|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
74-557 |
0e+00 |
|
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: 969.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 74 FRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAK 153
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 154 VLLVSPELQAAVEEILPSLKKDDVSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPESWRSEVTFSTPALYIYTSGTTG--- 230
Cdd:cd05938 81 VLVVAPELQEAVEEVLPALRADGVSVWYLSHTSNTEGVISLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGlpk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 231 --------------------------------------------------ATLALRTKFSASQFWDDCRKYNVTVIQYIG 260
Cdd:cd05938 161 aarishlrvlqcsgflslcgvtaddviyitlplyhssgfllgiggcielgATCVLKPKFSASQFWDDCRKHNVTVIQYIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 261 ELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDICIYEFYAATEGNIGFMNYARKVGAVGRVNYLQKKIIT 340
Cdd:cd05938 241 ELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 341 YDLIKYDVEKDEPVRDENGYCVRVPKGEVGLLVCKITQLTPFNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHEN 420
Cdd:cd05938 321 FELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSPFLGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 421 FIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIGMASIKMKENHEFDGKKLFQHIADYLPSY 500
Cdd:cd05938 401 FLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIGMAAVKLKPGHEFDGKKLYQHVREYLPAY 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 227499621 501 ARPRFLRIQDTIEITGTFKHRKMTLVEEGFNPAVIKDALYFLDDTAKMYVPMTEDIY 557
Cdd:cd05938 481 ARPRFLRIQDSLEITGTFKQQKVRLVEEGFNPSIISDPLYFLDETQKTYVPLTPDIY 537
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
30-567 |
0e+00 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 656.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 30 IGYFLKVAAVGRRVRSYGKRR---PARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDC 106
Cdd:PRK08279 11 LPRRLPDLPGILRGLKRTALItpdSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAA-RGVGKGDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 107 VALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKkDDVSIYYVSRTS 186
Cdd:PRK08279 90 VALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLA-RPPRLWVAGGDT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 187 NTD--GIDSFLDKVDEVSTEPipESWRSEVTFSTPALYIYTSGTTG---------------------------------- 230
Cdd:PRK08279 169 LDDpeGYEDLAAAAAGAPTTN--PASRSGVTAKDTAFYIYTSGTTGlpkaavmshmrwlkamggfggllrltpddvlycc 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 231 --------------------ATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRG 290
Cdd:PRK08279 247 lplyhntggtvawssvlaagATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGNGLRP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 291 DVWRQFVKRFGDICIYEFYAATEGNIGFMNYARKVGAVGRVNYLQKKiiTYDLIKYDVEKDEPVRDENGYCVRVPKGEVG 370
Cdd:PRK08279 327 DIWDEFQQRFGIPRILEFYAASEGNVGFINVFNFDGTVGRVPLWLAH--PYAIVKYDVDTGEPVRDADGRCIKVKPGEVG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 371 LLVCKITQLTPFNGYAGAKAqTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGL 450
Cdd:PRK08279 405 LLIGRITDRGPFDGYTDPEA-SEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSG 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 451 VDFVQEVNVYGVHVPDHEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVEEGF 530
Cdd:PRK08279 484 FPGVEEAVVYGVEVPGTDGRAGMAAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRKEGF 563
|
570 580 590
....*....|....*....|....*....|....*..
gi 227499621 531 NPAVIKDALYFLDDTAKMYVPMTEDIYNAISAKTLKL 567
Cdd:PRK08279 564 DPSKVDDPLYVLDPGSGGYVPLTAELYAEIAAGKFRL 600
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
76-532 |
0e+00 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 652.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 76 DETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVL 155
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSL-GLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 156 LVSPELQaaveeilpslkkddvsIYyvsrTSNTDGidsfLDKVDEVSTEPIpesWR-------------SEVTFSTPALY 222
Cdd:cd05940 80 VVDAALY----------------IY----TSGTTG----LPKAAIISHRRA---WRggaffagsggalpSDVLYTCLPLY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 223 IYTSGT--------TGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWR 294
Cdd:cd05940 133 HSTALIvgwsaclaSGATLVIRKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGNGLRPDIWE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 295 QFVKRFGDICIYEFYAATEGNIGFMNYARKVGAVGRVNYLQKKIITYDLIKYDVEKDEPVRDENGYCVRVPKGEVGLLVC 374
Cdd:cd05940 213 EFKERFGVPRIAEFYAATEGNSGFINFFGKPGAIGRNPSLLRKVAPLALVKYDLESGEPIRDAEGRCIKVPRGEPGLLIS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 375 KITQLTPFNGYAGAKAqTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFV 454
Cdd:cd05940 293 RINPLEPFDGYTDPAA-TEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGV 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227499621 455 QEVNVYGVHVPDHEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVEEGFNP 532
Cdd:cd05940 372 EEANVYGVQVPGTDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEGFDP 449
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
76-532 |
4.74e-143 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 421.83 E-value: 4.74e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 76 DETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVL 155
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQA-QGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 156 LVS--PELQAAVEEILPSLkkDDVS----IYYVSrTSNTDGID-------------------SFLDKVDEVSTEPIPesw 210
Cdd:cd05939 80 IFNllDPLLTQSSTEPPSQ--DDVNfrdkLFYIY-TSGTTGLPkaavivhsryyriaagayyAFGMRPEDVVYDCLP--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 211 rsevtfstpaLYiYTSGTT---------GATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVR 281
Cdd:cd05939 154 ----------LY-HSAGGImgvgqallhGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 282 LALGNGLRGDVWRQFVKRFGDICIYEFYAATEGNIGFMNYARKVGAVGRVNYLQKKIITYDLIKYDVEKDEPVRDENGYC 361
Cdd:cd05939 223 LAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNIDNHVGACGFNSRILPSVYPIRLIKVDEDTGELIRDSDGLC 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 362 VRVPKGEVGLLVCKITQLTP---FNGYAGAKAqTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGEN 438
Cdd:cd05939 303 IPCQPGEPGLLVGKIIQNDPlrrFDGYVNEGA-TNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGEN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 439 VATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIGMASIKMKENhEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTF 518
Cdd:cd05939 382 VSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAAIVDPER-KVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTF 460
|
490
....*....|....
gi 227499621 519 KHRKMTLVEEGFNP 532
Cdd:cd05939 461 KLQKTDLQKEGYDP 474
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
74-532 |
4.34e-142 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 419.14 E-value: 4.34e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 74 FRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAK 153
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 154 VLLVSPELQAAVeeilpslkkddvsIYyvsrTSNTDGIdsfldkvdevsTEPIPESWRSEV-----------------TF 216
Cdd:cd05937 81 FVIVDPDDPAIL-------------IY----TSGTTGL-----------PKAAAISWRRTLvtsnllshdlnlkngdrTY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 217 STPALYIYTSGTTGA--------TLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGL 288
Cdd:cd05937 133 TCMPLYHGTAAFLGAcnclmsggTLALSRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 289 RGDVWRQFVKRFGDICIYEFYAATEGNIGFMNYAR---KVGAVGRVNYLQKKIITYD--LIKYDVEKDEPVRD-ENGYCV 362
Cdd:cd05937 213 RPDIWERFRERFNVPEIGEFYAATEGVFALTNHNVgdfGAGAIGHHGLIRRWKFENQvvLVKMDPETDDPIRDpKTGFCV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 363 RVPKGEVGLLVCKITQ--LTPFNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVA 440
Cdd:cd05937 293 RAPVGEPGEMLGRVPFknREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 441 TTEVADTVGLVDFVQEVNVYGVHVPDHEGRIGMASIKMKENH----EFDGKKLFQHIADYLPSYARPRFLRIQDTIEITG 516
Cdd:cd05937 373 TTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLEESSavptEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTD 452
|
490
....*....|....*.
gi 227499621 517 TFKHRKMTLVEEGFNP 532
Cdd:cd05937 453 NHKQQKGVLRDEGVDP 468
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
80-525 |
6.22e-70 |
|
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: 231.03 E-value: 6.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 80 TYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSP 159
Cdd:cd05934 5 TYAELLRESARIAAALAA-LGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 160 elqaaveeilpslkkddVSIYYVS-RTSNTDGI---DSFLDKVDEVSTE--PIPESwrsEVTF-STPALYI-------YT 225
Cdd:cd05934 84 -----------------ASILYTSgTTGPPKGVvitHANLTFAGYYSARrfGLGED---DVYLtVLPLFHInaqavsvLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 226 SGTTGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGdICI 305
Cdd:cd05934 144 ALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFG-VRL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 306 YEFYAATEGNIGFMN---YARKVGAVGRVNYLqkkiitydlikYDVEkdepVRDENGYcvRVPKGEVGLLVCKITQ-LTP 381
Cdd:cd05934 223 LEGYGMTETIVGVIGprdEPRRPGSIGRPAPG-----------YEVR----IVDDDGQ--ELPAGEPGELVIRGLRgWGF 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 382 FNGYAGAKAQTEKkklrdVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYG 461
Cdd:cd05934 286 FKGYYNMPEATAE-----AMRNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVA 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227499621 462 VHVPDHEGRIgMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTL 525
Cdd:cd05934 359 VPDEVGEDEV-KAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
56-528 |
2.96e-69 |
|
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: 230.08 E-value: 2.96e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 56 LRAFLEK-ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACL 134
Cdd:COG0318 1 LADLLRRaAARHPDRPALVFGGRRLTYAELDARARRLAAALRA-LGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 135 NYNIRAKSLLHCFQCCGAKVLLVspelqAAVeeilpslkkddvsIYyvsrTSNTDGI--------DSFLdkvdeVSTEPI 206
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALVT-----ALI-------------LY----TSGTTGRpkgvmlthRNLL-----ANAAAI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 207 PESWR---SEVTFSTPALY--------IYTSGTTGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPND 275
Cdd:COG0318 133 AAALGltpGDVVLVALPLFhvfgltvgLLAPLLAGATLVLLPRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARY 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 276 RDHKVRLAL--GNGLRGDVWRQFVKRFGdICIYEFYAATEGN-IGFMN----YARKVGAVGRVnylqkkiitydLIKYDV 348
Cdd:COG0318 213 DLSSLRLVVsgGAPLPPELLERFEERFG-VRIVEGYGLTETSpVVTVNpedpGERRPGSVGRP-----------LPGVEV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 349 EkdepVRDENGycVRVPKGEVGLLVCKITQLTPfnGYAGAKAQTEKkklrdVFKKGdlYFNSGDLLMVDHENFIYFHDRV 428
Cdd:COG0318 281 R----IVDEDG--RELPPGEVGEIVVRGPNVMK--GYWNDPEATAE-----AFRDG--WLRTGDLGRLDEDGYLYIVGRK 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 429 GDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHeGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRI 508
Cdd:COG0318 346 KDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKW-GERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEF 424
|
490 500
....*....|....*....|
gi 227499621 509 QDTIEITGTFKHRKMTLVEE 528
Cdd:COG0318 425 VDELPRTASGKIDRRALRER 444
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
35-533 |
4.22e-59 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 205.76 E-value: 4.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 35 KVAAVGRRVRSYGKRRPARTILRAFLE-KARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGN 113
Cdd:PRK06155 2 EPLGAGLAARAVDPLPPSERTLPAMLArQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 114 EPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPS-LKKDDVSIyyvsrtsntdgid 192
Cdd:PRK06155 81 RIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGdLPLPAVWL------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 193 sfldkVDEVSTEPIPESWR-------------SEVTFSTPALYIYTSGTTG----------------------------- 230
Cdd:PRK06155 148 -----LDAPASVSVPAGWStaplppldapapaAAVQPGDTAAILYTSGTTGpskgvccphaqfywwgrnsaedleigadd 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 231 ------------------------ATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGN 286
Cdd:PRK06155 223 vlyttlplfhtnalnaffqallagATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 287 GLRGDVWRQFVKRFGdICIYEFYAATEGN--IGFMNYARKVGAVGRvnyLQKKIITYdlikydvekdepVRDENGycVRV 364
Cdd:PRK06155 303 GVPAALHAAFRERFG-VDLLDGYGSTETNfvIAVTHGSQRPGSMGR---LAPGFEAR------------VVDEHD--QEL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 365 PKGEVGLLVCKITQltPF---NGYAGAKAQTekkklrdVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVAT 441
Cdd:PRK06155 365 PDGEPGELLLRADE--PFafaTGYFGMPEKT-------VEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISS 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 442 TEVADTVGLVDFVQEVNVYGVHVPDHEGRIgMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHR 521
Cdd:PRK06155 436 FEVEQVLLSHPAVAAAAVFPVPSELGEDEV-MAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQ 514
|
570
....*....|..
gi 227499621 522 KMTLVEEGFNPA 533
Cdd:PRK06155 515 KFVLREQGVTAD 526
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
68-533 |
1.66e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 162.54 E-value: 1.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 68 HKPFLLFRDETLTYAQVDRRSNQVARALHDHLGlRQGDC-VALLMGNEPAYVwLWLGLVKL-GCAMACLNYNIRAKSLLH 145
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRARLD-PTRPPhVGVLLDNTPEFS-LLLGAAALsGIVPVGLNPTRRGAALAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 146 CFQCCGAKVLLVSPELQAAVEEILPslkkdDVSIYYVSRTSNTDGIDSFLDkvdevstEPIPeswRSEVTFSTPALYIYT 225
Cdd:PRK07867 96 DIAHADCQLVLTESAHAELLDGLDP-----GVRVINVDSPAWADELAAHRD-------AEPP---FRVADPDDLFMLIFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 226 SGTTG------------------------------------------------------ATLALRTKFSASQFWDDCRKY 251
Cdd:PRK07867 161 SGTSGdpkavrcthrkvasagvmlaqrfglgpddvcyvsmplfhsnavmagwavalaagASIALRRKFSASGFLPDVRRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 252 NVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGN-GLRGDVWRqFVKRFGdiC-IYEFYAATEGNIGFmnyARK----V 325
Cdd:PRK07867 241 GATYANYVGKPLSYVLATPERPDDADNPLRIVYGNeGAPGDIAR-FARRFG--CvVVDGFGSTEGGVAI---TRTpdtpP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 326 GAVGRvnylqkkiITYDLIKYDVEKDEP----VRDENGycvRVPKGE-VGLLVcKITQLTPFNGYAGaKAQTEKKKLRDv 400
Cdd:PRK07867 315 GALGP--------LPPGVAIVDPDTGTEcppaEDADGR---LLNADEaIGELV-NTAGPGGFEGYYN-DPEADAERMRG- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 401 fkkGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPD-HEGRIGMASIKMK 479
Cdd:PRK07867 381 ---G--VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYA--VPDpVVGDQVMAALVLA 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 227499621 480 ENHEFDGKKL--FQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVEEGFNPA 533
Cdd:PRK07867 454 PGAKFDPDAFaeFLAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVDCA 509
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
63-522 |
2.77e-43 |
|
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: 160.08 E-value: 2.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 63 ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKS 142
Cdd:cd17631 5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRA-LGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 143 LLHCFQCCGAKVLLvspelqaaveeilpslkKDDVSIYYvsrTSNTDG-------------------IDSFLDKVDEVST 203
Cdd:cd17631 84 VAYILADSGAKVLF-----------------DDLALLMY---TSGTTGrpkgamlthrnllwnavnaLAALDLGPDDVLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 204 EPIPeswrsevTFSTPALYIYTSGTT--GATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQkPNDRDH-KV 280
Cdd:cd17631 144 VVAP-------LFHIGGLGVFTLPTLlrGGTVVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPR-FATTDLsSL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 281 RLALGNG--LRGDVWRQFVKRfgDICIYEFYAATE--GNIGFM---NYARKVGAVGRVnylqkkiitydLIKYDVEkdep 353
Cdd:cd17631 216 RAVIYGGapMPERLLRALQAR--GVKFVQGYGMTEtsPGVTFLspeDHRRKLGSAGRP-----------VFFVEVR---- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 354 VRDENGycVRVPKGEVGLLVCKITQLTPfnGYAGAKAQTEKkklrdVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFR 433
Cdd:cd17631 279 IVDPDG--REVPPGEVGEIVVRGPHVMA--GYWNRPEATAA-----AFRDG--WFHTGDLGRLDEDGYLYIVDRKKDMII 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 434 WKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTI 512
Cdd:cd17631 348 SGGENVYPAEVEDVLYEHPAVAEVAVIG--VPDEKwGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDAL 425
|
490
....*....|
gi 227499621 513 EITGTFKHRK 522
Cdd:cd17631 426 PRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
59-435 |
1.37e-40 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 152.08 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 59 FLEKARQTPHKPFLL-FRDETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:pfam00501 1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLR-ALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 138 IRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPESWRSEvtfs 217
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPD---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 218 TPALYIYTSGTT----------------------------------------------------------GATLALRTKF 239
Cdd:pfam00501 156 DLAYIIYTSGTTgkpkgvmlthrnlvanvlsikrvrprgfglgpddrvlstlplfhdfglslgllgpllaGATVVLPPGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 240 SA---SQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLAL--GNGLRGDVWRQFVKRFGdICIYEFYAATEG 314
Cdd:pfam00501 236 PAldpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLsgGAPLPPELARRFRELFG-GALVNGYGLTET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 315 NIGFMNY------ARKVGAVGR-VNYLQKKIItydlikyDVEKDEPvrdengycvrVPKGEVGLLVCKITQLTPfnGYAG 387
Cdd:pfam00501 315 TGVVTTPlpldedLRSLGSVGRpLPGTEVKIV-------DDETGEP----------VPPGEPGELCVRGPGVMK--GYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 227499621 388 AKAQTEKkklrdVFKKGDlYFNSGDLLMVDHENFIYFHDRVGDTFRWK 435
Cdd:pfam00501 376 DPELTAE-----AFDEDG-WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
63-562 |
1.97e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 148.64 E-value: 1.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 63 ARQTPHKPFLLFRDETLTYAQVDRRSNQ---VARALHDHLGLRQgdcVALLMGNEPAYVwLWLGLVKLGCAMAC-LNYNI 138
Cdd:PRK13388 11 DRAGDDTIAVRYGDRTWTWREVLAEAAAraaALIALADPDRPLH---VGVLLGNTPEML-FWLAAAALGGYVLVgLNTTR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 139 RAKSLLHCFQCCGAKVLLVSPELQAaveeILPSLKKDDVSIYYVSRtsntdgiDSFLDKVDEV-STEPIPEswrseVTFS 217
Cdd:PRK13388 87 RGAALAADIRRADCQLLVTDAEHRP----LLDGLDLPGVRVLDVDT-------PAYAELVAAAgALTPHRE-----VDAM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 218 TPALYIYTSGTT------------------------------------------------------GATLALRTKFSASQ 243
Cdd:PRK13388 151 DPFMLIFTSGTTgapkavrcshgrlafagralterfgltrddvcyvsmplfhsnavmagwapavasGAAVALPAKFSASG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 244 FWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGdiC-IYEFYAATEGNIgfmNYA 322
Cdd:PRK13388 231 FLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFG--CqVEDGYGSSEGAV---IVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 323 RK----VGAVGRVnylqkkiiTYDLIKYDVEKDEP----VRDENGYcVRVPKGEVGLLVCKiTQLTPFNGYAGAKAQTEk 394
Cdd:PRK13388 306 REpgtpPGSIGRG--------APGVAIYNPETLTEcavaRFDAHGA-LLNADEAIGELVNT-AGAGFFEGYYNNPEATA- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 395 KKLRDvfkkGDLYfnSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPD-HEGRIGM 473
Cdd:PRK13388 375 ERMRH----GMYW--SGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYA--VPDeRVGDQVM 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 474 ASIKMKENHEFDGKKL--FQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVEEGFnpAVIKDALYFLDDTAKMYVP 551
Cdd:PRK13388 447 AALVLRDGATFDPDAFaaFLAAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQGW--ATGDPVTLWVRRGGPAYRL 524
|
570
....*....|.
gi 227499621 552 MTEDIYNAISA 562
Cdd:PRK13388 525 MSEPAKAALAA 535
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
61-561 |
5.92e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 146.79 E-value: 5.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 61 EKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGcAMACLnynIRA 140
Cdd:PRK07868 455 EQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIA-VGVRQGDRVGVLMETRPSALVAIAALSRLG-AVAVL---MPP 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 141 KSLLH-CFQCCGAKVLLVSPE-LQAAVEEILPSL-----KKDDVSIyyvsrTSNTDGIDsfLDKVDEVSTEpIPESWRSE 213
Cdd:PRK07868 530 DTDLAaAVRLGGVTEIITDPTnLEAARQLPGRVLvlgggESRDLDL-----PDDADVID--MEKIDPDAVE-LPGWYRPN 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 214 ---------VTFSTP--------------ALYIYTSGTT-------------------------------GATLALRTKF 239
Cdd:PRK07868 602 pglardlafIAFSTAggelvakqitnyrwALSAFGTASAaaldrrdtvycltplhhesgllvslggavvgGSRIALSRGL 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 240 SASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDICIYEFYAATEGNIGFM 319
Cdd:PRK07868 682 DPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMPTGLWERVVEAFAPAHVVEFFATTDGQAVLA 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 320 NYA-RKVGAVGRVNYLQKKIityDLIKYDVEKDEPVRDENGYCVRVPKGEVGLLVckitqltpfnGYAGAKAQTEKKKLR 398
Cdd:PRK07868 762 NVSgAKIGSKGRPLPGAGRV---ELAAYDPEHDLILEDDRGFVRRAEVNEVGVLL----------ARARGPIDPTASVKR 828
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 399 DVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEgrIGMASIKM 478
Cdd:PRK07868 829 GVFAPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGGRQ--LAVAAVTL 906
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 479 KENHEFDGKKLFQHIADyLPSYARPRFLRIQDTIEITGTFKHRKMTLVEEGFnPAVIKDALYFLDDTAKmYVPMTEDIYN 558
Cdd:PRK07868 907 RPGAAITAADLTEALAS-LPVGLGPDIVHVVPEIPLSATYRPTVSALRAAGI-PKPGRQAWYFDPETNR-YRRLTPAVRA 983
|
...
gi 227499621 559 AIS 561
Cdd:PRK07868 984 ELT 986
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
63-510 |
1.47e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 142.76 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 63 ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKS 142
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLD-LGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 143 LLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIYYVSRTsnTDGIDSFLDKVDEVSTEPIPESwRSEVTFSTPALY 222
Cdd:PRK08316 100 LAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGG--REAPGGWLDFADWAEAGSVAEP-DVELADDDLAQI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 223 IYTSGTT----GATLALR------------TKFSAsqfwDD----------CRKYNVTVIQYI--------------GEL 262
Cdd:PRK08316 177 LYTSGTEslpkGAMLTHRaliaeyvscivaGDMSA----DDiplhalplyhCAQLDVFLGPYLyvgatnvildapdpELI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 263 LRY------------------LCNSPqkpnDRDhKVRLAlgnGLR----------GDVWRQFVKRFGDICIYEFYAATEg 314
Cdd:PRK08316 253 LRTieaeritsffapptvwisLLRHP----DFD-TRDLS---SLRkgyygasimpVEVLKELRERLPGLRFYNCYGQTE- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 315 nIGFM-------NYARKVGAVGR-VNYLQKKIItydlikydvekDEPVRDengycvrVPKGEVGLLVCKITQLTpfNGYA 386
Cdd:PRK08316 324 -IAPLatvlgpeEHLRRPGSAGRpVLNVETRVV-----------DDDGND-------VAPGEVGEIVHRSPQLM--LGYW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 387 GAKAQTEkkklrDVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVhvpD 466
Cdd:PRK08316 383 DDPEKTA-----EAFRGG--WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGL---P 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 227499621 467 HEGRIG--MASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQD 510
Cdd:PRK08316 453 DPKWIEavTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVD 498
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
229-519 |
3.06e-35 |
|
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: 135.11 E-value: 3.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 229 TGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNG--LRGDVWRQFVKRFGDIcIY 306
Cdd:cd04433 65 AGGTVVLLPKFDPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGapLPPELLERFEEAPGIK-LV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 307 EFYAATEGNIGFM-----NYARKVGAVGRVnylqkkiitydLIKYDVEkdepVRDENGycVRVPKGEVGLLVCKItqLTP 381
Cdd:cd04433 144 NGYGLTETGGTVAtgppdDDARKPGSVGRP-----------VPGVEVR----IVDPDG--GELPPGEIGELVVRG--PSV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 382 FNGYAGAKAQTEkkklrdvFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYG 461
Cdd:cd04433 205 MKGYWNNPEATA-------AVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVG 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 227499621 462 vhVPDHE-GRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 519
Cdd:cd04433 278 --VPDPEwGERVVAVVVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGK 334
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
61-525 |
6.62e-34 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 135.20 E-value: 6.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 61 EKARQTPHKPFLLFRD-----ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLN 135
Cdd:PRK08008 15 DLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYS-LGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 136 YNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSlkkDDVSI--YYVSRTSN--TDGIDSFLDKVDEVSTEpipesWR 211
Cdd:PRK08008 94 ARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQE---DATPLrhICLTRVALpaDDGVSSFTQLKAQQPAT-----LC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 212 SEVTFST--PALYIYTSGTT------------------------------------------------------GATLAL 235
Cdd:PRK08008 166 YAPPLSTddTAEILFTSGTTsrpkgvvithynlrfagyysawqcalrdddvyltvmpafhidcqctaamaafsaGATFVL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 236 RTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVR-----LALGNGLRGDvwrqFVKRFGdICIYEFYA 310
Cdd:PRK08008 246 LEKYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLRevmfyLNLSDQEKDA----FEERFG-VRLLTSYG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 311 ATE---GNIG-FMNYARKVGAVGRVNylqkkiitydlIKYDVEkdepVRDENGYcvRVPKGEVGLLVCK-ITQLTPFNGY 385
Cdd:PRK08008 321 MTEtivGIIGdRPGDKRRWPSIGRPG-----------FCYEAE----IRDDHNR--PLPAGEIGEICIKgVPGKTIFKEY 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 386 AGAKAQTEKkklrdVFkKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVP 465
Cdd:PRK08008 384 YLDPKATAK-----VL-EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDS 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 466 DHEGRIgMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTL 525
Cdd:PRK08008 458 IRDEAI-KAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
55-519 |
2.83e-32 |
|
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: 129.61 E-value: 2.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 55 ILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACL 134
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQN-LGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 135 NYNIRAKSLLHCFQCCGAKVLLVspelqaaveeilpslkkddvsiyyvsrtsntdgIDSFLDKVDEvstePIPESWRSEV 214
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIV---------------------------------AVSFTDLLAA----GAPLGERVAL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 215 TFSTPALYIYTSGTTG--------------------------------------------------------ATLALRTK 238
Cdd:cd05936 123 TPEDVAVLQYTSGTTGvpkgamlthrnlvanalqikawledllegddvvlaalplfhvfgltvalllplalgATIVLIPR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 239 FSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNG--LRGDVWRQFVKRFGDIcIYEFYAATE--- 313
Cdd:cd05936 203 FRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELTGVP-IVEGYGLTEtsp 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 314 ---GNigFMNYARKVGAVGrvnylqkkiitYDLIKYDVEkdepVRDENGycVRVPKGEVGLLVCKITQLtpFNGYAGAKA 390
Cdd:cd05936 282 vvaVN--PLDGPRKPGSIG-----------IPLPGTEVK----IVDDDG--EELPPGEVGELWVRGPQV--MKGYWNRPE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 391 QTEKkklrdVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHeGR 470
Cdd:cd05936 341 ETAE-----AFVDG--WLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYS-GE 412
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 227499621 471 IGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 519
Cdd:cd05936 413 AVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGK 461
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
63-504 |
3.02e-32 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 130.62 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 63 ARQTPHKPFLLFRDE-----TLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:COG0365 19 AEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRA-LGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 138 IRAKSLLHCFQCCGAKVLLVSPE---------LQAAVEEIL---PSLKKddvsIYYVSRTSNT---DGIDSFLDKVDEVS 202
Cdd:COG0365 98 FGAEALADRIEDAEAKVLITADGglrggkvidLKEKVDEALeelPSLEH----VIVVGRTGADvpmEGDLDWDELLAAAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 203 TEPIPEswrsEVTFSTPALYIYTSGTT----------------------------------------------------- 229
Cdd:COG0365 174 AEFEPE----PTDADDPLFILYTSGTTgkpkgvvhthggylvhaattakyvldlkpgdvfwctadigwatghsyivygpl 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 230 --GATLAL---RTKF-SASQFWDDCRKYNVTViqyigellryLCNSP-----------QKPNDRD-HKVRLALGNG--LR 289
Cdd:COG0365 250 lnGATVVLyegRPDFpDPGRLWELIEKYGVTV----------FFTAPtairalmkagdEPLKKYDlSSLRLLGSAGepLN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 290 GDVWRQFVKRFGdICIYEFYAATEGNIGFMNYAR----KVGAVGRVNYLqkkiitydlikYDVEkdepVRDENGycVRVP 365
Cdd:COG0365 320 PEVWEWWYEAVG-VPIVDGWGQTETGGIFISNLPglpvKPGSMGKPVPG-----------YDVA----VVDEDG--NPVP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 366 KGEVGLLVCKITQLTPFNGYAGAKAQTeKKKLRDVFKkgDLYFnSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVA 445
Cdd:COG0365 382 PGEEGELVIKGPWPGMFRGYWNDPERY-RETYFGRFP--GWYR-TGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIE 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227499621 446 DTVGLVDFVQEVNVygVHVPDHEGRIGM-ASIKMKENHEFDG---KKLFQHIADYLPSYARPR 504
Cdd:COG0365 458 SALVSHPAVAEAAV--VGVPDEIRGQVVkAFVVLKPGVEPSDelaKELQAHVREELGPYAYPR 518
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
54-512 |
1.75e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 125.30 E-value: 1.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 54 TILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMAC 133
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRA-LGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 134 LNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLkkDDVSIYYVsrtsNTDGidsflDKVDEVSTEPIPESWRS- 212
Cdd:PRK06187 86 INIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQL--PTVRTVIV----EGDG-----PAAPLAPEVGEYEELLAa 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 213 --------EVTFSTPALYIYTSGTTG--------------------ATLALRTK-------------------------- 238
Cdd:PRK06187 155 asdtfdfpDIDENDAAAMLYTSGTTGhpkgvvlshrnlflhslavcAWLKLSRDdvylvivpmfhvhawglpylalmaga 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 239 -------FSASQFWDDCRKYNVTVIQYIGELLRYLCNSPqKPNDRD-HKVRLAL--GNGLRGDVWRQFVKRFGdICIYEF 308
Cdd:PRK06187 235 kqviprrFDPENLLDLIETERVTFFFAVPTIWQMLLKAP-RAYFVDfSSLRLVIygGAALPPALLREFKEKFG-IDLVQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 309 YAATE-GNIGFMNY--------ARKVGAVGRVnylqkkiitydLIKYDVEkdepVRDENGYCVRVPKGEVGLLVCK---I 376
Cdd:PRK06187 313 YGMTEtSPVVSVLPpedqlpgqWTKRRSAGRP-----------LPGVEAR----IVDDDGDELPPDGGEVGEIIVRgpwL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 377 TQltpfnGYAGAKAQTEKKklrdvFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQE 456
Cdd:PRK06187 378 MQ-----GYWNRPEATAET-----IDGG--WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAE 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 227499621 457 VNVYGvhVPD-HEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTI 512
Cdd:PRK06187 446 VAVIG--VPDeKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDEL 500
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
58-525 |
1.20e-25 |
|
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: 110.54 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 58 AFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:cd05959 9 VDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRA-LGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 138 IRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPES-WRSEvtf 216
Cdd:cd05959 88 LTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEAEQLKPAAtHADD--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 217 stPALYIYTSGTTGA---------------------TLALRTK---FSASQ----------------------------- 243
Cdd:cd05959 165 --PAFWLYSSGSTGRpkgvvhlhadiywtaelyarnVLGIREDdvcFSAAKlffayglgnsltfplsvgattvlmperpt 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 244 ---FWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLAL--GNGLRGDVWRQFVKRFGdICIYEFYAATE-GNIG 317
Cdd:cd05959 243 paaVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVsaGEALPAEVGERWKARFG-LDILDGIGSTEmLHIF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 318 FMNYARKV--GAVGRVnylqkkiitydLIKYDVEkdepVRDENGycVRVPKGEVGLLVCKITQLTPfnGYAGAKAQTekk 395
Cdd:cd05959 322 LSNRPGRVryGTTGKP-----------VPGYEVE----LRDEDG--GDVADGEPGELYVRGPSSAT--MYWNNRDKT--- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 396 klRDVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIgMAS 475
Cdd:cd05959 380 --RDTFQGE--WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKP-KAF 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 227499621 476 IKMKENHEFDGK---KLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTL 525
Cdd:cd05959 455 VVLRPGYEDSEAleeELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
62-527 |
2.56e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 106.48 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 62 KARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAK 141
Cdd:PRK06839 11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 142 SLLHCFQCCGAKVLLVSPELQAAVEEIlpslkkddVSIYYVSRTSNTDGIDSFLDKvdevstEPIPESWRSEvtfSTPAL 221
Cdd:PRK06839 91 ELIFQLKDSGTTVLFVEKTFQNMALSM--------QKVSYVQRVISITSLKEIEDR------KIDNFVEKNE---SASFI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 222 YIYTSGTTG--------------------ATLALRT----------------------------------KFSASQFWDD 247
Cdd:PRK06839 154 ICYTSGTTGkpkgavltqenmfwnalnntFAIDLTMhdrsivllplfhiggiglfafptlfaggviivprKFEPTKALSM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 248 CRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNG--LRGDVWRQFVKR---FGdiciyEFYAATEGN-IGFM-- 319
Cdd:PRK06839 234 IEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGapCPEELMREFIDRgflFG-----QGFGMTETSpTVFMls 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 320 --NYARKVGAVGR-VNYLQKKIItydlikydvekdepvrDENGYcvRVPKGEVGLLVCKITQLtpFNGYAGAKAQTEkKK 396
Cdd:PRK06839 309 eeDARRKVGSIGKpVLFCDYELI----------------DENKN--KVEVGEVGELLIRGPNV--MKEYWNRPDATE-ET 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 397 LRDVfkkgdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMAS 475
Cdd:PRK06839 368 IQDG------WLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVG--RQHVKwGEIPIAF 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 227499621 476 IKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVE 527
Cdd:PRK06839 440 IVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
76-468 |
9.81e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 104.60 E-value: 9.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 76 DETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVL 155
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRA-LGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 156 LVSPELQAAVEEILPSLKKdDVSIYYVSRtSNTDGIDSFLDKVDEVSTEPIPESWRSevtfstpALYIYTSGTTG----- 230
Cdd:PRK08276 88 IVSAALADTAAELAAELPA-GVPLLLVVA-GPVPGFRSYEEALAAQPDTPIADETAG-------ADMLYSSGTTGrpkgi 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 231 ------------------------------------------------------ATLALRTKFSASQFWDDCRKYNVTVI 256
Cdd:PRK08276 159 krplpgldpdeapgmmlallgfgmyggpdsvylspaplyhtaplrfgmsalalgGTVVVMEKFDAEEALALIERYRVTHS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 257 QYIgellrylcnspqkPNdrdHKVR-LALGNGLRG-------------------DVWRQFVKRFGDIcIYEFYAATEGN- 315
Cdd:PRK08276 239 QLV-------------PT---MFVRmLKLPEEVRArydvsslrvaihaaapcpvEVKRAMIDWWGPI-IHEYYASSEGGg 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 316 IGFMN---YARKVGAVGRVNYLQKKIItydlikydvekdepvrDENGycVRVPKGEVGLLVCKITQLtPFNgYAGAKAQT 392
Cdd:PRK08276 302 VTVITsedWLAHPGSVGKAVLGEVRIL----------------DEDG--NELPPGEIGTVYFEMDGY-PFE-YHNDPEKT 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227499621 393 EKKKLrdvfKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE 468
Cdd:PRK08276 362 AAARN----PHG--WVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFG--VPDEE 429
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
63-510 |
4.58e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 102.93 E-value: 4.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 63 ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKS 142
Cdd:PRK07786 27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 143 LLHCFQCCGAKVLLVSPELQ---AAVEEILPSLkkddvSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPeswrSEVTFSTP 219
Cdd:PRK07786 106 IAFLVSDCGAHVVVTEAALApvaTAVRDIVPLL-----STVVVAGGSSDDSVLGYEDLLAEAGPAHAP----VDIPNDSP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 220 ALYIYTSGTTG---------------ATLALRT-----------------------------------------KFSASQ 243
Cdd:PRK07786 177 ALIMYTSGTTGrpkgavlthanltgqAMTCLRTngadinsdvgfvgvplfhiagigsmlpglllgaptviyplgAFDPGQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 244 FWDDCRKYNVTVIQYIGELLRYLCnSPQKPNDRDHKVR-LALGNGLRGD-VWRQFVKRFGDICIYEFYAATEGN-IGFM- 319
Cdd:PRK07786 257 LLDVLEAEKVTGIFLVPAQWQAVC-AEQQARPRDLALRvLSWGAAPASDtLLRQMAATFPEAQILAAFGQTEMSpVTCMl 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 320 ---NYARKVGAVGRV-NYLQKKIItydlikydvekDEPVRDengycvrVPKGEVGLLVCKITQLtpFNGYAGAKAQTEkk 395
Cdd:PRK07786 336 lgeDAIRKLGSVGKViPTVAARVV-----------DENMND-------VPVGEVGEIVYRAPTL--MSGYWNNPEATA-- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 396 klrDVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhvPDHE--GRIGM 473
Cdd:PRK07786 394 ---EAFAGG--WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIG---RADEkwGEVPV 465
|
490 500 510
....*....|....*....|....*....|....*...
gi 227499621 474 ASIKMK-ENHEFDGKKLFQHIADYLPSYARPRFLRIQD 510
Cdd:PRK07786 466 AVAAVRnDDAALTLEDLAEFLTDRLARYKHPKALEIVD 503
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
51-230 |
7.90e-23 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 102.49 E-value: 7.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 51 PARTILRAFLEKARQTPHKPFLLFRD----ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVK 126
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLA-LGVKPGDRVAILSDNRPEWVIADLAILA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 127 LGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAA-VEEI---LPSLKKddvsIYYVSRTSNTDG-----IDSFLDK 197
Cdd:COG1022 88 AGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDkLLEVrdeLPSLRH----IVVLDPRGLRDDprllsLDELLAL 163
|
170 180 190
....*....|....*....|....*....|...
gi 227499621 198 VDEVSTEPIPESWRSEVTFSTPALYIYTSGTTG 230
Cdd:COG1022 164 GREVADPAELEARRAAVKPDDLATIIYTSGTTG 196
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
37-504 |
2.71e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 100.77 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 37 AAVGRRVRSYGkrrPARTILRAfleKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPA 116
Cdd:PRK07788 39 LRLAADIRRYG---PFAGLVAH---AARRAPDRAALIDERGTLTYAELDEQSNALARGLLA-LGVRAGDGVAVLARNHRG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 117 YVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIYYVSRTSNTD-GIDSFL 195
Cdd:PRK07788 112 FVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGsTDETLD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 196 DKVDEVSTEPIPeswrsevTFSTPA-LYIYTSGTTG-------------------------------------------- 230
Cdd:PRK07788 192 DLIAGSSTAPLP-------KPPKPGgIVILTSGTTGtpkgaprpepsplaplagllsrvpfragettllpapmfhatgwa 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 231 ---------ATLALRTKFSASQFWDDCRKYNVTVI----QYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFV 297
Cdd:PRK07788 265 hltlamalgSTVVLRRRFDPEATLEDIAKHKATALvvvpVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRAL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 298 KRFGDIcIYEFYAATEgnIGFM------NYARKVGAVGRVnylqkkIITYDLIKYdvekdepvrDENGYcvRVPKGEVGL 371
Cdd:PRK07788 345 EAFGPV-LYNLYGSTE--VAFAtiatpeDLAEAPGTVGRP------PKGVTVKIL---------DENGN--EVPRGVVGR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 372 LVCKITqlTPFNGYAGAKaqtEKKKLRDVFKKGDL-YFNSGDLLMVDhenfiyfhDRVGDTFRWKGENVATTEVADTVGL 450
Cdd:PRK07788 405 IFVGNG--FPFEGYTDGR---DKQIIDGLLSSGDVgYFDEDGLLFVD--------GRDDDMIVSGGENVFPAEVEDLLAG 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 227499621 451 VDFVQEVNVYGVHVPDHEGRIGmASIKMKENHEFDGKKLFQHIADYLPSYARPR 504
Cdd:PRK07788 472 HPDVVEAAVIGVDDEEFGQRLR-AFVVKAPGAALDEDAIKDYVRDNLARYKVPR 524
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
75-527 |
3.55e-22 |
|
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: 99.69 E-value: 3.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 75 RDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKV 154
Cdd:cd05926 11 STPALTYADLAELVDDLARQLAA-LGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 155 LLV-----SPELQAAVEEILPSLkkdDVSIYYVSRTSNTDGID-SFLDKV-DEVSTEPIPESwrsevtfSTPALYIYTSG 227
Cdd:cd05926 90 VLTpkgelGPASRAASKLGLAIL---ELALDVGVLIRAPSAESlSNLLADkKNAKSEGVPLP-------DDLALILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 228 TTG------------------------------------------------ATLA------LRTKFSASQFWDDCRKYNV 253
Cdd:cd05926 160 TTGrpkgvplthrnlaasatnitntykltpddrtlvvmplfhvhglvasllSTLAaggsvvLPPRFSASTFWPDVRDYNA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 254 TVIQYIGELLRYLCNSPQ-KPNDRDHKVRLA--LGNGLRGDVWRQFVKRFGdICIYEFYAATEG---------NIGfmny 321
Cdd:cd05926 240 TWYTAVPTIHQILLNRPEpNPESPPPKLRFIrsCSASLPPAVLEALEATFG-APVLEAYGMTEAahqmtsnplPPG---- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 322 ARKVGAVGRVNYLQKKIITydlikydvEKDEPVRDENgycvrvpKGEV---GLLVCKitqltpfnGYAGAKAQTekkklR 398
Cdd:cd05926 315 PRKPGSVGKPVGVEVRILD--------EDGEILPPGV-------VGEIclrGPNVTR--------GYLNNPEAN-----A 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 399 DVFKKGDlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPD-HEGRIGMASIK 477
Cdd:cd05926 367 EAAFKDG-WFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFG--VPDeKYGEEVAAAVV 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 227499621 478 MKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVE 527
Cdd:cd05926 444 LREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
67-515 |
6.49e-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: 6.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 67 PHKPFLLFRDETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHC 146
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLR-ERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 147 FQCCGAKVLLVSPELQAAVeeilpslkkddvsIYyvsrTSNT-----------DGIDSFLDKVDEvsTEPIPESWRseVT 215
Cdd:cd05930 80 LEDSGAKLVLTDPDDLAYV-------------IY----TSGStgkpkgvmvehRGLVNLLLWMQE--AYPLTPGDR--VL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 216 FSTPALY------IYTSGTTGATLAL---RTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQkpNDRDHKVRLAL-- 284
Cdd:cd05930 139 QFTSFSFdvsvweIFGALLAGATLVVlpeEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELE--LAALPSLRLVLvg 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 285 GNGLRGDVWRQFVKRFGDICIYEFYAATEGNIGfmnyarkvgavgrvnylqkkiITYDLIKYDVEKDEP----------- 353
Cdd:cd05930 217 GEALPPDLVRRWRELLPGARLVNLYGPTEATVD---------------------ATYYRVPPDDEEDGRvpigrpipntr 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 354 --VRDENGYCvrVPKGEVGLLVckIT--QLTpfNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVg 429
Cdd:cd05930 276 vyVLDENLRP--VPPGVPGELY--IGgaGLA--RGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRI- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 430 DT------FRwkgenVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIgMASIKMKENHEFDGKKLFQHIADYLPSYARP 503
Cdd:cd05930 349 DDqvkirgYR-----IELGEIEAALLAHPGVREAAVVAREDGDGEKRL-VAYVVPDEGGELDEEELRAHLAERLPDYMVP 422
|
490
....*....|..
gi 227499621 504 RFLRIQDTIEIT 515
Cdd:cd05930 423 SAFVVLDALPLT 434
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
76-500 |
1.24e-21 |
|
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: 98.05 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 76 DETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVL 155
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRK-LGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 156 LVSPELQAAVEEILPSLKKDDvSIYYVsrTSNTDGIDSFLDKVDEVSTEPIP-ESWRSEVTFSTPALYIYTSGTTG---- 230
Cdd:cd05911 87 FTDPDGLEKVKEAAKELGPKD-KIIVL--DDKPDGVLSIEDLLSPTLGEEDEdLPPPLKDGKDDTAAILYSSGTTGlpkg 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 231 ---------------------------------------------------ATLALRTKFSASQFWDDCRKYNVTVIQYI 259
Cdd:cd05911 164 vclshrnlianlsqvqtflygndgsndvilgflplyhiyglfttlasllngATVIIMPKFDSELFLDLIEKYKITFLYLV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 260 GELLRYLCNSPQKPNDRDHKVRLALGNGlrGDVWRQFV----KRFGDICIYEFYAATE-GNIGFMN--YARKVGAVGRV- 331
Cdd:cd05911 244 PPIAAALAKSPLLDKYDLSSLRVILSGG--APLSKELQellaKRFPNATIKQGYGMTEtGGILTVNpdGDDKPGSVGRLl 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 332 -NYlQKKIItydlikydvekDEPVRDENGYcvrvpkGEVGLLVCKITQLtpFNGY-----AGAKAQTEkkklrdvfkkgD 405
Cdd:cd05911 322 pNV-EAKIV-----------DDDGKDSLGP------NEPGEICVRGPQV--MKGYynnpeATKETFDE-----------D 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 406 LYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHeGRIGMASIKMKENHEFD 485
Cdd:cd05911 371 GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVS-GELPRAYVVRKPGEKLT 449
|
490
....*....|....*
gi 227499621 486 GKKLFQHIADYLPSY 500
Cdd:cd05911 450 EKEVKDYVAKKVASY 464
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
63-512 |
2.01e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 97.65 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 63 ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKS 142
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 143 LLHCFQCCGAKVLLVSPELQA---------------------------AVEEILPSLKKDDVSIYYVSRTsnTDGIDSFL 195
Cdd:PRK06145 91 VAYILGDAGAKLLLVDEEFDAivaletpkividaaaqadsrrlaqgglEIPPQAAVAPTDLVRLMYTSGT--TDRPKGVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 196 DKVDEVSTEPIPESWRSEVTFSTPALYI---YTSGT----------TGATLALRTKFSASQFWDDCRKYNVTVIQYIGEL 262
Cdd:PRK06145 169 HSYGNLHWKSIDHVIALGLTASERLLVVgplYHVGAfdlpgiavlwVGGTLRIHREFDPEAVLAAIERHRLTCAWMAPVM 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 263 LRYLCNSPQKPNDRDHKVRLALGNGLRGDVW--RQFVKRFGDICIYEFYAATEGNIG--FMNYAR---KVGAVGR-VNYL 334
Cdd:PRK06145 249 LSRVLTVPDRDRFDLDSLAWCIGGGEKTPESriRDFTRVFTRARYIDAYGLTETCSGdtLMEAGReieKIGSTGRaLAHV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 335 QKKIITydlikydvekdepvrDENGYCVRVPKGEVGLLVCKITQltpfnGYAGAKAQTEKKKLRDvfkkgdlYFNSGDLL 414
Cdd:PRK06145 329 EIRIAD---------------GAGRWLPPNMKGEICMRGPKVTK-----GYWKDPEKTAEAFYGD-------WFRSGDVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 415 MVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIgMASIKMKENHEFDGKKLFQHIA 494
Cdd:PRK06145 382 YLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERI-TAVVVLNPGATLTLEALDRHCR 460
|
490
....*....|....*...
gi 227499621 495 DYLPSYARPRFLRIQDTI 512
Cdd:PRK06145 461 QRLASFKVPRQLKVRDEL 478
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
51-512 |
5.13e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 93.43 E-value: 5.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 51 PARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCA 130
Cdd:PRK07656 3 EWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAA-LGIGKGDRVAIWAPNSPHWVIAALGALKAGAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 131 MACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEI---LPSLKkddvSIYYVSRTSNTDGIDSFLDKVDEVSTEPIP 207
Cdd:PRK07656 82 VVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSAttrLPALE----HVVICETEEDDPHTEKMKTFTDFLAAGDPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 208 ESWRsEVTFSTPALYIYTSGTT----GATLALRTKFSASQFWDDCRKYN------------------------------- 252
Cdd:PRK07656 158 ERAP-EVDPDDVADILFTSGTTgrpkGAMLTHRQLLSNAADWAEYLGLTegdrylaanpffhvfgykagvnaplmrgati 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 253 --------VTVIQYIGE-----------LLRYLCNSPQKPNDRDHKVRLALGNGLRGDV--WRQFVKRFGDICIYEFYAA 311
Cdd:PRK07656 237 lplpvfdpDEVFRLIETeritvlpgpptMYNSLLQHPDRSAEDLSSLRLAVTGAASMPValLERFESELGVDIVLTGYGL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 312 TEGN-IGFMNYA---RKVGA--VGRVnylqkkiitydlIKyDVEkdepVRDENGYCVRVPKGEVGLLVCKitqltPFN-- 383
Cdd:PRK07656 317 SEASgVTTFNRLdddRKTVAgtIGTA------------IA-GVE----NKIVNELGEEVPVGEVGELLVR-----GPNvm 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 384 -GYAGAKAQTEKKKLRDvfkkGDLYfnSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGv 462
Cdd:PRK07656 375 kGYYDDPEATAAAIDAD----GWLH--TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIG- 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 227499621 463 hVPDHE-GRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTI 512
Cdd:PRK07656 448 -VPDERlGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDEL 497
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
67-230 |
6.58e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 93.03 E-value: 6.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 67 PHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHC 146
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 147 FQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIyyvsRTSNTDGIDSFLDKVD--EVSTEPIPEswRSEVTFSTPALY-I 223
Cdd:PRK07798 96 LDDSDAVALVYEREFAPRVAEVLPRLPKLRTLV----VVEDGSGNDLLPGAVDyeDALAAGSPE--RDFGERSPDDLYlL 169
|
....*..
gi 227499621 224 YTSGTTG 230
Cdd:PRK07798 170 YTGGTTG 176
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
69-525 |
5.59e-19 |
|
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: 89.44 E-value: 5.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 69 KPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQ 148
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNL-GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 149 CCGAKVLLVSpelqaaveeilpslkKDDVSiyYVSRTSNTDG-----IDSFLDK---VDEVSTE--PIPEswrSEVTFST 218
Cdd:cd05919 80 DCEARLVVTS---------------ADDIA--YLLYSSGTTGppkgvMHAHRDPllfADAMAREalGLTP---GDRVFSS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 219 PALYI-YTSG-------TTGATLALR-TKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLAL--GNG 287
Cdd:cd05919 140 AKMFFgYGLGnslwfplAVGASAVLNpGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVsaGEA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 288 LRGDVWRQFVKRFG-DICiyEFYAATEgnIGFMNYARKVGAVgRVNYLQKKIITYDLikydvekdePVRDENGYcvRVPK 366
Cdd:cd05919 220 LPRGLGERWMEHFGgPIL--DGIGATE--VGHIFLSNRPGAW-RLGSTGRPVPGYEI---------RLVDEEGH--TIPP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 367 GEVGLLVCKITQLTPfnGYAGAKAQTEKKklrdvFKKGDLYfnSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVAD 446
Cdd:cd05919 284 GEEGDLLVRGPSAAV--GYWNNPEKSRAT-----FNGGWYR--TGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVES 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 447 TVGLVDFVQEVNVygVHVPDHEGRIGM-ASIKMKENHEFDGK---KLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRK 522
Cdd:cd05919 355 LIIQHPAVAEAAV--VAVPESTGLSRLtAFVVLKSPAAPQESlarDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
...
gi 227499621 523 MTL 525
Cdd:cd05919 433 FKL 435
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
79-525 |
7.76e-19 |
|
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: 88.93 E-value: 7.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 79 LTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVS 158
Cdd:cd05972 1 WSFRELKRESAKAANVLAKL-GLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 159 PElqaaveeilpslkkDDVSIYYVSRTS---------NTDGIDSFLDKVDEVSTEPipeswrSEVTFSTP----ALYIYT 225
Cdd:cd05972 80 AE--------------DPALIYFTSGTTglpkgvlhtHSYPLGHIPTAAYWLGLRP------DDIHWNIAdpgwAKGAWS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 226 SGTT----GAT--LALRTKFSASQFWDDCRKYNVTViqyigellryLCNSP--------QKPNDRDHK-VRLALGNG--L 288
Cdd:cd05972 140 SFFGpwllGATvfVYEGPRFDAERILELLERYGVTS----------FCGPPtayrmlikQDLSSYKFShLRLVVSAGepL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 289 RGDVWRQFVKRFGdICIYEFYAATEGNIGFMNYAR---KVGAVGRVnylqkkiitydLIKYDVEkdepVRDENGYcvRVP 365
Cdd:cd05972 210 NPEVIEWWRAATG-LPIRDGYGQTETGLTVGNFPDmpvKPGSMGRP-----------TPGYDVA----IIDDDGR--ELP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 366 KGEVGLLVCKITQLTPFNGYAGAKAQTEKkklrdvFKKGDlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVA 445
Cdd:cd05972 272 PGEEGDIAIKLPPPGLFLGYVGDPEKTEA------SIRGD-YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 446 DTvgLVDF--VQEVNVygVHVPDHE-GRIGMASIKMKENHEFD---GKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 519
Cdd:cd05972 345 SA--LLEHpaVAEAAV--VGSPDPVrGEVVKAFVVLTSGYEPSeelAEELQGHVKKVLAPYKYPREIEFVEELPKTISGK 420
|
....*.
gi 227499621 520 HRKMTL 525
Cdd:cd05972 421 IRRVEL 426
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
69-525 |
1.68e-18 |
|
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: 88.30 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 69 KPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQ 148
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 149 CCGAKVLLVSPELQAAveeilpslkkDDVSIY-YVSRTSNT-DGIDSFLDKVDEVSTEPIPESWR---SEVTFSTPALYi 223
Cdd:cd05958 81 KARITVALCAHALTAS----------DDICILaFTSGTTGApKATMHFHRDPLASADRYAVNVLRlreDDRFVGSPPLA- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 224 YTSGT---------TGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLAL--GNGLRGDV 292
Cdd:cd05958 150 FTFGLggvllfpfgVGASGVLLEEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVsaGEALPAAL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 293 WRQFVKRFGDICI---------YEFYAATEGNIgfmnyarKVGAVGRVnylqkkiitydLIKYDVEkdepVRDENGYcvR 363
Cdd:cd05958 230 HRAWKEATGIPIIdgigstemfHIFISARPGDA-------RPGATGKP-----------VPGYEAK----VVDDEGN--P 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 364 VPKGEVGLLVCKitqltpfnGYAGAKAQTEKKKlRDVFKKGDLYfnSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTE 443
Cdd:cd05958 286 VPDGTIGRLAVR--------GPTGCRYLADKRQ-RTYVQGGWNI--TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 444 VADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASIKMKENHEFD---GKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 519
Cdd:cd05958 355 VEDVLLQHPAVAECAVVG--HPDESrGVVVKAFVVLRPGVIPGpvlARELQDHAKAHIAPYKYPRAIEFVTELPRTATGK 432
|
....*.
gi 227499621 520 HRKMTL 525
Cdd:cd05958 433 LQRFAL 438
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
63-519 |
2.31e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 88.14 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 63 ARQTPHKPFLLFRD--ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEP-AYVWLWLGLvKLGCAMACLNYNIR 139
Cdd:PRK13390 7 AQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYD-AGLRTGDVVALLSDNSPeALVVLWAAL-RSGLYITAINHHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 140 AKSLLHCFQCCGAKVLLVSPELQAAVEEI---------------------------LPSLKKDD---VSIYYVSRTSNTD 189
Cdd:PRK13390 85 APEADYIVGDSGARVLVASAALDGLAAKVgadlplrlsfggeidgfgsfeaalagaGPRLTEQPcgaVMLYSSGTTGFPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 190 GIDSFLDKVD-EVSTEPIPESWR-------SEVTFSTPALY-------IYTSGTTGATLALRTKFSASQFWDDCRKYNVT 254
Cdd:PRK13390 165 GIQPDLPGRDvDAPGDPIVAIARafydiseSDIYYSSAPIYhaaplrwCSMVHALGGTVVLAKRFDAQATLGHVERYRIT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 255 VIQYIGEL-LRYLcnspqKPNDrDHKVRLALGNgLRG----------DVWRQFVKRFGDIcIYEFYAATEGN----IGFM 319
Cdd:PRK13390 245 VTQMVPTMfVRLL-----KLDA-DVRTRYDVSS-LRAvihaaapcpvDVKHAMIDWLGPI-VYEYYSSTEAHgmtfIDSP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 320 NYARKVGAVGRvnylqkkiitydlikyDVEKDEPVRDENGYcvRVPKGEVGLLVCKITQLtPFNgYAGAKAQTEKKKlrd 399
Cdd:PRK13390 317 DWLAHPGSVGR----------------SVLGDLHICDDDGN--ELPAGRIGTVYFERDRL-PFR-YLNDPEKTAAAQ--- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 400 vFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASIKM 478
Cdd:PRK13390 374 -HPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIG--VPDPEmGEQVKAVIQL 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 227499621 479 KENheFDG-KKLFQHIADYLPS----YARPRFLRIQDTIEITGTFK 519
Cdd:PRK13390 451 VEG--IRGsDELARELIDYTRSriahYKAPRSVEFVDELPRTPTGK 494
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
63-468 |
1.10e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 86.28 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 63 ARQTPHKP-FLLFR-DETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRA 140
Cdd:PRK13391 7 AQTTPDKPaVIMAStGEVVTYRELDERSNRLAHLFRSL-GLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 141 KSLLHCFQCCGAKVLLVSP---ELQAAVEEILPSLKKDDVsiyyVSRTSNTDGIDSFLDKVDEVSTEPIPESWR------ 211
Cdd:PRK13391 86 AEAAYIVDDSGARALITSAaklDVARALLKQCPGVRHRLV----LDGDGELEGFVGYAEAVAGLPATPIADESLgtdmly 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 212 ---------------SEVTFSTP--------ALYIYTSGTT----------------------GATLALRTKFSASQFWD 246
Cdd:PRK13391 162 ssgttgrpkgikrplPEQPPDTPlpltaflqRLWGFRSDMVylspaplyhsapqravmlvirlGGTVIVMEHFDAEQYLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 247 DCRKYNVTVIQYIGELLRYLCNSPQKPNDR-DH---KVRLALGNGLRGDVWRQFVKRFGDIcIYEFYAATEGNiGFM--- 319
Cdd:PRK13391 242 LIEEYGVTHTQLVPTMFSRMLKLPEEVRDKyDLsslEVAIHAAAPCPPQVKEQMIDWWGPI-IHEYYAATEGL-GFTacd 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 320 --NYARKVGAVGRVnylqkkiitydlikydVEKDEPVRDENGYcvRVPKGEVGLLVCKitQLTPFNgYAGAKAQTEKKKL 397
Cdd:PRK13391 320 seEWLAHPGTVGRA----------------MFGDLHILDDDGA--ELPPGEPGTIWFE--GGRPFE-YLNDPAKTAEARH 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227499621 398 RDvfkkGDlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE 468
Cdd:PRK13391 379 PD----GT-WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFG--VPNED 442
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
57-230 |
5.29e-17 |
|
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: 83.79 E-value: 5.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 57 RAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNY 136
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 137 NIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPslkkddvsiyyvsrtsntdgidsFLDKVDEVSTEPiPESWRSEVTF 216
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLTDRSLAGRAGGLEV-----------------------AVVIDEALDAGP-AGNPAVPVSP 135
|
170
....*....|....
gi 227499621 217 STPALYIYTSGTTG 230
Cdd:cd12117 136 DDLAYVMYTSGSTG 149
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
57-528 |
3.29e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 81.16 E-value: 3.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 57 RAFLekarqTPHKPFLLFRDETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNY 136
Cdd:PRK03640 11 RAFL-----TPDRTAIEFEEKKVTFMELHEAVVSVAGKLA-ALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 137 NIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSlkkddvsiyyvsrtsntdgidsfldKVDEVSTEPIPE-SWRSEVT 215
Cdd:PRK03640 85 RLSREELLWQLDDAEVKCLITDDDFEAKLIPGISV-------------------------KFAELMNGPKEEaEIQEEFD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 216 FSTPALYIYTSGTT-----------------------------------------------------GATLALRTKFSAS 242
Cdd:PRK03640 140 LDEVATIMYTSGTTgkpkgviqtygnhwwsavgsalnlglteddcwlaavpifhisglsilmrsviyGMRVVLVEKFDAE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 243 QFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGdICIYEFYAATEG-----NIG 317
Cdd:PRK03640 220 KINKLLQTGGVTIISVVSTMLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKEKG-IPVYQSYGMTETasqivTLS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 318 FMNYARKVGAVGRVNY-LQKKIitydlikydvEKDEPVrdengycvrVPKGEVGLLVCKITQLTPfnGYAGAKAQTEKkk 396
Cdd:PRK03640 299 PEDALTKLGSAGKPLFpCELKI----------EKDGVV---------VPPFEEGEIVVKGPNVTK--GYLNREDATRE-- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 397 lrdVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMAS 475
Cdd:PRK03640 356 ---TFQDG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVG--VPDDKwGQVPVAF 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 227499621 476 IKMkeNHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK---HRKMTLVEE 528
Cdd:PRK03640 429 VVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKllrHELKQLVEE 482
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
49-519 |
1.11e-15 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 79.80 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 49 RRPARTILRAFLEKARQTPHKPFLLfrDE--TLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVK 126
Cdd:PRK13382 39 RREGMGPTSGFAIAAQRCPDRPGLI--DElgTLTWRELDERSDALAAALQ-ALPIGEPRVVGIMCRNHRGFVEALLAANR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 127 LGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSpelqaavEEILPSLKKDDVSIYYVSRTSN-TDGIDSFLdkVDEVSTEP 205
Cdd:PRK13382 116 IGADILLLNTSFAGPALAEVVTREGVDTVIYD-------EEFSATVDRALADCPQATRIVAwTDEDHDLT--VEVLIAAH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 206 IPEswRSEVTFSTPALYIYTSGTTGA-----------------------------------------------------T 232
Cdd:PRK13382 187 AGQ--RPEPTGRKGRVILLTSGTTGTpkgarrsgpggigtlkaildrtpwraeeptvivapmfhawgfsqlvlaaslacT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 233 LALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDH----KVRLALGNGLRGDVWRQFVKRFGDIcIYEF 308
Cdd:PRK13382 265 IVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSgrslRFAAASGSRMRPDVVIAFMDQFGDV-IYNN 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 309 YAATE-GNIGFMNYARkvgavgrvnyLQKKIITYDliKYDVEKDEPVRDENGYcvRVPKGEVG-LLVCKITQltpFNGYA 386
Cdd:PRK13382 344 YNATEaGMIATATPAD----------LRAAPDTAG--RPAEGTEIRILDQDFR--EVPTGEVGtIFVRNDTQ---FDGYT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 387 GAKAQTekkklrdvFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPD 466
Cdd:PRK13382 407 SGSTKD--------FHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIG--VDD 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 227499621 467 HE-GRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 519
Cdd:PRK13382 475 EQyGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGK 528
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
52-230 |
2.15e-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: 79.90 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 52 ARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAm 131
Cdd:COG1020 475 DATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRA-LGVGPGDLVGVCLERSLEMVVALLAVLKAGAA- 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 132 aclnY-----NIRAKSLLHCFQCCGAKVLLVspelQAAVEEILPSLKKDDVSiyyvsrtsntdgidsfldkVDEVSTEPI 206
Cdd:COG1020 553 ----YvpldpAYPAERLAYMLEDAGARLVLT----QSALAARLPELGVPVLA-------------------LDALALAAE 605
|
170 180
....*....|....*....|....*.
gi 227499621 207 PESW-RSEVTFSTPAlY-IYTSGTTG 230
Cdd:COG1020 606 PATNpPVPVTPDDLA-YvIYTSGSTG 630
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
63-515 |
5.97e-15 |
|
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: 77.29 E-value: 5.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 63 ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKS 142
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALA-SLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 143 LLHCFQCCGAKVLLVSPelqaaveeilpslkkDDVsiYYVSRTSNT-----------DGIDSFLDKvdEVSTEPIPESWR 211
Cdd:cd05945 80 IREILDAAKPALLIADG---------------DDN--AYIIFTSGStgrpkgvqishDNLVSFTNW--MLSDFPLGPGDV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 212 ----SEVTFSTPALYIYTSGTTGATLALRTKfsasqfwddcrkynvTVIQYIGELLRYLcnspqkpndRDHKV------- 280
Cdd:cd05945 141 flnqAPFSFDLSVMDLYPALASGATLVPVPR---------------DATADPKQLFRFL---------AEHGItvwvstp 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 281 ---RLALGNG---------LR-----GDVW-----RQFVKRFGDICIYEFYAATEGNIgfmnyarkvgAVGRVNYLQKKI 338
Cdd:cd05945 197 sfaAMCLLSPtftpeslpsLRhflfcGEVLphktaRALQQRFPDARIYNTYGPTEATV----------AVTYIEVTPEVL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 339 ITYD-----LIKYDVEKDepVRDENGYCvrVPKGEVGLLVckITQLTPFNGYAGAKAQTEKKKLRDvfkKGDLYFNSGDL 413
Cdd:cd05945 267 DGYDrlpigYAKPGAKLV--ILDEDGRP--VPPGEKGELV--ISGPSVSKGYLNNPEKTAAAFFPD---EGQRAYRTGDL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 414 LMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVygVHVPDHEGRIGM-ASIKMKENHEF-DGKKLFQ 491
Cdd:cd05945 338 VRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVV--VPKYKGEKVTELiAFVVPKPGAEAgLTKAIKA 415
|
490 500
....*....|....*....|....
gi 227499621 492 HIADYLPSYARPRFLRIQDTIEIT 515
Cdd:cd05945 416 ELAERLPPYMIPRRFVYLDELPLN 439
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
76-509 |
1.50e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 76.28 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 76 DETLTYAQVDRRSNQVARALhDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVL 155
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGL-AALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 156 LVSPELQAAVEEILPSlkkddvSIYYVSRTSNTDGIDSFldKVDEVSTEPIP-----ESWRSEVTFST------PALYIY 224
Cdd:PRK12406 88 IAHADLLHGLASALPA------GVTVLSVPTPPEIAAAY--RISPALLTPPAgaidwEGWLAQQEPYDgppvpqPQSMIY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 225 TSGTTG--------------------------------------------------------ATLALRTKFSASQFWDDC 248
Cdd:PRK12406 160 TSGTTGhpkgvrraaptpeqaaaaeqmraliyglkpgiralltgplyhsapnayglragrlgGVLVLQPRFDPEELLQLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 249 RKYNVTVIQYIGELLRYLCNSPQkpndrdhKVRLALG-NGLR----------GDVWRQFVKRFGDIcIYEFYAATE-GNI 316
Cdd:PRK12406 240 ERHRITHMHMVPTMFIRLLKLPE-------EVRAKYDvSSLRhvihaaapcpADVKRAMIEWWGPV-IYEYYGSTEsGAV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 317 GFMN---YARKVGAVGRVNY-LQKKIItydlikydvekdepvrDENGYcvRVPKGEVGLLVCKITQLTPFNgYAGakaqt 392
Cdd:PRK12406 312 TFATsedALSHPGTVGKAAPgAELRFV----------------DEDGR--PLPQGEIGEIYSRIAGNPDFT-YHN----- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 393 EKKKLRDVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRI 471
Cdd:PRK12406 368 KPEKRAEIDRGG--FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFG--IPDAEfGEA 443
|
490 500 510
....*....|....*....|....*....|....*...
gi 227499621 472 GMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQ 509
Cdd:PRK12406 444 LMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIM 481
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
79-504 |
3.13e-13 |
|
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: 71.78 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 79 LTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVS 158
Cdd:cd05973 1 LTFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 159 pelqaaveeiLPSLKKDDVSIYYVSRTSNTDGIDSFLdkvdevstePIPESW--------------RSEVTFSTPA---- 220
Cdd:cd05973 80 ----------AANRHKLDSDPFVMMFTSGTTGLPKGV---------PVPLRAlaafgaylrdavdlRPEDSFWNAAdpgw 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 221 ---LYIYTSG--TTG-ATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYL----CNSPQKPNDRDHKVRLAlGNGLRG 290
Cdd:cd05973 141 aygLYYAITGplALGhPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLmaagAEVPARPKGRLRRVSSA-GEPLTP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 291 DVWRQFVKRFGdICIYEFYAATEGNIGFMNY-----ARKVGAVGRVnylqkkiitydLIKYDVEkdepVRDENGycVRVP 365
Cdd:cd05973 220 EVIRWFDAALG-VPIHDHYGQTELGMVLANHhalehPVHAGSAGRA-----------MPGWRVA----VLDDDG--DELG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 366 KGEVGLLVCKI--TQLTPFNGYAGAKAQTekkklrdvfKKGDlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTE 443
Cdd:cd05973 282 PGEPGRLAIDIanSPLMWFRGYQLPDTPA---------IDGG-YYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFD 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227499621 444 VADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASIKMKENHEFD---GKKLFQHIADYLPSYARPR 504
Cdd:cd05973 352 VESALIEHPAVAEAAVIG--VPDPErTEVVKAFVVLRGGHEGTpalADELQLHVKKRLSAHAYPR 414
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
80-230 |
5.23e-13 |
|
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: 70.76 E-value: 5.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 80 TYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEP-AYVWLwLGLVKLGCA---------MACLNYNIRAksllhcfqc 149
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAeLVVAI-LAVLKAGAAyvpldpaypAERLAFILED--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 150 CGAKVLLVSPELQAAVEEILPslkkddvSIYYVSRTSNTDGIDSFLDKVDEVSTEPipeswrsevtfSTPALYIYTSGTT 229
Cdd:TIGR01733 71 AGARLLLTDSALASRLAGLVL-------PVILLDPLELAALDDAPAPPPPDAPSGP-----------DDLAYVIYTSGST 132
|
.
gi 227499621 230 G 230
Cdd:TIGR01733 133 G 133
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
53-525 |
6.54e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 70.96 E-value: 6.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 53 RTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHLGlrQGDCVALLMGNEPAYVWLWLGLVKLGCAma 132
Cdd:PRK07638 1 MGITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKES--KNKTIAILLENRIEFLQLFAGAAMAGWT-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 133 CLNYNIRAKS--------------------LLHCFQCCGAKVLLVSpELQAAVEEILPS-LKKDDV--SIYYVSRTSNTD 189
Cdd:PRK07638 77 CVPLDIKWKQdelkerlaisnadmivteryKLNDLPDEEGRVIEID-EWKRMIEKYLPTyAPIENVqnAPFYMGFTSGST 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 190 G------------IDSFLDKVDEVSTEP-----IPESWRSevtfstpALYIYTSGTT---GATLALRTKFSASQFWDDCR 249
Cdd:PRK07638 156 GkpkaflraqqswLHSFDCNVHDFHMKRedsvlIAGTLVH-------SLFLYGAISTlyvGQTVHLMRKFIPNQVLDKLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 250 KYNVTVIQYIGELLrylcNSPQKPND-RDHKVRLALGnglrGDVW-----RQFVKRFGDICIYEFYAATEgnIGFMNY-- 321
Cdd:PRK07638 229 TENISVMYTVPTML----ESLYKENRvIENKMKIISS----GAKWeaeakEKIKNIFPYAKLYEFYGASE--LSFVTAlv 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 322 ----ARKVGAVGR-VNYLQKKIitydlikydvekdepvRDENGycVRVPKGEVGLLVCKITQLtpFNGYAGAKAQTEKKK 396
Cdd:PRK07638 299 deesERRPNSVGRpFHNVQVRI----------------CNEAG--EEVQKGEIGTVYVKSPQF--FMGYIIGGVLARELN 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 397 LrdvfkkgDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPD-HEGRIGMAS 475
Cdd:PRK07638 359 A-------DGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIG--VPDsYWGEKPVAI 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 227499621 476 IKMKENHefdgKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTL 525
Cdd:PRK07638 430 IKGSATK----QQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
79-519 |
7.26e-13 |
|
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: 70.59 E-value: 7.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 79 LTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVS 158
Cdd:cd05935 2 LTYLELLEVVKKLASFLSN-KGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 159 PELqaaveeilpslkkDDVSIyyVSRTSNTDGIDS--FLDKVDEVSTEPIPESWR----SEVTFSTPALY--------IY 224
Cdd:cd05935 81 SEL-------------DDLAL--IPYTSGTTGLPKgcMHTHFSAAANALQSAVWTgltpSDVILACLPLFhvtgfvgsLN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 225 TSGTTGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPqKPNDRDHKVRLALGNG---LRGDVWRQFVKRFG 301
Cdd:cd05935 146 TAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATP-EFKTRDLSSLKVLTGGgapMPPAVAEKLLKLTG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 302 dICIYEFYAATEgnigfmnyarkVGAVGRVN-YLQKKIITYDLIKYDVekDEPVRD-ENGycVRVPKGEVGLLVCKITQL 379
Cdd:cd05935 225 -LRFVEGYGLTE-----------TMSQTHTNpPLRPKLQCLGIP*FGV--DARVIDiETG--RELPPNEVGEIVVRGPQI 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 380 tpFNGYAGAKAQTEKKKLRDvfkKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNV 459
Cdd:cd05935 289 --FKGYWNRPEETEESFIEI---KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCV 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227499621 460 YGvhVPDHE-GRIGMASIKMKEnhEFDGKKLFQHIADY----LPSYARPRFLRIQDTIEITGTFK 519
Cdd:cd05935 364 IS--VPDERvGEEVKAFIVLRP--EYRGKVTEEDIIEWareqMAAYKYPREVEFVDELPRSASGK 424
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
49-230 |
1.18e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 70.46 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 49 RRPARTILRAFlekARQTPHKPFLLFRDETLTYAQVDRRSNQVArALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLG 128
Cdd:PRK06178 32 ERPLTEYLRAW---ARERPQRPAIIFYGHVITYAELDELSDRFA-ALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 129 CAMACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPslkkdDVSIYYVSRTSNTDGI---------DSF----- 194
Cdd:PRK06178 108 AVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRA-----ETSLRHVIVTSLADVLpaeptlplpDSLraprl 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 227499621 195 -----LDKVDEVSTEPIPESWRSeVTFSTPALYIYTSGTTG 230
Cdd:PRK06178 183 aaagaIDLLPALRACTAPVPLPP-PALDALAALNYTGGTTG 222
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
46-521 |
1.67e-12 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 69.98 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 46 YGKRRPARTILRAFLEKARQTPHKP---FLLFRD-----ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAY 117
Cdd:PRK07529 18 LAARDLPASTYELLSRAAARHPDAPalsFLLDADpldrpETWTYAELLADVTRTANLLHS-LGVGPGDVVAFLLPNLPET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 118 VWLWLGLVKLGCAMAcLNYNIRAKSLLHCFQCCGAKVLL-VSPELQ-------AAVEEILPSLK------------KDDV 177
Cdd:PRK07529 97 HFALWGGEAAGIANP-INPLLEPEQIAELLRAAGAKVLVtLGPFPGtdiwqkvAEVLAALPELRtvvevdlarylpGPKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 178 SIYYVSRTSNTDGIDSFLdkvDEVSTEPIPESWRSE-VTFSTPALYIYTSGTTGA-TLALRTK----------------- 238
Cdd:PRK07529 176 LAVPLIRRKAHARILDFD---AELARQPGDRLFSGRpIGPDDVAAYFHTGGTTGMpKLAQHTHgnevanawlgalllglg 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 239 ------------------------FSASQ------------------FWDDCRKYNVTVIQYIGELLRYLCNSPqkPNDR 276
Cdd:PRK07529 253 pgdtvfcglplfhvnallvtglapLARGAhvvlatpqgyrgpgvianFWKIVERYRINFLSGVPTVYAALLQVP--VDGH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 277 D-HKVRLALGNG--LRGDVWRQFVKRFGdICIYEFYAATEGN-IGFMNYA---RKVGAVG-RVNYLQKKIItydlikydv 348
Cdd:PRK07529 331 DiSSLRYALCGAapLPVEVFRRFEAATG-VRIVEGYGLTEATcVSSVNPPdgeRRIGSVGlRLPYQRVRVV--------- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 349 ekdepVRDENGYCVR-VPKGEVGLLVckITQLTPFNGYagakaqTEKKKLRDVFKKGDlYFNSGDLLMVDHENFIYFHDR 427
Cdd:PRK07529 401 -----ILDDAGRYLRdCAVDEVGVLC--IAGPNVFSGY------LEAAHNKGLWLEDG-WLNTGDLGRIDADGYFWLTGR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 428 VGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPD-HEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYAR-PRF 505
Cdd:PRK07529 467 AKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVG--RPDaHAGELPVAYVQLKPGASATEAELLAFARDHIAERAAvPKH 544
|
570
....*....|....*....
gi 227499621 506 LRIQDTIEITG---TFKHR 521
Cdd:PRK07529 545 VRILDALPKTAvgkIFKPA 563
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
59-231 |
1.92e-12 |
|
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: 69.68 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 59 FLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNI 138
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRA-RGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 139 RAKSLLHCFQCCGAKVLLVSPELQ--AAVEEILPSLkkddvsiyyvsrtsntdgIDSFLDkVDEVSTEPIPESWRSEvtf 216
Cdd:cd17651 80 PAERLAFMLADAGPVLVLTHPALAgeLAVELVAVTL------------------LDQPGA-AAGADAEPDPALDADD--- 137
|
170
....*....|....*
gi 227499621 217 stPALYIYTSGTTGA 231
Cdd:cd17651 138 --LAYVIYTSGSTGR 150
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
77-526 |
2.09e-12 |
|
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: 69.38 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 77 ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLL 156
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKE-IGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 157 VSpelqaaveeilpsLKKDDVSIYYVSRTS-NTDGI---DSFL---DKVDEVSTEPIPeswRSEVTFSTPALYIYTSGTT 229
Cdd:cd05971 84 TD-------------GSDDPALIIYTSGTTgPPKGAlhaHRVLlghLPGVQFPFNLFP---RDGDLYWTPADWAWIGGLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 230 GATLAL-----------RTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVR-LALGNGLRGDVWRQFV 297
Cdd:cd05971 148 DVLLPSlyfgvpvlahrMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRaIATGGESLGEELLGWA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 298 KRFGDICIYEFYAATEGNIGFMN----YARKVGAVGRvnylqkkiityDLIKYDVEkdepVRDENGycVRVPKGEVGLLV 373
Cdd:cd05971 228 REQFGVEVNEFYGQTECNLVIGNcsalFPIKPGSMGK-----------PIPGHRVA----IVDDNG--TPLPPGEVGEIA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 374 CKITQLTPFNGYAGAKAQTEKKklrdvfKKGDlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTvgLVDF 453
Cdd:cd05971 291 VELPDPVAFLGYWNNPSATEKK------MAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEEC--LLKH 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227499621 454 VQEVNVYGVHVPDHE-GRIGMASIKMKENHEFD---GKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLV 526
Cdd:cd05971 362 PAVLMAAVVGIPDPIrGEIVKAFVVLNPGETPSdalAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
78-504 |
3.02e-12 |
|
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: 68.53 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 78 TLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLhcFQCCGAKVllv 157
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLA-ALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELA--FQLKDSDV--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 158 spelqaaveeilpslKKDDV-SIYYvsrTSNTDG-----IDSF---------------LDKVDevstepipeSWRSEVtf 216
Cdd:cd05912 75 ---------------KLDDIaTIMY---TSGTTGkpkgvQQTFgnhwwsaigsalnlgLTEDD---------NWLCAL-- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 217 stPALYIytSGTT--------GATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLC---NSPQKPNDRdhkvRLALG 285
Cdd:cd05912 126 --PLFHI--SGLSilmrsviyGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLeilGEGYPNNLR----CILLG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 286 NG-LRGDVWRQFVKRfgDICIYEFYAATEG-----NIGFMNYARKVGAVGRvnylqkkiityDLIKYDVEkdepVRDENG 359
Cdd:cd05912 198 GGpAPKPLLEQCKEK--GIPVYQSYGMTETcsqivTLSPEDALNKIGSAGK-----------PLFPVELK----IEDDGQ 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 360 ycvrvPKGEVGLLVCKITQLTPfnGYAGAKAQTEKkklrdVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENV 439
Cdd:cd05912 261 -----PPYEVGEILLKGPNVTK--GYLNRPDATEE-----SFENG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENI 326
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227499621 440 ATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASIKMKEnhEFDGKKLFQHIADYLPSYARPR 504
Cdd:cd05912 327 YPAEIEEVLLSHPAIKEAGVVG--IPDDKwGQVPVAFVVSER--PISEEELIAYCSEKLAKYKVPK 388
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
79-519 |
3.17e-12 |
|
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: 68.68 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 79 LTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVS 158
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSL-GVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 159 PELQAAVEeilpslKKDDVSIYYVSRTSNT-DGIdsfLDKVDEVSTEPIPESW----RSEVTFSTPALYIYTSGTTGATL 233
Cdd:cd05969 80 EELYERTD------PEDPTLLHYTSGTTGTpKGV---LHVHDAMIFYYFTGKYvldlHPDDIYWCTADPGWVTGTVYGIW 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 234 A----------LRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNS---PQKPNDRDH-KVRLALGNGLRGDVWRQFVKR 299
Cdd:cd05969 151 ApwlngvtnvvYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEgdeLARKYDLSSlRFIHSVGEPLNPEAIRWGMEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 300 FGdICIYEFYAATE-GNIGFMNYAR---KVGAVGR-VNYLQKKIItydlikydvekdepvrDENGYcvRVPKGEVGLLVC 374
Cdd:cd05969 231 FG-VPIHDTWWQTEtGSIMIANYPCmpiKPGSMGKpLPGVKAAVV----------------DENGN--ELPPGTKGILAL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 375 KITQLTPFNGYAGakaqtEKKKLRDVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADtvGLVDF- 453
Cdd:cd05969 292 KPGWPSMFRGIWN-----DEERYKNSFIDG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVES--ALMEHp 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227499621 454 -VQEVNVYGvhVPDHE-GRIGMASIKMKENHEFD---GKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 519
Cdd:cd05969 363 aVAEAGVIG--KPDPLrGEIIKAFISLKEGFEPSdelKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGK 431
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
51-230 |
8.31e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 67.76 E-value: 8.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 51 PARTILRAFLEKARQTPHKPFLLFRD------ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGL 124
Cdd:PRK12582 47 YPRSIPHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLD-LGLDPGRPVMILSGNSIEHALMTLAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 125 VKLGCAMACL--NYNI----RAKsLLHCFQCCGAKVLLVspELQAAVEEILPSLKKDDVSIYYVSRTSNTDGIDSFLDKV 198
Cdd:PRK12582 126 MQAGVPAAPVspAYSLmshdHAK-LKHLFDLVKPRVVFA--QSGAPFARALAALDLLDVTVVHVTGPGEGIASIAFADLA 202
|
170 180 190
....*....|....*....|....*....|..
gi 227499621 199 DEVSTEPIPESwRSEVTFSTPALYIYTSGTTG 230
Cdd:PRK12582 203 ATPPTAAVAAA-IAAITPDTVAKYLFTSGSTG 233
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
75-230 |
8.72e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 67.61 E-value: 8.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 75 RDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKV 154
Cdd:PRK04319 70 RKEKYTYKELKELSNKFANVLKE-LGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 155 LLVSPEL-QAAVEEILPSLKK-----DDVsiyyvsrtSNTDGIDSFLDKVDEVSTEPIPESWRSEvtfsTPALYIYTSGT 228
Cdd:PRK04319 149 LITTPALlERKPADDLPSLKHvllvgEDV--------EEGPGTLDFNALMEQASDEFDIEWTDRE----DGAILHYTSGS 216
|
..
gi 227499621 229 TG 230
Cdd:PRK04319 217 TG 218
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
53-230 |
1.32e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 66.91 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 53 RTILRAFLE-KARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAM 131
Cdd:PRK08314 9 ETSLFHNLEvSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 132 ACLNYNIRAKSLLHCFQCCGAKVLLVSPELqaaVEEILPSLKKDDVSIYYVSRtsntdgidsFLDKVDEVSTEPIPE--- 208
Cdd:PRK08314 89 VPVNPMNREEELAHYVTDSGARVAIVGSEL---APKVAPAVGNLRLRHVIVAQ---------YSDYLPAEPEIAVPAwlr 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 227499621 209 --------------SWRS-----------EVTFSTPALYIYTSGTTG 230
Cdd:PRK08314 157 aepplqalapggvvAWKEalaaglappphTAGPDDLAVLPYTSGTTG 203
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
57-515 |
1.62e-11 |
|
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: 66.58 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 57 RAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNY 136
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 137 NIRAKSLLHCFQCCGAKVLLVSPELQA--AVEEILPSLKKDDVSIY---------------YVSRTSNTDG------ID- 192
Cdd:cd17655 80 DYPEERIQYILEDSGADILLTQSHLQPpiAFIGLIDLLDEDTIYHEesenlepvsksddlaYVIYTSGSTGkpkgvmIEh 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 193 -------SFLDKV---DEVSTEPIPESwrseVTFSTPALYIYTSGTTGATLAL---RTKFSASQFWDDCRKYNVTVIQYI 259
Cdd:cd17655 160 rgvvnlvEWANKViyqGEHLRVALFAS----ISFDASVTEIFASLLSGNTLYIvrkETVLDGQALTQYIRQNRITIIDLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 260 GELLRYLcNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDIC-IYEFYAATEGNIGFMNYarkvgavgrvnylqkki 338
Cdd:cd17655 236 PAHLKLL-DAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPtITNAYGPTETTVDASIY----------------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 339 itydliKYDVEKDEPVR---------------DENGYCvrVPKGEVGLL------VCKitqltpfnGYAGAKAQTEKKKL 397
Cdd:cd17655 298 ------QYEPETDQQVSvpigkplgntriyilDQYGRP--QPVGVAGELyiggegVAR--------GYLNRPELTAEKFV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 398 RDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVygVHVPDHEGRIGMASIK 477
Cdd:cd17655 362 DDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVV--IARKDEQGQNYLCAYI 439
|
490 500 510
....*....|....*....|....*....|....*...
gi 227499621 478 MKENhEFDGKKLFQHIADYLPSYARPRFLRIQDTIEIT 515
Cdd:cd17655 440 VSEK-ELPVAQLREFLARELPDYMIPSYFIKLDEIPLT 476
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
68-527 |
2.45e-11 |
|
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: 65.77 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 68 HKPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVwlwlgLVKLGCAMAclnyniraksllhcf 147
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYV-----VAQLAIWRA--------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 148 qccGAKVLLVSP-----ELQAAVEEILPSLKKDDVSIYYvsrTSNTDGI--------DSFLDKVDEVSTEpipESWRSE- 213
Cdd:cd05941 61 ---GGVAVPLNPsyplaELEYVITDSEPSLVLDPALILY---TSGTTGRpkgvvlthANLAANVRALVDA---WRWTEDd 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 214 --------------VTFSTPALYiytsgtTGATLALRTKFSASQFWDDCRKYNVTVIQ-----YIgELLRYLcnsPQKPN 274
Cdd:cd05941 132 vllhvlplhhvhglVNALLCPLF------AGASVEFLPKFDPKEVAISRLMPSITVFMgvptiYT-RLLQYY---EAHFT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 275 DRDHKVRLALGN---------GLRGDVWRQFVKRFGDIcIYEFYAATEGNIGFMNYA---RKVGAVGR----VnylQKKI 338
Cdd:cd05941 202 DPQFARAAAAERlrlmvsgsaALPVPTLEEWEAITGHT-LLERYGMTEIGMALSNPLdgeRRPGTVGMplpgV---QARI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 339 itydlikydvekdepVRDENGycVRVPKGEVGLLVCKITQLtpFNGY-----AGAKAQTEkkklrdvfkkgDLYFNSGDL 413
Cdd:cd05941 278 ---------------VDEETG--EPLPRGEVGEIQVRGPSV--FKEYwnkpeATKEEFTD-----------DGWFKTGDL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 414 LMVDHENFIYFHDRVG-DTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASIKMKEN-HEFDGKKLF 490
Cdd:cd05941 328 GVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIG--VPDPDwGERVVAVVVLRAGaAALSLEELK 405
|
490 500 510
....*....|....*....|....*....|....*..
gi 227499621 491 QHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVE 527
Cdd:cd05941 406 EWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
54-316 |
4.27e-11 |
|
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: 65.15 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 54 TILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMAC 133
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQS-LGVKSESLVGICVERSLEMIIGLLAILKAGGAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 134 LNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVeeilpslkkddvsIYYVSRTSNTDGI----DSFLDKVDEVSTE-PIPE 208
Cdd:cd17644 80 LDPNYPQERLTYILEDAQISVLLTQPENLAYV-------------IYTSGSTGKPKGVmiehQSLVNLSHGLIKEyGITS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 209 SWR----SEVTFSTPALYIYTSGTTGATLALRTK---FSASQFWDDCRKYNVTVI--------QYIGELLRYLCNSPQKP 273
Cdd:cd17644 147 SDRvlqfASIAFDVAAEEIYVTLLSGATLVLRPEemrSSLEDFVQYIQQWQLTVLslppaywhLLVLELLLSTIDLPSSL 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 227499621 274 ndrdhKVRLALGNGLRGDVWRQFVKRFGD-ICIYEFYAATEGNI 316
Cdd:cd17644 227 -----RLVIVGGEAVQPELVRQWQKNVGNfIQLINVYGPTEATI 265
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
56-504 |
6.24e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 65.06 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 56 LRAFLEK-ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACL 134
Cdd:PRK07470 9 LAHFLRQaARRFPDRIALVWGDRSWTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 135 NYNIRAKSLLHCFQCCGAKVLLVS---PELQAAVEEILPSLKKdDVSIyyvsrtSNTDGIDSFLDKVDEVSTEPIPEswr 211
Cdd:PRK07470 88 NFRQTPDEVAYLAEASGARAMICHadfPEHAAAVRAASPDLTH-VVAI------GGARAGLDYEALVARHLGARVAN--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 212 SEVTFSTPALYIYTSGTTG-------------------------------------------------------ATLALR 236
Cdd:PRK07470 158 AAVDHDDPCWFFFTSGTTGrpkaavlthgqmafvitnhladlmpgtteqdaslvvaplshgagihqlcqvargaATVLLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 237 T-KFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNdRDH-KVRLALGNG---LRGDVWRQfVKRFGDIcIYEFYAA 311
Cdd:PRK07470 238 SeRFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDR-YDHsSLRYVIYAGapmYRADQKRA-LAKLGKV-LVQYFGL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 312 TE--GNIGFMNYA---------RKVGAVGrvnylqkkiitYDLIKYDVEkdepVRDENGYcvRVPKGEVGllvcKITQLT 380
Cdd:PRK07470 315 GEvtGNITVLPPAlhdaedgpdARIGTCG-----------FERTGMEVQ----IQDDEGR--ELPPGETG----EICVIG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 381 P--FNGY-----AGAKAqtekkklrdvFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDF 453
Cdd:PRK07470 374 PavFAGYynnpeANAKA----------FRDG--WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPA 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 227499621 454 VQEVNVYGvhVPDHE-GRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPR 504
Cdd:PRK07470 442 VSEVAVLG--VPDPVwGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPK 491
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
443-519 |
7.95e-11 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 57.94 E-value: 7.95e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227499621 443 EVADTVGLVDFVQEVNVYGVHVPDhEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 519
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDEL-KGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
53-317 |
8.01e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 65.57 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 53 RTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMA 132
Cdd:PRK12467 512 DCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYV 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 133 CLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVE---------------------EILPSLKKDDVSIYYVSRTSNTDGI 191
Cdd:PRK12467 591 PLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPvpaglrslcldepadllcgysGHNPEVALDPDNLAYVIYTSGSTGQ 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 192 --------DSFLDKVDEVSTEPIPESWRSEVTFSTPA-----LYIYTSGTTGATLALRTK---FSASQFWDDCRKYNVTV 255
Cdd:PRK12467 671 pkgvaishGALANYVCVIAERLQLAADDSMLMVSTFAfdlgvTELFGALASGATLHLLPPdcaRDAEAFAALMADQGVTV 750
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227499621 256 IQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQfVKRFGDIC-IYEFYAATEGNIG 317
Cdd:PRK12467 751 LKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLAR-VRALGPGArLINHYGPTETTVG 812
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
72-245 |
9.46e-11 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 64.40 E-value: 9.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 72 LLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCG 151
Cdd:cd17632 61 LLPRFETITYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 152 AKVLLVSPE-LQAAVEEIL--PSLKKDDVSIYYVSRTSNTDGIDSFLDK--------------VDEVSTEPIPESWRSEV 214
Cdd:cd17632 141 PRLLAVSAEhLDLAVEAVLegGTPPRLVVFDHRPEVDAHRAALESARERlaavgipvttltliAVRGRDLPPAPLFRPEP 220
|
170 180 190
....*....|....*....|....*....|..
gi 227499621 215 TFSTPALYIYTSGTTGATL-ALRTKFSASQFW 245
Cdd:cd17632 221 DDDPLALLIYTSGSTGTPKgAMYTERLVATFW 252
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
80-525 |
1.08e-10 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 64.19 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 80 TYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNynIR------AKSLLHCfqccGAK 153
Cdd:cd12119 27 TYAEVAERARRLANALRR-LGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTIN--PRlfpeqiAYIINHA----EDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 154 VLLVSPELQAAVEEILPSLKKDDVSIYYVSRTSNT-DGIDSFLDKVDEVSTEPIPESWrSEVTFSTPALYIYTSGTTGA- 231
Cdd:cd12119 100 VVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAMPePAGVGVLAYEELLAAESPEYDW-PDFDENTAAAICYTSGTTGNp 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 232 -------------TLALRTK----FSAS--------QF----W-------------------DD-------CRKYNVTVI 256
Cdd:cd12119 179 kgvvyshrslvlhAMAALLTdglgLSESdvvlpvvpMFhvnaWglpyaaamvgaklvlpgpyLDpaslaelIEREGVTFA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 257 QYIGELLRYLCNSPQKPNDRDHKVRLALGNGlrGDVWRQFVKRFGD--ICIYEFYAATE-GNIGFMNY----ARKVGAVG 329
Cdd:cd12119 259 AGVPTVWQGLLDHLEANGRDLSSLRRVVIGG--SAVPRSLIEAFEErgVRVIHAWGMTEtSPLGTVARppseHSNLSEDE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 330 RVNYLQKkiITYDLIKYDVEkdepVRDENGycVRVPK--GEVGLLVCK---ITQltpfnGYAGAKAQTEkkklrdvFKKG 404
Cdd:cd12119 337 QLALRAK--QGRPVPGVELR----IVDDDG--RELPWdgKAVGELQVRgpwVTK-----SYYKNDEESE-------ALTE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 405 DLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVhvpDHE--GRIGMASIKMKENH 482
Cdd:cd12119 397 DGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGV---PHPkwGERPLAVVVLKEGA 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 227499621 483 EFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTL 525
Cdd:cd12119 474 TVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
60-230 |
1.34e-10 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 63.85 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 60 LEKARQTPHKPFLLfrD----ETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLN 135
Cdd:PLN02246 30 FERLSEFSDRPCLI--DgatgRVYTYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTAN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 136 YNIRAKSLLHCFQCCGAKVLLVSPelqAAVEEILPSLKKDDVSIyyVSRTSNTDGIDSF--LDKVDEvstEPIPEswrSE 213
Cdd:PLN02246 107 PFYTPAEIAKQAKASGAKLIITQS---CYVDKLKGLAEDDGVTV--VTIDDPPEGCLHFseLTQADE---NELPE---VE 175
|
170
....*....|....*..
gi 227499621 214 VTFSTPALYIYTSGTTG 230
Cdd:PLN02246 176 ISPDDVVALPYSSGTTG 192
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
53-519 |
2.37e-10 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 62.97 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 53 RTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMA 132
Cdd:PRK08751 25 RTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 133 CLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPslkkdDVSIYYVSRTSNTDGID----SFLDKVDEVSTEPIPE 208
Cdd:PRK08751 105 NVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIA-----DTPVKQVITTGLGDMLGfpkaALVNFVVKYVKKLVPE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 209 -------SWRSEVTF----STPALYI---------YTSGTTG----ATLALRTKFSASQ--------------------- 243
Cdd:PRK08751 180 yringaiRFREALALgrkhSMPTLQIepddiaflqYTGGTTGvakgAMLTHRNLVANMQqahqwlagtgkleegcevvit 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 244 -----------------------------------FWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGL 288
Cdd:PRK08751 260 alplyhifaltanglvfmkiggcnhlisnprdmpgFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGM 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 289 RgdVWRQFVKRFGDIC---IYEFYAATEGN----IGFMNYARKVGAVGRvnylqkKIITYDLIkydvekdepVRDENGYC 361
Cdd:PRK08751 340 A--VQRSVAERWKQVTgltLVEAYGLTETSpaacINPLTLKEYNGSIGL------PIPSTDAC---------IKDDAGTV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 362 VrvPKGEVGLLVCKITQLtpFNGYAgaKAQTEKKKLRDvfkkGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVAT 441
Cdd:PRK08751 403 L--AIGEIGELCIKGPQV--MKGYW--KRPEETAKVMD----ADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYP 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227499621 442 TEVADTVGLVDFVQEVNVYGvhVPDHEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 519
Cdd:PRK08751 473 NEIEDVIAMMPGVLEVAAVG--VPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGK 548
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-230 |
2.95e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.44 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 52 ARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAM 131
Cdd:PRK12316 510 QRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIEMVVALLAILKAGGAY 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 132 ACLNYNIRAKSLLHCFQCCGAKVLLVspelQAAVEEILPSLKKDDVSIYyvsrtsntDGIDSFLDKvdeVSTEPiPEswr 211
Cdd:PRK12316 589 VPLDPEYPAERLAYMLEDSGVQLLLS----QSHLGRKLPLAAGVQVLDL--------DRPAAWLEG---YSEEN-PG--- 649
|
170
....*....|....*....
gi 227499621 212 SEVTFSTPALYIYTSGTTG 230
Cdd:PRK12316 650 TELNPENLAYVIYTSGSTG 668
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
86-519 |
2.98e-10 |
|
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: 62.46 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 86 RRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMAC----LNYNIRAKSLLHCFQCCGAKVLLVSPEL 161
Cdd:cd05922 1 LGVSAAASALLEA-GGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLvfvpLNPTLKESVLRYLVADAGGRIVLADAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 162 QAAVEEILPSLKKDDVSIyyvsrtsNTDGIDSFLDKVDEVstEPIPESwrsevtfstPALYIYTSGTT------------ 229
Cdd:cd05922 80 ADRLRDALPASPDPGTVL-------DADGIRAARASAPAH--EVSHED---------LALLLYTSGSTgspklvrlshqn 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 230 -----------------------------------------GATLALRTKFSASQ-FWDDCRKYNVT---VIQYIGEL-- 262
Cdd:cd05922 142 llanarsiaeylgitaddraltvlplsydyglsvlnthllrGATLVLTNDGVLDDaFWEDLREHGATglaGVPSTYAMlt 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 263 -----------LRYLCNSpqkpndrdhkvrlalGNGLRGDVWRQFVKRFGDICIYEFYAATEGNiGFMNY------ARKV 325
Cdd:cd05922 222 rlgfdpaklpsLRYLTQA---------------GGRLPQETIARLRELLPGAQVYVMYGQTEAT-RRMTYlpperiLEKP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 326 GAVGRVnyLQKKIITydlikydvekdepVRDENGYcvRVPKGEVGLLVckITQLTPFNGYAGAKAQTEKKKLrdvfKKGD 405
Cdd:cd05922 286 GSIGLA--IPGGEFE-------------ILDDDGT--PTPPGEPGEIV--HRGPNVMKGYWNDPPYRRKEGR----GGGV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 406 LYfnSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIGMASIKMKEnhefD 485
Cdd:cd05922 343 LH--TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKI----D 416
|
490 500 510
....*....|....*....|....*....|....
gi 227499621 486 GKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 519
Cdd:cd05922 417 PKDVLRSLAERLPPYKVPATVRVVDELPLTASGK 450
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
78-519 |
4.42e-10 |
|
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: 61.96 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 78 TLTYAQVDRRSNQVARALHDhlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLV 157
Cdd:cd05909 7 SLTYRKLLTGAIALARKLAK--MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 158 SPELQAAVEEILPSLKKDDVSIYYVSRTSNTDgidSFLDKVDEVSTEPIPESW------RSEVTFSTPALYIYTSGTTGA 231
Cdd:cd05909 85 SKQFIEKLKLHHLFDVEYDARIVYLEDLRAKI---SKADKCKAFLAGKFPPKWllrifgVAPVQPDDPAVILFTSGSEGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 232 --------------TLALRTKFSASQfwDD----------CRKYNVT----------VIQY--------IGELLR----- 264
Cdd:cd05909 162 pkgvvlshknllanVEQITAIFDPNP--EDvvfgalpffhSFGLTGClwlpllsgikVVFHpnpldykkIPELIYdkkat 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 265 YLCNSP--------QKPNDRDHKVRLAL--GNGLRGDVWRQFVKRFGdICIYEFYAATEGN----IGFMNYARKVGAVGR 330
Cdd:cd05909 240 ILLGTPtflrgyarAAHPEDFSSLRLVVagAEKLKDTLRQEFQEKFG-IRILEGYGTTECSpvisVNTPQSPNKEGTVGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 331 -VNYLQKKIItydlikyDVEKDEPVrdengycvrvPKGEVGLLVCKITQLtpFNGYAGAKAQTekkklrdVFKKGDLYFN 409
Cdd:cd05909 319 pLPGMEVKIV-------SVETHEEV----------PIGEGGLLLVRGPNV--MLGYLNEPELT-------SFAFGDGWYD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 410 SGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVdFVQEVNVYGVHVPDheGRIGMASIKMKENHEFDGKKL 489
Cdd:cd05909 373 TGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEI-LPEDNEVAVVSVPD--GRKGEKIVLLTTTTDTDPSSL 449
|
490 500 510
....*....|....*....|....*....|.
gi 227499621 490 FQHI-ADYLPSYARPRFLRIQDTIEITGTFK 519
Cdd:cd05909 450 NDILkNAGISNLAKPSYIHQVEEIPLLGTGK 480
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
59-230 |
4.58e-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: 61.91 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 59 FLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNI 138
Cdd:cd17646 4 VAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRA-RGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 139 RAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVsiyyvsrtsntdGIDSFLDKVDEVSTEPipeswrsevtfST 218
Cdd:cd17646 83 PADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDE------------ALAAPPATPPLVPPRP-----------DN 139
|
170
....*....|..
gi 227499621 219 PALYIYTSGTTG 230
Cdd:cd17646 140 LAYVIYTSGSTG 151
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
220-519 |
4.98e-10 |
|
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: 60.88 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 220 ALYiytsgtTGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSpqkpNDRDHKVRLAL--GNGLRGDVWRQFV 297
Cdd:cd17633 62 ALY------LGGTFIGQRKFNPKSWIRKINQYNATVIYLVPTMLQALART----LEPESKIKSIFssGQKLFESTKKKLK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 298 KRFGDICIYEFYAATEGNigFMNY-----ARKVGAVGRVnylqkkiitydLIKYDVEkdepVRDENGycvrvpkGEVGLL 372
Cdd:cd17633 132 NIFPKANLIEFYGTSELS--FITYnfnqeSRPPNSVGRP-----------FPNVEIE----IRNADG-------GEIGKI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 373 VCKITQLtpFNGYAGAKAQTEkkklrdvfkkgDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVD 452
Cdd:cd17633 188 FVKSEMV--FSGYVRGGFSNP-----------DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIP 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227499621 453 FVQEVNVYGvhVPDHE-GRIGMASIKMKenhEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 519
Cdd:cd17633 255 GIEEAIVVG--IPDARfGEIAVALYSGD---KLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGK 317
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
51-231 |
5.03e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 62.07 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 51 PARTILRAFL-EKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALhDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGC 129
Cdd:PRK06164 7 PRADTLASLLdAHARARPDAVALIDEDRPLSRAELRALVDRLAAWL-AAQGVRRGDRVAVWLPNCIEWVVLFLACARLGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 130 AMACLNYNIRAKSLLHCFQCCGAKVLLVSP-----ELQAAVEEILPSLKKDDVSIYYVSRTSNTDGIDSFLDKVDEV--- 201
Cdd:PRK06164 86 TVIAVNTRYRSHEVAHILGRGRARWLVVWPgfkgiDFAAILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFalp 165
|
170 180 190
....*....|....*....|....*....|
gi 227499621 202 STEPIPESWRSEVTFSTPALYIYTSGTTGA 231
Cdd:PRK06164 166 DPAPPAAAGERAADPDAGALLFTTSGTTSG 195
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
53-230 |
6.26e-10 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 61.61 E-value: 6.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 53 RTILRAFLEKARQTPHKPFLL-FRD-----ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVK 126
Cdd:PRK13295 24 RTINDDLDACVASCPDKTAVTaVRLgtgapRRFTYRELAALVDRVAVGLAR-LGVGRGDVVSCQLPNWWEFTVLYLACSR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 127 LGCAMACLNYNIRAKSLLHCFQCCGAKVLLVS--------PELQAAVEEILPSLKKddvsIYYVsrtsNTDGIDSFldkv 198
Cdd:PRK13295 103 IGAVLNPLMPIFRERELSFMLKHAESKVLVVPktfrgfdhAAMARRLRPELPALRH----VVVV----GGDGADSF---- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 227499621 199 DEVSTEPIPESWRSE---VTFSTP-----ALYIYTSGTTG 230
Cdd:PRK13295 171 EALLITPAWEQEPDApaiLARLRPgpddvTQLIYTSGTTG 210
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
59-504 |
6.48e-10 |
|
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: 61.55 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 59 FLEKARQT-PHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:cd12118 9 FLERAAAVyPDRTSIVYGDRRYTWRQTYDRCRRLASALAA-LGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 138 IRAKSLLHCFQCCGAKVLLVSPELQ--AAVEE-------ILPSLKKDDVSIYYVS-RTSNTDGI-----DSFLDKVDEVS 202
Cdd:cd12118 88 LDAEEIAFILRHSEAKVLFVDREFEyeDLLAEgdpdfewIPPADEWDPIALNYTSgTTGRPKGVvyhhrGAYLNALANIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 203 TEPIPES----WRSEVTFSTPALYIYTSGTTGAT-LALRtKFSASQFWDDCRKYNVTviQYIGE--LLRYLCNSPqkPND 275
Cdd:cd12118 168 EWEMKQHpvylWTLPMFHCNGWCFPWTVAAVGGTnVCLR-KVDAKAIYDLIEKHKVT--HFCGAptVLNMLANAP--PSD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 276 R---DHKVRLALGNGLRGDVWRQFVKRFGdICIYEFYAATE--GNIGFMNY------------ARKVGAVGrVNYLQKKI 338
Cdd:cd12118 243 ArplPHRVHVMTAGAPPPAAVLAKMEELG-FDVTHVYGLTEtyGPATVCAWkpewdelpteerARLKARQG-VRYVGLEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 339 ItyDLIKYDVEKDEPvRDenGYCVrvpkGEV---GLLVCKitqltpfnGYAGAKAQTEKkklrdVFKKGdlYFNSGDLLM 415
Cdd:cd12118 321 V--DVLDPETMKPVP-RD--GKTI----GEIvfrGNIVMK--------GYLKNPEATAE-----AFRGG--WFHSGDLAV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 416 VDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPD-HEGRIGMASIKMKENHEFDGKKLFQHIA 494
Cdd:cd12118 377 IHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVA--RPDeKWGEVPCAFVELKEGAKVTEEEIIAFCR 454
|
490
....*....|
gi 227499621 495 DYLPSYARPR 504
Cdd:cd12118 455 EHLAGFMVPK 464
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
58-230 |
6.87e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 62.28 E-value: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 58 AFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:PRK12316 2008 RIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRA-RGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPN 2086
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 138 IRAKSLLHCFQCCGAKVLLVspelQAAVEEILPSlkkddvsiyyvsrtsnTDGIDSF-LDKVDEVSTEPI--PESwrsEV 214
Cdd:PRK12316 2087 YPAERLAYMLEDSGAALLLT----QRHLLERLPL----------------PAGVARLpLDRDAEWADYPDtaPAV---QL 2143
|
170
....*....|....*.
gi 227499621 215 TFSTPALYIYTSGTTG 230
Cdd:PRK12316 2144 AGENLAYVIYTSGSTG 2159
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
54-504 |
7.08e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 61.55 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 54 TILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMAC 133
Cdd:PRK05605 33 TLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRA-LGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 134 LNYNIRAKSLLHCFQCCGAKVLLV----SPELQ-----AAVEEI--------------------LPSLKKddvsiyyvSR 184
Cdd:PRK05605 112 HNPLYTAHELEHPFEDHGARVAIVwdkvAPTVErlrrtTPLETIvsvnmiaampllqrlalrlpIPALRK--------AR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 185 TSNTDGIDSFLDKVDEVSTEPIPESWRS---EVTFSTPALYIYTSGTT----GATLALRTKFS---ASQFW------DDC 248
Cdd:PRK05605 184 AALTGPAPGTVPWETLVDAAIGGDGSDVshpRPTPDDVALILYTSGTTgkpkGAQLTHRNLFAnaaQGKAWvpglgdGPE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 249 RKY-------------NVTVIQYIG-ELLryLCNSPQKP------------------------------NDRD-HKVRLA 283
Cdd:PRK05605 264 RVLaalpmfhaygltlCLTLAVSIGgELV--LLPAPDIDlildamkkhpptwlpgvpplyekiaeaaeeRGVDlSGVRNA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 284 LGNG--LRGDVWRQFVKRFGDICIyEFYAATE------GNIgfMNYARKVGAVG--------RVnylqkkiitydlikyd 347
Cdd:PRK05605 342 FSGAmaLPVSTVELWEKLTGGLLV-EGYGLTEtspiivGNP--MSDDRRPGYVGvpfpdtevRI---------------- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 348 VEKDEPVRDengycvrVPKGEVGLLVCKITQLtpFNGYAGAKAQTEKkklrdVFKKGdlYFNSGDLLMVDHENFIYFHDR 427
Cdd:PRK05605 403 VDPEDPDET-------MPDGEEGELLVRGPQV--FKGYWNRPEETAK-----SFLDG--WFRTGDVVVMEEDGFIRIVDR 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227499621 428 VGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIgMASIKMKENHEFDGKKLFQHIADYLPSYARPR 504
Cdd:PRK05605 467 IKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEV-VAAVVLEPGAALDPEGLRAYCREHLTRYKVPR 542
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
364-528 |
8.22e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 61.59 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 364 VPKGEVGLLVCKITQLtpFNGYAGAKAQTEKkklrdVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTE 443
Cdd:PRK06710 398 LPPGEIGEIVVKGPQI--MKGYWNKPEETAA-----VLQDG--WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPRE 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 444 VADTVGLVDFVQEVNVYGVHVPdHEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKM 523
Cdd:PRK06710 469 VEEVLYEHEKVQEVVTIGVPDP-YRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRR 547
|
....*
gi 227499621 524 TLVEE 528
Cdd:PRK06710 548 VLIEE 552
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
82-527 |
8.33e-10 |
|
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: 61.24 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 82 AQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYV-WLWLGLvklGCAMACLNYNIRAKSLLH---CFQCCGAKVLLV 157
Cdd:cd05929 1 LEARDLDRAQVFHQRR-LLLLDVYSIALNRNARAAAAeGVWIAD---GVYIYLINSILTVFAAAAawkCGACPAYKSSRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 158 SPELQAAVEEILPSLKkdDVSIYYVSRTSntDGIDSFLDKVDEVSTEPIPESWRsevtfstPALYIYTSGTTG------- 230
Cdd:cd05929 77 PRAEACAIIEIKAAAL--VCGLFTGGGAL--DGLEDYEAAEGGSPETPIEDEAA-------GWKMLYSGGTTGrpkgikr 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 231 -------------------------------------------------ATLALRTKFSASQFWDDCRKYNVTVIQYIGE 261
Cdd:cd05929 146 glpggppdndtlmaaalgfgpgadsvylspaplyhaapfrwsmtalfmgGTLVLMEKFDPEEFLRLIERYRVTFAQFVPT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 262 LLRYLCNSPQKPNDRDH--KVRLALGNGLRGDVW--RQFVKRFGDIcIYEFYAATEGN----IGFMNYARKVGAVGRVny 333
Cdd:cd05929 226 MFVRLLKLPEAVRNAYDlsSLKRVIHAAAPCPPWvkEQWIDWGGPI-IWEYYGGTEGQgltiINGEEWLTHPGSVGRA-- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 334 lqkkiitydlikydVEKDEPVRDENGYcvRVPKGEVGLLVCKITQ-LTPFNGYAGAKAQTEKKKLRDVfkkgdlyfnsGD 412
Cdd:cd05929 303 --------------VLGKVHILDEDGN--EVPPGEIGEVYFANGPgFEYTNDPEKTAAARNEGGWSTL----------GD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 413 LLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASI---KMKENHEFDGKK 488
Cdd:cd05929 357 VGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVG--VPDEElGQRVHAVVqpaPGADAGTALAEE 434
|
490 500 510
....*....|....*....|....*....|....*....
gi 227499621 489 LFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVE 527
Cdd:cd05929 435 LIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
63-230 |
9.00e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 61.04 E-value: 9.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 63 ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKlgcamaclnyniraks 142
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFA-QQGVVEGSGVALRGKNSPETLLAYLALLQ---------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 143 llhcfqcCGAKVLLVSPELQAA-VEEILPSLKKDdvSIYYVSRTSNTDGIDSFLdkVDEVSTEPiPESWRSEvtfsTPAL 221
Cdd:PRK09029 76 -------CGARVLPLNPQLPQPlLEELLPSLTLD--FALVLEGENTFSALTSLH--LQLVEGAH-AVAWQPQ----RLAT 139
|
....*....
gi 227499621 222 YIYTSGTTG 230
Cdd:PRK09029 140 MTLTSGSTG 148
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
57-509 |
9.86e-10 |
|
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: 60.79 E-value: 9.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 57 RAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNY 136
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 137 NIRAKSLLHCFQCCGAKvLLVSPElqaaveeilpslKKDDVSiyYVSRTSNTDGI--------DSFLDKVDEVS----TE 204
Cdd:cd17653 80 KLPSARIQAILRTSGAT-LLLTTD------------SPDDLA--YIIFTSGSTGIpkgvmvphRGVLNYVSQPParldVG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 205 PipeSWRS----EVTFSTPALYIYTSGTTGATLALRTkfSASQFWDDCRKYNVTVIQyiGELLRYLcnspqKPNDRDHKV 280
Cdd:cd17653 145 P---GSRVaqvlSIAFDACIGEIFSTLCNGGTLVLAD--PSDPFAHVARTVDALMST--PSILSTL-----SPQDFPNLK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 281 RLALGN-----GLRgDVWRqfvkrfGDICIYEFYAATEGNIGfmnyarkvgavgrVNYLQKKIITYDLIKYdvekdePVR 355
Cdd:cd17653 213 TIFLGGeavppSLL-DRWS------PGRRLYNAYGPTECTIS-------------STMTELLPGQPVTIGK------PIP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 356 deNGYCV-------RVPKGEVGLLVCKITQLTPfnGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRV 428
Cdd:cd17653 267 --NSTCYildadlqPVPEGVVGEICISGVQVAR--GYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGRE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 429 GDTFRWKGENVATTEVADTVGLvdfvQEVNVYGVHVPDHEGRIGM----ASIkmkenhefDGKKLFQHIADYLPSYARP- 503
Cdd:cd17653 343 DNQVKVRGFRINLEEIEEVVLQ----SQPEVTQAAAIVVNGRLVAfvtpETV--------DVDGLRSELAKHLPSYAVPd 410
|
....*.
gi 227499621 504 RFLRIQ 509
Cdd:cd17653 411 RIIALD 416
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
60-443 |
1.24e-09 |
|
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: 60.71 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 60 LEKARQTPHKPFLLfrD----ETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLN 135
Cdd:cd05904 12 FLFASAHPSRPALI--DaatgRALTYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTAN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 136 YNIRAKSLLHCFQCCGAKVLLVSPELQAAVEE------ILPSLkkDDVSIYYVSRTSNTDGidsfldkvDEVSTEPIPES 209
Cdd:cd05904 89 PLSTPAEIAKQVKDSGAKLAFTTAELAEKLASlalpvvLLDSA--EFDSLSFSDLLFEADE--------AEPPVVVIKQD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 210 wrsevtfSTPALyIYTSGTTG--------------------------------------------------------ATL 233
Cdd:cd05904 159 -------DVAAL-LYSSGTTGrskgvmlthrnliamvaqfvagegsnsdsedvflcvlpmfhiyglssfalgllrlgATV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 234 ALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPqKPNDRDHKVRLALGNG---LRGDVWRQFVKRFGDICIYEFYA 310
Cdd:cd05904 231 VVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSP-IVDKYDLSSLRQIMSGaapLGKELIEAFRAKFPNVDLGQGYG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 311 ATE-GNIGFMNYA-----RKVGAVGRV--NyLQKKIItydlikyDVE--KDEPVRDENGYCVRVPKgevgllVCKitqlt 380
Cdd:cd05904 310 MTEsTGVVAMCFApekdrAKYGSVGRLvpN-VEAKIV-------DPEtgESLPPNQTGELWIRGPS------IMK----- 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227499621 381 pfnGYAGAKAQTEkkklRDVFKKGDLYfnSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTE 443
Cdd:cd05904 371 ---GYLNNPEATA----ATIDKEGWLH--TGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAE 424
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
59-230 |
2.25e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 59.96 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 59 FLEKARQT-PHKPFLLFRDETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:PRK08162 23 FLERAAEVyPDRPAVIHGDRRRTWAETYARCRRLASALA-RRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 138 IRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIYYVSRTSNTDGidsflDKVDEVSTEPIPESWRSEVTFS 217
Cdd:PRK08162 102 LDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVIDVDDPEYPGG-----RFIGALDYEAFLASGDPDFAWT 176
|
170
....*....|....*....
gi 227499621 218 TP-----ALYI-YTSGTTG 230
Cdd:PRK08162 177 LPadewdAIALnYTSGTTG 195
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
213-538 |
2.44e-09 |
|
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: 59.42 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 213 EVTFSTPALYiytsgttgatlalRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCnspQKPNDRD-HKVRLALGNG--LR 289
Cdd:cd05944 71 HVVLAGPAGY-------------RNPGLFDNFWKLVERYRITSLSTVPTVYAALL---QVPVNADiSSLRFAMSGAapLP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 290 GDVWRQFVKRFGdICIYEFYAATEGNIG----FMNYARKVGAVG-RVNYLQKKIITYDlikydvekdepvrDENGYCVRV 364
Cdd:cd05944 135 VELRARFEDATG-LPVVEGYGLTEATCLvavnPPDGPKRPGSVGlRLPYARVRIKVLD-------------GVGRLLRDC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 365 PKGEVGLLVckITQLTPFNGYAgakaQTEKKKLRDVfkkGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEV 444
Cdd:cd05944 201 APDEVGEIC--VAGPGVFGGYL----YTEGNKNAFV---ADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 445 ADTVGLVDFVQEVNVYGvhVPD-HEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYAR-PRFLRIQDTIEITGtfkhrk 522
Cdd:cd05944 272 EEALLRHPAVAFAGAVG--QPDaHAGELPVAYVQLKPGAVVEEEELLAWARDHVPERAAvPKHIEVLEELPVTA------ 343
|
330
....*....|....*.
gi 227499621 523 mtlVEEGFNPAVIKDA 538
Cdd:cd05944 344 ---VGKVFKPALRADA 356
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
55-504 |
2.56e-09 |
|
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: 59.81 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 55 ILRAFLEK-ARQTPHKPFLLFRDE-----TLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLG 128
Cdd:cd05968 62 IVEQLLDKwLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLR-ALGVGKGDRVGIYLPMIPEIVPAFLAVARIG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 129 CAMACLNYNIRAKSLLHCFQCCGAKVLLVS-------------PELQAAVEEiLPSLKKddvsIYYVSRTSNTDGIDSFL 195
Cdd:cd05968 141 GIVVPIFSGFGKEAAATRLQDAEAKALITAdgftrrgrevnlkEEADKACAQ-CPTVEK----VVVVRHLGNDFTPAKGR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 196 DK-VDEVSTEPIPESWRSEVtfSTPALYIYTSGTTG-------------------------------------------- 230
Cdd:cd05968 216 DLsYDEEKETAGDGAERTES--EDPLMIIYTSGTTGkpkgtvhvhagfplkaaqdmyfqfdlkpgdlltwftdlgwmmgp 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 231 ----ATLALR-TKF---------SASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHK--VRLALGNG--LRGDV 292
Cdd:cd05968 294 wlifGGLILGaTMVlydgapdhpKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLssLRVLGSTGepWNPEP 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 293 WRQFVKRFGDiciyefyaateGNIGFMNYARKVGAVGRV--NYLQKKI--ITYDLIKYDVEKDepVRDENGYCVRvpkGE 368
Cdd:cd05968 374 WNWLFETVGK-----------GRNPIINYSGGTEISGGIlgNVLIKPIkpSSFNGPVPGMKAD--VLDESGKPAR---PE 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 369 VGLLVCkitqLTPFNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTV 448
Cdd:cd05968 438 VGELVL----LAPWPGMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVL 513
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 449 GLVDFVQEVNVYGvhVPDH-EGRIGMASIKMKENHEFDG---KKLFQHIADYLPSYARPR 504
Cdd:cd05968 514 NAHPAVLESAAIG--VPHPvKGEAIVCFVVLKPGVTPTEalaEELMERVADELGKPLSPE 571
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
53-128 |
3.13e-09 |
|
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: 59.39 E-value: 3.13e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227499621 53 RTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLG 128
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLA-LGLRPGDRVVVQLPNVAEFVIVFFALFRAG 99
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
67-165 |
4.14e-09 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 58.80 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 67 PHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHC 146
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAAR-GVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYM 79
|
90
....*....|....*....
gi 227499621 147 FQCCGAKVLLVSPELQAAV 165
Cdd:cd17652 80 LADARPALLLTTPDNLAYV 98
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
63-231 |
1.81e-08 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 57.25 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 63 ARQTPHKPFLLF------RDETLTYAQVDRRSNQVARALHDHlgLRQGDCVALLMGNEPAYVwlwLGLvkLGCAMACL-- 134
Cdd:cd05931 3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAV--GKPGDRVLLLAPPGLDFV---AAF--LGCLYAGAia 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 135 ------NYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILpslkkddvsiyyvsRTSNTDGIDSFLDkVDEVSTEPiPE 208
Cdd:cd05931 76 vplpppTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFA--------------ASRPAAGTPRLLV-VDLLPDTS-AA 139
|
170 180
....*....|....*....|....
gi 227499621 209 SWR-SEVTFSTPALYIYTSGTTGA 231
Cdd:cd05931 140 DWPpPSPDPDDIAYLQYTSGSTGT 163
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
80-525 |
3.74e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 55.97 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 80 TYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNiraksllhcfqccgakvlLVSP 159
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRR-GCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWR------------------LSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 160 ELQAAVEEILPSLKKDDVSIYyVSRTSNTDgIDSFLDKVDEVS---TEPIPESwrsevtfsTPALYIYTSGTTG----AT 232
Cdd:PRK09088 85 ELDALLQDAEPRLLLGDDAVA-AGRTDVED-LAAFIASADALEpadTPSIPPE--------RVSLILFTSGTSGqpkgVM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 233 LALRTKFSASqfwddcrkYNVTVIQYIGELLRYLCNSPQKpndrdH------KVRLALGNGLRGDVWRQF-----VKRFG 301
Cdd:PRK09088 155 LSERNLQQTA--------HNFGVLGRVDAHSSFLCDAPMF-----HiiglitSVRPVLAVGGSILVSNGFepkrtLGRLG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 302 D--------ICIYEFYAATEGNIGFMNYA-RKVGAV---GRVN-------YLQKKIITYD---------LIKYDVEKD-- 351
Cdd:PRK09088 222 DpalgithyFCVPQMAQAFRAQPGFDAAAlRHLTALftgGAPHaaedilgWLDDGIPMVDgfgmseagtVFGMSVDCDvi 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 352 ----------EP-----VRDENGYcvRVPKGEVGLLVCKITQLTPfnGY-----AGAKAQTekkklrdvfkkGDLYFNSG 411
Cdd:PRK09088 302 rakagaagipTPtvqtrVVDDQGN--DCPAGVPGELLLRGPNLSP--GYwrrpqATARAFT-----------GDGWFRTG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 412 DLLMVDHENFIYFHDRVGDTFRWKGENVATTEVaDTVgLVDF--VQEVNVYGvhVPDHE-GRIGMASIKMKENHEFDGKK 488
Cdd:PRK09088 367 DIARRDADGFFWVVDRKKDMFISGGENVYPAEI-EAV-LADHpgIRECAVVG--MADAQwGEVGYLAIVPADGAPLDLER 442
|
490 500 510
....*....|....*....|....*....|....*..
gi 227499621 489 LFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTL 525
Cdd:PRK09088 443 IRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
53-233 |
6.95e-08 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 55.20 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 53 RTILRAFLEKARQTPHKPFLLFRDETL--TYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCA 130
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLA-LGIEKGDRVGIWAPNVPEWVLTQFATAKIGAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 131 MACLNYNIRAKSLLHCFQCCGAKVLL----------------VSPELQAAV-----EEILPSLKkddvSIYYV--SRTSN 187
Cdd:PRK08315 95 LVTINPAYRLSELEYALNQSGCKALIaadgfkdsdyvamlyeLAPELATCEpgqlqSARLPELR----RVIFLgdEKHPG 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 227499621 188 TDGIDSFLDKVDEVSTEPIPESwRSEVTFSTPALYIYTSGTT----GATL 233
Cdd:PRK08315 171 MLNFDELLALGRAVDDAELAAR-QATLDPDDPINIQYTSGTTgfpkGATL 219
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
51-230 |
7.93e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.56 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 51 PARTILRAFL-EKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGC 129
Cdd:PRK05691 1128 PAQAWLPELLnEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERSPQLLVGLLAILKAGG 1206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 130 AMACLNYNIRAKSLLHCFQCCGAKVLLVspelQAAVEEILPSlkkddvsiyyvsrtsnTDGIDSF-LDKVDevstepiPE 208
Cdd:PRK05691 1207 AYVPLDPDYPAERLAYMLADSGVELLLT----QSHLLERLPQ----------------AEGVSAIaLDSLH-------LD 1259
|
170 180 190
....*....|....*....|....*....|.
gi 227499621 209 SWRSevtfSTPALY---------IYTSGTTG 230
Cdd:PRK05691 1260 SWPS----QAPGLHlhgdnlayvIYTSGSTG 1286
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
59-230 |
8.69e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 55.73 E-value: 8.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 59 FLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNI 138
Cdd:PRK12316 4557 VAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIAR-GVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEY 4635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 139 RAKSLLHCFQCCGAKVLLVSPELQAAveeiLPSlkKDDVSIYYVSRTSNTDGidsFLDKVDEVSTEPipeswrsevtfST 218
Cdd:PRK12316 4636 PRERLAYMMEDSGAALLLTQSHLLQR----LPI--PDGLASLALDRDEDWEG---FPAHDPAVRLHP-----------DN 4695
|
170
....*....|..
gi 227499621 219 PALYIYTSGTTG 230
Cdd:PRK12316 4696 LAYVIYTSGSTG 4707
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
56-230 |
1.54e-07 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 54.11 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 56 LRAFLEKARQTPHKPFLLFRD-ETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACL 134
Cdd:PRK07514 5 LFDALRAAFADRDAPFIETPDgLRYTYGDLDAASARLANLLV-ALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 135 NYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVsiyyvsRTSNTDGIDSFLDKVDEVST--EPIPeswRS 212
Cdd:PRK07514 84 NTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHV------ETLDADGTGSLLEAAAAAPDdfETVP---RG 154
|
170
....*....|....*...
gi 227499621 213 EvtfSTPALYIYTSGTTG 230
Cdd:PRK07514 155 A---DDLAAILYTSGTTG 169
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
51-230 |
1.61e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 54.78 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 51 PARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCA 130
Cdd:PRK12467 1572 LARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIAL-GVGPEVLVGIAVERSLEMVVGLLAILKAGGA 1650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 131 MACLNYNIRAKSLLHCFQCCGAKVLLVspelQAAVEEILPSlkkddvsiyyvsrtsnTDGIDS-FLDKVDEVSTEPIPES 209
Cdd:PRK12467 1651 YVPLDPEYPRERLAYMIEDSGIELLLT----QSHLQARLPL----------------PDGLRSlVLDQEDDWLEGYSDSN 1710
|
170 180
....*....|....*....|.
gi 227499621 210 WRSEVTFSTPALYIYTSGTTG 230
Cdd:PRK12467 1711 PAVNLAPQNLAYVIYTSGSTG 1731
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
63-522 |
2.16e-07 |
|
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: 53.65 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 63 ARQTPHKPFLLFRDET-----LTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:cd05970 27 AKEYPDKLALVWCDDAgeeriFTFAELADYSDKTANFFKAM-GIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 138 IRAKSLLHCFQCCGAKVLLVSPE--LQAAVEEILPSLKKDDVSIYYvsRTSNTDGIDSFLDKVDEVSTEPIPESWRSEVT 215
Cdd:cd05970 106 LTAKDIVYRIESADIKMIVAIAEdnIPEEIEKAAPECPSKPKLVWV--GDPVPEGWIDFRKLIKNASPDFERPTANSYPC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 216 FSTPALYIYTSGTTGATLALRTKFS-------ASQFWDDCR--------------------------------------- 249
Cdd:cd05970 184 GEDILLVYFSSGTTGMPKMVEHDFTyplghivTAKYWQNVRegglhltvadtgwgkavwgkiygqwiagaavfvydydkf 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 250 ----------KYNVTVIQYIGELLRYLCNspQKPNDRD-HKVRLAL--GNGLRGDVWRQFvKRFGDICIYEFYAATE--- 313
Cdd:cd05970 264 dpkalleklsKYGVTTFCAPPTIYRFLIR--EDLSRYDlSSLRYCTtaGEALNPEVFNTF-KEKTGIKLMEGFGQTEttl 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 314 --GNIGFMNyaRKVGAVGRVNylqkkiitydlIKYDVEkdepVRDENGYcvRVPKGEVGLLVCKITQLTP---FNGYAGA 388
Cdd:cd05970 341 tiATFPWME--PKPGSMGKPA-----------PGYEID----LIDREGR--SCEAGEEGEIVIRTSKGKPvglFGGYYKD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 389 KAQTEkkklrDVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDH- 467
Cdd:cd05970 402 AEKTA-----EVWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTG--VPDPi 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 227499621 468 EGRIGMASIKMKENHEFDG---KKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRK 522
Cdd:cd05970 473 RGQVVKATIVLAKGYEPSEelkKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
62-230 |
2.69e-07 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 53.20 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 62 KARQTPHKPFLLFRD-----ETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLN- 135
Cdd:cd05921 4 WARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDL-GLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 136 -YNIRAKS---LLHCFQCCGAKVLLVS--PELQAAVEEILPslkkDDVSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPES 209
Cdd:cd05921 83 aYSLMSQDlakLKHLFELLKPGLVFAQdaAPFARALAAIFP----LGTPLVVSRNAVAGRGAISFAELAATPPTAAVDAA 158
|
170 180
....*....|....*....|.
gi 227499621 210 wRSEVTFSTPALYIYTSGTTG 230
Cdd:cd05921 159 -FAAVGPDTVAKFLFTSGSTG 178
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
55-466 |
2.77e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 53.45 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 55 ILRAFlekaRQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAyVWLWLGlvkLGCAMACl 134
Cdd:PRK06188 18 LVSAL----KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEA-LGLGTGDAVALLSLNRPE-VLMAIG---AAQLAGL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 135 nyniRAKSLL-------HCFQC--CGAKVLLVSP----ELQAAVEEILPSLKKddvsIYYVSRTSntDGIDsFLDKVDEV 201
Cdd:PRK06188 88 ----RRTALHplgslddHAYVLedAGISTLIVDPapfvERALALLARVPSLKH----VLTLGPVP--DGVD-LLAAAAKF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 202 STEPIpeswRSEVTFSTPALYIYTSGTT---------------------------------------------------- 229
Cdd:PRK06188 157 GPAPL----VAAALPPDIAGLAYTGGTTgkpkgvmgthrsiatmaqiqlaewewpadprflmctplshaggafflptllr 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 230 GATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQkPNDRD--------------HKVRLALGnglrgdvwrq 295
Cdd:PRK06188 233 GGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPD-LRTRDlssletvyygaspmSPVRLAEA---------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 296 fVKRFGDIcIYEFYAATEgnigfmnyarkvgAVGRVNYLQKKiitydlikyDVEKDEPVR----------------DENG 359
Cdd:PRK06188 302 -IERFGPI-FAQYYGQTE-------------APMVITYLRKR---------DHDPDDPKRltscgrptpglrvallDEDG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 360 YcvRVPKGEVGLLVCKITQLtpFNGYAGAKAQTEKkklrdVFKKGDLYfnSGDLLMVDHENFIYFHDRVGDTFRWKGENV 439
Cdd:PRK06188 358 R--EVAQGEVGEICVRGPLV--MDGYWNRPEETAE-----AFRDGWLH--TGDVAREDEDGFYYIVDRKKDMIVTGGFNV 426
|
490 500
....*....|....*....|....*..
gi 227499621 440 ATTEVADTVGLVDFVQEVNVYGvhVPD 466
Cdd:PRK06188 427 FPREVEDVLAEHPAVAQVAVIG--VPD 451
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
66-232 |
2.98e-07 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 53.25 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 66 TPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLH 145
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLRE-KGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 146 CFQCCGAKVLLVSPELqaaveeilPSLKKDDVSIYYVSRTSNTDGIDSFLDKVDEvstepipeswrsevtfSTPALY-IY 224
Cdd:cd17656 80 IMLDSGVRVVLTQRHL--------KSKLSFNKSTILLEDPSISQEDTSNIDYINN----------------SDDLLYiIY 135
|
....*...
gi 227499621 225 TSGTTGAT 232
Cdd:cd17656 136 TSGTTGKP 143
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-503 |
3.20e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.81 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 52 ARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAM 131
Cdd:PRK12316 3056 ERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIE-RGVGPDVLVGVAVERSLEMVVGLLAILKAGGAY 3134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 132 ACLNYNIRAKSLLHCFQCCGAKVLLVSPELQ----AAVEEIL------------PSLKKDDVSIYYVSRTSNTDG----- 190
Cdd:PRK12316 3135 VPLDPEYPEERLAYMLEDSGAQLLLSQSHLRlplaQGVQVLDldrgdenyaeanPAIRTMPENLAYVIYTSGSTGkpkgv 3214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 191 ------IDSFLDKVDEVSTEPIPESWRSEVTFS--TPALYIYTSGTTGATLALRtkfsASQFWDDCRKY-------NVTV 255
Cdd:PRK12316 3215 girhsaLSNHLCWMQQAYGLGVGDRVLQFTTFSfdVFVEELFWPLMSGARVVLA----GPEDWRDPALLvelinseGVDV 3290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 256 IQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFvkrFGDICIYEFYAATEGNIGFMNYARKVGAVGRVNYLQ 335
Cdd:PRK12316 3291 LHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQV---FAGLPLYNLYGPTEATITVTHWQCVEEGKDAVPIGR 3367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 336 KKIITYDLIKYDVEKDEPVrdenGYCVRVPKGEVGLLvckitqltpfNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLM 415
Cdd:PRK12316 3368 PIANRACYILDGSLEPVPV----GALGELYLGGEGLA----------RGYHNRPGLTAERFVPDPFVPGERLYRTGDLAR 3433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 416 VDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVhvpdhEGRIGMASIKMKENHEFDGKKLFQHIAD 495
Cdd:PRK12316 3434 YRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAV-----DGRQLVAYVVPEDEAGDLREALKAHLKA 3508
|
....*...
gi 227499621 496 YLPSYARP 503
Cdd:PRK12316 3509 SLPEYMVP 3516
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
59-160 |
3.64e-07 |
|
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: 52.56 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 59 FLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNI 138
Cdd:cd17645 4 FEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGK-GVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82
|
90 100
....*....|....*....|..
gi 227499621 139 RAKSLLHCFQCCGAKVLLVSPE 160
Cdd:cd17645 83 PGERIAYMLADSSAKILLTNPD 104
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
67-156 |
5.07e-07 |
|
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: 52.37 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 67 PHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHC 146
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRAL-GVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYM 79
|
90
....*....|
gi 227499621 147 FQCCGAKVLL 156
Cdd:cd17649 80 LEDSGAGLLL 89
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
67-519 |
8.30e-07 |
|
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: 51.70 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 67 PHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHC 146
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRG-LGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 147 FQCCGAKVLLVSPELQAAVeeilpslkkddvsIYYVSRTSNTDGIdsfldKVDEVSTEPIPESWRSEV---TFSTPALYI 223
Cdd:cd17650 80 LEDSGAKLLLTQPEDLAYV-------------IYTSGTTGKPKGV-----MVEHRNVAHAAHAWRREYeldSFPVRLLQM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 224 YT------------SGTTGATLAL---RTKFSASQFWDDCRKYNVTVIQYIGELLR----YLCNSPQKPNDRDhkvRLAL 284
Cdd:cd17650 142 ASfsfdvfagdfarSLLNGGTLVIcpdEVKLDPAALYDLILKSRITLMESTPALIRpvmaYVYRNGLDLSAMR---LLIV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 285 GNGLRGDVW-RQFVKRFGD-ICIYEFYAATEGNIGFMNYARKVGAVGRVNY--LQKKIITYDLIKYDvEKDEPvrdengy 360
Cdd:cd17650 219 GSDGCKAQDfKTLAARFGQgMRIINSYGVTEATIDSTYYEEGRDPLGDSANvpIGRPLPNTAMYVLD-ERLQP------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 361 cvrVPKGEVGLL------VCKitqltpfnGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRW 434
Cdd:cd17650 291 ---QPVGVAGELyiggagVAR--------GYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 435 KGENVATTEVADTVGLVDFVQEVNVYGVHvpDHEGRIGMASIKMKEnHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEI 514
Cdd:cd17650 360 RGFRIELGEIESQLARHPAIDEAVVAVRE--DKGGEARLCAYVVAA-ATLNTAELRAFLAKELPSYMIPSYYVQLDALPL 436
|
....*
gi 227499621 515 TGTFK 519
Cdd:cd17650 437 TPNGK 441
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
75-504 |
1.00e-06 |
|
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: 51.36 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 75 RDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQccgakv 154
Cdd:cd05923 25 RGLRLTYSELRARIEAVAARLHA-RGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIE------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 155 llvSPELQAAV-EEILPSLKKDDVSIYYVSRTSNTDGidsflDKVDEVSTEPIPESWRSEvtfSTPALYIYTSGTTGA-- 231
Cdd:cd05923 98 ---RGEMTAAViAVDAQVMDAIFQSGVRVLALSDLVG-----LGEPESAGPLIEDPPREP---EQPAFVFYTSGTTGLpk 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 232 -------TLALRTKFSASQFWDDCRKYNVT--------VIQYIGELLRYLC----------NSPQK-------------- 272
Cdd:cd05923 167 gavipqrAAESRVLFMSTQAGLRHGRHNVVlglmplyhVIGFFAVLVAALAldgtyvvveeFDPADalklieqervtslf 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 273 --PNDRDHKVRLALGNGLRGDVWRQF--------------VKRFGDICIYEFYAATEG-NIGFMNYARKvGAVGRVNYLQ 335
Cdd:cd05923 247 atPTHLDALAAAAEFAGLKLSSLRHVtfagatmpdavlerVNQHLPGEKVNIYGTTEAmNSLYMRDART-GTEMRPGFFS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 336 KKIItydlikydvekdepVRDENGYCVRVPKGEVGLLVCKITQLTPFNGYAGaKAQTEKKKLRDVfkkgdlYFNSGDLLM 415
Cdd:cd05923 326 EVRI--------------VRIGGSPDEALANGEEGELIVAAAADAAFTGYLN-QPEATAKKLQDG------WYRTGDVGY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 416 VDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASIKMKENhEFDGKKLFQH-I 493
Cdd:cd05923 385 VDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIG--VADERwGQSVTACVVPREG-TLSADELDQFcR 461
|
490
....*....|.
gi 227499621 494 ADYLPSYARPR 504
Cdd:cd05923 462 ASELADFKRPR 472
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
51-231 |
1.73e-06 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 51.03 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 51 PARTILRAFLEKARQTPHKPFLLFRD-----ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLV 125
Cdd:PRK08180 37 YPRRLTDRLVHWAQEAPDRVFLAERGadggwRRLTYAEALERVRAIAQALLD-RGLSAERPLMILSGNSIEHALLALAAM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 126 KLGCAMACLN--YNIRAKS---LLHCFQCCGAKVLLVS--PELQAAVEEILPslkkDDVSIYYVSRTSNTDGIDSFLDKV 198
Cdd:PRK08180 116 YAGVPYAPVSpaYSLVSQDfgkLRHVLELLTPGLVFADdgAAFARALAAVVP----ADVEVVAVRGAVPGRAATPFAALL 191
|
170 180 190
....*....|....*....|....*....|...
gi 227499621 199 DEVSTEPIPESWRSeVTFSTPALYIYTSGTTGA 231
Cdd:PRK08180 192 ATPPTAAVDAAHAA-VGPDTIAKFLFTSGSTGL 223
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
77-244 |
1.86e-06 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 50.61 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 77 ETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLL 156
Cdd:PLN02574 65 FSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 157 VSPElqaAVEEiLPSLKkddVSIYYVSRTSNTDGIDSFLDKVDEV---STEPIPeswRSEVTFSTPALYIYTSGTTG--- 230
Cdd:PLN02574 145 TSPE---NVEK-LSPLG---VPVIGVPENYDFDSKRIEFPKFYELikeDFDFVP---KPVIKQDDVAAIMYSSGTTGask 214
|
170 180
....*....|....*....|....
gi 227499621 231 ----------ATLALRTKFSASQF 244
Cdd:PLN02574 215 gvvlthrnliAMVELFVRFEASQY 238
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
47-98 |
5.30e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.78 E-value: 5.30e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 227499621 47 GKRRPARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDH 98
Cdd:PRK05691 2182 GEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRER 2233
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
59-130 |
5.40e-06 |
|
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: 48.85 E-value: 5.40e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227499621 59 FLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCA 130
Cdd:cd12115 5 VEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLR-AAGVGPESRVGVCLERTPDLVVALLAVLKAGAA 75
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
323-527 |
1.09e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 48.23 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 323 RKVGAVGRVN-YLQKKIItydlikydvekdepvrDENGycVRVPKGEVGLLvCkitqltpFNGYAGAKAQTEKKKLRDVF 401
Cdd:PRK12583 370 RRVETVGRTQpHLEVKVV----------------DPDG--ATVPRGEIGEL-C-------TRGYSVMKGYWNNPEATAES 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 402 KKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVhvPDHE-GRIGMASIKMKE 480
Cdd:PRK12583 424 IDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGV--PDEKyGEEIVAWVRLHP 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 227499621 481 NHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVE 527
Cdd:PRK12583 502 GHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMRE 548
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
67-165 |
1.24e-05 |
|
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: 47.69 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 67 PHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHC 146
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRA-EGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFI 79
|
90
....*....|....*....
gi 227499621 147 FQCCGAKVLLVSPELQAAV 165
Cdd:cd17643 80 LADSGPSLLLTDPDDLAYV 98
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
64-462 |
1.62e-05 |
|
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: 47.57 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 64 RQTPHKPFLLFRDE------TLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:cd17634 64 RENGDRTAIIYEGDdtsqsrTISYRELHREVCRFAGTLLD-LGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 138 IRAKSLLHCFQCCGAKVLLVSPE---------LQAAVEEILPSLKKDDVSIYYVSRTSNTDGID--SFLDKVDEVSTEPi 206
Cdd:cd17634 143 FAPEAVAGRIIDSSSRLLITADGgvragrsvpLKKNVDDALNPNVTSVEHVIVLKRTGSDIDWQegRDLWWRDLIAKAS- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 207 PESWRSEVTFSTPALYIYTSGTTG---------------ATLALRTKF-------------------------------- 239
Cdd:cd17634 222 PEHQPEAMNAEDPLFILYTSGTTGkpkgvlhttggylvyAATTMKYVFdygpgdiywctadvgwvtghsyllygplacga 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 240 ------------SASQFWDDCRKYNVTVIQYIGELLRYLcnSPQKPN-----DRDH-KVRLALGNGLRGDVWRQFVKRFG 301
Cdd:cd17634 302 ttllyegvpnwpTPARMWQVVDKHGVNILYTAPTAIRAL--MAAGDDaiegtDRSSlRILGSVGEPINPEAYEWYWKKIG 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 302 DI-C-IYEFYAATEGNiGFMNYARKVgavgrVNYLQKKIITYDLIKYDVEkdepVRDENGYcvRVPKGEVGLLVckITql 379
Cdd:cd17634 380 KEkCpVVDTWWQTETG-GFMITPLPG-----AIELKAGSATRPVFGVQPA----VVDNEGH--PQPGGTEGNLV--IT-- 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 380 TPFNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNV 459
Cdd:cd17634 444 DPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAV 523
|
...
gi 227499621 460 YGV 462
Cdd:cd17634 524 VGI 526
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
63-231 |
1.69e-05 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 47.57 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 63 ARQTPHKPFLLFRDE--TLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRA 140
Cdd:PRK05852 26 ATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 141 KSLLHCFQCCGAKVLLVSPElqAAVEEILPSLKKDDVSiyyVSRTSNTDGIDSFLDKVDEVSTEPIPESWRSEVTFSTPA 220
Cdd:PRK05852 105 AEQRVRSQAAGARVVLIDAD--GPHDRAEPTTRWWPLT---VNVGGDSGPSGGTLSVHLDAATEPTPATSTPEGLRPDDA 179
|
170
....*....|.
gi 227499621 221 LYIYTSGTTGA 231
Cdd:PRK05852 180 MIMFTGGTTGL 190
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
79-508 |
2.18e-05 |
|
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: 47.18 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 79 LTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAyvwLW---LGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVl 155
Cdd:cd05974 1 VSFAEMSARSSRVANFLRS-IGVGRGDRILLMLGNVVE---LWeamLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVY- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 156 lvspelqAAVEEIlpSLKKDDVSIYYVSRTSNTDGIDSFLDK---VDEVST------EPIPESWrsevTFSTPALY---- 222
Cdd:cd05974 76 -------AAVDEN--THADDPMLLYFTSGTTSKPKLVEHTHRsypVGHLSTmywiglKPGDVHW----NISSPGWAkhaw 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 223 --IYTSGTTGATLAL--RTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQfVK 298
Cdd:cd05974 143 scFFAPWNAGATVFLfnYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQ-VR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 299 RFGDICIYEFYAATEGNIGFMN---YARKVGAVGRvnylqkkiityDLIKYDVEKDEPVRDEngycvrVPKGEVGLLVCK 375
Cdd:cd05974 222 RAWGLTIRDGYGQTETTALVGNspgQPVKAGSMGR-----------PLPGYRVALLDPDGAP------ATEGEVALDLGD 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 376 ITQLTPFNGYAGAKAQTEKkklrdvfKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQ 455
Cdd:cd05974 285 TRPVGLMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVA 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 227499621 456 EVNVygVHVPDHEgRIGM--ASIKMKENHEFD---GKKLFQHIADYLPSYARPRFLRI 508
Cdd:cd05974 358 EAAV--VPSPDPV-RLSVpkAFIVLRAGYEPSpetALEIFRFSRERLAPYKRIRRLEF 412
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
77-230 |
2.23e-05 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 47.42 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 77 ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLL 156
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLA-LGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 157 VSPELQA-AVEEILPSLKKDDVSIYYVSR-TSNTDgiDSFLDKVDEVSTEPI------PESWRSEVTFSTP---ALYIYT 225
Cdd:cd17641 89 AEDEEQVdKLLEIADRIPSVRYVIYCDPRgMRKYD--DPRLISFEDVVALGRaldrrdPGLYEREVAAGKGedvAVLCTT 166
|
....*
gi 227499621 226 SGTTG 230
Cdd:cd17641 167 SGTTG 171
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
78-182 |
2.36e-05 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 47.12 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 78 TLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLV 157
Cdd:PRK12492 49 TLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVY 128
|
90 100
....*....|....*....|....*
gi 227499621 158 SPELQAAVEEILPslkkdDVSIYYV 182
Cdd:PRK12492 129 LNMFGKLVQEVLP-----DTGIEYL 148
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
77-231 |
2.92e-05 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 46.70 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 77 ETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLL 156
Cdd:PRK05620 37 EQTTFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 157 VSPELQAAVEEILPSLKK---------DDVSIYYVSRTSNTDgIDSFLDKVDEVSTEpipESWrSEVTFSTPALYIYTSG 227
Cdd:PRK05620 117 ADPRLAEQLGEILKECPCvravvfigpSDADSAAAHMPEGIK-VYSYEALLDGRSTV---YDW-PELDETTAAAICYSTG 191
|
....
gi 227499621 228 TTGA 231
Cdd:PRK05620 192 TTGA 195
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
54-230 |
3.16e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 46.96 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 54 TILRAFLEK-ARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMgnePAYVWLWLGLVKLgcama 132
Cdd:PRK10252 458 TTLSALVAQqAAKTPDAPALADARYQFSYREMREQVVALANLLRE-RGVKPGDSVAVAL---PRSVFLTLALHAI----- 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 133 clnynIRAksllhcfqccGAKVLLVSPE-----LQAAVEEILPSL--KKDDVSiyyvSRTSntDGIDSFLDKVDEVSTEP 205
Cdd:PRK10252 529 -----VEA----------GAAWLPLDTGypddrLKMMLEDARPSLliTTADQL----PRFA--DVPDLTSLCYNAPLAPQ 587
|
170 180
....*....|....*....|....*
gi 227499621 206 IPESWRSEVTfSTPALYIYTSGTTG 230
Cdd:PRK10252 588 GAAPLQLSQP-HHTAYIIFTSGSTG 611
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
78-170 |
7.07e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 45.52 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 78 TLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLV 157
Cdd:PRK05677 49 TLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVC 128
|
90
....*....|...
gi 227499621 158 SPELQAAVEEILP 170
Cdd:PRK05677 129 LANMAHLAEKVLP 141
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
60-462 |
9.35e-05 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 45.04 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 60 LEKA-RQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLN--Y 136
Cdd:PRK08974 29 FEQAvARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNplY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 137 NIRakSLLHCFQCCGAKVLLVSPELQAAVEEILpslkkDDVSIYYVSRTSNTD----GIDSFLDKVDEVSTEPIPE---- 208
Cdd:PRK08974 109 TPR--ELEHQLNDSGAKAIVIVSNFAHTLEKVV-----FKTPVKHVILTRMGDqlstAKGTLVNFVVKYIKRLVPKyhlp 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 209 ---SWRS-------------EVTFSTPALYIYTSGTT----GATLA--------LRTKFSASQFWDDCRKYNVTVIQ--- 257
Cdd:PRK08974 182 daiSFRSalhkgrrmqyvkpELVPEDLAFLQYTGGTTgvakGAMLThrnmlanlEQAKAAYGPLLHPGKELVVTALPlyh 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 258 -----------------------------YIGELLRY--------------LCNSPQKPNDRDHKVRLALGNGLrgDVWR 294
Cdd:PRK08974 262 ifaltvncllfielggqnllitnprdipgFVKELKKYpftaitgvntlfnaLLNNEEFQELDFSSLKLSVGGGM--AVQQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 295 QFVKRFGDIC---IYEFYAATEGNigfmnyarkvgavgrvnylqkKIIT---YDLIKYDVEKDEPV-------RDENGYc 361
Cdd:PRK08974 340 AVAERWVKLTgqyLLEGYGLTECS---------------------PLVSvnpYDLDYYSGSIGLPVpsteiklVDDDGN- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 362 vRVPKGEVGLLVCKITQLtpFNGYAGAKAQTEkkklrDVFKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVAT 441
Cdd:PRK08974 398 -EVPPGEPGELWVKGPQV--MLGYWQRPEATD-----EVIKDG--WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYP 467
|
490 500
....*....|....*....|.
gi 227499621 442 TEVADTVGLVDFVQEVNVYGV 462
Cdd:PRK08974 468 NEIEDVVMLHPKVLEVAAVGV 488
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
198-519 |
1.73e-04 |
|
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: 43.79 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 198 VDEVSTEPIPES------WRSEVTFSTPALYIYTSGTTgatlaLRTKFSASQFwddcrkYNVTVIQYIGELLRYLCNSPQ 271
Cdd:cd17635 42 VGDVTYLPLPAThigglwWILTCLIHGGLCVTGGENTT-----YKSLFKILTT------NAVTTTCLVPTLLSKLVSELK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 272 KPNDRDHKVRLALGNGLR---GDVwrQFVKRFGDICIYEFYAATE-GNIGFMNYAR---KVGAVGRvnylqkkiiTYDLI 344
Cdd:cd17635 111 SANATVPSLRLIGYGGSRaiaADV--RFIEATGLTNTAQVYGLSEtGTALCLPTDDdsiEINAVGR---------PYPGV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 345 kyDVEkdepVRDENGycVRVPKGEVGLLVCKitqlTPFN--GYAGAKAQTEkkklrDVFKKGdlYFNSGDLLMVDHENFI 422
Cdd:cd17635 180 --DVY----LAATDG--IAGPSASFGTIWIK----SPANmlGYWNNPERTA-----EVLIDG--WVNTGDLGERREDGFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 423 YFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYgvHVPDHE--GRIGMASIKMKENHEFDGKKLFQHIADYLPSY 500
Cdd:cd17635 241 FITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACY--EISDEEfgELVGLAVVASAELDENAIRALKHTIRRELEPY 318
|
330
....*....|....*....
gi 227499621 501 ARPRFLRIQDTIEITGTFK 519
Cdd:cd17635 319 ARPSTIVIVTDIPRTQSGK 337
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
63-230 |
1.94e-04 |
|
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: 44.09 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 63 ARQTPHKPFLLF------RDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNY 136
Cdd:cd05966 63 LKERGDKVAIIWegdepdQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 137 NIRAKSLLHCFQCCGAKVLLVSPE---------LQAAVEEIL---PSLKKDDVsiyyVSRTSN----TDGIDSFLDK-VD 199
Cdd:cd05966 142 GFSAESLADRINDAQCKLVITADGgyrggkvipLKEIVDEALekcPSVEKVLV----VKRTGGevpmTEGRDLWWHDlMA 217
|
170 180 190
....*....|....*....|....*....|.
gi 227499621 200 EVSTEPIPESWRSEvtfsTPALYIYTSGTTG 230
Cdd:cd05966 218 KQSPECEPEWMDSE----DPLFILYTSGSTG 244
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
77-230 |
3.33e-04 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 43.50 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 77 ETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLL 156
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFL-KLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 157 VSPELQA----AVEEILPSLK-----KDDVSiyyvSRTSNTDGIDSFLDKVDEVSTEPIPESWRSEVTFSTPALyIYTSG 227
Cdd:cd05933 86 VENQKQLqkilQIQDKLPHLKaiiqyKEPLK----EKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTL-IYTSG 160
|
...
gi 227499621 228 TTG 230
Cdd:cd05933 161 TTG 163
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
77-512 |
3.56e-04 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 43.43 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 77 ETLTYAQVDRRSNQVARALHDhLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLL 156
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRS-LGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 157 VSPELQAAVEEI-LPSLKKDDVSIY-YVSRTSNTDGIDSFLDKVDEvstEPIPESWRSEVTFST---------------- 218
Cdd:PLN02330 133 TNDTNYGKVKGLgLPVIVLGEEKIEgAVNWKELLEAADRAGDTSDN---EEILQTDLCALPFSSgttgiskgvmlthrnl 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 219 -------------------------PALYIYtsGTTGATLA-LRTK--------FSASQFWDDCRKYNVTVIQYIGELLR 264
Cdd:PLN02330 210 vanlcsslfsvgpemigqvvtlgliPFFHIY--GITGICCAtLRNKgkvvvmsrFELRTFLNALITQEVSFAPIVPPIIL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 265 YLCNSPQKPNDRDHKVRL----ALGNGLRGDVWRQFVKRFGDICIYEFYAATEGNIGFMNYARKVGAVGrvnYLQKKIIT 340
Cdd:PLN02330 288 NLVKNPIVEEFDLSKLKLqaimTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITLTHGDPEKGHG---IAKKNSVG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 341 YDLIKYDVEKDEPvrdENGycVRVPKGEVGLlVCKITQLTpFNGYAGAKAQTEkkklRDVFKKGdlYFNSGDLLMVDHEN 420
Cdd:PLN02330 365 FILPNLEVKFIDP---DTG--RSLPKNTPGE-LCVRSQCV-MQGYYNNKEETD----RTIDEDG--WLHTGDIGYIDDDG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 421 FIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVygVHVPDHE-GRIGMASIKMKENHEFDGKKLFQHIADYLPS 499
Cdd:PLN02330 432 DIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAV--VPLPDEEaGEIPAACVVINPKAKESEEDILNFVAANVAH 509
|
490
....*....|...
gi 227499621 500 YARPRFLRIQDTI 512
Cdd:PLN02330 510 YKKVRVVQFVDSI 522
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
63-230 |
5.32e-04 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 42.81 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 63 ARQTPHKPFLLfrDET---LTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIR 139
Cdd:PRK06087 33 ARAMPDKIAVV--DNHgasYTYSALDHAASRLANWLLAK-GIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 140 AKSLLHCFQCCGAKVLL-------VSPELQA-AVEEILPSLKKdDVSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPESwr 211
Cdd:PRK06087 110 EAELVWVLNKCQAKMFFaptlfkqTRPVDLIlPLQNQLPQLQQ-IVGVDKLAPATSSLSLSQIIADYEPLTTAITTHG-- 186
|
170
....*....|....*....
gi 227499621 212 SEVtfstpALYIYTSGTTG 230
Cdd:PRK06087 187 DEL-----AAVLFTSGTEG 200
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
80-230 |
5.92e-04 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 42.82 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 80 TYAQVDRRSNQVARALhDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSP 159
Cdd:PRK06018 41 TYAQIHDRALKVSQAL-DRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 160 ELQAAVEEILPSLKKDDVSIYYVSRT-------SNTDGIDSFLDKVDEVStepipeSWRsevTF--STPALYIYTSGTTG 230
Cdd:PRK06018 120 TFVPILEKIADKLPSVERYVVLTDAAhmpqttlKNAVAYEEWIAEADGDF------AWK---TFdeNTAAGMCYTSGTTG 190
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
354-506 |
6.66e-04 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 42.31 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 354 VRDENGYcvRVPKGEVGLLVCKITQLTPfnGY-----AGAKAQTEkkklrdvfkkgDLYFNSGDLLMVDHENFIYFHDRV 428
Cdd:PRK07059 393 IRDDDGN--DLPLGEPGEICIRGPQVMA--GYwnrpdETAKVMTA-----------DGFFRTGDVGVMDERGYTKIVDRK 457
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227499621 429 GDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVhvPD-HEGRIGMASIkMKENHEFDGKKLFQHIADYLPSYARPRFL 506
Cdd:PRK07059 458 KDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGV--PDeHSGEAVKLFV-VKKDPALTEEDVKAFCKERLTNYKRPKFV 533
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
77-230 |
1.06e-03 |
|
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: 41.69 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 77 ETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLL 156
Cdd:cd05932 5 VEFTWGEVADKARRLAAALR-ALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227499621 157 VS-----PELQAAVEEILPSlkkddVSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPESwrsevtfSTPALYIYTSGTTG 230
Cdd:cd05932 84 VGklddwKAMAPGVPEGLIS-----ISLPPPSAANCQYQWDDLIAQHPPLEERPTRFP-------EQLATLIYTSGTTG 150
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
408-519 |
1.17e-03 |
|
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: 41.16 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 408 FNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGvhVPDHE-GRIGMASIKMkeNHEFDG 486
Cdd:cd17630 207 FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVG--VPDEElGQRPVAVIVG--RGPADP 282
|
90 100 110
....*....|....*....|....*....|...
gi 227499621 487 KKLFQHIADYLPSYARPRFLRIQDTIEITGTFK 519
Cdd:cd17630 283 AELRAWLKDKLARFKLPKRIYPVPELPRTGGGK 315
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
228-504 |
2.53e-03 |
|
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: 40.59 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 228 TTGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSP-QKPNDRDHKVRLALGNG-LRGDVWRQFVKRFGDICI 305
Cdd:cd17642 251 ICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTlVDKYDLSNLHEIASGGApLSKEVGEAVAKRFKLPGI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 306 YEFYAATEGNIGFM---NYARKVGAVGRVnylqKKIITYDLIKYDVEKDEPVRDENGYCVRvpkgevGLLVCKitqltpf 382
Cdd:cd17642 331 RQGYGLTETTSAILitpEGDDKPGAVGKV----VPFFYAKVVDLDTGKTLGPNERGELCVK------GPMIMK------- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 383 nGYAGAKAQTekKKLRDvfKKGdlYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGv 462
Cdd:cd17642 394 -GYVNNPEAT--KALID--KDG--WLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAG- 465
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 227499621 463 hVPDHE-GRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPR 504
Cdd:cd17642 466 -IPDEDaGELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKRLR 507
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
76-230 |
2.75e-03 |
|
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: 40.34 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 76 DETLTYAQVDRRSNQVARALHdHLGLRQGDCVALLMGNEPAYV-WLWLGL------VKLGCAMACLNYNIRAKSLLHCFQ 148
Cdd:cd05906 37 EEFQSYQDLLEDARRLAAGLR-QLGLRPGDSVILQFDDNEDFIpAFWACVlagfvpAPLTVPPTYDEPNARLRKLRHIWQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 149 CCGAKVLLVSPELQAAVEEILpslkkddvsiyyvsrtsNTDGIDSF-LDKVDEVSTEPIPESWRsEVTFSTPALYIYTSG 227
Cdd:cd05906 116 LLGSPVVLTDAELVAEFAGLE-----------------TLSGLPGIrVLSIEELLDTAADHDLP-QSRPDDLALLMLTSG 177
|
...
gi 227499621 228 TTG 230
Cdd:cd05906 178 STG 180
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
59-169 |
5.89e-03 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 39.44 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227499621 59 FLEKARQT-PHKPFLLFRDETLTYAQVDRRSNQVARALHDHlGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYN 137
Cdd:PLN02479 25 FLERAAVVhPTRKSVVHGSVRYTWAQTYQRCRRLASALAKR-SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIR 103
|
90 100 110
....*....|....*....|....*....|..
gi 227499621 138 IRAKSLLHCFQCCGAKVLLVSPELQAAVEEIL 169
Cdd:PLN02479 104 LNAPTIAFLLEHSKSEVVMVDQEFFTLAEEAL 135
|
|
| |
