLKQ 340
Cdd:cd05922 162 LTvlpLSYDYGLSVLNTHLL----RGATLVL-TNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLG-FDPAKLPSLRY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 341 CVAAGGPISPGVIedwKRITKL----DIYEGYGQTETGLLCAT--SKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEE 414
Cdd:cd05922 236 LTQAGGRLPQETI---ARLRELlpgaQVYVMYGQTEATRRMTYlpPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEP 312
|
....*.
gi 2217275610 415 GNIAIR 420
Cdd:cd05922 313 GEIVHR 318
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
102-420 |
3.11e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 97.03 E-value: 3.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 102 LSDTCA---LSHG----DRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNS 174
Cdd:PRK06178 67 LSDRFAallRQRGvgagDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 175 AVSDC-----------------PTLKTKLLVSDKSY--DGWLDFKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKM 235
Cdd:PRK06178 147 VRAETslrhvivtsladvlpaePTLPLPDSLRAPRLaaAGAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 236 VEYSQYglGMGFSQASRRWMDLQ--PTDVL-------WSLGDAFGgslslsaVLGTWFQGACVFLchMPTFCPETVLNVL 306
Cdd:PRK06178 227 CEHTQR--DMVYTAAAAYAVAVVggEDSVFlsflpefWIAGENFG-------LLFPLFSGATLVL--LARWDAVAFMAAV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 307 SRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQ--CVAAGGPISPGVIEDWKRITKLDIYEG-YGQTETgllcATSKTI 383
Cdd:PRK06178 296 ERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQvrVVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTET----HTCDTF 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2217275610 384 KL-----------KPSSLGKPLPPYIVQIVD-ENSNLLPPGEEGNIAIR 420
Cdd:PRK06178 372 TAgfqdddfdllsQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVR 420
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
111-420 |
6.99e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 96.00 E-value: 6.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 111 GDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSDCPTLKTKLLVSD 190
Cdd:PRK07786 67 GDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 191 KSYDGWLDFKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLgMGFSQASRRWMDLQPTDVLWSLGDAF 270
Cdd:PRK07786 147 SSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANL-TGQAMTCLRTNGADINSDVGFVGVPL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 271 GGSLSLSAVLGTWFQGACVFLCHMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKcftSYRFKSLKQCVAAGG--PI 348
Cdd:PRK07786 226 FHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQ---QARPRDLALRVLSWGaaPA 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217275610 349 SPGVIED-WKRITKLDIYEGYGQTE----TGLLCATSKTIKLkpSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK07786 303 SDTLLRQmAATFPEAQILAAFGQTEmspvTCMLLGEDAIRKL--GSVGKVIPTVAARVVDENMNDVPVGEVGEIVYR 377
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
68-423 |
8.28e-21 |
|
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: 95.85 E-value: 8.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 68 RGPYPALWKVSA-KGEEDKWSFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEAYWICLACVRLGIT--FVPG--- 141
Cdd:cd05967 64 RGDQIALIYDSPvTGTERTYTYAELLDEVSRLAGVLRKL-GVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsVVFGgfa 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 142 SPQLTAkkiryqlRMSKAQ---CIVANEAM--------APVVNSAVSDCPTLKTKLLVSDKS--------YDGWLDFKKL 202
Cdd:cd05967 143 AKELAS-------RIDDAKpklIVTASCGIepgkvvpyKPLLDKALELSGHKPHHVLVLNRPqvpadltkPGRDLDWSEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 203 IQVAPPKQtYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLGMGFSQASRRWMDLQPTDVLWSLGD---AFGGSLSlsaV 279
Cdd:cd05967 216 LAKAEPVD-CVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDvgwVVGHSYI---V 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 280 LGTWFQGA-CVFLCHMPTFCPE--TVLNVLSRFPITTLSANPE----MYQELLQHKCFTSYRFKSLKQCVAAGGPISPGV 352
Cdd:cd05967 292 YGPLLHGAtTVLYEGKPVGTPDpgAFWRVIEKYQVNALFTAPTairaIRKEDPDGKYIKKYDLSSLRTLFLAGERLDPPT 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217275610 353 IEDWKRITKLDIYEGYGQTETGLLCATS----KTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIRIKL 423
Cdd:cd05967 372 LEWAENTLGVPVIDHWWQTETGWPITANpvglEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPL 446
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
50-420 |
1.36e-20 |
|
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: 95.25 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 50 NFAKDVLDQWSqlekdGLRGPYPALWKVSAKGEEDKWSFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEAYWICL 129
Cdd:cd05968 61 NIVEQLLDKWL-----ADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRAL-GVGKGDRVGIYLPMIPEIVPAFL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 130 ACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEA---------MAPVVNSAVSDCPTLKTKLLVSD-KSYDGWLDF 199
Cdd:cd05968 135 AVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGftrrgrevnLKEEADKACAQCPTVEKVVVVRHlGNDFTPAKG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 200 KKL---IQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLGMGFSQASRRWMDLQPTDVLWSLGDaFGGSLSL 276
Cdd:cd05968 215 RDLsydEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTD-LGWMMGP 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 277 SAVLGTWFQGACVFLCH-MPTF-CPETVLNVLSRFPITTLSANPEMYQELLQHKCfTSYRFKSLKQCVAAGGPISPGVIE 354
Cdd:cd05968 294 WLIFGGLILGATMVLYDgAPDHpKADRLWRMVEDHEITHLGLSPTLIRALKPRGD-APVNAHDLSSLRVLGSTGEPWNPE 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217275610 355 DWK------RITKLDIYEGYGQTET--GLLCATskTIK-LKPSSLGKPLPPYIVQIVDENSNLLPPgEEGNIAIR 420
Cdd:cd05968 373 PWNwlfetvGKGRNPIINYSGGTEIsgGILGNV--LIKpIKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLL 444
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
68-420 |
2.71e-20 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 94.17 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 68 RGPYPALWKVSAKGEEDkwsfermtQLSKKAASILSDTCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTA 147
Cdd:PRK08751 41 RPAYHSFGKTITYREAD--------QLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 148 KKIRYQLRMSKAQCIVANEAMAPVVNSAVSDCPTLKT------------------------KLLVSDKSYDGWLDFKKLI 203
Cdd:PRK08751 113 RELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVittglgdmlgfpkaalvnfvvkyvKKLVPEYRINGAIRFREAL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 204 QVAppKQTYMRTKSQDPMAIFF---TKGTTGAPKMVEYSQYGLGMGFSQASrRWmdLQPTDVLWSLGDAFGGSLSLSAVL 280
Cdd:PRK08751 193 ALG--RKHSMPTLQIEPDDIAFlqyTGGTTGVAKGAMLTHRNLVANMQQAH-QW--LAGTGKLEEGCEVVITALPLYHIF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 281 -----GTWFQ--GACVFLC----HMPTFCPEtvlnvLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPIS 349
Cdd:PRK08751 268 altanGLVFMkiGGCNHLIsnprDMPGFVKE-----LKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQ 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217275610 350 PGVIEDWKRITKLDIYEGYGQTETG-LLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK08751 343 RSVAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK 414
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
83-420 |
2.76e-20 |
|
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: 93.51 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 83 EDKWSFERMTQLSKKAASILSDTCALSHGDRLMIILPPTPE---AYWiclACVRLGITFVPGSPQLTAKKIRYQLRmska 159
Cdd:cd05941 9 GDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEyvvAQL---AIWRAGGVAVPLNPSYPLAELEYVIT---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 160 qcivaneamapvvNSAVSdcptlktkLLVsdksydgwldfkkliqvappkqtymrtksqDPMAIFFTKGTTGAPKMVEYS 239
Cdd:cd05941 82 -------------DSEPS--------LVL------------------------------DPALILYTSGTTGRPKGVVLT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 240 QYGLGmgfSQAsrrwmdlqptDVL-----WSLGDAFGGSLSL-------SAVLGTWFQGA-CVFlchMPTFCPETVLNVL 306
Cdd:cd05941 111 HANLA---ANV----------RALvdawrWTEDDVLLHVLPLhhvhglvNALLCPLFAGAsVEF---LPKFDPKEVAISR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 307 SRFPITTLSANPEMYQELLQ--------HKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGLlcA 378
Cdd:cd05941 175 LMPSITVFMGVPTIYTRLLQyyeahftdPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGM--A 252
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2217275610 379 TSKTIK--LKPSSLGKPLPPYIVQIVDEN-SNLLPPGEEGNIAIR 420
Cdd:cd05941 253 LSNPLDgeRRPGTVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVR 297
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
111-420 |
9.02e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 92.37 E-value: 9.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 111 GDRLMIILPPTPE---AYWiclACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSDC-------- 179
Cdd:PRK05605 82 GDRVAIVLPNCPQhivAFY---AVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTpletivsv 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 180 ------------------PTLKTKLLVSDKSYDGWLDFKKLIQVAPPKQTYM----RTKSQDPMAIFFTKGTTGAPKMVE 237
Cdd:PRK05605 159 nmiaampllqrlalrlpiPALRKARAALTGPAPGTVPWETLVDAAIGGDGSDvshpRPTPDDVALILYTSGTTGKPKGAQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 238 YSQYGLgmgFSQA--SRRWMDL---QPTDVLWSLG--DAFGgsLSLSAVLGTWFQGACVFLchmPTFCPETVLNVLSRFP 310
Cdd:PRK05605 239 LTHRNL---FANAaqGKAWVPGlgdGPERVLAALPmfHAYG--LTLCLTLAVSIGGELVLL---PAPDIDLILDAMKKHP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 311 ITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETG-LLCATSKTIKLKPSS 389
Cdd:PRK05605 311 PTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGY 390
|
330 340 350
....*....|....*....|....*....|...
gi 2217275610 390 LGKPLPPYIVQIVD-EN-SNLLPPGEEGNIAIR 420
Cdd:PRK05605 391 VGVPFPDTEVRIVDpEDpDETMPDGEEGELLVR 423
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
129-421 |
9.21e-20 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 92.07 E-value: 9.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 129 LACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVAN----EAMAPVVNSA-----VSDCPTLKTKLLVSDKS------- 192
Cdd:PRK12406 54 YAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHadllHGLASALPAGvtvlsVPTPPEIAAAYRISPALltppaga 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 193 --YDGWLdfkkliQVAPPkqtYMRTKSQDPMAIFFTKGTTGAPKMV-------EYSQY-----GLGMGFSQASRRWMdlq 258
Cdd:PRK12406 134 idWEGWL------AQQEP---YDGPPVPQPQSMIYTSGTTGHPKGVrraaptpEQAAAaeqmrALIYGLKPGIRALL--- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 259 PTDVLWSLGDAFGgslSLSAVLGtwfqGACVFlchMPTFCPETVLNVLSRFPITTLSANPEMYQELLQ--HKCFTSYRFK 336
Cdd:PRK12406 202 TGPLYHSAPNAYG---LRAGRLG----GVLVL---QPRFDPEELLQLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDVS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 337 SLKQCVAAGGPISPGV----IEDWKRItkldIYEGYGQTETGLLC-ATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPP 411
Cdd:PRK12406 272 SLRHVIHAAAPCPADVkramIEWWGPV----IYEYYGSTESGAVTfATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQ 347
|
330
....*....|
gi 2217275610 412 GEEGNIAIRI 421
Cdd:PRK12406 348 GEIGEIYSRI 357
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
108-420 |
1.52e-19 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 92.02 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 108 LSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVsdcpTLKTKLL 187
Cdd:PRK06060 52 LSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSR----VAEAAEL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 188 VSDKSYDGWLDFKKLIQVAPPKQTYmrtksqdpmaiffTKGTTGAPKMVEYSQYGLGMGFSQASRRWMDLQPTDV-LWSL 266
Cdd:PRK06060 128 MSEAARVAPGGYEPMGGDALAYATY-------------TSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTgLCSA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 267 GDAFGGSLSLSavlgTWF---QGACVFLCHMPTfCPETVLNVLSRFPITTLSANPEMYQELLQhKCfTSYRFKSLKQCVA 343
Cdd:PRK06060 195 RMYFAYGLGNS----VWFplaTGGSAVINSAPV-TPEAAAILSARFGPSVLYGVPNFFARVID-SC-SPDSFRSLRCVVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 344 AGGPISPGVIEdwkRITK----LDIYEGYGQTETGLLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAI 419
Cdd:PRK06060 268 AGEALELGLAE---RLMEffggIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWV 344
|
.
gi 2217275610 420 R 420
Cdd:PRK06060 345 R 345
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
219-420 |
2.06e-19 |
|
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: 89.64 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 219 DPMAIFFTKGTTGAPKMVEYSQYG-LGMGFSQASRrwMDLQPTDVL---WSLGDAFGGSLSLSAVLGTwfQGACVFLChm 294
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNiVNNGYFIGER--LGLTEQDRLcipVPLFHCFGSVLGVLACLTH--GATMVFPS-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 295 PTFCPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIedwKRITKL----DIYEGYGQ 370
Cdd:cd05917 77 PSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELM---KRVIEVmnmkDVTIAYGM 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217275610 371 TETGLLCATSKT---IKLKPSSLGKPLPPYIVQIVDENSNLLPP-GEEGNIAIR 420
Cdd:cd05917 154 TETSPVSTQTRTddsIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIR 207
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
87-420 |
2.54e-19 |
|
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: 90.23 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 87 SFERMTQLSKKAASILSDtCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAqcivane 166
Cdd:cd05935 3 TYLELLEVVKKLASFLSN-KGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGA------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 167 amapvvnsavsdcptlktKLLVSDKSYDgwldfkkliqvappkqtymrtksqDPMAIFFTKGTTGAPKMVEYSQYGLGMG 246
Cdd:cd05935 75 ------------------KVAVVGSELD------------------------DLALIPYTSGTTGLPKGCMHTHFSAAAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 247 FSQaSRRWMDLQPTDVlwSLG-------DAFGGSLSLSAVLGtwfqgACVFLchMPTFCPETVLNVLSRFPITTLSANPE 319
Cdd:cd05935 113 ALQ-SAVWTGLTPSDV--ILAclplfhvTGFVGSLNTAVYVG-----GTYVL--MARWDRETALELIEKYKVTFWTNIPT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 320 MYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGLLCATSKTIKLKPSSLGKPLPPYIV 399
Cdd:cd05935 183 MLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDA 262
|
330 340
....*....|....*....|..
gi 2217275610 400 QIVD-ENSNLLPPGEEGNIAIR 420
Cdd:cd05935 263 RVIDiETGRELPPNEVGEIVVR 284
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
76-420 |
2.84e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 90.69 E-value: 2.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 76 KVSAKGEEDKWSFERMTQLSKKAASILSDTCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLR 155
Cdd:PRK06839 18 RIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 156 MSKAQCIVANEAMApvvNSAVSDCPTLKTKLLVSDKSYDGWLDfKKLIQVAPPKQTymrtksqDPMAIFFTKGTTGAPKm 235
Cdd:PRK06839 98 DSGTTVLFVEKTFQ---NMALSMQKVSYVQRVISITSLKEIED-RKIDNFVEKNES-------ASFIICYTSGTTGKPK- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 236 veysqyglGMGFSQASRRW--------MDLQPTDVLWSLGDAFG-GSLSLSAvLGTWFQGACVFLCHmpTFCPETVLNVL 306
Cdd:PRK06839 166 --------GAVLTQENMFWnalnntfaIDLTMHDRSIVLLPLFHiGGIGLFA-FPTLFAGGVIIVPR--KFEPTKALSMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 307 SRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRiTKLDIYEGYGQTETG--LLCATSKTIK 384
Cdd:PRK06839 235 EKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTETSptVFMLSEEDAR 313
|
330 340 350
....*....|....*....|....*....|....*.
gi 2217275610 385 LKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK06839 314 RKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIR 349
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
111-420 |
2.31e-18 |
|
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: 88.39 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 111 GDRLMIILPPTPEAYWICLACVRLG----ITFVPGSPQLTAKkiryqlRMSKAQC---IVANEAM--------APVVNSA 175
Cdd:cd05966 109 GDRVAIYMPMIPELVIAMLACARIGavhsVVFAGFSAESLAD------RINDAQCklvITADGGYrggkviplKEIVDEA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 176 VSDCPTLKTKLLVS--------DKSYDGWLDfkKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLgMGF 247
Cdd:cd05966 183 LEKCPSVEKVLVVKrtggevpmTEGRDLWWH--DLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGY-LLY 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 248 SQASRRWM-DLQPTDVLWSLGDaFG----------GSLSLSAVlGTWFQGACVFlchmPTfcPETVLNVLSRFPITTLSA 316
Cdd:cd05966 260 AATTFKYVfDYHPDDIYWCTAD-IGwitghsyivyGPLANGAT-TVMFEGTPTY----PD--PGRYWDIVEKHKVTIFYT 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 317 NPEMYQELLQH--KCFTSYRFKSLKQCVAAGGPISPgviEDW----KRI--TKLDIYEGYGQTETGLLCATS--KTIKLK 386
Cdd:cd05966 332 APTAIRALMKFgdEWVKKHDLSSLRVLGSVGEPINP---EAWmwyyEVIgkERCPIVDTWWQTETGGIMITPlpGATPLK 408
|
330 340 350
....*....|....*....|....*....|....
gi 2217275610 387 PSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:cd05966 409 PGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIK 442
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
111-420 |
9.61e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 86.37 E-value: 9.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 111 GDRLMIILPPTPEayWICL--ACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEA------------MAPVVNS-- 174
Cdd:PRK12583 70 GDRVGIWAPNCAE--WLLTqfATARIGAILVNINPAYRASELEYALGQSGVRWVICADAfktsdyhamlqeLLPGLAEgq 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 175 ----AVSDCPTLKTKLLVSDKSYDGWLDFKKLIQVA---PPKQTYMRTKS---QDPMAIFFTKGTTGAPKMVEYSQYG-L 243
Cdd:PRK12583 148 pgalACERLPELRGVVSLAPAPPPGFLAWHELQARGetvSREALAERQASldrDDPINIQYTSGTTGFPKGATLSHHNiL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 244 GMGFSQASRrwMDLQPTDVLW---SLGDAFGGSLslsAVLGTWFQGACVFLchmPT--FCPETVLNVLSRFPITTLSANP 318
Cdd:PRK12583 228 NNGYFVAES--LGLTEHDRLCvpvPLYHCFGMVL---ANLGCMTVGACLVY---PNeaFDPLATLQAVEEERCTALYGVP 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 319 EMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIedwKRITK----LDIYEGYGQTETG---LLCATSKTIKLKPSSLG 391
Cdd:PRK12583 300 TMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVM---RRVMDemhmAEVQIAYGMTETSpvsLQTTAADDLERRVETVG 376
|
330 340
....*....|....*....|....*....
gi 2217275610 392 KPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK12583 377 RTQPHLEVKVVDPDGATVPRGEIGELCTR 405
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
82-420 |
1.70e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 85.01 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 82 EEDKWSFERMTQLSKKAASILSDTCaLSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQC 161
Cdd:PRK03640 24 EEKKVTFMELHEAVVSVAGKLAALG-VKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKC 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 162 IVANEAMApvvnsavsdcptlktKLLVSDKSydgwLDFKKLIQVAPPKQTYMRTKSQDPMA-IFFTKGTTGAPKMVE--- 237
Cdd:PRK03640 103 LITDDDFE---------------AKLIPGIS----VKFAELMNGPKEEAEIQEEFDLDEVAtIMYTSGTTGKPKGVIqty 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 238 ----YSQYG--LGMGFsQASRRWMDLQPTdvlwslgdaFGGSlSLSAVLGTWFQGACVFLchMPTFCPETVLNVLSRFPI 311
Cdd:PRK03640 164 gnhwWSAVGsaLNLGL-TEDDCWLAAVPI---------FHIS-GLSILMRSVIYGMRVVL--VEKFDAEKINKLLQTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 312 TTLSANPEMYQELL----QHKCFTSYRfkslkqCV-AAGGPISPGVIEDWKRiTKLDIYEGYGQTETgllcaTSKTIKLK 386
Cdd:PRK03640 231 TIISVVSTMLQRLLerlgEGTYPSSFR------CMlLGGGPAPKPLLEQCKE-KGIPVYQSYGMTET-----ASQIVTLS 298
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2217275610 387 PS-------SLGKPLPPYIVQIVDeNSNLLPPGEEGNIAIR 420
Cdd:PRK03640 299 PEdaltklgSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVK 338
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
107-417 |
8.89e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 82.82 E-value: 8.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 107 ALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSDCPTLKTKL 186
Cdd:PRK13391 45 GLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 187 LV-SDKSYDGWLDFKKLIQVAPPkqTYMRTKSQ-DPMaiFFTKGTTGAPKMVeYSQYGLGmGFSQASRRWMDLQPtdvLW 264
Cdd:PRK13391 125 VLdGDGELEGFVGYAEAVAGLPA--TPIADESLgTDM--LYSSGTTGRPKGI-KRPLPEQ-PPDTPLPLTAFLQR---LW 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 265 SLGDafgGSLSLS-----------AVLGTWFQGACVFLchMPTFCPETVLNVLSRFPITTLSANPEMYQELLQ--HKCFT 331
Cdd:PRK13391 196 GFRS---DMVYLSpaplyhsapqrAVMLVIRLGGTVIV--MEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKlpEEVRD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 332 SYRFKSLKQCVAAGGPISPGVIED----WKRItkldIYEGYGQTETGLLCA-TSKTIKLKPSSLGKPLPPyIVQIVDENS 406
Cdd:PRK13391 271 KYDLSSLEVAIHAAAPCPPQVKEQmidwWGPI----IHEYYAATEGLGFTAcDSEEWLAHPGTVGRAMFG-DLHILDDDG 345
|
330
....*....|.
gi 2217275610 407 NLLPPGEEGNI 417
Cdd:PRK13391 346 AELPPGEPGTI 356
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
72-420 |
1.23e-16 |
|
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: 82.29 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 72 PALWkvsakGEEDKWSFERMTQLSKKAASILSDTCaLSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIR 151
Cdd:cd05945 8 PAVV-----EGGRTLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 152 YQLRMSKAQCIVANEAmapvvnsavsdcptlktkllvsdksydgwldfkkliqvappkqtymrtksqDPMAIFFTKGTTG 231
Cdd:cd05945 82 EILDAAKPALLIADGD---------------------------------------------------DNAYIIFTSGSTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 232 APKMVEYSQYGLgMGFSqasrRWM----DLQPTDVLwsLGDA-FGGSLSLSAVLGTWFQGACVFLChmptfcPETVLNV- 305
Cdd:cd05945 111 RPKGVQISHDNL-VSFT----NWMlsdfPLGPGDVF--LNQApFSFDLSVMDLYPALASGATLVPV------PRDATADp 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 306 ------LSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWK-RITKLDIYEGYGQTETGLLCA 378
Cdd:cd05945 178 kqlfrfLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQqRFPDARIYNTYGPTEATVAVT 257
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2217275610 379 ----TSKTI-KLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:cd05945 258 yievTPEVLdGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVIS 304
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
129-420 |
1.85e-16 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 82.11 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 129 LACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSDCPtlKTKLLVSDKSYDGWLDFKKLIQvAPP 208
Cdd:PRK13382 111 LAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDRALADCP--QATRIVAWTDEDHDLTVEVLIA-AHA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 209 KQTYMRTKSQDPMaIFFTKGTTGAPKMVEYSQYGLGMGFSQASRR--WMDLQPTDVLWSLGDAFGGS-LSLSAVLGtwfq 285
Cdd:PRK13382 188 GQRPEPTGRKGRV-ILLTSGTTGTPKGARRSGPGGIGTLKAILDRtpWRAEEPTVIVAPMFHAWGFSqLVLAASLA---- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 286 gacvflCHMPT---FCPETVLNVLSRFPITTLSANPEMYQELLQ--HKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRIT 360
Cdd:PRK13382 263 ------CTIVTrrrFDPEATLDLIDRHRATGLAVVPVMFDRIMDlpAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQF 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217275610 361 KLDIYEGYGQTETGLLC-ATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK13382 337 GDVIYNNYNATEAGMIAtATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVR 397
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
111-420 |
2.61e-16 |
|
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: 81.27 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 111 GDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVAneamapvvnsavsdcPTLktkllvsd 190
Cdd:cd05903 26 GDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV---------------PER-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 191 ksydgwldFKKLIQVAPPkqtymrtksQDPMAIFFTKGTTGAPKMVEYSQYGLGMGFSQASRRWMdLQPTDVLWS---LG 267
Cdd:cd05903 83 --------FRQFDPAAMP---------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG-LGPGDVFLVaspMA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 268 DAFGgslSLSAVLGTWFQGACVFLCHmpTFCPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGP 347
Cdd:cd05903 145 HQTG---FVYGFTLPLLLGAPVVLQD--IWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGAT 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217275610 348 ISPGVIEDWKRITKLDIYEGYGQTETgllCATSKTIKLKPSSL-----GKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:cd05903 220 VPRSLARRAAELLGAKVCSAYGSTEC---PGAVTSITPAPEDRrlytdGRPLPGVEIKVVDDTGATLAPGVEGELLSR 294
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
220-430 |
2.89e-16 |
|
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: 81.27 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 220 PMAIFFTKGTTGAPKMVEYsqyGLGMGFSQAsrrwmdlqPTDVLWSLGDAFGGS---LS---------LSAVLGTWFQGA 287
Cdd:cd05929 127 GWKMLYSGGTTGRPKGIKR---GLPGGPPDN--------DTLMAAALGFGPGADsvyLSpaplyhaapFRWSMTALFMGG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 288 CVFLchMPTFCPETVLNVLSRFPITTLSANPEMYQELLQ--HKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIY 365
Cdd:cd05929 196 TLVL--MEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKlpEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIW 273
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217275610 366 EGYGQTETGLLCATSKTIKLK-PSSLGKPLPPyIVQIVDENSNLLPPGEEGNIAIRiklNQPASLY 430
Cdd:cd05929 274 EYYGGTEGQGLTIINGEEWLThPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFA---NGPGFEY 335
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
108-405 |
4.24e-16 |
|
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: 80.72 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 108 LSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYqlrmskaqciVANEAMAPVvnsavsdcptlktkLL 187
Cdd:cd05907 27 VEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAY----------ILNDSEAKA--------------LF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 188 VSDKSydgwldfkkliqvappkqtymrtksqDPMAIFFTKGTTGAPKMVEYSQYGLgMGFSQASRRWMDLQPTDVLWS-- 265
Cdd:cd05907 83 VEDPD--------------------------DLATIIYTSGTTGRPKGVMLSHRNI-LSNALALAERLPATEGDRHLSfl 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 266 -LGDAFGGSLSLSAVLGTwfqGACVFLCHMPtfcpETVLNVLSRFPITTLSANPEMYQEL-----------LQHKCFTSY 333
Cdd:cd05907 136 pLAHVFERRAGLYVPLLA---GARIYFASSA----ETLLDDLSEVRPTVFLAVPRVWEKVyaaikvkavpgLKRKLFDLA 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217275610 334 RFKSLKQCVAAGGPISPGVIEdWKRITKLDIYEGYGQTETGLLCATSKTIKLKPSSLGKPLPPYIVQIVDEN 405
Cdd:cd05907 209 VGGRLRFAASGGAPLPAELLH-FFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADDG 279
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
54-420 |
4.93e-16 |
|
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: 80.57 E-value: 4.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 54 DVLDQWSQLekdglRGPYPALwkVsakGEEDKWSFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEAYWICLACVR 133
Cdd:COG1021 29 DLLRRRAER-----HPDRIAV--V---DGERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 134 LGITFVPGSPQLTAKKIRYQLRMSKAQCIVA--------NEAMApvvNSAVSDCPTLKTKLLVSDKsyDGWLDFKKLIQV 205
Cdd:COG1021 98 AGAIPVFALPAHRRAEISHFAEQSEAVAYIIpdrhrgfdYRALA---RELQAEVPSLRHVLVVGDA--GEFTSLDALLAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 206 APPKQTYmRTKSQDPmAIF-FTKGTTGAPKMVE-------YSqyglgmgfSQASRRWMDLQPTDV-LWSLGDAFGGSLSL 276
Cdd:COG1021 173 PADLSEP-RPDPDDV-AFFqLSGGTTGLPKLIPrthddylYS--------VRASAEICGLDADTVyLAALPAAHNFPLSS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 277 SAVLGTWFQGACVFLChmPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPgviEDW 356
Cdd:COG1021 243 PGVLGVLYAGGTVVLA--PDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSP---ELA 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217275610 357 KRITKL---DIYEGYGQTEtGLLCATS---------KTIklkpsslGKPLPPYI-VQIVDENSNLLPPGEEGNIAIR 420
Cdd:COG1021 318 RRVRPAlgcTLQQVFGMAE-GLVNYTRlddpeevilTTQ-------GRPISPDDeVRIVDEDGNPVPPGEVGELLTR 386
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
83-420 |
6.23e-16 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 80.57 E-value: 6.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 83 EDKWSFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCI 162
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 163 VANEAMAPVVNSAVSDCPTLKTKLLVSDKSYDGW------LDFKKLIQVAPPKQtymrTKSQDPMAIFFTKGTTGAPKMV 236
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLDAPASVSVpagwstAPLPPLDAPAPAAA----VQPGDTAAILYTSGTTGPSKGV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 237 ---EYSQYGLGMgfsqASRRWMDLQPTDVLWSlgdafggSLSL--SAVLGTWFQ----GACVFLchMPTFCPETVLNVLS 307
Cdd:PRK06155 199 ccpHAQFYWWGR----NSAEDLEIGADDVLYT-------TLPLfhTNALNAFFQallaGATYVL--EPRFSASGFWPAVR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 308 RFPITTLSANPEMYQELLQHKCFTSYRFKSLKqcVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGLLCATSKTIKlKP 387
Cdd:PRK06155 266 RHGATVTYLLGAMVSILLSQPARESDRAHRVR--VALGPGVPAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RP 342
|
330 340 350
....*....|....*....|....*....|...
gi 2217275610 388 SSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK06155 343 GSMGRLAPGFEARVVDEHDQELPDGEPGELLLR 375
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
108-420 |
7.86e-16 |
|
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: 80.05 E-value: 7.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 108 LSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVA-NEAMAPVVNSAVSDCPTLKTkL 186
Cdd:cd05926 36 IKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTpKGELGPASRAASKLGLAILE-L 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 187 LVSDKSYDGWLDFKKLIQVAP-PKQTYMRTKSQ--DPMAIFFTKGTTGAPKMVEYSQYGL--GMGFSQASRRwmdLQPTD 261
Cdd:cd05926 115 ALDVGVLIRAPSAESLSNLLAdKKNAKSEGVPLpdDLALILHTSGTTGRPKGVPLTHRNLaaSATNITNTYK---LTPDD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 262 VLWSLGDAFGGSLSLSAVLGTWFQGACVFLchMPTFCPETVLNVLSRFPITTLSANPEMYQELLQ-HKCFTSYRFKSLKQ 340
Cdd:cd05926 192 RTLVVMPLFHVHGLVASLLSTLAAGGSVVL--PPRFSASTFWPDVRDYNATWYTAVPTIHQILLNrPEPNPESPPPKLRF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 341 CVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGLLCATSK--TIKLKPSSLGKPLPPYiVQIVDENSNLLPPGEEGNIA 418
Cdd:cd05926 270 IRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNPlpPGPRKPGSVGKPVGVE-VRILDEDGEILPPGVVGEIC 348
|
..
gi 2217275610 419 IR 420
Cdd:cd05926 349 LR 350
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
111-420 |
1.11e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 79.69 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 111 GDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSdcpTLKTKLLVSD 190
Cdd:PRK06710 74 GDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQS---ATKIEHVIVT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 191 KSYDgWLDFKK--LIQVAPPKQTYMRTKSQ-----------------------DP---MAIF-FTKGTTGAPKMVEYSQY 241
Cdd:PRK06710 151 RIAD-FLPFPKnlLYPFVQKKQSNLVVKVSesetihlwnsvekevntgvevpcDPendLALLqYTGGTTGFPKGVMLTHK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 242 GLgmgfsqASRRWMDLQ--------PTDVLWSLgdAFGGSLSLSAVLG-TWFQGACVFLchMPTFCPETVLNVLSRFPIT 312
Cdd:PRK06710 230 NL------VSNTLMGVQwlynckegEEVVLGVL--PFFHVYGMTAVMNlSIMQGYKMVL--IPKFDMKMVFEAIKKHKVT 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 313 TLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGLLCATSKTIKLK-PSSLG 391
Cdd:PRK06710 300 LFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRvPGSIG 379
|
330 340 350
....*....|....*....|....*....|
gi 2217275610 392 KPLPPYIVQIVD-ENSNLLPPGEEGNIAIR 420
Cdd:PRK06710 380 VPWPDTEAMIMSlETGEALPPGEIGEIVVK 409
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
78-420 |
1.35e-15 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 79.34 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 78 SAKGEEDKWSFERMTQLSKKAASiLSDTCALSHGDRLMIILPPTPEAY--WICLACVrlGITFVPGSPQLTAKKIRYQLR 155
Cdd:PRK08008 30 SSGGVVRRYSYLELNEEINRTAN-LFYSLGIRKGDKVALHLDNCPEFIfcWFGLAKI--GAIMVPINARLLREESAWILQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 156 MSKAQCIVANEAMAPVVNSAVSDCPTLKTKLLVSD---KSYDGWLDFKKLIQVAPPKQTYMRTKSQDPMA-IFFTKGTTG 231
Cdd:PRK08008 107 NSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTRvalPADDGVSSFTQLKAQQPATLCYAPPLSTDDTAeILFTSGTTS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 232 APKMVEYSQYGLgmGFSQASRRWM-DLQPTDVLWSLGDAFGGSLSLSAVLGTWFQGACVFLCH----------------- 293
Cdd:PRK08008 187 RPKGVVITHYNL--RFAGYYSAWQcALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEkysarafwgqvckyrat 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 294 ----MPTFcpetvlnvlsrfpITTLSANPEMYQEllQHKCFTSYRFKSlkqcvaaggPISPGVIEDWKRITKLDIYEGYG 369
Cdd:PRK08008 265 itecIPMM-------------IRTLMVQPPSAND--RQHCLREVMFYL---------NLSDQEKDAFEERFGVRLLTSYG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2217275610 370 QTET--GLLcATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK08008 321 MTETivGII-GDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIK 372
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
85-420 |
1.97e-15 |
|
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: 78.16 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 85 KWSFERMTQLSKKAASILSDTCAlSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCiva 164
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGV-RKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 165 nEAMApvvnsavsdcptlktkllvsdksydgwldfkkliqvappkqtymrtksqdpmAIFFTKGTTGAPKMVE------- 237
Cdd:cd05912 77 -DDIA----------------------------------------------------TIMYTSGTTGKPKGVQqtfgnhw 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 238 YSQYG--LGMGFSqASRRWMDLQPtdvLWSLGdafggslSLSAVLGTWFQGACVFLchMPTFCPETVLNVLSRFPITTLS 315
Cdd:cd05912 104 WSAIGsaLNLGLT-EDDNWLCALP---LFHIS-------GLSILMRSVIYGMTVYL--VDKFDAEQVLHLINSGKVTIIS 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 316 ANPEMYQELLQ--HKCFTSyrfkSLKQCVAAGGPISPGVIEDWKRiTKLDIYEGYGQTETgllCATSKTIK-----LKPS 388
Cdd:cd05912 171 VVPTMLQRLLEilGEGYPN----NLRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTET---CSQIVTLSpedalNKIG 242
|
330 340 350
....*....|....*....|....*....|..
gi 2217275610 389 SLGKPLPPYIVQIVDENSnllPPGEEGNIAIR 420
Cdd:cd05912 243 SAGKPLFPVELKIEDDGQ---PPYEVGEILLK 271
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
117-420 |
2.28e-15 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 78.84 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 117 ILPPTPEAYWICLACVRLGITFvPGSPQLTAKKIRYQLRMSKAQCIVANEAM-----APVVNSAVSDCPTLKTKLLV--- 188
Cdd:PRK07529 89 LLPNLPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVLVTLGPFpgtdiWQKVAEVLAALPELRTVVEVdla 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 189 --------------SDKSYDGWLDFKKLI--QVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGlgmgfsQASR 252
Cdd:PRK07529 168 rylpgpkrlavpliRRKAHARILDFDAELarQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN------EVAN 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 253 RWM-----DLQPTDVLWS---LGDAFGgslSLSAVLGTWFQGACVFLchmPT---FCPETVLN----VLSRFPITTLSAN 317
Cdd:PRK07529 242 AWLgalllGLGPGDTVFCglpLFHVNA---LLVTGLAPLARGAHVVL---ATpqgYRGPGVIAnfwkIVERYRINFLSGV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 318 PEMYQELLQHKCfTSYRFKSLKqcVAAGG--PISPGVIEDWKRITKLDIYEGYGQTETGLLCATS-KTIKLKPSSLGKPL 394
Cdd:PRK07529 316 PTVYAALLQVPV-DGHDISSLR--YALCGaaPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNpPDGERRIGSVGLRL 392
|
330 340 350
....*....|....*....|....*....|.
gi 2217275610 395 PPYIVQIV--DENSNLL---PPGEEGNIAIR 420
Cdd:PRK07529 393 PYQRVRVVilDDAGRYLrdcAVDEVGVLCIA 423
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
129-419 |
5.04e-15 |
|
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: 78.36 E-value: 5.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 129 LACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVnsavsdcPTLKTKLLVSDKSydgwldfkkLIQVAPP 208
Cdd:COG1020 544 LAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARL-------PELGVPVLALDAL---------ALAAEPA 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 209 KQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLgMGFSQASRRWMDLQPTDV---LWSLG-DAfggslSLSAVLGTWF 284
Cdd:COG1020 608 TNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRAL-VNLLAWMQRRYGLGPGDRvlqFASLSfDA-----SVWEIFGALL 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 285 QGACVFLC----HMPtfcPETVLNVLSRFPITTLSANPEMYQELLQHkcfTSYRFKSLKQCVAAGGPISPGVIEDWKRIT 360
Cdd:COG1020 682 SGATLVLAppeaRRD---PAALAELLARHRVTVLNLTPSLLRALLDA---APEALPSLRLVLVGGEALPPELVRRWRARL 755
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217275610 361 K-LDIYEGYGQTETGLlCATSKTI-----KLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAI 419
Cdd:COG1020 756 PgARLVNLYGPTETTV-DSTYYEVtppdaDGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYI 819
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
85-420 |
5.39e-15 |
|
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: 77.37 E-value: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 85 KWSFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAqciva 164
Cdd:cd05920 40 RLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEA----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 165 neamapvvnsavsdcptlktKLLVSDKSYDGWlDFKKLIQvappkqtYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLG 244
Cdd:cd05920 114 --------------------VAYIVPDRHAGF-DHRALAR-------ELAESIPEVALFLLSGGTTGTPKLIPRTHNDYA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 245 MGFSqASRRWMDLQPTDV-LWSLGDAFGGSLSLSAVLGTWFQGACVFLCHMPTfcPETVLNVLSRFPITTLSANPEMYQE 323
Cdd:cd05920 166 YNVR-ASAEVCGLDQDTVyLAVLPAAHNFPLACPGVLGTLLAGGRVVLAPDPS--PDAAFPLIEREGVTVTALVPALVSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 324 LLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTEtGLLCAT----SKTIKLkpSSLGKPLPPYI- 398
Cdd:cd05920 243 WLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE-GLLNYTrlddPDEVII--HTQGRPMSPDDe 319
|
330 340
....*....|....*....|..
gi 2217275610 399 VQIVDENSNLLPPGEEGNIAIR 420
Cdd:cd05920 320 IRVVDEEGNPVPPGEEGELLTR 341
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
215-419 |
5.72e-15 |
|
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: 76.96 E-value: 5.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 215 TKSQDPMAIFFTKGTTGAPKMVEYSQYGLGMGFSQASRRwMDLQPTD-VLWSLGDAFggSLSLSAVLGTWFQGACVFLC- 292
Cdd:cd17653 102 DSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPAR-LDVGPGSrVAQVLSIAF--DACIGEIFSTLCNGGTLVLAd 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 293 HMPTFcpETVLNVLSRFPIT-----TLSANPemyqellqhkcftsyrFKSLKQCVAAGGPISPGVIEDWKRITKLdiYEG 367
Cdd:cd17653 179 PSDPF--AHVARTVDALMSTpsilsTLSPQD----------------FPNLKTIFLGGEAVPPSLLDRWSPGRRL--YNA 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2217275610 368 YGQTETGLLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAI 419
Cdd:cd17653 239 YGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICI 290
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
75-420 |
8.76e-15 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 76.71 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 75 WKVSAKGEEDK----------WSFERMTQLSKKAASILSDtCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQ 144
Cdd:PRK06087 29 WQQTARAMPDKiavvdnhgasYTYSALDHAASRLANWLLA-KGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 145 LTAKKIRYQLRMSKAQCIVA-----NEAMAPVVNSAVSDCPTLKTKLLVsDK--SYDGWLDFKKLIQVAPPKQTYMRTKS 217
Cdd:PRK06087 108 WREAELVWVLNKCQAKMFFAptlfkQTRPVDLILPLQNQLPQLQQIVGV-DKlaPATSSLSLSQIIADYEPLTTAITTHG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 218 QDPMAIFFTKGTTGAPKMVEYSQYGLgmgfsQASRRW----MDLQPTDVLW---SLGDAFGgslSLSAVLGTWFQGACVF 290
Cdd:PRK06087 187 DELAAVLFTSGTEGLPKGVMLTHNNI-----LASERAycarLNLTWQDVFMmpaPLGHATG---FLHGVTAPFLIGARSV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 291 LchMPTFCPETVLNVLSRFPIT-TLSANPEMYqELLQHKCFTSYRFKSLKQCVAAGGPISPGVIED-WKRITKLdiYEGY 368
Cdd:PRK06087 259 L--LDIFTPDACLALLEQQRCTcMLGATPFIY-DLLNLLEKQPADLSALRFFLCGGTTIPKKVAREcQQRGIKL--LSVY 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2217275610 369 GQTETG--LLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK06087 334 GSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASR 387
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
99-374 |
1.11e-14 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 76.75 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 99 ASILSDTCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSD 178
Cdd:PRK05620 52 AHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEILKE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 179 CPTLKTKLLVSDKSYDG----------WLDFKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLgmgFS 248
Cdd:PRK05620 132 CPCVRAVVFIGPSDADSaaahmpegikVYSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPKGVVYSHRSL---YL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 249 QAsrrwMDLQPTDvlwSLGDAFGGS----------LSLSAVLGTWFQGACVFLCHmPTFCPETVLNVLSRFPITTLSANP 318
Cdd:PRK05620 209 QS----LSLRTTD---SLAVTHGESflccvpiyhvLSWGVPLAAFMSGTPLVFPG-PDLSAPTLAKIIATAMPRVAHGVP 280
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217275610 319 EMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETG 374
Cdd:PRK05620 281 TLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETS 336
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
108-395 |
2.96e-14 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 75.52 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 108 LSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQ-CIVANEAMAPVVNSAVSDCPTLKTKL 186
Cdd:COG1022 62 VKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKvLFVEDQEQLDKLLEVRDELPSLRHIV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 187 LVSDK---SYDGWLDFKKLI----QVAPPKQTYMR---TKSQDPMAIFFTKGTTGAPKMVEYSQYGLgMGFSQASRRWMD 256
Cdd:COG1022 142 VLDPRglrDDPRLLSLDELLalgrEVADPAELEARraaVKPDDLATIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 257 LQPTDVLWSLgdafggsLSLSAVLGTWFQ------GACVflchmpTFC--PETVLNVLSRFPITTLSANPEMYQ------ 322
Cdd:COG1022 221 LGPGDRTLSF-------LPLAHVFERTVSyyalaaGATV------AFAesPDTLAEDLREVKPTFMLAVPRVWEkvyagi 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 323 --------------------------------------ELLQHKCFTSYRFKSLKQ--------CVAAGGPISPGVIEdW 356
Cdd:COG1022 288 qakaeeagglkrklfrwalavgrryararlagkspsllLRLKHALADKLVFSKLREalggrlrfAVSGGAALGPELAR-F 366
|
330 340 350
....*....|....*....|....*....|....*....
gi 2217275610 357 KRITKLDIYEGYGQTETGLLCATSKTIKLKPSSLGKPLP 395
Cdd:COG1022 367 FRALGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLP 405
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
111-427 |
3.77e-14 |
|
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: 74.65 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 111 GDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVaneamapvvnsavsdcptlktkllvsd 190
Cdd:cd17643 37 GDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLL--------------------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 191 ksydgwldfkkliqvappkqtymrTKSQDPMAIFFTKGTTGAPKMVEYSQYGLGMGFSqASRRWMDLQPTDVlWSLGDAF 270
Cdd:cd17643 90 ------------------------TDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFA-ATQRWFGFNEDDV-WTLFHSY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 271 GGSLSLSAVLGTWFQGA-CVFLCHMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPIS 349
Cdd:cd17643 144 AFDFSVWEIWGALLHGGrLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 350 PGVIEDW---KRITKLDIYEGYGQTETgllCATSKTIKLKP--------SSLGKPLPPYIVQIVDENSNLLPPGEEGNIA 418
Cdd:cd17643 224 AAMLRPWagrFGLDRPQLVNMYGITET---TVHVTFRPLDAadlpaaaaSPIGRPLPGLRVYVLDADGRPVPPGVVGELY 300
|
330
....*....|....*
gi 2217275610 419 I------RIKLNQPA 427
Cdd:cd17643 301 VsgagvaRGYLGRPE 315
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
219-420 |
4.51e-14 |
|
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: 73.46 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 219 DPMAIFFTKGTTGAPKMVEYSQYGLGMGFSQASRRWmDLQPTDVLWSLGDAF--GGslsLSAVLGTWFQGACVFLchMPT 296
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAM-GLTEADVYLNMLPLFhiAG---LNLALATFHAGGANVV--MEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 297 FCPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKqcvAAGGPISPGVIEDWKRITKLDIYEGYGQTETGLL 376
Cdd:cd17637 75 FDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLR---HVLGLDAPETIQRFEETTGATFWSLYGQTETSGL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217275610 377 cATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:cd17637 152 -VTLSPYRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVR 194
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
306-420 |
6.42e-14 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 74.32 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 306 LSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETG-LLCATSKTIK 384
Cdd:PRK08974 295 LKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSpLVSVNPYDLD 374
|
90 100 110
....*....|....*....|....*....|....*.
gi 2217275610 385 LKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK08974 375 YYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVK 410
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
87-420 |
1.01e-13 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 73.52 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 87 SFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEaYWICLACV-RLGITFVPGSPQLTAKKIRYQLRMSKAQCIVAN 165
Cdd:PRK07059 50 TYGELDELSRALAAWLQSR-GLAKGARVAIMMPNVLQ-YPVAIAAVlRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 166 EAMAPVVNSAVSDCP-----------------------TLKTKLLVSDKSYDGWLDFKKLIQvAPPKQTYMRTKsQDPMA 222
Cdd:PRK07059 128 ENFATTVQQVLAKTAvkhvvvasmgdllgfkghivnfvVRRVKKMVPAWSLPGHVRFNDALA-EGARQTFKPVK-LGPDD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 223 IFF---TKGTTGAPK---------MVEYSQYGLGMGFSQASRRWMDLQPTDVLWSLGDAFggSLSLSAVLGTWFQGACVF 290
Cdd:PRK07059 206 VAFlqyTGGTTGVSKgatllhrniVANVLQMEAWLQPAFEKKPRPDQLNFVCALPLYHIF--ALTVCGLLGMRTGGRNIL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 291 LCH---MPTFCPEtvlnvLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEG 367
Cdd:PRK07059 284 IPNprdIPGFIKE-----LKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEG 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2217275610 368 YGQTETG-LLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK07059 359 YGLSETSpVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIR 412
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
76-417 |
1.11e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 73.27 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 76 KVSAKGEEDKWSFERMTQLSKKAASILSDTCalSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLR 155
Cdd:PRK07638 17 KIAIKENDRVLTYKDWFESVCKVANWLNEKE--SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 156 MSKAQCIVANEAMapvvnsaVSDCPTLKTKLLVSDKsydgWldfKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKm 235
Cdd:PRK07638 95 ISNADMIVTERYK-------LNDLPDEEGRVIEIDE----W---KRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPK- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 236 veysqyglgmGFSQASRRWMD----------LQPTDVLWSLGDAFGgSLSLSAVLGTWFQGACVFLchMPTFCPETVLNV 305
Cdd:PRK07638 160 ----------AFLRAQQSWLHsfdcnvhdfhMKREDSVLIAGTLVH-SLFLYGAISTLYVGQTVHL--MRKFIPNQVLDK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 306 LSRFPITTLSANPEMYQELLQHKCFTSYRFKSlkqcvaaggpISPGVieDWKRITK---------LDIYEGYGQTETGLL 376
Cdd:PRK07638 227 LETENISVMYTVPTMLESLYKENRVIENKMKI----------ISSGA--KWEAEAKekiknifpyAKLYEFYGASELSFV 294
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2217275610 377 CA-TSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNI 417
Cdd:PRK07638 295 TAlVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTV 336
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
93-426 |
1.19e-13 |
|
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: 73.31 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 93 QLSKKAASILSDtcALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVV 172
Cdd:cd05923 37 RIEAVAARLHAR--GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAVDAQVMD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 173 NSAVSDCPTLKTKLLVSDKSYDgwlDFKKLIQVAPPkqtymrtKSQDPMAIFFTKGTTGAPKMVEYSQYG-----LGMGf 247
Cdd:cd05923 115 AIFQSGVRVLALSDLVGLGEPE---SAGPLIEDPPR-------EPEQPAFVFYTSGTTGLPKGAVIPQRAaesrvLFMS- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 248 SQASRRWMDLQPTDVLWSLGDAFG--GSLSLSAVLGTwfqgacvFLCHMPTFCPETVLNVLSRFPITTLSANPEMYQELL 325
Cdd:cd05923 184 TQAGLRHGRHNVVLGLMPLYHVIGffAVLVAALALDG-------TYVVVEEFDPADALKLIEQERVTSLFATPTHLDALA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 326 QHKCFTSYRFKSLKQCVAAGGPISPGVIE---DWKRITKLDIyegYGQTEtgllcATSKTI--KLKPSSLGKP---LPPY 397
Cdd:cd05923 257 AAAEFAGLKLSSLRHVTFAGATMPDAVLErvnQHLPGEKVNI---YGTTE-----AMNSLYmrDARTGTEMRPgffSEVR 328
|
330 340 350
....*....|....*....|....*....|....*..
gi 2217275610 398 IVQIVDENSNLLPPGEEGNI--------AIRIKLNQP 426
Cdd:cd05923 329 IVRIGGSPDEALANGEEGELivaaaadaAFTGYLNQP 365
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
129-420 |
1.82e-13 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 72.78 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 129 LACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVA--------NEAMApvvNSAVSDCPTLKTKLLVSDksyDGWLDFK 200
Cdd:PRK13295 98 LACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVpktfrgfdHAAMA---RRLRPELPALRHVVVVGG---DGADSFE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 201 KLI--------QVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLGMGFSQASRRwMDLQPTDVLW-------S 265
Cdd:PRK13295 172 ALLitpaweqePDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAER-LGLGADDVILmaspmahQ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 266 LGDAFGGSLSLSAvlgtwfqGACVFLchMPTFCPETVLNVLSRFPIT-TLSANPeMYQELLQHKCFTSYRFKSLKQCVAA 344
Cdd:PRK13295 251 TGFMYGLMMPVML-------GATAVL--QDIWDPARAAELIRTEGVTfTMASTP-FLTDLTRAVKESGRPVSSLRTFLCA 320
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217275610 345 GGPISPGVIEDWKRITKLDIYEGYGQTETGLLCATSKTIKLKPSSL--GKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK13295 321 GAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPDERASTtdGCPLPGVEVRVVDADGAPLPAGQIGRLQVR 398
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
87-420 |
1.87e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 72.61 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 87 SFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANE 166
Cdd:PRK06145 29 SYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 167 AMAPVvnsavsdcPTLKTKLLVSDKSYDGwlDFKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSqYG---- 242
Cdd:PRK06145 108 EFDAI--------VALETPKIVIDAAAQA--DSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHS-YGnlhw 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 243 ------LGMGFSqASRRWMDLQPtdvLWSLGdafggSLSLSAVLGTWFQGacvFLCHMPTFCPETVLNVLSRFPITTLSA 316
Cdd:PRK06145 177 ksidhvIALGLT-ASERLLVVGP---LYHVG-----AFDLPGIAVLWVGG---TLRIHREFDPEAVLAAIERHRLTCAWM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 317 NPEMYQELLqhKCFTSYRFK--SLKQCVAAGGPISPGVIEDWKRI-TKLDIYEGYGQTET---GLLCATSKTIKlKPSSL 390
Cdd:PRK06145 245 APVMLSRVL--TVPDRDRFDldSLAWCIGGGEKTPESRIRDFTRVfTRARYIDAYGLTETcsgDTLMEAGREIE-KIGST 321
|
330 340 350
....*....|....*....|....*....|
gi 2217275610 391 GKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK06145 322 GRALAHVEIRIADGAGRWLPPNMKGEICMR 351
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
86-420 |
3.62e-13 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 71.83 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 86 WSFERMTQLSKKAASILsDTCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVAN 165
Cdd:PRK07514 29 YTYGDLDAASARLANLL-VALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 166 EAMAPVVNSAVSDCPTLKTKLLVSDKSydGWLdfKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLGM 245
Cdd:PRK07514 108 PANFAWLSKIAAAAGAPHVETLDADGT--GSL--LEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 246 GfSQASRRWMDLQPTDVLWSLGDAFGGSLSLSAVLGTWFQGACVFLChmPTFCPETVLNVLSRfpITTLSANPEMYQELL 325
Cdd:PRK07514 184 N-ALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFL--PKFDPDAVLALMPR--ATVMMGVPTFYTRLL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 326 QHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGLLcaTSKTI--KLKPSSLGKPLPPYIVQIVD 403
Cdd:PRK07514 259 QEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMN--TSNPYdgERRAGTVGFPLPGVSLRVTD 336
|
330
....*....|....*...
gi 2217275610 404 -ENSNLLPPGEEGNIAIR 420
Cdd:PRK07514 337 pETGAELPPGEIGMIEVK 354
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
223-427 |
5.59e-13 |
|
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: 70.86 E-value: 5.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 223 IFFTKGTTGAPKMVEYSQYGLGMgFSQASRRWMDLQPTDVLWSLGdAFGGSLSLSAVLGTWFQGACVFLCHMPTFC-PET 301
Cdd:cd17649 99 VIYTSGSTGTPKGVAVSHGPLAA-HCQATAERYGLTPGDRELQFA-SFNFDGAHEQLLPPLICGACVVLRPDELWAsADE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 302 VLNVLSRFPITTLSANPEMYQELLQH-KCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLdIYEGYGQTE---TGLLC 377
Cdd:cd17649 177 LAEMVRELGVTVLDLPPAYLQQLAEEaDRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPVR-LFNAYGPTEatvTPLVW 255
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217275610 378 ATSKTIKLKPSSL--GKPLPPYIVQIVDENSNLLPPGEEGNIAI------RIKLNQPA 427
Cdd:cd17649 256 KCEAGAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGELYIggeglaRGYLGRPE 313
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
111-419 |
6.36e-13 |
|
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: 70.84 E-value: 6.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 111 GDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPvvnsavsdcptlktklLVSD 190
Cdd:cd17651 45 GDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPALAG----------------ELAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 191 KSYDGWLDFKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLgMGFSQASRRWMDLQPTD--VLWSlgd 268
Cdd:cd17651 109 ELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSL-ANLVAWQARASSLGPGArtLQFA--- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 269 AFGGSLSLSAVLGTWFQGACVflcHMPT----FCPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAA 344
Cdd:cd17651 185 GLGFDVSVQEIFSTLCAGATL---VLPPeevrTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 345 GGPISPGV-IEDW-KRITKLDIYEGYGQTETGLlcATSKTIKLKPS------SLGKPLPPYIVQIVDENSNLLPPGEEGN 416
Cdd:cd17651 262 GEQLVLTEdLREFcAGLPGLRLHNHYGPTETHV--VTALSLPGDPAawpappPIGRPIDNTRVYVLDAALRPVPPGVPGE 339
|
...
gi 2217275610 417 IAI 419
Cdd:cd17651 340 LYI 342
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
215-419 |
7.78e-13 |
|
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: 70.57 E-value: 7.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 215 TKSQDPMAIFFTKGTTGAPKMVEYSqYGLGMGFSQASRRWMDLQPTDV------LWSLgdaFGGSLSLSAVLgtwfqGAC 288
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYR-HGTFAAQIDALRQLYGIRPGEVdlatfpLFAL---FGPALGLTSVI-----PDM 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 289 VFLChmPTFC-PETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRIT--KLDIY 365
Cdd:cd05910 153 DPTR--PARAdPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLsdEAEIL 230
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217275610 366 EGYGQTETGLLCA----------TSKTIKLKPSSLGKPLPPY---IVQIVDE------NSNLLPPGEEGNIAI 419
Cdd:cd05910 231 TPYGATEALPVSSigsrellattTAATSGGAGTCVGRPIPGVrvrIIEIDDEpiaewdDTLELPRGEIGEITV 303
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
111-420 |
8.72e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 70.94 E-value: 8.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 111 GDRLMIILPPTPEAYWICLACVRLGITF--VPG--SPQLTAKkiryqlRMSKAQC---IVANE--------AMAPVVNSA 175
Cdd:PRK00174 123 GDRVAIYMPMIPEAAVAMLACARIGAVHsvVFGgfSAEALAD------RIIDAGAklvITADEgvrggkpiPLKANVDEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 176 VSDCPTLKTKLLVS--------DKSYDGWLDfkKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLgMGF 247
Cdd:PRK00174 197 LANCPSVEKVIVVRrtggdvdwVEGRDLWWH--ELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGY-LVY 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 248 SQASRRWM-DLQPTDVLWSLGDaFG----------GSLSLSA--VLgtwFQGAcvflchmPTFcPETvlnvlSRF----- 309
Cdd:PRK00174 274 AAMTMKYVfDYKDGDVYWCTAD-VGwvtghsyivyGPLANGAttLM---FEGV-------PNY-PDP-----GRFwevid 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 310 --PITTLSANPEMYQELLQH--KCFTSYRFKSLKQCVAAGGPISPgviEDW----KRI--TKLDIYEGYGQTETG--LLC 377
Cdd:PRK00174 337 khKVTIFYTAPTAIRALMKEgdEHPKKYDLSSLRLLGSVGEPINP---EAWewyyKVVggERCPIVDTWWQTETGgiMIT 413
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2217275610 378 ATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK00174 414 PLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIK 456
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
87-420 |
1.56e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 69.60 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 87 SFERMTQLSKKAASILSDTCALSHGDRLMIILPPTPEayWI--CLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVA 164
Cdd:PRK08314 37 SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQ--FViaYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 165 NEAMAPVVNSAVSDCPTlkTKLLVSdkSYDGWLD------FKKLIQVAPPKQTY--------------------MRTKSQ 218
Cdd:PRK08314 115 GSELAPKVAPAVGNLRL--RHVIVA--QYSDYLPaepeiaVPAWLRAEPPLQALapggvvawkealaaglapppHTAGPD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 219 DPMAIFFTKGTTGAPKMVEYSQYGLgMGFSQASRRWMDLQPTDVLWSLGDAFGGSLSLSAVLGTWFQGACVFLchMPTFC 298
Cdd:PRK08314 191 DLAVLPYTSGTTGVPKGCMHTHRTV-MANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL--MPRWD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 299 PETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKqCVAAGGPISP-GVIEDWKRITKLDIYEGYGQTETGLLC 377
Cdd:PRK08314 268 REAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLR-YIGGGGAAMPeAVAERLKELTGLDYVEGYGLTETMAQT 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2217275610 378 ATSKTIKLKPSSLGKPLPPYIVQIVD-ENSNLLPPGEEGNIAIR 420
Cdd:PRK08314 347 HSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVH 390
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
90-420 |
2.31e-12 |
|
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: 69.09 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 90 RMTQLSKKAASILSDTCALSHGDRLMIILPptpeaywiCLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMA 169
Cdd:cd17642 56 RLAEALKKYGLKQNDRIAVCSENSLQFFLP--------VIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 170 PVVNSAVSDCPTLKTKLLVSDK-SYDGWLDFKKLI-QVAPPKQTYMRTKS------QDPMAIFFTKGTTGAPKMVEYSQY 241
Cdd:cd17642 128 QKVLNVQKKLKIIKTIIILDSKeDYKGYQCLYTFItQNLPPGFNEYDFKPpsfdrdEQVALIMNSSGSTGLPKGVQLTHK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 242 GLGMGFSQASRRWMDLQP-------TDVLWSLGdaFGgslsLSAVLGTWFQGACVFLchMPTFCPETVLNVLSRFPITTL 314
Cdd:cd17642 208 NIVARFSHARDPIFGNQIipdtailTVIPFHHG--FG----MFTTLGYLICGFRVVL--MYKFEEELFLRSLQDYKVQSA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 315 SANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLD-IYEGYGQTETGLLCATSKTIKLKPSSLGKP 393
Cdd:cd17642 280 LLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKV 359
|
330 340
....*....|....*....|....*...
gi 2217275610 394 LPPYIVQIVD-ENSNLLPPGEEGNIAIR 420
Cdd:cd17642 360 VPFFYAKVVDlDTGKTLGPNERGELCVK 387
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
77-417 |
4.64e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 77 VSAKGEEdkWSFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRM 156
Cdd:PRK13390 18 VAETGEQ--VSYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 157 SKAQCIVANEAMAPVVNSAVSDCPTlktkLLVSDKSYDGWLDFKKLIQVAPPKQTymrtksQDP--MAIFFTKGTTGAPK 234
Cdd:PRK13390 95 SGARVLVASAALDGLAAKVGADLPL----RLSFGGEIDGFGSFEAALAGAGPRLT------EQPcgAVMLYSSGTTGFPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 235 MV-----EYSQYGLGMGFSQASRRWMDLQPTDVLWSLGDAFGGS----LSLSAVLGtwfqGACVFlchMPTFCPETVLNV 305
Cdd:PRK13390 165 GIqpdlpGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAplrwCSMVHALG----GTVVL---AKRFDAQATLGH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 306 LSRFPITTLSANPEMYQELLQ--HKCFTSYRFKSLKQCVAAGGPISPGVIE---DWKRITkldIYEGYGQTET-GLLCAT 379
Cdd:PRK13390 238 VERYRITVTQMVPTMFVRLLKldADVRTRYDVSSLRAVIHAAAPCPVDVKHamiDWLGPI---VYEYYSSTEAhGMTFID 314
|
330 340 350
....*....|....*....|....*....|....*...
gi 2217275610 380 SKTIKLKPSSLGKPLPPYIvQIVDENSNLLPPGEEGNI 417
Cdd:PRK13390 315 SPDWLAHPGSVGRSVLGDL-HICDDDGNELPAGRIGTV 351
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
108-420 |
4.93e-12 |
|
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: 68.26 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 108 LSHGDRLMIILPPTpeAYWIC--LACVRLGITFVPGSPQLTAKKIRYQLRMSKAQ-CIV----ANEAMAPVVNSAVSDCP 180
Cdd:cd05932 28 LEPGSKIALISKNC--AEWFItdLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKaLFVgkldDWKAMAPGVPEGLISIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 181 TLktkLLVSDKSYDGWLDfkkLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPK--MVEYSQYGLGmgfSQASRRWMDLQ 258
Cdd:cd05932 106 LP---PPSAANCQYQWDD---LIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKgvMLTFGSFAWA---AQAGIEHIGTE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 259 PTDVLWSLgdafggsLSLSAV-------LGTWFQGACVFLC------------HMPTF------------------CPET 301
Cdd:cd05932 177 ENDRMLSY-------LPLAHVtervfveGGSLYGGVLVAFAesldtfvedvqrARPTLffsvprlwtkfqqgvqdkIPQQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 302 VLNVLSRFPITTlsanpemyqELLQHKCFTSYrfkSLKQC-VAAGG--PISPGVIeDWKRITKLDIYEGYGQTETGLLCA 378
Cdd:cd05932 250 KLNLLLKIPVVN---------SLVKRKVLKGL---GLDQCrLAGCGsaPVPPALL-EWYRSLGLNILEAYGMTENFAYSH 316
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2217275610 379 TSKTIKLKPSSLGKPLPPYIVQIvdensnllppGEEGNIAIR 420
Cdd:cd05932 317 LNYPGRDKIGTVGNAGPGVEVRI----------SEDGEILVR 348
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
215-420 |
6.22e-12 |
|
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: 67.74 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 215 TKSQDPMAIFFTKGTTGAPKMVEYSQYGLgMGFSQASRRWMDLQPTDVLWS---LGDAFGGSLSLSAVLGTwfqGACVFL 291
Cdd:cd05909 144 VQPDDPAVILFTSGSEGLPKGVVLSHKNL-LANVEQITAIFDPNPEDVVFGalpFFHSFGLTGCLWLPLLS---GIKVVF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 292 CHMPTFcPETVLNVLSRFPITTLSANPEMYQELLQHKcfTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQT 371
Cdd:cd05909 220 HPNPLD-YKKIPELIYDKKATILLGTPTFLRGYARAA--HPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTT 296
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217275610 372 ETG-LLCATSKTIKLKPSSLGKPLPPYIVQIVD-ENSNLLPPGEEGNIAIR 420
Cdd:cd05909 297 ECSpVISVNTPQSPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVR 347
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
216-419 |
6.98e-12 |
|
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: 67.57 E-value: 6.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 216 KSQDPMAIFFTKGTTGAPK--MVEYS-------QYGLGMGFSQASRrwmdlqptdVLWSLGDAFGgsLSLSAVLGTWFQG 286
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKgvVIEHRalstsalAHGRALGLTSESR---------VLQFASYTFD--VSILEIFTTLAAG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 287 ACVflchmptfC-P--ETVLNVLSRFpITTLSAN-----PEMyQELLQHKCFTsyrfkSLKQCVAAGGPISPGVIEDWkr 358
Cdd:cd05918 173 GCL--------CiPseEDRLNDLAGF-INRLRVTwafltPSV-ARLLDPEDVP-----SLRTLVLGGEALTQSDVDTW-- 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217275610 359 ITKLDIYEGYGQTETGLLCATSKTIKL-KPSSLGKPLP--PYIVQIVDENSnLLPPGEEGNIAI 419
Cdd:cd05918 236 ADRVRLINAYGPAECTIAATVSPVVPStDPRNIGRPLGatCWVVDPDNHDR-LVPIGAVGELLI 298
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
108-420 |
7.65e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 67.62 E-value: 7.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 108 LSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANeAMAPVVNSAVS-DCPTLKTKL 186
Cdd:PRK09274 63 IGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGI-PKAHLARRLFGwGKPSVRRLV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 187 LVSDKSYDGWLDFKKLIQVAPPKQTYMR-TKSQDPMAIFFTKGTTGAPKMVEYSQyglGMGFSQ--ASRRWMDLQPTDV- 262
Cdd:PRK09274 142 TVGGRLLWGGTTLATLLRDGAAAPFPMAdLAPDDMAAILFTSGSTGTPKGVVYTH---GMFEAQieALREDYGIEPGEId 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 263 -----LWSLgdaFGGSLSLSAVLGtwfqgacvflcHM----PTFC-PETVLNVLSRFPITTLSANPEMYQELLQHKCFTS 332
Cdd:PRK09274 219 lptfpLFAL---FGPALGMTSVIP-----------DMdptrPATVdPAKLFAAIERYGVTNLFGSPALLERLGRYGEANG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 333 YRFKSLKQCVAAGGPISPGVIEdwkRITKL-----DIYEGYGQTE----------TGLLCATSKTIKLKPSSLGKPLPPY 397
Cdd:PRK09274 285 IKLPSLRRVISAGAPVPIAVIE---RFRAMlppdaEILTPYGATEalpissiesrEILFATRAATDNGAGICVGRPVDGV 361
|
330 340 350
....*....|....*....|....*....|..
gi 2217275610 398 ---IVQIVDE------NSNLLPPGEEGNIAIR 420
Cdd:PRK09274 362 evrIIAISDApipewdDALRLATGEIGEIVVA 393
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
111-420 |
9.23e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 67.22 E-value: 9.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 111 GDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSDCPTLKTKLLVSD 190
Cdd:PRK07798 53 GDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVED 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 191 KS----YDGWLDFKKLIQVAPPKQTyMRTKSQDPMAIFFTKGTTGAPKMVEYSQ---YGLGMGfsqaSRRWMDLQPTDVL 263
Cdd:PRK07798 133 GSgndlLPGAVDYEDALAAGSPERD-FGERSPDDLYLLYTGGTTGMPKGVMWRQediFRVLLG----GRDFATGEPIEDE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 264 WSL---GDAFGGSL-----------SLSAVLGTWFQGACVFLCHMPTFCPETVLNVLSRFPITTLS------ANPeMYQE 323
Cdd:PRK07798 208 EELakrAAAGPGMRrfpapplmhgaGQWAAFAALFSGQTVVLLPDVRFDADEVWRTIEREKVNVITivgdamARP-LLDA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 324 LLQHKcftSYRFKSLKQCVAAGGPISPGVIEDW-KRITKLDIYEGYGQTETGLlCATSKTIKlKPSSLGKP---LPPYIV 399
Cdd:PRK07798 287 LEARG---PYDLSSLFAIASGGALFSPSVKEALlELLPNVVLTDSIGSSETGF-GGSGTVAK-GAVHTGGPrftIGPRTV 361
|
330 340
....*....|....*....|...
gi 2217275610 400 qIVDENSNLLPPGEE--GNIAIR 420
Cdd:PRK07798 362 -VLDEDGNPVEPGSGeiGWIARR 383
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
82-419 |
1.08e-11 |
|
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: 66.93 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 82 EEDKWSFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQC 161
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 162 IVANEAMApvvNSAVSDCPTLKTKLLVSDKSYDgwldfkkliQVAPPkqtymrTKSQDPMAIFFTKGTTGAPKMVEYSQY 241
Cdd:cd12116 88 VLTDDALP---DRLPAGLPVLLLALAAAAAAPA---------APRTP------VSPDDLAYVIYTSGSTGRPKGVVVSHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 242 GLgMGFSQASRRWMDLQPTDVLWSLGD-AFggSLSLSAVLGTWFQGACVFLCHMPTFC-PETVLNVLSRFPITTLSANPE 319
Cdd:cd12116 150 NL-VNFLHSMRERLGLGPGDRLLAVTTyAF--DISLLELLLPLLAGARVVIAPRETQRdPEALARLIEAHSITVMQATPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 320 MYQELLQHKCFTSYRFKSLkqcvaAGG-PISPGVIEdwkRITKL--DIYEGYGQTETGLL-CATSKTIKLKPSSLGKPLP 395
Cdd:cd12116 227 TWRMLLDAGWQGRAGLTAL-----CGGeALPPDLAA---RLLSRvgSLWNLYGPTETTIWsTAARVTAAAGPIPIGRPLA 298
|
330 340
....*....|....*....|....
gi 2217275610 396 PYIVQIVDENSNLLPPGEEGNIAI 419
Cdd:cd12116 299 NTQVYVLDAALRPVPPGVPGELYI 322
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
180-420 |
1.24e-11 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 67.14 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 180 PTLKTKLLVSDKSYDGWLDFKKLIQ--VAPPKQTYMRTKSQ----DPMAIFFTKGTTGAPKMVEYSQYG-LGMGFSQASR 252
Cdd:PRK08315 155 PELRRVIFLGDEKHPGMLNFDELLAlgRAVDDAELAARQATldpdDPINIQYTSGTTGFPKGATLTHRNiLNNGYFIGEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 253 rwMDLQPTDVLW---SLGDAFGGSLslsAVLGTWFQGAC-VFLchMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHK 328
Cdd:PRK08315 235 --MKLTEEDRLCipvPLYHCFGMVL---GNLACVTHGATmVYP--GEGFDPLATLAAVEEERCTALYGVPTMFIAELDHP 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 329 CFTSYRFKSLKQCVAAGgpiSPGVIEDWKR-ITKLDIYE---GYGQTETG-LLCATSKT--IKLKPSSLGKPLPPYIVQI 401
Cdd:PRK08315 308 DFARFDLSSLRTGIMAG---SPCPIEVMKRvIDKMHMSEvtiAYGMTETSpVSTQTRTDdpLEKRVTTVGRALPHLEVKI 384
|
250 260
....*....|....*....|
gi 2217275610 402 VD-ENSNLLPPGEEGNIAIR 420
Cdd:PRK08315 385 VDpETGETVPRGEQGELCTR 404
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
86-420 |
1.38e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 66.55 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 86 WSFERMTQLSKKAASILSDtCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQC-IVA 164
Cdd:PRK06188 38 LTYGQLADRISRYIQAFEA-LGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTlIVD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 165 NEAMAPVVNSAVSDCPTLKTKLLVSDksYDGWLDFKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVE-YSQYGL 243
Cdd:PRK06188 117 PAPFVERALALLARVPSLKHVLTLGP--VPDGVDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMgTHRSIA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 244 GMGFSQ-ASRRWMD----LQPTdvlwSLGDAfGGSLslsaVLGTWFQGACVFLChmPTFCPETVLNVLSRFPITTLSANP 318
Cdd:PRK06188 195 TMAQIQlAEWEWPAdprfLMCT----PLSHA-GGAF----FLPTLLRGGTVIVL--AKFDPAEVLRAIEEQRITATFLVP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 319 EMYQELLQHKCFTSYRFKSLKQCVAAGGPISPG-VIEDWKRITKLdIYEGYGQTETGLLCATSKTIKLKP------SSLG 391
Cdd:PRK06188 264 TMIYALLDHPDLRTRDLSSLETVYYGASPMSPVrLAEAIERFGPI-FAQYYGQTEAPMVITYLRKRDHDPddpkrlTSCG 342
|
330 340
....*....|....*....|....*....
gi 2217275610 392 KPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK06188 343 RPTPGLRVALLDEDGREVAQGEVGEICVR 371
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
87-420 |
1.99e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 66.38 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 87 SFERMTQLSKKAASILSDTCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANE 166
Cdd:PRK12492 51 SYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 167 AMAPVVNSAVSDC--------------PTLK----------TKLLVSDKSYDGWLDFKKLIQVAPPKQTYMRTKSQDPMA 222
Cdd:PRK12492 131 MFGKLVQEVLPDTgieylieakmgdllPAAKgwlvntvvdkVKKMVPAYHLPQAVPFKQALRQGRGLSLKPVPVGLDDIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 223 IF-FTKGTTGAPK--MVEYSQYGLGMGFSQASRRWMDLQPTDVLWSLGDAFGGSLSLSAVLGtwFQGACvfLCHM----- 294
Cdd:PRK12492 211 VLqYTGGTTGLAKgaMLTHGNLVANMLQVRACLSQLGPDGQPLMKEGQEVMIAPLPLYHIYA--FTANC--MCMMvsgnh 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 295 ----------PTFCPEtvlnvLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDI 364
Cdd:PRK12492 287 nvlitnprdiPGFIKE-----LGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTI 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217275610 365 YEGYGQTETG-LLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK12492 362 VEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIK 418
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
85-420 |
2.28e-11 |
|
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: 65.84 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 85 KWSFERMTQLSKKAASILSDtCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVa 164
Cdd:cd17640 5 RITYKDLYQEILDFAAGLRS-LGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 165 neamapVVNSavsdcptlktkllvsdksydgwldfkkliqvappkqtymrtkSQDPMAIFFTKGTTGAPKMVEYSQYGLG 244
Cdd:cd17640 83 ------VEND------------------------------------------SDDLATIIYTSGTTGNPKGVMLTHANLL 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 245 MGFSQASRrWMDLQPTDVLWSlgdafggslslsaVLGTW--FQGAC---VFLCHMPTFC--PETVLNVLSRFPITTLSAN 317
Cdd:cd17640 115 HQIRSLSD-IVPPQPGDRFLS-------------ILPIWhsYERSAeyfIFACGCSQAYtsIRTLKDDLKRVKPHYIVSV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 318 PEMYQEL---LQHKCFTSYRFKS-----------LKQCVAAGGPISPGViEDWKRITKLDIYEGYGQTETGLLCATSKTI 383
Cdd:cd17640 181 PRLWESLysgIQKQVSKSSPIKQflflfflsggiFKFGISGGGALPPHV-DTFFEAIGIEVLNGYGLTETSPVVSARRLK 259
|
330 340 350
....*....|....*....|....*....|....*...
gi 2217275610 384 KLKPSSLGKPLPPYIVQIVDENSN-LLPPGEEGNIAIR 420
Cdd:cd17640 260 CNVRGSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVR 297
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
111-420 |
7.43e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 64.38 E-value: 7.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 111 GDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEA-----MAPVVNSAVSDC-PTLKT 184
Cdd:PRK06164 60 GDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGfkgidFAAILAAVPPDAlPPLRA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 185 KLLVSDKSYD-------GWLDFKKLIQVAPPKQTYMRTKSQDPMAIFFT-KGTTGAPKMVEYSQYGLgMGFSQASRRWMD 256
Cdd:PRK06164 140 IAVVDDAADAtpapapgARVQLFALPDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATL-LRHARAIARAYG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 257 LQPTDVLWSLGdAFGGSLSLSAVLGTWFQGACVFLchMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKCfTSYRFK 336
Cdd:PRK06164 219 YDPGAVLLAAL-PFCGVFGFSTLLGALAGGAPLVC--EPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAG-ERADFP 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 337 SLKQC-VAAGGPISPGVIEdWKRITKLDIYEGYGQTETGLLCAtsktikLKPSSL---------GKPLPPYI-VQIVD-E 404
Cdd:PRK06164 295 SARLFgFASFAPALGELAA-LARARGVPLTGLYGSSEVQALVA------LQPATDpvsvrieggGRPASPEArVRARDpQ 367
|
330
....*....|....*.
gi 2217275610 405 NSNLLPPGEEGNIAIR 420
Cdd:PRK06164 368 DGALLPDGESGEIEIR 383
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
87-420 |
7.66e-11 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 64.48 E-value: 7.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 87 SFERMTQLSKKAASILSDTCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRmskaQCivaNE 166
Cdd:PLN02574 68 SYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVV----DC---SV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 167 AMAPVVNSAVSDCPTLKTKLLVSDKSYD------GWLDFKKLIQ------VAPPkqtymrTKSQDPMAIFFTKGTTGAPK 234
Cdd:PLN02574 141 GLAFTSPENVEKLSPLGVPVIGVPENYDfdskriEFPKFYELIKedfdfvPKPV------IKQDDVAAIMYSSGTTGASK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 235 MV-----------------EYSQYGlgmgFSQASRRWMDLQPTDVLWSLGDAFGGSLSLsavlgtwfqGACVFLchMPTF 297
Cdd:PLN02574 215 GVvlthrnliamvelfvrfEASQYE----YPGSDNVYLAALPMFHIYGLSLFVVGLLSL---------GSTIVV--MRRF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 298 CPETVLNVLSRFPITTLSANPEMYQELLQH-KCFTSYRFKSLKQCVAAGGPISPGVIEDW-KRITKLDIYEGYGQTET-- 373
Cdd:PLN02574 280 DASDMVKVIDRFKVTHFPVVPPILMALTKKaKGVCGEVLKSLKQVSCGAAPLSGKFIQDFvQTLPHVDFIQGYGMTESta 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2217275610 374 -GLLCATSKTIKlKPSSLGKPLPPYIVQIVD-ENSNLLPPGEEGNIAIR 420
Cdd:PLN02574 360 vGTRGFNTEKLS-KYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQ 407
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
217-417 |
8.49e-11 |
|
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: 63.65 E-value: 8.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 217 SQDPMAIFFTKGTTGAPKMVEYSQYGlgmgfsQASRRWM-----DLQPTDVLWSLGDAFGGSLSLSAVLGTWFQGACVFL 291
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSN------EVYNAWMlalnsLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 292 CHMPTFCPETVLN----VLSRFPITTLSANPEMYQELLQHKcfTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEG 367
Cdd:cd05944 75 AGPAGYRNPGLFDnfwkLVERYRITSLSTVPTVYAALLQVP--VNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217275610 368 YGQTETGllCATSKTIK---LKPSSLGKPLPPYIVQIVDENSN---LLP--PGEEGNI 417
Cdd:cd05944 153 YGLTEAT--CLVAVNPPdgpKRPGSVGLRLPYARVRIKVLDGVgrlLRDcaPDEVGEI 208
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
113-419 |
8.72e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.98 E-value: 8.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 113 RLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSdcptLKTKLLVSDKS 192
Cdd:PRK12316 4603 LVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPDG----LASLALDRDED 4678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 193 YDGWLDFKKLIQVAPPKQTYmrtksqdpmaIFFTKGTTGAPKMVEYSQYGLgMGFSQASRRWMDLQPTD-VLWSLGDAFG 271
Cdd:PRK12316 4679 WEGFPAHDPAVRLHPDNLAY----------VIYTSGSTGRPKGVAVSHGSL-VNHLHATGERYELTPDDrVLQFMSFSFD 4747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 272 GS-LSLSAVLGTwfqGACVFLCHMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKCfTSYRFKSLKQCVAAGGPISP 350
Cdd:PRK12316 4748 GShEGLYHPLIN---GASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPPSLRVYCFGGEAVAQ 4823
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217275610 351 GVIEDWKRITKLD-IYEGYGQTETGLLCATSKTIKLKPSS-----LGKPLPPYIVQIVDENSNLLPPGEEGNIAI 419
Cdd:PRK12316 4824 ASYDLAWRALKPVyLFNGYGPTETTVTVLLWKARDGDACGaaympIGTPLGNRSGYVLDGQLNPLPVGVAGELYL 4898
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
215-420 |
1.19e-10 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 64.17 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 215 TKSQDPMAIFFTKGTTGAPKMVEYSQYGLgMGFSQASRRWMDLQPTDVLWS---LGDAFGGSLSLSAVLGTWFQGACV-- 289
Cdd:PRK08633 779 FKPDDTATIIFSSGSEGEPKGVMLSHHNI-LSNIEQISDVFNLRNDDVILSslpFFHSFGLTVTLWLPLLEGIKVVYHpd 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 290 -----------------FLCHMPTFCpetvlnvlsRFPITTLSANPEMyqellqhkcftsyrFKSLKQCVAAGGPISPGV 352
Cdd:PRK08633 858 ptdalgiaklvakhratILLGTPTFL---------RLYLRNKKLHPLM--------------FASLRLVVAGAEKLKPEV 914
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217275610 353 IEDWKRITKLDIYEGYGQTETGLLCA----------TSKTIKLKPSSLGKPLPPYIVQIVD-ENSNLLPPGEEGNIAIR 420
Cdd:PRK08633 915 ADAFEEKFGIRILEGYGATETSPVASvnlpdvlaadFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIG 993
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
111-427 |
1.91e-10 |
|
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: 63.06 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 111 GDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVvnSAVSDCPTLKTkllvsd 190
Cdd:cd17646 48 EDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTTADLAAR--LPAGGDVALLG------ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 191 ksYDGWLDFkkliQVAPPKQTYmrtKSQDPMAIFFTKGTTGAPKMVEYSQYGLgmgfsqASR-RWM----DLQPTDVLws 265
Cdd:cd17646 120 --DEALAAP----PATPPLVPP---RPDNLAYVIYTSGSTGRPKGVMVTHAGI------VNRlLWMqdeyPLGPGDRV-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 266 LGDA-FGGSLSLSAVLGTWFQGACVFLC----HMPtfcPETVLNVLSRFPITTLSANPEMYQELLQHKcfTSYRFKSLKQ 340
Cdd:cd17646 183 LQKTpLSFDVSVWELFWPLVAGARLVVArpggHRD---PAYLAALIREHGVTTCHFVPSMLRVFLAEP--AAGSCASLRR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 341 CVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGL---LCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNI 417
Cdd:cd17646 258 VFCSGEALPPELAARFLALPGAELHNLYGPTEAAIdvtHWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGEL 337
|
330
....*....|....*.
gi 2217275610 418 AI------RIKLNQPA 427
Cdd:cd17646 338 YLggvqlaRGYLGRPA 353
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
108-420 |
5.03e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 61.98 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 108 LSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSDCPTLKTKll 187
Cdd:PRK07470 54 VRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHV-- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 188 VSDKSYDGWLDFKKLIQVAPPKQTYMRTKSQD-PMAIFFTKGTTGAPK--MVEYSQyglgMGFSQASrRWMDLQP----T 260
Cdd:PRK07470 132 VAIGGARAGLDYEALVARHLGARVANAAVDHDdPCWFFFTSGTTGRPKaaVLTHGQ----MAFVITN-HLADLMPgtteQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 261 DVlwSLGDAfggSLSLSAVLGTWFQ---GACVFLCHMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKS 337
Cdd:PRK07470 207 DA--SLVVA---PLSHGAGIHQLCQvarGAATVLLPSERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 338 LKQCVAAGGPIspgVIEDWKR-ITKLD--IYEGYGQTE-TGllcatskTIKLKPSSL--------------GKPLPPYIV 399
Cdd:PRK07470 282 LRYVIYAGAPM---YRADQKRaLAKLGkvLVQYFGLGEvTG-------NITVLPPALhdaedgpdarigtcGFERTGMEV 351
|
330 340
....*....|....*....|.
gi 2217275610 400 QIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK07470 352 QIQDDEGRELPPGETGEICVI 372
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
111-419 |
5.38e-10 |
|
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: 61.45 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 111 GDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVnsavsDCPTLKTKLLVSD 190
Cdd:cd12117 47 GDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTDRSLAGRA-----GGLEVAVVIDEAL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 191 KSYDGwldfkkliqvAPPKqtymRTKSQDPMA-IFFTKGTTGAPKMVEYSQYG---LGMGfsqasRRWMDLQPTDVLwsl 266
Cdd:cd12117 122 DAGPA----------GNPA----VPVSPDDLAyVMYTSGSTGRPKGVAVTHRGvvrLVKN-----TNYVTLGPDDRV--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 267 gdAFGGSLSLSA----VLGTWFQGACVFLCHmptfcPETVLN------VLSRFPITTLSANPEMYQELLQH--KCFTSYR 334
Cdd:cd12117 180 --LQTSPLAFDAstfeIWGALLNGARLVLAP-----KGTLLDpdalgaLIAEEGVTVLWLTAALFNQLADEdpECFAGLR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 335 fkslkqCVAAGG-PISPG----VIEDWKRITkldIYEGYGQTETgLLCATSKTIK---LKPSSL--GKPLPPYIVQIVDE 404
Cdd:cd12117 253 ------ELLTGGeVVSPPhvrrVLAACPGLR---LVNGYGPTEN-TTFTTSHVVTeldEVAGSIpiGRPIANTRVYVLDE 322
|
330
....*....|....*
gi 2217275610 405 NSNLLPPGEEGNIAI 419
Cdd:cd12117 323 DGRPVPPGVPGELYV 337
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
113-427 |
9.01e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.90 E-value: 9.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 113 RLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMapvvnSAVSDCPTLKTKLLVSDKs 192
Cdd:PRK12316 2055 RVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHL-----LERLPLPAGVARLPLDRD- 2128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 193 yDGWLDFkkliqvaPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLGMgFSQASRRWMDLQPTD-VLWSLGDAFG 271
Cdd:PRK12316 2129 -AEWADY-------PDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVA-HCQAAGERYELSPADcELQFMSFSFD 2199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 272 GSLSlsavlgTWF----QGACVFLCHMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHkCFTSYRFKSLKQCVAAGGP 347
Cdd:PRK12316 2200 GAHE------QWFhpllNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEH-AERDGRPPAVRVYCFGGEA 2272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 348 ISPGVIEDWKRITKLD-IYEGYGQTETGLLCATSKTIKLKPSS-----LGKPLPPYIVQIVDENSNLLPPGEEGNIAI-- 419
Cdd:PRK12316 2273 VPAASLRLAWEALRPVyLFNGYGPTEAVVTPLLWKCRPQDPCGaayvpIGRALGNRRAYILDADLNLLAPGMAGELYLgg 2352
|
330
....*....|..
gi 2217275610 420 ----RIKLNQPA 427
Cdd:PRK12316 2353 eglaRGYLNRPG 2364
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
94-420 |
1.22e-09 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 60.76 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 94 LSKKAASILSDTcALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVN 173
Cdd:PLN02246 59 LSRRVAAGLHKL-GIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 174 SAVSDCPtlkTKLLVSDKSYDGWLDFKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLGMGFSQAsrr 253
Cdd:PLN02246 138 GLAEDDG---VTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQ--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 254 wMDLQPTDVLWSLGDAFGGSL------SLSAVLGTWFQ-GACVFLchMPTFCPETVLNVLSRFPITTLSANPEMYQELLQ 326
Cdd:PLN02246 212 -VDGENPNLYFHSDDVILCVLpmfhiySLNSVLLCGLRvGAAILI--MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 327 HKCFTSYRFKSLKQCVAAGGPISPGvIEDWKRiTKLD---IYEGYGQTETGLLCATS----KT-IKLKPSSLGKPLPPYI 398
Cdd:PLN02246 289 SPVVEKYDLSSIRMVLSGAAPLGKE-LEDAFR-AKLPnavLGQGYGMTEAGPVLAMClafaKEpFPVKSGSCGTVVRNAE 366
|
330 340
....*....|....*....|...
gi 2217275610 399 VQIVD-ENSNLLPPGEEGNIAIR 420
Cdd:PLN02246 367 LKIVDpETGASLPRNQPGEICIR 389
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
324-420 |
1.80e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 60.16 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 324 LLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGLLCATSKTIKLKPSSLGKPLPPYIVQIVD 403
Cdd:PRK05677 314 LCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVID 393
|
90
....*....|....*..
gi 2217275610 404 ENSNLLPPGEEGNIAIR 420
Cdd:PRK05677 394 DDGNELPLGEVGELCVK 410
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
85-420 |
2.12e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 59.82 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 85 KWSFERMTQLSKKAASILSdTCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVA 164
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLR-RRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 165 NEAMApvvnsavsdcptlktkllvsDKSYDGwLDFKKLIQVAPpKQTYMRTKSQDPMA---IFFTKGTTGAPKMVEYSQY 241
Cdd:PRK09088 101 DDAVA--------------------AGRTDV-EDLAAFIASAD-ALEPADTPSIPPERvslILFTSGTSGQPKGVMLSER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 242 GLgmgfSQASRRWMDLQPTDVLWS-LGDA-----FGGSLSLSAVLgtwFQGACVFLChmPTFCPETVLNVLS--RFPITT 313
Cdd:PRK09088 159 NL----QQTAHNFGVLGRVDAHSSfLCDApmfhiIGLITSVRPVL---AVGGSILVS--NGFEPKRTLGRLGdpALGITH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 314 LSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIEDWkritkLD----IYEGYGQTETGL---LCATSKTIKLK 386
Cdd:PRK09088 230 YFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGW-----LDdgipMVDGFGMSEAGTvfgMSVDCDVIRAK 304
|
330 340 350
....*....|....*....|....*....|....
gi 2217275610 387 PSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:PRK09088 305 AGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLR 338
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
93-420 |
3.52e-09 |
|
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: 58.99 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 93 QLSKKAA--SILSDTCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQcivaneamap 170
Cdd:cd05914 12 DLADNIAkfALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 171 vvnsavsdcptlktKLLVSDKsydgwldfkkliqvappkqtymrtksQDPMAIFFTKGTTGAPK--MVEYSQYglgMGFS 248
Cdd:cd05914 82 --------------AIFVSDE--------------------------DDVALINYTSGTTGNSKgvMLTYRNI---VSNV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 249 QASRRWMDLQPTDVLWS---LGDAFGgsLSLSAVLGTWFQGACVFLCHMPTfcpeTVLNVLSRFPITTLSANPEMYQ--- 322
Cdd:cd05914 119 DGVKEVVLLGKGDKILSilpLHHIYP--LTFTLLLPLLNGAHVVFLDKIPS----AKIIALAFAQVTPTLGVPVPLViek 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 323 ----ELLQHKCFTSYRFK------------------------SLKQCVAAGGPISPGVIEDWKRItKLDIYEGYGQTETG 374
Cdd:cd05914 193 ifkmDIIPKLTLKKFKFKlakkinnrkirklafkkvheafggNIKEFVIGGAKINPDVEEFLRTI-GFPYTIGYGMTETA 271
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2217275610 375 LLCATSKTIKLKPSSLGKPLPPYIVQIVDENsnllPPGEEGNIAIR 420
Cdd:cd05914 272 PIISYSPPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVR 313
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
129-419 |
4.29e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 59.40 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 129 LACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMApvvnsAVSDCPTLKTKLLVSDKSydgwldfkKLIQVAPP 208
Cdd:PRK12467 580 LAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLL-----AQLPVPAGLRSLCLDEPA--------DLLCGYSG 646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 209 KQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLgMGFSQASRRWMDLQPTDVlWSLGDAFGGSLSLSAVLGTWFQGAC 288
Cdd:PRK12467 647 HNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGAL-ANYVCVIAERLQLAADDS-MLMVSTFAFDLGVTELFGALASGAT 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 289 VFLC-HMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRfkSLKQCVAAGGPISPGVIEDWKRIT-KLDIYE 366
Cdd:PRK12467 725 LHLLpPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPR--PQRALVCGGEALQVDLLARVRALGpGARLIN 802
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217275610 367 GYGQTETGLLCATsKTIKLKP-----SSLGKPLPPYIVQIVDENSNLLPPGEEGNIAI 419
Cdd:PRK12467 803 HYGPTETTVGVST-YELSDEErdfgnVPIGQPLANLGLYILDHYLNPVPVGVVGELYI 859
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
26-420 |
6.62e-09 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 58.42 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 26 QKCATQTI---RPPDSRCLVQAVSqnfNFAKDVLDQWsqLEKdglRGPYPALWKVSAK-GEEDKWSFERMTQLSKKAASI 101
Cdd:PRK10524 29 QTPFTQVLdysNPPFARWFVGGRT---NLCHNAVDRH--LAK---RPEQLALIAVSTEtDEERTYTFRQLHDEVNRMAAM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 102 LSDTcALSHGDRLMIILPPTPEAYWICLACVRLGI--TFVPG---SPQLTAkkiryqlRMSKAQ--CIVANEAMA----- 169
Cdd:PRK10524 101 LRSL-GVQRGDRVLIYMPMIAEAAFAMLACARIGAihSVVFGgfaSHSLAA-------RIDDAKpvLIVSADAGSrggkv 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 170 ----PVVNSAVSDCPTLKTKLLVSDKsydGWLDFKKL----IQVAPPKQTYMRTK-------SQDPMAIFFTKGTTGAPK 234
Cdd:PRK10524 173 vpykPLLDEAIALAQHKPRHVLLVDR---GLAPMARVagrdVDYATLRAQHLGARvpvewleSNEPSYILYTSGTTGKPK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 235 MVeysQYGLGmGFSQASRRWMDL----QPTDVLWSLGD---AFGGSLSLSAVL------------------GTWFQgacv 289
Cdd:PRK10524 250 GV---QRDTG-GYAVALATSMDTifggKAGETFFCASDigwVVGHSYIVYAPLlagmatimyeglptrpdaGIWWR---- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 290 fLC------HMptFCPETVLNVLSRFPittlsanPEmyqellqhkCFTSYRFKSLKQCVAAGGP--------ISPGVied 355
Cdd:PRK10524 322 -IVekykvnRM--FSAPTAIRVLKKQD-------PA---------LLRKHDLSSLRALFLAGEPldeptaswISEAL--- 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 356 wkritKLDIYEGYGQTETGL-LCATSKTIKLKPSSLGKPLPP---YIVQIVDENS-NLLPPGEEGNIAIR 420
Cdd:PRK10524 380 -----GVPVIDNYWQTETGWpILAIARGVEDRPTRLGSPGVPmygYNVKLLNEVTgEPCGPNEKGVLVIE 444
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
87-377 |
1.65e-08 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 56.95 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 87 SFERMTQLskkAASILSdtCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANE 166
Cdd:PLN03102 45 TYDRCCRL---AASLIS--LNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 167 AMAPVVNSAVSDCPTLKTKL-----LVSD-----KSYDGWLDFKKLIQVAPPK-----QTYMRTKSQDPMAIFFTKGTTG 231
Cdd:PLN03102 120 SFEPLAREVLHLLSSEDSNLnlpviFIHEidfpkRPSSEELDYECLIQRGEPTpslvaRMFRIQDEHDPISLNYTSGTTA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 232 APKMVEYSQYGLGMGFSQASRRW-MDLQPTdVLWSLG----DAFGGSLSLSAVLGTwfqgacvFLCHMPTFCPETVLNVl 306
Cdd:PLN03102 200 DPKGVVISHRGAYLSTLSAIIGWeMGTCPV-YLWTLPmfhcNGWTFTWGTAARGGT-------SVCMRHVTAPEIYKNI- 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217275610 307 SRFPITTLSANPEMYQELLQHKCfTSYRFKSLKQCVAAGGPISPGVIedWKRITKL--DIYEGYGQTE-TG--LLC 377
Cdd:PLN03102 271 EMHNVTHMCCVPTVFNILLKGNS-LDLSPRSGPVHVLTGGSPPPAAL--VKKVQRLgfQVMHAYGLTEaTGpvLFC 343
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
74-407 |
4.85e-08 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 55.67 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 74 LWKVSAKGEEDKWSFERMTQLSKKAASILSDTcALSHGDRLMIILPPTPEAYWICLACVRLG----ITFVPGSPQLTAKK 149
Cdd:PLN02654 109 YWEGNEPGFDASLTYSELLDRVCQLANYLKDV-GVKKGDAVVIYLPMLMELPIAMLACARIGavhsVVFAGFSAESLAQR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 150 I--------------RYQLRMSKAQCIVaNEAMAPVVNSAVS--DCPTLKTKLLV---SDKSYDG----WLDFkklIQVA 206
Cdd:PLN02654 188 IvdckpkvvitcnavKRGPKTINLKDIV-DAALDESAKNGVSvgICLTYENQLAMkreDTKWQEGrdvwWQDV---VPNY 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 207 PPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLgMGFSQASRRW-MDLQPTDVLWSLGD----------AFGGSLS 275
Cdd:PLN02654 264 PTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGY-MVYTATTFKYaFDYKPTDVYWCTADcgwitghsyvTYGPMLN 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 276 LSAVLgtWFQGAcvflchmPTFcPET--VLNVLSRFPITTLSANPEMYQELLQH--KCFTSYRFKSLKQCVAAGGPISPG 351
Cdd:PLN02654 343 GATVL--VFEGA-------PNY-PDSgrCWDIVDKYKVTIFYTAPTLVRSLMRDgdEYVTRHSRKSLRVLGSVGEPINPS 412
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217275610 352 -------VIEDwkriTKLDIYEGYGQTETG--LLCATSKTIKLKPSSlgKPLPPYIVQ--IVDENSN 407
Cdd:PLN02654 413 awrwffnVVGD----SRCPISDTWWQTETGgfMITPLPGAWPQKPGS--ATFPFFGVQpvIVDEKGK 473
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
118-293 |
5.30e-08 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 55.21 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 118 LPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAM----------APVVNSAVSDC---PTLKT 184
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVlrggralplySKVVEAAPAKAivlPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 185 KLLVSDKSYD-GWLDFkkLIQVAPPKQT---YMRTKSQD---PMAIFFTKGTTGAPKMVEYSQYGlgmGFSQASRRW--M 255
Cdd:PLN03051 81 PVAVPLREQDlSWCDF--LGVAAAQGSVggnEYSPVYAPvesVTNILFSSGTTGEPKAIPWTHLS---PLRCASDGWahM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217275610 256 DLQPTDVL-W--SLGDAFGGSLSLSAvlgtWFQGACVFLCH 293
Cdd:PLN03051 156 DIQPGDVVcWptNLGWMMGPWLLYSA----FLNGATLALYG 192
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
223-405 |
6.00e-08 |
|
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: 54.64 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 223 IFFTKGTTGAPKMVEYSQYGLGMGFsQASRRWMDLQPTDVlWSLgdafggSLSLSAVLGTWFQGACVFLCHMPTFCPETV 302
Cdd:cd17630 5 VILTSGSTGTPKAVVHTAANLLASA-AGLHSRLGFGGGDS-WLL------SLPLYHVGGLAILVRSLLAGAELVLLERNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 303 LNVLSR--FPITTLSANPEMYQELLQHKcFTSYRFKSLKQCVAAGGPISPgviEDWKRITKLDI--YEGYGQTETGLLCA 378
Cdd:cd17630 77 ALAEDLapPGVTHVSLVPTQLQRLLDSG-QGPAALKSLRAVLLGGAPIPP---ELLERAADRGIplYTTYGMTETASQVA 152
|
170 180
....*....|....*....|....*..
gi 2217275610 379 TSKTIKLKPSSLGKPLPPYIVQIVDEN 405
Cdd:cd17630 153 TKRPDGFGRGGVGVLLPGRELRIVEDG 179
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
218-420 |
7.46e-08 |
|
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: 54.19 E-value: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 218 QDPMAIFFTKGTTGAPKMVEYSQYGLGMGFSQASRRWMDLQPTDVLWSLGDAFGGSLSLSAVLGTWFQGACVFLCHMPTF 297
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 298 cpETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKqCVAAGGPIspgVIEDWKRITKL----DIYEGYGQTET 373
Cdd:cd17635 81 --KSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLR-LIGYGGSR---AIAADVRFIEAtgltNTAQVYGLSET 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2217275610 374 G-LLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:cd17635 155 GtALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIK 202
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
107-405 |
7.62e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 55.01 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 107 ALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKI-RYQLRMSKAQCIVANEAMApvvnSAVSDCPTLKTK 185
Cdd:PRK05857 62 SVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIeRFCQITDPAAALVAPGSKM----ASSAVPEALHSI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 186 LLVSDKSYDGWLDFKKLIQVAPPKqTYMRTKSQDPMAIFFTKGTTGAPKMV---EYSQYGLGMGFSQASRRWMDlqptdv 262
Cdd:PRK05857 138 PVIAVDIAAVTRESEHSLDAASLA-GNADQGSEDPLAMIFTSGTTGEPKAVllaNRTFFAVPDILQKEGLNWVT------ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 263 lWSLGDAFGGSLSLSAVLGTWFQGACVF---LCHMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLK 339
Cdd:PRK05857 211 -WVVGETTYSPLPATHIGGLWWILTCLMhggLCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLR 289
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217275610 340 qCVAAGGpiSPGVIEDWKRI--TKLDIYEGYGQTETGL--LC--ATSKTI-KLKPSSLGKPLPPYIVQIVDEN 405
Cdd:PRK05857 290 -LVGYGG--SRAIAADVRFIeaTGVRTAQVYGLSETGCtaLClpTDDGSIvKIEAGAVGRPYPGVDVYLAATD 359
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
297-417 |
1.47e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 54.16 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 297 FCPETVLNVLSRFPITTLSANPEMYQELLQH--KCFTSYRFKSLKQCVAAGGPISPGVIedwKRITKL---DIYEGYGQT 371
Cdd:PRK07788 282 FDPEATLEDIAKHKATALVVVPVMLSRILDLgpEVLAKYDTSSLKIIFVSGSALSPELA---TRALEAfgpVLYNLYGST 358
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2217275610 372 ETGLLC-ATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEGNI 417
Cdd:PRK07788 359 EVAFATiATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRI 405
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
108-420 |
1.58e-07 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 53.74 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 108 LSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSDCPTLKTKLL 187
Cdd:PRK05852 65 LLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 188 VSDKSYDGWLDFKKLIQVAP-PKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLGmgfsqASRRWM----DLQPTDV 262
Cdd:PRK05852 145 GDSGPSGGTLSVHLDAATEPtPATSTPEGLRPDDAMIMFTGGTTGLPKMVPWTHANIA-----SSVRAIitgyRLSPRDA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 263 LWSLGDAFGGSLSLSAVLGTWFQGACVFLCHMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKS----- 337
Cdd:PRK05852 220 TVAVMPLYHGHGLIAALLATLASGGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPaalrf 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 338 LKQCVAaggPISPGVIEDWKRITKLDIYEGYGQTETGLLCAT--------SKTIKLKPSSLGKPLPPYIvQIVDENSNLL 409
Cdd:PRK05852 300 IRSCSA---PLTAETAQALQTEFAAPVVCAFGMTEATHQVTTtqiegigqTENPVVSTGLVGRSTGAQI-RIVGSDGLPL 375
|
330
....*....|.
gi 2217275610 410 PPGEEGNIAIR 420
Cdd:PRK05852 376 PAGAVGEVWLR 386
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
177-373 |
2.29e-07 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 53.26 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 177 SDCPTLKTKLLVSDKSYDGWLDFKKLIQVAPPKQTYMRTKSQDP-------MAIFFTKGTTGAPKMVEYSQYGLgMGFSQ 249
Cdd:PLN02860 124 DRLPSLMWQVFLESPSSSVFIFLNSFLTTEMLKQRALGTTELDYawapddaVLICFTSGTTGRPKGVTISHSAL-IVQSL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 250 ASRRWMDLQPTDVLwsLGDA----FGGslsLSAVLGTWFQGAC-VFLchmPTFCPETVLNVLSRFPITTLSANPEMYQEL 324
Cdd:PLN02860 203 AKIAIVGYGEDDVY--LHTAplchIGG---LSSALAMLMVGAChVLL---PKFDAKAALQAIKQHNVTSMITVPAMMADL 274
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2217275610 325 LQ--HKCFTSYRFKSLKQCVAAGGPISPGVIEDWKRI-TKLDIYEGYGQTET 373
Cdd:PLN02860 275 ISltRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLfPNAKLFSAYGMTEA 326
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
219-420 |
2.88e-07 |
|
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: 52.41 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 219 DPMAIFFTKGTTGAPKmVEYSQYGLGMGFSQASRRWMDLQPTDVLWSLGdAFGGSLSLSAVLGTWFQGACVflCHMPTFC 298
Cdd:cd17633 1 NPFYIGFTSGTTGLPK-AYYRSERSWIESFVCNEDLFNISGEDAILAPG-PLSHSLFLYGAISALYLGGTF--IGQRKFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 299 PETVLNVLSRFPITTLSANPEMYQELLQHKCFTSyrfkSLKQCVAAGGPISPGVIEDWKRIT-KLDIYEGYGQTETGLLC 377
Cdd:cd17633 77 PKSWIRKINQYNATVIYLVPTMLQALARTLEPES----KIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSFIT 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2217275610 378 ATSKTIKLKPSSLGKPLPPYIVQIVDENSnllppGEEGNIAIR 420
Cdd:cd17633 153 YNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVK 190
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
129-426 |
5.43e-07 |
|
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: 51.94 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 129 LACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAvsdcptlKTKLLVSDKSydgwLDFKKLIQVAPP 208
Cdd:cd17655 65 LGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQSHLQPPIAFI-------GLIDLLDEDT----IYHEESENLEPV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 209 kqtymrTKSQDPMAIFFTKGTTGAPKMVEYSQYGLGMGFSQASRRWMDLQPTDVlwslgdAFGGSLSLSAVLGTWFQ--- 285
Cdd:cd17655 134 ------SKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRV------ALFASISFDASVTEIFAsll 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 286 -GACVFLCHMPTFCPETVL-NVLSRFPITTLSANPEMYQELLQHKCFTsyrFKSLKQCVAAGGPISPGVIEDWKRI--TK 361
Cdd:cd17655 202 sGNTLYIVRKETVLDGQALtQYIRQNRITIIDLTPAHLKLLDAADDSE---GLSLKHLIVGGEALSTELAKKIIELfgTN 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217275610 362 LDIYEGYGQTETgLLCAT------SKTIKLKPSsLGKPLPPYIVQIVDENSNLLPPGEEGNIAI------RIKLNQP 426
Cdd:cd17655 279 PTITNAYGPTET-TVDASiyqyepETDQQVSVP-IGKPLGNTRIYILDQYGRPQPVGVAGELYIggegvaRGYLNRP 353
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
186-403 |
8.34e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 51.57 E-value: 8.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 186 LLVSDKSYdgwldfKKLIQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLGM-GFSQASRRwmDLQPTDVLW 264
Cdd:PRK13388 124 LDVDTPAY------AELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFaGRALTERF--GLTRDDVCY 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 265 SLGDAFGGslslSAVLGTW----FQGACVflCHMPTFCPETVLNVLSRF----------PITTLSANPEMYQEllqhkcf 330
Cdd:PRK13388 196 VSMPLFHS----NAVMAGWapavASGAAV--ALPAKFSASGFLDDVRRYgatyfnyvgkPLAYILATPERPDD------- 262
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217275610 331 tsyRFKSLKqcVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGllCATSKTIKLKPSSLGKPLPPyiVQIVD 403
Cdd:PRK13388 263 ---ADNPLR--VAFGNEASPRDIAEFSRRFGCQVEDGYGSSEGA--VIVVREPGTPPGSIGRGAPG--VAIYN 326
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
82-246 |
8.72e-07 |
|
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: 51.52 E-value: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 82 EEDKWSFERMTQLSKKAASILSDTCALSHGDRLMIILPPTPEAYWICLACVRLG--ITFVPgsPQLTAKKIRYQLRMSKA 159
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLN--TNIRSKSLLHCFRCCGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 160 QCIVANEAMAPVVNsavSDCPTLKTK-----LLVSDKSYDGWLDFKKLIQVAP--PKQTYMRTKS--QDPMAIFFTKGTT 230
Cdd:cd05938 80 KVLVVAPELQEAVE---EVLPALRADgvsvwYLSHTSNTEGVISLLDKVDAASdePVPASLRAHVtiKSPALYIYTSGTT 156
|
170
....*....|....*.
gi 2217275610 231 GAPKMVEYSQYGLGMG 246
Cdd:cd05938 157 GLPKAARISHLRVLQC 172
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
182-395 |
9.38e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 51.63 E-value: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 182 LKTKLLVSDKSydgWLDFKKLIqvapPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQYGLGMGFSQAsRRWMDLQPTD 261
Cdd:PRK08043 336 LKDDVTTADKL---WIFAHLLM----PRLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQI-KTIADFTPND 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 262 VLWS---LGDAFGGSLSLSAVLGTwfqGACVFLCHMP-----------------TFCPETVLNVLSRFpittlsANPemy 321
Cdd:PRK08043 408 RFMSalpLFHSFGLTVGLFTPLLT---GAEVFLYPSPlhyrivpelvydrnctvLFGTSTFLGNYARF------ANP--- 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217275610 322 qellqhkcftsYRFKSLKQCVAAGGPISPGVIEDWKRITKLDIYEGYGQTETGLLCATSKTIKLKPSSLGKPLP 395
Cdd:PRK08043 476 -----------YDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILP 538
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
212-428 |
1.29e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 51.28 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 212 YMRTKSQDPMAIFFTKGTTGAPKMVEYSQYG--LGMGFSQASRRWMD-----LQPTDVLW-SLGDAFGGSLSLSAVLgTW 283
Cdd:PTZ00237 248 YVPVESSHPLYILYTSGTTGNSKAVVRSNGPhlVGLKYYWRSIIEKDiptvvFSHSSIGWvSFHGFLYGSLSLGNTF-VM 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 284 FQGACVFLCHMPTFcpetVLNVLSRFPITTLSANPEMYQELLQH-----KCFTSYRFKSLKQCVAAGGPISPGVIEDWKR 358
Cdd:PTZ00237 327 FEGGIIKNKHIEDD----LWNTIEKHKVTHTLTLPKTIRYLIKTdpeatIIRSKYDLSNLKEIWCGGEVIEESIPEYIEN 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217275610 359 ITKLDIYEGYGQTETGLLCATSKTIKLKP-SSLGKPLPPYIVQIVDENSNLLPPGEEGNIAirIKLNQPAS 428
Cdd:PTZ00237 403 KLKIKSSRGYGQTEIGITYLYCYGHINIPyNATGVPSIFIKPSILSEDGKELNVNEIGEVA--FKLPMPPS 471
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
120-407 |
1.49e-06 |
|
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: 50.55 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 120 PTPEAYWICLACVRLGITFVPGSPqltakkiryqlrMSKAQCIVaneamapvvnsavsdcpTLKTKLLVSDKSYDGWLDF 199
Cdd:cd17654 50 RGTESPVAILAILFLGAAYAPIDP------------ASPEQRSL-----------------TVMKKCHVSYLLQNKELDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 200 KKLIQVAPPKQTYMRTksQDPMA-IFFTKGTTGAPKMVEYSQYGLgMGFSQASRRWMDLQPTDVLwslgdaFGGSL---- 274
Cdd:cd17654 101 APLSFTPEHRHFNIRT--DECLAyVIHTSGTTGTPKIVAVPHKCI-LPNIQHFRSLFNITSEDIL------FLTSPltfd 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 275 -SLSAVLGTWFQGACVFLC-HMPTFCPETVLNVL-SRFPITTLSANPEMYQELLQ--HKCFTSYRFKSLKQCVAAGGPI- 348
Cdd:cd17654 172 pSVVEIFLSLSSGATLLIVpTSVKVLPSKLADILfKRHRITVLQATPTLFRRFGSqsIKSTVLSATSSLRVLALGGEPFp 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217275610 349 SPGVIEDW-KRITKLDIYEGYGQTETgllCATSKTIKLK----PSSLGKPLPPYIVQIVDENSN 407
Cdd:cd17654 252 SLVILSSWrGKGNRTRIFNIYGITEV---SCWALAYKVPeedsPVQLGSPLLGTVIEVRDQNGS 312
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
111-240 |
3.11e-06 |
|
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: 49.58 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 111 GDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPvvnsAVSDCPTLKTKLLVSd 190
Cdd:cd12114 37 GDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDGPDAQ----LDVAVFDVLILDLDA- 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2217275610 191 ksydgwldfkkliQVAPPKQTYMRTKSQDPMAIFFTKGTTGAPKMVEYSQ 240
Cdd:cd12114 112 -------------LAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISH 148
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
99-373 |
3.55e-06 |
|
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: 49.60 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 99 ASILSDTcALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAqcivaneamapvvnsavsd 178
Cdd:cd12118 43 ASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEA------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 179 cptlktKLLVSDKSYDgwldFKKLIQVAPPKQTYMRTKSQ-DPMAIFFTKGTTGAPKMVEYSQYGLGMGFSQASRRW-MD 256
Cdd:cd12118 103 ------KVLFVDREFE----YEDLLAEGDPDFEWIPPADEwDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWeMK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 257 LQPTdVLWSLGD----AFGGSLSLSAVLGTwfqgacvFLChMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKCFTS 332
Cdd:cd12118 173 QHPV-YLWTLPMfhcnGWCFPWTVAAVGGT-------NVC-LRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDA 243
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2217275610 333 YRFKSLKQCVAAGGPISPGVIEDWKRItKLDIYEGYGQTET 373
Cdd:cd12118 244 RPLPHRVHVMTAGAPPPAAVLAKMEEL-GFDVTHVYGLTET 283
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
223-426 |
5.03e-06 |
|
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: 48.97 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 223 IFFTKGTTGAPK--MVEYSQYglgMGFSQASRRWMDLQPTDVLwSLGDAFGGSLSLSAVLGTWFQGACVFLChmptfcPE 300
Cdd:cd17644 111 VIYTSGSTGKPKgvMIEHQSL---VNLSHGLIKEYGITSSDRV-LQFASIAFDVAAEEIYVTLLSGATLVLR------PE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 301 TVLNVLSRF-------PITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGG-PISPGVIEDWKRITKLDI--YEGYGQ 370
Cdd:cd17644 181 EMRSSLEDFvqyiqqwQLTVLSLPPAYWHLLVLELLLSTIDLPSSLRLVIVGGeAVQPELVRQWQKNVGNFIqlINVYGP 260
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217275610 371 TE---TGLLCATSKTIKLKPSS--LGKPLPPYIVQIVDENSNLLPPGEEGNIAI------RIKLNQP 426
Cdd:cd17644 261 TEatiAATVCRLTQLTERNITSvpIGRPIANTQVYILDENLQPVPVGVPGELHIggvglaRGYLNRP 327
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
215-427 |
3.92e-05 |
|
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: 46.16 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 215 TKSQDPMAIFFTKGTTGAPKMVEYSQYGLGmgfsqASRRW-MDLQPTD----VLWSLGDAFggSLSLSAVLGTWFQGACV 289
Cdd:cd12115 102 TDPDDLAYVIYTSGSTGRPKGVAIEHRNAA-----AFLQWaAAAFSAEelagVLASTSICF--DLSVFELFGPLATGGKV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 290 FLChmptfcpETVLNVLS---RFPITTLSANPEMYQELLQHKCF-TSYRFKSLkqcvaAGGPISPGVIED-WKRITKLDI 364
Cdd:cd12115 175 VLA-------DNVLALPDlpaAAEVTLINTVPSAAAELLRHDALpASVRVVNL-----AGEPLPRDLVQRlYARLQVERV 242
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217275610 365 YEGYGQTETgllcATSKTIKLKPS------SLGKPLPPYIVQIVDENSNLLPPGEEGNIAI------RIKLNQPA 427
Cdd:cd12115 243 VNLYGPSED----TTYSTVAPVPPgasgevSIGRPLANTQAYVLDRALQPVPLGVPGELYIggagvaRGYLGRPG 313
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
129-415 |
7.45e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 45.72 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 129 LACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEAMAPVVNSAVSdcptlkTKLLVSDKSyDGWLDFKkliQVAPP 208
Cdd:PRK12316 579 LAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAG------VQVLDLDRP-AAWLEGY---SEENP 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 209 KQtymRTKSQDPMAIFFTKGTTGAPK---------------MVEYSQYGLGMGFSQASRRWMDLQPTDVLWSLgdAFGGS 273
Cdd:PRK12316 649 GT---ELNPENLAYVIYTSGSTGKPKgagnrhralsnrlcwMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPL--MSGAR 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 274 LSLSAvlgtwfQGAcvflchmpTFCPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSyrFKSLKQCVAAGGPISPGVI 353
Cdd:PRK12316 724 LVVAA------PGD--------HRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS--CTSLRRIVCSGEALPADAQ 787
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217275610 354 ED-WKRITKLDIYEGYGQTET--GLLCATSKTIKLKPSSLGKPLPPYIVQIVDENSNLLPPGEEG 415
Cdd:PRK12316 788 EQvFAKLPQAGLYNLYGPTEAaiDVTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLG 852
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
280-420 |
1.31e-04 |
|
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: 44.22 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 280 LGTWFQGACVFLC-----HMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAGGPISPGVIE 354
Cdd:cd17636 53 IGTLMFTLATFHAggtnvFVRRVDAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEWNDMATVD 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217275610 355 DWKRITKLdiyEGYGQTE-TGLLCATSKTIKLKpSSLGKPLPPYIVQIVDENSNLLPPGEEGNIAIR 420
Cdd:cd17636 133 TSPWGRKP---GGYGQTEvMGLATFAALGGGAI-GGAGRPSPLVQVRILDEDGREVPDGEVGEIVAR 195
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
82-426 |
1.66e-04 |
|
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: 44.08 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 82 EEDKWSFERMTQLSKKAASILSDtCALSHGDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAqc 161
Cdd:cd17645 20 RGQSLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSA-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 162 ivaneamapvvnsavsdcptlktKLLVSDksydgwldfkkliqvappkqtymrtkSQDPMAIFFTKGTTGAPKMVEYSQY 241
Cdd:cd17645 97 -----------------------KILLTN--------------------------PDDLAYVIYTSGSTGLPKGVMIEHH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 242 GLgMGFSQASRRWMDLQPTDVLwSLGDAFGGSLSLSAVLGTWFQGACVFLCHMPTFCPETVLNVLSRFPITTLSANPEMY 321
Cdd:cd17645 128 NL-VNLCEWHRPYFGVTPADKS-LVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 322 QELlqhkcFTSYRFKSLKQCVAAGGPISPGVIEDWKritkldIYEGYGQTETGLLcATSKTIKLKPSSL--GKPLPPYIV 399
Cdd:cd17645 206 AEQ-----FMQLDNQSLRVLLTGGDKLKKIERKGYK------LVNNYGPTENTVV-ATSFEIDKPYANIpiGKPIDNTRV 273
|
330 340 350
....*....|....*....|....*....|...
gi 2217275610 400 QIVDENSNLLPPGEEGNIAI------RIKLNQP 426
Cdd:cd17645 274 YILDEALQLQPIGVAGELCIageglaRGYLNRP 306
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
123-420 |
1.68e-04 |
|
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: 44.20 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 123 EAYWiclACVRLGITFVPGSPQLT-------AKKIRYQLRMSKAQCIVANEAMAPVVNSAVSDCPTLKTKLLVSDKSYDG 195
Cdd:cd05906 79 PAFW---ACVLAGFVPAPLTVPPTydepnarLRKLRHIWQLLGSPVVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 196 WLDFkkliqVAPPKQtymrtkSQDPMAIFFTKGTTGAPKMVEYSQYGLgMGFSQASRRWMDLQPTDVL--WSLGDAFGGS 273
Cdd:cd05906 156 AADH-----DLPQSR------PDDLALLMLTSGSTGFPKAVPLTHRNI-LARSAGKIQHNGLTPQDVFlnWVPLDHVGGL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 274 LSLSAvlgtwfqgACVFL-CHMPTFCPETV-------LNVLSRFPIT-TLSANpEMYQELLQHKC-FTSYRF--KSLKQC 341
Cdd:cd05906 224 VELHL--------RAVYLgCQQVHVPTEEIladplrwLDLIDRYRVTiTWAPN-FAFALLNDLLEeIEDGTWdlSSLRYL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 342 VAAGGPISPGVIEDWKRITK------LDIYEGYGQTETG------LLCATSKTI-KLKPSSLGKPLPPYIVQIVDENSNL 408
Cdd:cd05906 295 VNAGEAVVAKTIRRLLRLLEpyglppDAIRPAFGMTETCsgviysRSFPTYDHSqALEFVSLGRPIPGVSMRIVDDEGQL 374
|
330
....*....|..
gi 2217275610 409 LPPGEEGNIAIR 420
Cdd:cd05906 375 LPEGEVGRLQVR 386
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
215-419 |
3.08e-04 |
|
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: 43.22 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 215 TKSQDPMAIFFTKGTTGAPK--MVEYSQYgLGMGFSQASRRWMDLQPTDVL----WSLgDAFGGSLSLSAVLGtwfqGAC 288
Cdd:cd17650 90 TQPEDLAYVIYTSGTTGKPKgvMVEHRNV-AHAAHAWRREYELDSFPVRLLqmasFSF-DVFAGDFARSLLNG----GTL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 289 VFLCHMPTFCPETVLNVLSRFPITTLSANPEMYQELLQHKCFTSYRFKSLKQCVAAggpiSPGVIEDWK-----RI-TKL 362
Cdd:cd17650 164 VICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVG----SDGCKAQDFktlaaRFgQGM 239
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217275610 363 DIYEGYGQTETG-------LLCATSKTIKLKPssLGKPLPPYIVQIVDENSNLLPPGEEGNIAI 419
Cdd:cd17650 240 RIINSYGVTEATidstyyeEGRDPLGDSANVP--IGRPLPNTAMYVLDERLQPQPVGVAGELYI 301
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
97-372 |
3.15e-04 |
|
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: 43.19 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 97 KAASILSDTcALSHGDRLMIILPPTP---EAYWIC-----LACVrLGITFVPGSPQLTAKKIRYQLRMSKAQCI-VANEA 167
Cdd:cd05915 36 RLMGGLRAL-GVGVGDRVATLGFNHFrhlEAYFAVpgmgaVLHT-ANPRLSPKEIAYILNHAEDKVLLFDPNLLpLVEAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 168 MAPVVNsaVSDCPTLKTKllvsdksYDGWLDFkklIQVAPPKQTYMRTKSQ-DPMAIFFTKGTTGAPKMVEYSQYGLGMG 246
Cdd:cd05915 114 RGELKT--VQHFVVMDEK-------APEGYLA---YEEALGEEADPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 247 FSQAS-RRWMDLQPTDV---------------LWSLgDAFGGslslsavlgtwfqgacVFLCHMPTFCPETVLNVLSRFP 310
Cdd:cd05915 182 SLAASlVDGTALSEKDVvlpvvpmfhvnawclPYAA-TLVGA----------------KQVLPGPRLDPASLVELFDGEG 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217275610 311 ITTLSANPEMYQELLQHKCFTSYRFKSLKQcVAAGGPISPGVIEDWKRITKLDIYEGYGQTE 372
Cdd:cd05915 245 VTFTAGVPTVWLALADYLESTGHRLKTLRR-LVVGGSAAPRSLIARFERMGVEVRQGYGLTE 305
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
216-415 |
4.00e-04 |
|
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: 42.75 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 216 KSQDPMAIFFTKGTTGAPKMVEYSQYGLGMGfSQASRRWMDLQPTDVLWSLGDAFG--------------GSLSLSAVLG 281
Cdd:cd05924 1 RSADDLYILYTGGTTGMPKGVMWRQEDIFRM-LMGGADFGTGEFTPSEDAHKAAAAaagtvmfpapplmhGTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 282 TWFQGACVFlcHMPTFCPETVLNVLSRFPITTLS------ANPeMYQELLQHKcftSYRFKSLKQCVAAGGPISPGVIED 355
Cdd:cd05924 80 LLGGQTVVL--PDDRFDPEEVWRTIEKHKVTSMTivgdamARP-LIDALRDAG---PYDLSSLFAISSGGALLSPEVKQG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217275610 356 WKRIT-KLDIYEGYGQTETGLLcaTSKTIKLKPSSLGK-PLPPYIVQIVDENSNLLPPGEEG 415
Cdd:cd05924 154 LLELVpNITLVDAFGSSETGFT--GSGHSAGSGPETGPfTRANPDTVVLDDDGRVVPPGSGG 213
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
111-236 |
1.21e-03 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); 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. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 41.49 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 111 GDRLMIILPPTPEAYWICLACVRLGITFVPGSPQLTAKKIRYQLRMSKAQCIVANEA---------MAPVVNSAVSDCPT 181
Cdd:cd05943 123 GDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAytyngkrhdVREKVAELVKGLPS 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217275610 182 LKTKLLVSDKSYDG------------WLDFKKLIQVAPPkqTYMRTKSQDPMAIFFTKGTTGAPK-MV 236
Cdd:cd05943 203 LLAVVVVPYTVAAGqpdlskiakaltLEDFLATGAAGEL--EFEPLPFDHPLYILYSSGTTGLPKcIV 268
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
217-420 |
1.77e-03 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 40.95 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 217 SQDPMAIFFTKGTTGAPKMVEYSQYGLgMGFSQASRRWMDLQPTDVLWSLGDAFGGSLSLSAVLGTWFQGACVFLCHMPT 296
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANL-LANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNPL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 297 FcPETVLNVLSRFPITTLSANPEMYQELL-----QHKCFTSYRFkslkqcVAAGG-----PISPGVIEDWKRITkldIYE 366
Cdd:PRK06334 261 Y-PKKIVEMIDEAKVTFLGSTPVFFDYILktakkQESCLPSLRF------VVIGGdafkdSLYQEALKTFPHIQ---LRQ 330
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217275610 367 GYGQTEtgllCATSKTIKLKPSS-----LGKPLPPYIVQIVDENSNL-LPPGEEGNIAIR 420
Cdd:PRK06334 331 GYGTTE----CSPVITINTVNSPkhescVGMPIRGMDVLIVSEETKVpVSSGETGLVLTR 386
|
|
| |
