|
Name |
Accession |
Description |
Interval |
E-value |
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
121-479 |
1.28e-163 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 476.32 E-value: 1.28e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASY 200
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 201 LITSvellesklkaalldincvkhiiyvdnktinraeypegleihsmqsveelgskpenssippsrPTPSDMAIVMYTSG 280
Cdd:cd17639 81 IFTD--------------------------------------------------------------GKPDDLACIMYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 281 STGRPKGVMMHHSNLIAGMTGQCERIPG-LGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDqssKIKKGS 359
Cdd:cd17639 99 STGNPKGVMLTHGNLVAGIAGLGDRVPElLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGYGSPRTLTD---KSKRGC 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 360 KGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLCNLILFKKVKALLGGNVRMM 439
Cdd:cd17639 176 KGDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPGTPLLDELVFKKVRAALGGRLRYM 255
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958806453 440 LSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTE 479
Cdd:cd17639 256 LSGGAPLSADTQEFLNI-VLCPVIQGYGLTETCAGGTVQD 294
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
11-479 |
1.97e-163 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 482.31 E-value: 1.97e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 11 VLLPvhLLITIYsalifipwyfLTNAKKKnamAKRIKAKPTSDKPGSPYRSvTHFDSLavIDIP--GADTLDKLFDHAVA 88
Cdd:PLN02387 8 VLVP--LLLTLL----------LRGSKKG---KKRGVPVDVGGEPGYAIRN-ARFPEL--VETPweGATTLAALFEQSCK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 89 KFGKKDSLGTREILSEENEMQPNGKVFKKLILGNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQ 168
Cdd:PLN02387 70 KYSDKRLLGTRKLISREFETSSDGRKFEKLHLGEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 169 TCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLEsKLKAALLDINCVKHIIYVDNKTINRAEYPEGLE---IH 245
Cdd:PLN02387 150 GCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLK-KLIDISSQLETVKRVIYMDDEGVDSDSSLSGSSnwtVS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 246 SMQSVEELGskpENSSIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVL 325
Cdd:PLN02387 229 SFSEVEKLG---KENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVYLAYLPLAHIL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 326 ELTAEISCFTYGCRIGYSSPLTLSDQSSKIKKGSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYD 405
Cdd:PLN02387 306 ELAAESVMAAVGAAIGYGSPLTLTDTSNKIKKGTKGDASALKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKLFDIAYK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 406 YKLEQIKK------GYDAPLCNLILFKKVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTE 479
Cdd:PLN02387 386 RRLAAIEGswfgawGLEKLLWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSE 465
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
121-479 |
2.47e-95 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 301.83 E-value: 2.47e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNT--IAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEA 198
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 199 SylitsvellesklkaalldincvkhIIYVDnktinraeypEGLEIHSMQSVEELGskpENSSIPPSRPTPSDMAIVMYT 278
Cdd:cd05927 81 S-------------------------IVFCD----------AGVKVYSLEEFEKLG---KKNKVPPPPPKPEDLATICYT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 279 SGSTGRPKGVMMHHSNLIAGMTGQC---ERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSS--PLTLSDqss 353
Cdd:cd05927 123 SGTTGNPKGVMLTHGNIVSNVAGVFkilEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSgdIRLLLD--- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 354 kikkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKG--YDAPLCNLILFKKVKAL 431
Cdd:cd05927 200 --------DIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSGvvRASPFWDKLVFNKIKQA 271
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958806453 432 LGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTE 479
Cdd:cd05927 272 LGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTL 319
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
124-477 |
7.91e-87 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 283.79 E-value: 7.91e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 124 KWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLIT 203
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 204 S---VELLESKLKAALLDiNCVkhIIYVDnktinraEYPEGLEIHSMQ-----SVEELGsKPENSSIPPSRPTPSD-MAI 274
Cdd:PTZ00216 200 NgknVPNLLRLMKSGGMP-NTT--IIYLD-------SLPASVDTEGCRlvawtDVVAKG-HSAGSHHPLNIPENNDdLAL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 275 VMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGL-GPK---DTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSD 350
Cdd:PTZ00216 269 IMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLiGPPeedETYCSYLPLAHIMEFGVTNIFLARGALIGFGSPRTLTD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 351 QSSKikkgSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYDAPLCNLILFKKVKA 430
Cdd:PTZ00216 349 TFAR----PHGDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLRALKEGKDTPYWNEKVFSAPRA 424
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1958806453 431 LLGGNVRMMLSGGAPLSPQTHRFMNVCFcCPIGQGYGLTESCGAGTV 477
Cdd:PTZ00216 425 VLGGRVRAMLSGGGPLSAATQEFVNVVF-GMVIQGWGLTETVCCGGI 470
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
72-483 |
1.88e-82 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 269.66 E-value: 1.88e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 72 DIPGADTLDKLFDHAVAKFGKKDSLGTREilseenemqpngkvfkkliLGNYKWINYLEVNCRVNNFGSGLTALGLKPKN 151
Cdd:COG1022 6 DVPPADTLPDLLRRRAARFPDRVALREKE-------------------DGIWQSLTWAEFAERVRALAAGLLALGVKPGD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 152 TIAIFCETRAEWMIA--------AQTcfkynfplVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKAALLDINCVK 223
Cdd:COG1022 67 RVAILSDNRPEWVIAdlailaagAVT--------VPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDELPSLR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 224 HIIYVDNKTInraeyPEGLEIHSMQSVEELGSKPENSSIPPSR---PTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMT 300
Cdd:COG1022 139 HIVVLDPRGL-----RDDPRLLSLDELLALGREVADPAELEARraaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNAR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 301 GQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYS-SPLTLSDqsskikkgskgDCTVLKPTLMAAVPEIMD 379
Cdd:COG1022 214 ALLERLP-LGPGDRTLSFLPLAHVFERTVSYYALAAGATVAFAeSPDTLAE-----------DLREVKPTFMLAVPRVWE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 380 RIYKNVMSKVQEMNYIQKTLF----KIGYDYKlEQIKKGYDAP--------LCNLILFKKVKALLGGNVRMMLSGGAPLS 447
Cdd:COG1022 282 KVYAGIQAKAEEAGGLKRKLFrwalAVGRRYA-RARLAGKSPSlllrlkhaLADKLVFSKLREALGGRLRFAVSGGAALG 360
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1958806453 448 PQTHRF---MNVcfccPIGQGYGLTESCGAGTV-TEGKHR 483
Cdd:COG1022 361 PELARFfraLGI----PVLEGYGLTETSPVITVnRPGDNR 396
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
56-480 |
6.53e-82 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 269.66 E-value: 6.53e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 56 GSPYRSVTHFDslaviDIPGADTLDKLFDHAVAKFGKKDSLGTReilseeneMQPNGKVfkklilGNYKWINYLEVNCRV 135
Cdd:PLN02736 28 RSPLKLVSRFP-----DHPEIGTLHDNFVYAVETFRDYKYLGTR--------IRVDGTV------GEYKWMTYGEAGTAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 136 NNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLkAA 215
Cdd:PLN02736 89 TAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLL-SC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 216 LLDINCVKHIIYVDNKTINRAEYPE--GLEIHSMQSVEELGSKpenSSIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHS 293
Cdd:PLN02736 168 LSEIPSVRLIVVVGGADEPLPSLPSgtGVEIVTYSKLLAQGRS---SPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 294 NLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSP--LTLSDqsskikkgskgDCTVLKPTLM 371
Cdd:PLN02736 245 NLIANVAGSSLSTK-FYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGdnLKLMD-----------DLAALRPTIF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 372 AAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYD-APLCNLILFKKVKALLGGNVRMMLSGGAPLSPQT 450
Cdd:PLN02736 313 CSVPRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALENGKNpSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDV 392
|
410 420 430
....*....|....*....|....*....|.
gi 1958806453 451 HRFMNVCFCCPIGQGYGLTE-SCGAGTVTEG 480
Cdd:PLN02736 393 MEFLRICFGGRVLEGYGMTEtSCVISGMDEG 423
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
118-491 |
1.51e-72 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 238.37 E-value: 1.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 118 LILGNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESE 197
Cdd:pfam00501 14 LEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 198 ASYLITSVELLESKLKAALLDINCVKHIIYVDNKTINRAEypegleihsmqSVEELGSKPENSSIPPSRPTPSDMAIVMY 277
Cdd:pfam00501 94 AKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEE-----------PLPEEAKPADVPPPPPPPPDPDDLAYIIY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 278 TSGSTGRPKGVMMHHSNLIAGMTGQ---CERIPGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGCRIGYSSPLTLSDQss 353
Cdd:pfam00501 163 TSGTTGKPKGVMLTHRNLVANVLSIkrvRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLPPGFPALDP-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 354 kikKGSKGDCTVLKPTLMAAVPEIMDRIYKNvmskvqemnyiqktlfkigydykleqikkgydaplcnlilfKKVKALLG 433
Cdd:pfam00501 241 ---AALLELIERYKVTVLYGVPTLLNMLLEA-----------------------------------------GAPKRALL 276
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 434 GNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGT--VTEGKHRSCISITGK 491
Cdd:pfam00501 277 SSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTtpLPLDEDLRSLGSVGR 336
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
44-477 |
7.35e-66 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 227.01 E-value: 7.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 44 KRIKAKPTSdkpGSPYRSVTHFDSLAVIDiPGADTLDKLFDHAVAKFGKKDSLGTREILseenemqpNGKVfkklilGNY 123
Cdd:PLN02430 13 KGKDGKPSV---GPVYRNLLSKKGFPPID-SDITTAWDIFSKSVEKYPDNKMLGWRRIV--------DGKV------GPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 124 KWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEasylIT 203
Cdd:PLN02430 75 MWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAE----ID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 204 SVELLESKLKAaLLDINC-----VKHIIYVDNKTINRAEYPEGLEIHSMQSVEELGSKPENSSiPPSRPTPSDMAIVMYT 278
Cdd:PLN02430 151 FVFVQDKKIKE-LLEPDCksakrLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGKENPS-ETNPPKPLDICTIMYT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 279 SGSTGRPKGVMMHHSNLIAGMTG------QCEriPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSpltlSDQS 352
Cdd:PLN02430 229 SGTSGDPKGVVLTHEAVATFVRGvdlfmeQFE--DKMTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYH----GDLN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 353 SkikkgSKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYD----APLCNLILFKKV 428
Cdd:PLN02430 303 A-----LRDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGYShkkaSPMADFLAFRKV 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1958806453 429 KALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTV 477
Cdd:PLN02430 378 KAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTL 426
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
121-478 |
9.48e-62 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 210.91 E-value: 9.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASY 200
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 201 LITSvellesklkaalldincvkhiiyvdnktinraeypegleihsmqsveelgskpenssippsrpTPSDMAIVMYTSG 280
Cdd:cd05907 81 LFVE---------------------------------------------------------------DPDDLATIIYTSG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 281 STGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLE-LTAEISCFTYGCRIGYSSPL-TLSDQSSKIkkg 358
Cdd:cd05907 98 TTGRPKGVMLSHRNILSNALALAERLP-ATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFASSAeTLLDDLSEV--- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 359 skgdctvlKPTLMAAVPEIMDRIYKNVmsKVQEMNYIQKTLFKIGydykleqikkgydaplcnlilfkkvkalLGGNVRM 438
Cdd:cd05907 174 --------RPTVFLAVPRVWEKVYAAI--KVKAVPGLKRKLFDLA----------------------------VGGRLRF 215
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1958806453 439 MLSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVT 478
Cdd:cd05907 216 AASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLN 254
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
47-473 |
9.48e-62 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 215.86 E-value: 9.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 47 KAKPTSD-KP--GSPYRSVTHFDSLavIDIP-GADTLDKLFDHAVAKFGKKDSLGTREILseenemqpNGKVfkklilGN 122
Cdd:PLN02861 11 ESRPATGgKPsaGPVYRSIYAKDGL--LDLPaDIDSPWQFFSDAVKKYPNNQMLGRRQVT--------DSKV------GP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 123 YKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASylI 202
Cdd:PLN02861 75 YVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS--I 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 203 TSVEllESKLKAALLDI-NCVKHIIYV----DNKTINRAEYPE-GLEIHSMQSVEELGSkpENSSIPPSRPTpsDMAIVM 276
Cdd:PLN02861 153 AFVQ--ESKISSILSCLpKCSSNLKTIvsfgDVSSEQKEEAEElGVSCFSWEEFSLMGS--LDCELPPKQKT--DICTIM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 277 YTSGSTGRPKGVMMHHSNLIAG------MTGQCERIpgLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSpltlSD 350
Cdd:PLN02861 227 YTSGTTGEPKGVILTNRAIIAEvlstdhLLKVTDRV--ATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQ----GD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 351 QSSKIKkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYD----APLCNLILFK 426
Cdd:PLN02861 301 IRYLME-----DVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGLKqeeaSPRLDRLVFD 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958806453 427 KVKALLGGNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCG 473
Cdd:PLN02861 376 KIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCG 422
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
48-476 |
1.29e-61 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 215.65 E-value: 1.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 48 AKPTSD-KP--GSPYRSVTHFDSLAViDIPGADTLDKLFDHAVAKFGKKDSLGTREILseenemqpNGKVfkklilGNYK 124
Cdd:PLN02614 14 GKEGSDgRPsvGPVYRSIFAKDGFPN-PIEGMDSCWDVFRMSVEKYPNNPMLGRREIV--------DGKP------GKYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 125 WINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITS 204
Cdd:PLN02614 79 WQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 205 VELLESKLKAALLDINCVKHIIYVDNKTINRAEYPE--GLEIHSMQSVEELGsKPENSSIPPSRPtpSDMAIVMYTSGST 282
Cdd:PLN02614 159 EKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAEtfGLVIYAWDEFLKLG-EGKQYDLPIKKK--SDICTIMYTSGTT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 283 GRPKGVMMHHSNLIAGMTGQCERI----PGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSpltlSDQSSKIKkg 358
Cdd:PLN02614 236 GDPKGVMISNESIVTLIAGVIRLLksanAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGFWR----GDVKLLIE-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 359 skgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIKKGYD----APLCNLILFKKVKALLGG 434
Cdd:PLN02614 310 ---DLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQShveaSPLCDKLVFNKVKQGLGG 386
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958806453 435 NVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCgAGT 476
Cdd:PLN02614 387 NVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESC-AGT 427
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
121-482 |
1.29e-39 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 150.97 E-value: 1.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFkynfplvtlyaTLGKEAVVHGLNES--EA 198
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIM-----------ALGAVDVVRGSDSSveEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 199 SYLITSVEllesklkaalldinCVkhIIYVDNktinraeypegleihsmqsveelgskpenssippsrpTPSDMAIVMYT 278
Cdd:cd17640 70 LYILNHSE--------------SV--ALVVEN-------------------------------------DSDDLATIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 279 SGSTGRPKGVMMHHSNLIAGMTGQCERIPGlGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDqsskikkg 358
Cdd:cd17640 97 SGTTGNPKGVMLTHANLLHQIRSLSDIVPP-QPGDRFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTLKD-------- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 359 skgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIgydykleqikkgydaplcnlilfkkvkALLGGNVRM 438
Cdd:cd17640 168 ---DLKRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLF---------------------------FLSGGIFKF 217
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1958806453 439 MLSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEGKH 482
Cdd:cd17640 218 GISGGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKC 260
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
125-477 |
8.74e-37 |
|
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: 144.49 E-value: 8.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 125 WINYLEvncRVNNFGSGLTALGLKPKNTIAIFCETRAEW---MIAAQTCFKYNFPLvtlYATLGKEAVVHGLNESEASYL 201
Cdd:cd17641 14 WADYAD---RVRAFALGLLALGVGRGDVVAILGDNRPEWvwaELAAQAIGALSLGI---YQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 202 ITSVELLESKLKAALLDINCVKHIIYVDNKTINRAEYPEgleIHSMQSVEELGSK-----PENSSIPPSRPTPSDMAIVM 276
Cdd:cd17641 88 IAEDEEQVDKLLEIADRIPSVRYVIYCDPRGMRKYDDPR---LISFEDVVALGRAldrrdPGLYEREVAAGKGEDVAVLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 277 YTSGSTGRPKGVMMHHSNLIaGMTGQCERIPGLGPKDTYIGYLPLAHVLELT-----AEISCFTYGCrigYSSPLTLsdq 351
Cdd:cd17641 165 TTSGTTGKPKLAMLSHGNFL-GHCAAYLAADPLGPGDEYVSVLPLPWIGEQMysvgqALVCGFIVNF---PEEPETM--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 352 sskikkgsKGDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYD--YK-LEQIKKGYDAP--------LC 420
Cdd:cd17641 238 --------MEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKlgLRaLDRGKRGRPVSlwlrlaswLA 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958806453 421 NLILFKKVKALLG-GNVRMMLSGGAPLSPQTHRF---MNVcfccPIGQGYGLTESCGAGTV 477
Cdd:cd17641 310 DALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFfhaIGV----PLKQLYGQTELAGAYTV 366
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
78-477 |
4.24e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 129.92 E-value: 4.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 78 TLDKLFDHAVAKFGKKdslgtrEILSEEnemqpnGKVFkklilgnykwiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFC 157
Cdd:PRK06187 7 TIGRILRHGARKHPDK------EAVYFD------GRRT-----------TYAELDERVNRLANALRALGVKKGDRVAVFD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 158 ETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESkLKAALLDINCVKHIIYVDnktinraE 237
Cdd:PRK06187 64 WNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPL-LAAILPQLPTVRTVIVEG-------D 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 238 YPEGLEIHSMQSVEELGSKpENSSIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIG 317
Cdd:PRK06187 136 GPAAPLAPEVGEYEELLAA-ASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFL-HSLAVCAWLKLSRDDVYLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 318 YLPLAHVLELTAEISCFTYGCRIGYS---SPLTLSDQsskIKKgskgdctvLKPTLMAAVPEImdriyknvmskvqeMNY 394
Cdd:PRK06187 214 IVPMFHVHAWGLPYLALMAGAKQVIPrrfDPENLLDL---IET--------ERVTFFFAVPTI--------------WQM 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 395 IQKTLFKIGYDYkleqikkgydaplcnlilfkkvkallgGNVRMMLSGGAPLSPQT-HRFMNVcFCCPIGQGYGLTESCG 473
Cdd:PRK06187 269 LLKAPRAYFVDF---------------------------SSLRLVIYGGAALPPALlREFKEK-FGIDLVQGYGMTETSP 320
|
....
gi 1958806453 474 AGTV 477
Cdd:PRK06187 321 VVSV 324
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
126-470 |
2.39e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 121.40 E-value: 2.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSv 205
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ellesklkaalldincvkhiiyvdnktinraeypegleihsmqsveelgskpenssippsrpTPSDMAIVMYTSGSTGRP 285
Cdd:cd05914 87 --------------------------------------------------------------DEDDVALINYTSGTTGNS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 286 KGVMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAHVLELtaeisCFTYGCRIGYSSPLTLSDQ--SSKIKKGSKGDc 363
Cdd:cd05914 105 KGVMLTYRNIVSNVDG-VKEVVLLGKGDKILSILPLHHIYPL-----TFTLLLPLLNGAHVVFLDKipSAKIIALAFAQ- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 364 tvLKPTLMAAVPEIMDRIYKNVmskVQEMNYIQKTLFKIGYDYKLEQIKKgydaplcnlILFKKVKALLGGNVRMMLSGG 443
Cdd:cd05914 178 --VTPTLGVPVPLVIEKIFKMD---IIPKLTLKKFKFKLAKKINNRKIRK---------LAFKKVHEAFGGNIKEFVIGG 243
|
330 340 350
....*....|....*....|....*....|
gi 1958806453 444 APLSPQTHRF---MNVCFCcpigQGYGLTE 470
Cdd:cd05914 244 AKINPDVEEFlrtIGFPYT----IGYGMTE 269
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
121-478 |
6.23e-28 |
|
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: 117.57 E-value: 6.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASY 200
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 201 LITsvellesklkAALLDINCVKHIIyvdnktinraeyPEGLEIHSMQSVEELGSKPENSSI----PPS----RPTPSDM 272
Cdd:cd05932 82 LFV----------GKLDDWKAMAPGV------------PEGLISISLPPPSAANCQYQWDDLiaqhPPLeerpTRFPEQL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 273 AIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTA-EISCFTYGCRIGYSSPLTLSDQ 351
Cdd:cd05932 140 ATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHI-GTEENDRMLSYLPLAHVTERVFvEGGSLYGGVLVAFAESLDTFVE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 352 sskikkgskgDCTVLKPTLMAAVPEIMDRIYKNVMSKV--QEMNyiqkTLFKIgydykleqikkgydaPLCNLILFKKVK 429
Cdd:cd05932 219 ----------DVQRARPTLFFSVPRLWTKFQQGVQDKIpqQKLN----LLLKI---------------PVVNSLVKRKVL 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958806453 430 ALLGGN-VRMMLSGGAPLSPQT-HRFMNVCFccPIGQGYGLTESCGAGTVT 478
Cdd:cd05932 270 KGLGLDqCRLAGCGSAPVPPALlEWYRSLGL--NILEAYGMTENFAYSHLN 318
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
126-478 |
2.27e-27 |
|
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: 115.29 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITsv 205
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ellesklkaalldincvkhiiyvdnktinraeypegleihsmqsveelgskpenssippsrptpsdmAIVMYTSGSTGRP 285
Cdd:COG0318 103 -------------------------------------------------------------------ALILYTSGTTGRP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 286 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGCRI---GYSSPLTLSDQsskIKKGskg 361
Cdd:COG0318 116 KGVMLTHRNLLANAAAIAAAL-GLTPGDVVLVALPLFHVFGLTVGLlAPLLAGATLvllPRFDPERVLEL---IERE--- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 362 dctvlKPTLMAAVPEIMDRIyknvmskvqeMNYIQKTlfkigydykleqikkGYDAPlcnlilfkkvkallggNVRMMLS 441
Cdd:COG0318 189 -----RVTVLFGVPTMLARL----------LRHPEFA---------------RYDLS----------------SLRLVVS 222
|
330 340 350
....*....|....*....|....*....|....*...
gi 1958806453 442 GGAPLSPQT-HRFMNVcFCCPIGQGYGLTESCGAGTVT 478
Cdd:COG0318 223 GGAPLPPELlERFEER-FGVRIVEGYGLTETSPVVTVN 259
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
126-478 |
7.49e-26 |
|
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: 111.15 E-value: 7.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ELLEsKLKAALLDINCVKHIIYVDNKtinraeypegleIHSMQSVEELGSKPENSSI---PPSRPT-PSDMAIVMYTSGS 281
Cdd:cd05911 91 DGLE-KVKEAAKELGPKDKIIVLDDK------------PDGVLSIEDLLSPTLGEEDedlPPPLKDgKDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 282 TGRPKGVMMHHSNLIAGMTGQCERIPG-LGPKDTYIGYLPLAHVleltaeiscftYGCRIGYSSPLtlsdqsskikKGsk 360
Cdd:cd05911 158 TGLPKGVCLSHRNLIANLSQVQTFLYGnDGSNDVILGFLPLYHI-----------YGLFTTLASLL----------NG-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 361 gdCTVLkptlmaavpeIMDRIYKNVMskvqeMNYIQKtlfkigydYKleqIKKGYDAPLCNLILFK---KVKALLgGNVR 437
Cdd:cd05911 215 --ATVI----------IMPKFDSELF-----LDLIEK--------YK---ITFLYLVPPIAAALAKsplLDKYDL-SSLR 265
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958806453 438 MMLSGGAPLSPQTHRFMNVCFC-CPIGQGYGLTESCGAGTVT 478
Cdd:cd05911 266 VILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVN 307
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
126-322 |
1.89e-25 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 110.26 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIA------AQTCFKYNFPLvtlyatLGKEAVVHGLNESEAS 199
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAmfgaalAGGVFVPINPL------LKAEQVAHILADCNVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 200 YLITSVELLEsKLKAALLDINCVKHIIYVDNKTINRAEYPeGLEIHSMQSVEELGSkpensSIPPSRPTPSDMAIVMYTS 279
Cdd:TIGR03098 100 LLVTSSERLD-LLHPALPGCHDLRTLIIVGDPAHASEGHP-GEEPASWPKLLALGD-----ADPPHPVIDSDMAAILYTS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1958806453 280 GSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLA 322
Cdd:TIGR03098 173 GSTGRPKGVVLSHRNLVAGAQSVATYLE-NRPDDRLLAVLPLS 214
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
124-477 |
1.67e-24 |
|
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: 106.88 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 124 KWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLIT 203
Cdd:cd05936 23 RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 204 SVELlesklkaalldincvkhiiyvdnktinraeypegleihsmqsvEELGSKPENSSIPPSRpTPSDMAIVMYTSGSTG 283
Cdd:cd05936 103 AVSF-------------------------------------------TDLLAAGAPLGERVAL-TPEDVAVLQYTSGTTG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 284 RPKGVMMHHSNLIAGMTgQCERI--PGLGPKDTYIGYLPLAHVLELTAeisCFTYGCRIGYS-------SPLTLSDQssk 354
Cdd:cd05936 139 VPKGAMLTHRNLVANAL-QIKAWleDLLEGDDVVLAALPLFHVFGLTV---ALLLPLALGATivliprfRPIGVLKE--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 355 IKKGskgdctvlKPTLMAAVPeimdriyknvmskvqemnyiqkTLFkIGydykleqikkgydaplcnLILFKKVKALLGG 434
Cdd:cd05936 212 IRKH--------RVTIFPGVP----------------------TMY-IA------------------LLNAPEFKKRDFS 242
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1958806453 435 NVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTV 477
Cdd:cd05936 243 SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAV 285
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
121-478 |
2.05e-24 |
|
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: 107.44 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 121 GNYKW--INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAA-QTCFKYNFpLVTLYATLGKEAVVHGLNESE 197
Cdd:cd05933 2 RGDKWhtLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAvGAIFAGGI-AVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 198 ASYLITSVELLESKLKAALLDINCVKHIIyvdnktINRAEYPEGL-EIHSMQSVEELGSKPENSSIPP--SRPTPSDMAI 274
Cdd:cd05933 81 ANILVVENQKQLQKILQIQDKLPHLKAII------QYKEPLKEKEpNLYSWDEFMELGRSIPDEQLDAiiSSQKPNQCCT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 275 VMYTSGSTGRPKGVMMHHSNL--IAGMTGQ-CERIPGLGPKDTYIGYLPLAHVLELTAEI-SCFTYGCRIGYSSPLTLsd 350
Cdd:cd05933 155 LIYTSGTTGMPKGVMLSHDNItwTAKAASQhMDLRPATVGQESVVSYLPLSHIAAQILDIwLPIKVGGQVYFAQPDAL-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 351 qsskikKGSKGDcTV--LKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLF----KIGYDYKLEQIKKGYDAPLC---- 420
Cdd:cd05933 233 ------KGTLVK-TLreVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIAswakGVGLETNLKLMGGESPSPLFyrla 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806453 421 NLILFKKVKALLG-GNVRMMLSGGAPLSPQTHRF---MNVcfccPIGQGYGLTESCGAGTVT 478
Cdd:cd05933 306 KKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFflsLNI----PIMELYGMSETSGPHTIS 363
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
106-490 |
1.48e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 99.02 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 106 NEMQPNGKvFKKLILGNYKWINYLEVNCrvNNFGSGLTALGLKPKNTIAIFC----ETRAEWM------IAAQTCFKYNF 175
Cdd:PTZ00342 122 NEEQNNGK-FKLLGLYGSNSINWLVADL--ACMLSGVTTLVMHSKFSIDVIVdilnETKLEWLcldldlVEGLLERKNEL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 176 P----LVTLyATLGKEAVVHGLNESE-------ASYLITSVELLESKLKAALLDINCVKHIIYvDNKTINR----AEYPE 240
Cdd:PTZ00342 199 PhlkkLIIL-DTLIKSKEININKEEKnngsnvnNNGNKNNKEEQKGNDLSNELEDISLGPLEY-DKEKLEKikdlKEKAK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 241 GLEIHSMQSVEELGSKPENSSIppSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCER--IPGLGPKdTYIGY 318
Cdd:PTZ00342 277 KLGISIILFDDMTKNKTTNYKI--QNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHsiFKKYNPK-THLSY 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 319 LPLAHVLELTAEISCFTYGCRIgysspltlsDQSSK-IKKGSKgDCTVLKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQK 397
Cdd:PTZ00342 354 LPISHIYERVIAYLSFMLGGTI---------NIWSKdINYFSK-DIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKR 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 398 TLFKigydyKLEQIKKG-YDAPLCNLI-----LFKKVKALLGGNVRMMLSGGAPLSPQTHR----FMNVCFCcpigQGYG 467
Cdd:PTZ00342 424 FLVK-----KILSLRKSnNNGGFSKFLegithISSKIKDKVNPNLEVILNGGGKLSPKIAEelsvLLNVNYY----QGYG 494
|
410 420
....*....|....*....|...
gi 1958806453 468 LTESCGAGTVTEGKHRSCISITG 490
Cdd:PTZ00342 495 LTETTGPIFVQHADDNNTESIGG 517
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
126-478 |
2.42e-21 |
|
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: 97.69 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEwmiaaqtcfkynFPLVTLYAT-LGkeAVVHGLN---------- 194
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIE------------FPVAFLAVLsLG--AVVTTANplstpaeiak 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 195 ---ESEASYLITSVELLEsKLKAALLDINCVkhiiyvdnktinraeypEGLEIHSMQSVEELGSKPEnSSIPPSRPTPSD 271
Cdd:cd05904 99 qvkDSGAKLAFTTAELAE-KLASLALPVVLL-----------------DSAEFDSLSFSDLLFEADE-AEPPVVVIKQDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 272 MAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERI-PGLGPKDTYIGYLPLAHVLELTAeiscFTYGcrigyssplTLSd 350
Cdd:cd05904 160 VAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEgSNSDSEDVFLCVLPMFHIYGLSS----FALG---------LLR- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 351 qsskikkgskgdctvLKPTLMaavpeimdriyknVMSK---VQEMNYIQKtlFKIGYdykleqikkgydAPLCNLILFKK 427
Cdd:cd05904 226 ---------------LGATVV-------------VMPRfdlEELLAAIER--YKVTH------------LPVVPPIVLAL 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958806453 428 VKALLGGN-----VRMMLSGGAPLSPQT-----HRFMNVcfccPIGQGYGLTESCGAGTVT 478
Cdd:cd05904 264 VKSPIVDKydlssLRQIMSGAAPLGKELieafrAKFPNV----DLGQGYGMTESTGVVAMC 320
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
271-478 |
3.41e-20 |
|
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: 91.96 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRI---GYSSPLT 347
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLA-AAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 348 LSDqssKIKKgskgdctvLKPTLMAAVPEIMDRIyknvmskvqemnyiqktlfkigydykLEQIK-KGYDAPlcnlilfk 426
Cdd:cd04433 80 ALE---LIER--------EKVTILLGVPTLLARL--------------------------LKAPEsAGYDLS-------- 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958806453 427 kvkallggNVRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVT 478
Cdd:cd04433 115 --------SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATG 158
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
126-329 |
5.53e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 93.43 E-value: 5.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAqtcfkynfplvtlYATLGKEAVVHGLNE----SEASY- 200
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAA-------------LGALKAGAVVVPLNTrytaDEAAYi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 201 -------LITSVELLESKLKAALLDINCVKHIIYVDNktinRAEYPEGLEIHSMQSVEELGSKPENSsipPSRpTPSDMA 273
Cdd:PRK07656 98 largdakALFVLGLFLGVDYSATTRLPALEHVVICET----EEDDPHTEKMKTFTDFLAAGDPAERA---PEV-DPDDVA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806453 274 IVMYTSGSTGRPKGVMMHHSNLIAGMTGQCErIPGLGPKDTYIGYLPLAHVLELTA 329
Cdd:PRK07656 170 DILFTSGTTGRPKGAMLTHRQLLSNAADWAE-YLGLTEGDRYLAANPFFHVFGYKA 224
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
79-478 |
4.63e-18 |
|
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: 87.90 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 79 LDKLFDHAVAKFGKKDSLGTREilSEENEMQPNGKVFKKLiLGNYKWINYLEVNCRVNNFGSGL-TALGLKPKNTIAIFC 157
Cdd:cd17632 24 LAQIIATVMTGYADRPALGQRA--TELVTDPATGRTTLRL-LPRFETITYAELWERVGAVAAAHdPEQPVRPGDFVAVLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 158 ETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLkAALLDINCVKHIIYVDNK---TIN 234
Cdd:cd17632 101 FTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAV-EAVLEGGTPPRLVVFDHRpevDAH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 235 R----------AEYPEGLEIHSMQSVEELGSKPEnssiPPSRPTPSDMAIVM--YTSGSTGRPKGVMMHHSNLIAGMTGQ 302
Cdd:cd17632 180 RaalesarerlAAVGIPVTTLTLIAVRGRDLPPA----PLFRPEPDDDPLALliYTSGSTGTPKGAMYTERLVATFWLKV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 303 CERIPGLGPKDTYIGYLPLAHVLeltAEISCFTYGCRIGYSSPLTLSDQSSKIKkgskgDCTVLKPTLMAAVPEIMDRIY 382
Cdd:cd17632 256 SSIQDIRPPASITLNFMPMSHIA---GRISLYGTLARGGTAYFAAASDMSTLFD-----DLALVRPTELFLVPRVCDMLF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 383 KNVMSKVqemnyiqktlfkigyDYKLEQikkGYDAplcnLILFKKVKA-----LLGGNVRMMLSGGAPLSPQTHRFMNVC 457
Cdd:cd17632 328 QRYQAEL---------------DRRSVA---GADA----ETLAERVKAelrerVLGGRLLAAVCGSAPLSAEMKAFMESL 385
|
410 420
....*....|....*....|.
gi 1958806453 458 FCCPIGQGYGLTEscgAGTVT 478
Cdd:cd17632 386 LDLDLHDGYGSTE---AGAVI 403
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
126-315 |
2.40e-17 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 85.55 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ELLE--------SKLKAALLDINCVKHIIYVDNkTINRAEYPEGLEIHsmqsvEELGSKPENssiPPSRPTPS-DMAIVM 276
Cdd:COG0365 120 GGLRggkvidlkEKVDEALEELPSLEHVIVVGR-TGADVPMEGDLDWD-----ELLAAASAE---FEPEPTDAdDPLFIL 190
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958806453 277 YTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTY 315
Cdd:COG0365 191 YTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVF 229
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
126-313 |
2.92e-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: 79.52 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCEtRAEWMIAAqtcfkynfplvtLYATL--G-----------KEAVVHG 192
Cdd:COG1020 502 LTYAELNARANRLAHHLRALGVGPGDLVGVCLE-RSLEMVVA------------LLAVLkaGaayvpldpaypAERLAYM 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 193 LNESEASYLITsvellESKLKAALLDINCvkHIIYVDNKTInrAEYPEGLeihsmqsveelgskpenssiPPSRPTPSDM 272
Cdd:COG1020 569 LEDAGARLVLT-----QSALAARLPELGV--PVLALDALAL--AAEPATN--------------------PPVPVTPDDL 619
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958806453 273 AIVMYTSGSTGRPKGVMMHH---SNLIAGMTGQCeripGLGPKD 313
Cdd:COG1020 620 AYVIYTSGSTGRPKGVMVEHralVNLLAWMQRRY----GLGPGD 659
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
125-314 |
1.68e-14 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 76.18 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 125 WINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITS 204
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 205 VELLESklkaalldincvkhiiyvdnktinraeYPEGLEIhsmqsVEELGSKPENSSIPPSRPT-PSDMAIVMYTSGSTG 283
Cdd:cd12116 92 DALPDR---------------------------LPAGLPV-----LLLALAAAAAAPAAPRTPVsPDDLAYVIYTSGSTG 139
|
170 180 190
....*....|....*....|....*....|.
gi 1958806453 284 RPKGVMMHHSNLIAGMTGQCERiPGLGPKDT 314
Cdd:cd12116 140 RPKGVVVSHRNLVNFLHSMRER-LGLGPGDR 169
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
122-478 |
1.81e-14 |
|
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: 76.03 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 122 NYKWINYLEVNCRVnnfGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYL 201
Cdd:cd17642 44 NYSYAEYLEMSVRL---AEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 202 ITSVELLESKLKAALlDINCVKHIIYVDNKTinraEYPEGLEIHSMQSVEELGSKPENSSIPPSRPTPSDMAIVMYTSGS 281
Cdd:cd17642 121 FCSKKGLQKVLNVQK-KLKIIKTIIILDSKE----DYKGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 282 TGRPKGVMMHHSNLIAGMTGQCERIPG--LGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGY----SSPLTLSD-QSSK 354
Cdd:cd17642 196 TGLPKGVQLTHKNIVARFSHARDPIFGnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmykfEEELFLRSlQDYK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 355 IKKgskgdcTVLKPTLMAAVPeimdriyknvmskvqemnyiqktlfkigydyKLEQIKKgYDapLCNLIlfkkvkallgg 434
Cdd:cd17642 276 VQS------ALLVPTLFAFFA-------------------------------KSTLVDK-YD--LSNLH----------- 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1958806453 435 nvrMMLSGGAPLSPQTHRFMNVCFCCP-IGQGYGLTESCGAGTVT 478
Cdd:cd17642 305 ---EIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILIT 346
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
262-381 |
2.12e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 76.19 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 262 IPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIA-GMTGQCeRIPGLGPKD-TYIGYLPLAHVLELTAeisCFTYGCR 339
Cdd:PRK05605 211 VSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFAnAAQGKA-WVPGLGDGPeRVLAALPMFHAYGLTL---CLTLAVS 286
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1958806453 340 IG--------YSSPLTLsdqsSKIKKGskgdctvlKPTLMAAVPEIMDRI 381
Cdd:PRK05605 287 IGgelvllpaPDIDLIL----DAMKKH--------PPTWLPGVPPLYEKI 324
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
121-472 |
5.34e-14 |
|
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: 74.66 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAaqtcfkynfplvtLYATLGKEAVVHGLN------ 194
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVA-------------FLAAARAGAVVAPLNpaykka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 195 -------ESEASYLITSVELLESKLKAALldincvkhiiyVDNKTINRAEYPEGLEIHSMQSvEELGSKPENSSIPPSR- 266
Cdd:cd05926 77 efefylaDLGSKLVLTPKGELGPASRAAS-----------KLGLAILELALDVGVLIRAPSA-ESLSNLLADKKNAKSEg 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 267 -PTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCeRIPGLGPKDTYIGYLPLAHVLELTAEI--SCFTYGCrigys 343
Cdd:cd05926 145 vPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNIT-NTYKLTPDDRTLVVMPLFHVHGLVASLlsTLAAGGS----- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 344 spLTLSDQSSkikkGSK--GDCTVLKPTLMAAVPEIMDRIYKNVMSKvqemnyiqktlfkigydykleqikkgydaplcn 421
Cdd:cd05926 219 --VVLPPRFS----ASTfwPDVRDYNATWYTAVPTIHQILLNRPEPN--------------------------------- 259
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1958806453 422 lilFKKVKALLggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESC 472
Cdd:cd05926 260 ---PESPPPKL----RFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAA 303
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
101-339 |
2.16e-13 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 72.87 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 101 ILSEENEMQPNgkvfKKLILGNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAE---------WMIAAQTcf 171
Cdd:PRK06155 26 MLARQAERYPD----RPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEfldvflgcaWLGAIAV-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 172 kynfPLVTlyATLGKEaVVHGLNESEASYLITSVELLESkLKAALLDINCVKHIIYVDNKTINRAeyPEGLEIHSMqsve 251
Cdd:PRK06155 100 ----PINT--ALRGPQ-LEHILRNSGARLLVVEAALLAA-LEAADPGDLPLPAVWLLDAPASVSV--PAGWSTAPL---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 252 elgsKPENSSIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNL-IAG-MTGqceRIPGLGPKDTYIGYLPLAHVLELTA 329
Cdd:PRK06155 166 ----PPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFyWWGrNSA---EDLEIGADDVLYTTLPLFHTNALNA 238
|
250
....*....|
gi 1958806453 330 EISCFTYGCR 339
Cdd:PRK06155 239 FFQALLAGAT 248
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
118-472 |
2.95e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 72.30 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 118 LILGNYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKynfplvtlyatLGKEAVvhglnese 197
Cdd:PRK03640 21 IEFEEKKV-TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQ-----------LGAVAV-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 198 asylitsveLLESKLKAA-----LLDINcVKHIIYVDnktinraEYPEGLEIHSMQSVEELGSKPENSSIPPSRPTPSDM 272
Cdd:PRK03640 81 ---------LLNTRLSREellwqLDDAE-VKCLITDD-------DFEAKLIPGISVKFAELMNGPKEEAEIQEEFDLDEV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 273 AIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIgyssplTLSDQ- 351
Cdd:PRK03640 144 ATIMYTSGTTGKPKGVIQTYGNHWWSAVGSALNL-GLTEDDCWLAAVPIFHISGLSILMRSVIYGMRV------VLVEKf 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 352 -SSKIKKGSKGDctvlKPTLMAAVPEIMDRIyknvMSKVQEMNYiqktlfkigydykleqikkgydaplcnlilfkkvka 430
Cdd:PRK03640 217 dAEKINKLLQTG----GVTIISVVSTMLQRL----LERLGEGTY------------------------------------ 252
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958806453 431 llGGNVRMMLSGGAPLSPQT------HRFmnvcfccPIGQGYGLTESC 472
Cdd:PRK03640 253 --PSSFRCMLLGGGPAPKPLleqckeKGI-------PVYQSYGMTETA 291
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-322 |
1.63e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 71.14 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQS 4656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ELLEsklkaalldincvkhiiyvdnktinRAEYPEGLEIHSMQSVEELGSKPENSsiPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:PRK12316 4657 HLLQ-------------------------RLPIPDGLASLALDRDEDWEGFPAHD--PAVRLHPDNLAYVIYTSGSTGRP 4709
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958806453 286 KGVMMHHSNLIAGMTGQCERiPGLGPKDTYIGYLPLA 322
Cdd:PRK12316 4710 KGVAVSHGSLVNHLHATGER-YELTPDDRVLQFMSFS 4745
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-322 |
1.84e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 70.76 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ELLEsklkaalldincvkhiiyvdnktinRAEYPEGLEIHSMQSVEELGSKPENSsiPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:PRK12316 2109 HLLE-------------------------RLPLPAGVARLPLDRDAEWADYPDTA--PAVQLAGENLAYVIYTSGSTGLP 2161
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958806453 286 KGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLA 322
Cdd:PRK12316 2162 KGVAVSHGALVAHCQAAGERY-ELSPADCELQFMSFS 2197
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
126-297 |
2.51e-12 |
|
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: 69.32 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ELLESKLKAALLDINCVKHIIYVDnktinraeyPEGLEIHSMQSVEELGSkpENSSIPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:cd05959 110 ELAPVLAAALTKSEHTLVVLIVSG---------GAGPEAGALLLAELVAA--EAEQLKPAATHADDPAFWLYSSGSTGRP 178
|
170
....*....|..
gi 1958806453 286 KGVMMHHSNLIA 297
Cdd:cd05959 179 KGVVHLHADIYW 190
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
126-293 |
2.79e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 69.14 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFK---------YNF---PLVTLYATLGKEAVVHgl 193
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKaravpvnvnYRYvedELRYLLDDSDAVALVY-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 194 nesEASYLITSVELLESKLKaalldincVKHIIYVDNKTINrAEYPEGLEIHSMQSveelGSKPENSSIPPSrptPSDMa 273
Cdd:PRK07798 107 ---EREFAPRVAEVLPRLPK--------LRTLVVVEDGSGN-DLLPGAVDYEDALA----AGSPERDFGERS---PDDL- 166
|
170 180
....*....|....*....|
gi 1958806453 274 IVMYTSGSTGRPKGVMMHHS 293
Cdd:PRK07798 167 YLLYTGGTTGMPKGVMWRQE 186
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
125-323 |
2.92e-12 |
|
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: 69.19 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 125 WINYLEVNCRVNNFGSGLTALGlKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYA-TLGKEA--VVHGLNESEASYL 201
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPpTPGRHAerLAAILADAGPRVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 202 ITSvelleSKLKAALLDIncvkhiiyvdnktinrAEYPEGLEIHSMQSVEELGSKPENSSIPPSrPTPSDMAIVMYTSGS 281
Cdd:cd05931 103 LTT-----AAALAAVRAF----------------AASRPAAGTPRLLVVDLLPDTSAADWPPPS-PDPDDIAYLQYTSGS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958806453 282 TGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAH 323
Cdd:cd05931 161 TGTPKGVVVTHRNLLANVRQIRRAY-GLDPGDVVVSWLPLYH 201
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
267-479 |
4.13e-12 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 68.56 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 267 PTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHvleltaeISCFTYGcrigysspl 346
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERL-GLGPGDVFLVASPMAH-------QTGFVYG--------- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 347 tlsdqsskikkgskgdctVLKPTLMAAvPEIMDRIYkNVMSKVQEMNYiQKTLFKIGYDYKLEQI---KKGYDAPLCNLi 423
Cdd:cd05903 153 ------------------FTLPLLLGA-PVVLQDIW-DPDKALALMRE-HGVTFMMGATPFLTDLlnaVEEAGEPLSRL- 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806453 424 lfkkvkallggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTE 479
Cdd:cd05903 211 -------------RTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSIT 253
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
126-297 |
4.78e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 68.77 E-value: 4.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKyNFPLVT-LYATLGKEAVVHGLNESEASYLITS 204
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALK-NGAIVGpLFEAFMEEAVRDRLEDSEAKVLITT 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 205 VELLESKLKAallDINCVKHIIYVDnktinrAEYPEGLEIHSMQsvEELGSKPENSSIPPSrpTPSDMAIVMYTSGSTGR 284
Cdd:PRK04319 153 PALLERKPAD---DLPSLKHVLLVG------EDVEEGPGTLDFN--ALMEQASDEFDIEWT--DREDGAILHYTSGSTGK 219
|
170
....*....|...
gi 1958806453 285 PKGVMMHHSNLIA 297
Cdd:PRK04319 220 PKGVLHVHNAMLQ 232
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
126-297 |
9.45e-12 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 67.56 E-value: 9.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:TIGR02262 31 LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ELLESkLKAALLDINCVKHIIYVdnktiNRAEYPEgleihsMQSVEELGSKPENSSIPPSRPtpSDMAIVMYTSGSTGRP 285
Cdd:TIGR02262 111 ALLPV-IKAALGKSPHLEHRVVV-----GRPEAGE------VQLAELLATESEQFKPAATQA--DDPAFWLYSSGSTGMP 176
|
170
....*....|..
gi 1958806453 286 KGVMMHHSNLIA 297
Cdd:TIGR02262 177 KGVVHTHSNPYW 188
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
128-327 |
5.39e-11 |
|
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: 64.59 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 128 YLEVNCRVNNFGSGL-TALGLKPKNTIAIFCEtRAEWMIAAQ-TCFK----YnFPLVTLYATLGKEAVvhgLNESEASYL 201
Cdd:TIGR01733 2 YRELDERANRLARHLrAAGGVGPGDRVAVLLE-RSAELVVAIlAVLKagaaY-VPLDPAYPAERLAFI---LEDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 202 ITSVELLESKLKAALLDINCVKhiiyVDNKTINRAEYPEGleihsmqsveelgskpenssiPPSRPTPSDMAIVMYTSGS 281
Cdd:TIGR01733 77 LTDSALASRLAGLVLPVILLDP----LELAALDDAPAPPP---------------------PDAPSGPDDLAYVIYTSGS 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958806453 282 TGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAH---VLEL 327
Cdd:TIGR01733 132 TGRPKGVVVTHRSLVN-LLAWLARRYGLDPDDRVLQFASLSFdasVEEI 179
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
118-323 |
6.65e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 64.95 E-value: 6.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 118 LILGNYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESE 197
Cdd:PRK08316 30 LVFGDRSW-TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 198 ASYLITSVELLEsKLKAALLDINCVKHIiyVDNKTINRaEYPEGLeiHSMQSVEELGSKPEnssiPPSRPTPSDMAIVMY 277
Cdd:PRK08316 109 ARAFLVDPALAP-TAEAALALLPVDTLI--LSLVLGGR-EAPGGW--LDFADWAEAGSVAE----PDVELADDDLAQILY 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958806453 278 TSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAH 323
Cdd:PRK08316 179 TSGTESLPKGAMLTHRALIAEYVS-CIVAGDMSADDIPLHALPLYH 223
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
233-324 |
6.83e-11 |
|
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: 65.00 E-value: 6.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 233 INRAEYPEGLEIHSMQSVEELGSKPENSSIPPSRPTpsDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCeRIPGLGPK 312
Cdd:cd05906 132 FAGLETLSGLPGIRVLSIEELLDTAADHDLPQSRPD--DLALLMLTSGSTGFPKAVPLTHRNILARSAGKI-QHNGLTPQ 208
|
90
....*....|..
gi 1958806453 313 DTYIGYLPLAHV 324
Cdd:cd05906 209 DVFLNWVPLDHV 220
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
126-322 |
1.10e-10 |
|
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: 64.27 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITsv 205
Cdd:cd17655 23 LTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLT-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ellESKLKAALLDIncvKHIIYVDNKTInRAEYPEGLEihsmqsveelgskpenssiPPSRPtpSDMAIVMYTSGSTGRP 285
Cdd:cd17655 101 ---QSHLQPPIAFI---GLIDLLDEDTI-YHEESENLE-------------------PVSKS--DDLAYVIYTSGSTGKP 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958806453 286 KGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLA 322
Cdd:cd17655 153 KGVMIEHRGVVNLVEWANKVIY-QGEHLRVALFASIS 188
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
263-325 |
1.11e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 64.21 E-value: 1.11e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806453 263 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHH---SNLIAGMTgqcERIpGLGPKDTYIGYLPLAHVL 325
Cdd:cd12114 119 PPVDVAPDDLAYVIFTSGSTGTPKGVMISHraaLNTILDIN---RRF-AVGPDDRVLALSSLSFDL 180
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
144-325 |
1.49e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 63.83 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 144 ALGLKPKNTIAIFCETRAEWMIAAqtcfkynfplvtlYATLGKEAVV-------------HGLNESEASYLITSVELLEs 210
Cdd:PRK08314 55 ECGVRKGDRVLLYMQNSPQFVIAY-------------YAILRANAVVvpvnpmnreeelaHYVTDSGARVAIVGSELAP- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 211 KLKAALLDINcVKHIIYVDNKTINRAEY----PEGLEI-HSMQSVEELGSKPENSSI------PPSRPTPSDMAIVMYTS 279
Cdd:PRK08314 121 KVAPAVGNLR-LRHVIVAQYSDYLPAEPeiavPAWLRAePPLQALAPGGVVAWKEALaaglapPPHTAGPDDLAVLPYTS 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1958806453 280 GSTGRPKGVMMHHSNLIAGMTGQCeRIPGLGPKDTYIGYLPLAHVL 325
Cdd:PRK08314 200 GTTGVPKGCMHTHRTVMANAVGSV-LWSNSTPESVVLAVLPLFHVT 244
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
125-323 |
1.77e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 63.43 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 125 WINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEwMIAAQtcfkYNFP-----LVTLYATLGKEAVVHGLNESEAS 199
Cdd:PRK08162 43 RRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPA-MVEAH----FGVPmagavLNTLNTRLDAASIAFMLRHGEAK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 200 YLITSVELleSKLKAALLDINCVKHIIYVDnktINRAEYPEGLEIHSMqSVEEL--GSKPEnssIPPSRPTPSDMAIVM- 276
Cdd:PRK08162 118 VLIVDTEF--AEVAREALALLPGPKPLVID---VDDPEYPGGRFIGAL-DYEAFlaSGDPD---FAWTLPADEWDAIALn 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958806453 277 YTSGSTGRPKGVMMHH--------SNLIAGmtgqceripGLGPKDTYIGYLPLAH 323
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHrgaylnalSNILAW---------GMPKHPVYLWTLPMFH 234
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
69-329 |
1.77e-10 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 63.74 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 69 AVIDIPGADTLDKLFDHAVAKFGKKdslgtreilseenemqPNGKVFKKLIlgnykwiNYLEVNCRVNNFGSGLTA-LGL 147
Cdd:PRK08751 17 AEIDLEQFRTVAEVFATSVAKFADR----------------PAYHSFGKTI-------TYREADQLVEQFAAYLLGeLQL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 148 KPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLI------TSVE----------LLESK 211
Cdd:PRK08751 74 KKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVvidnfgTTVQqviadtpvkqVITTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 212 L-------KAALLDInCVKHII-YVDNKTINRA-EYPEGLEihsmqsveeLGSKpenSSIPPSRPTPSDMAIVMYTSGST 282
Cdd:PRK08751 154 LgdmlgfpKAALVNF-VVKYVKkLVPEYRINGAiRFREALA---------LGRK---HSMPTLQIEPDDIAFLQYTGGTT 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958806453 283 GRPKGVMMHHSNLIAGMTGQCERIPGLGP----KDTYIGYLPLAHVLELTA 329
Cdd:PRK08751 221 GVAKGAMLTHRNLVANMQQAHQWLAGTGKleegCEVVITALPLYHIFALTA 271
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
268-315 |
2.31e-10 |
|
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: 62.93 E-value: 2.31e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1958806453 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTY 315
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYP-LTPGDRV 137
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-322 |
2.92e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 63.64 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:PRK12467 1600 LTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQS 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ELLEsklkaalldincvkhiiyvdnktinRAEYPEGLEIHSM-QSVEELGSKPEnsSIPPSRPTPSDMAIVMYTSGSTGR 284
Cdd:PRK12467 1680 HLQA-------------------------RLPLPDGLRSLVLdQEDDWLEGYSD--SNPAVNLAPQNLAYVIYTSGSTGR 1732
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958806453 285 PKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLA 322
Cdd:PRK12467 1733 PKGAGNRHGALVNRLCATQEAY-QLSAADVVLQFTSFA 1769
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
128-322 |
3.15e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 62.60 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 128 YLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEwMIAAQtcfkynfpLVTLYAtlgkeavvhGlneseASYLITSVEL 207
Cdd:cd12117 25 YAELNERANRLARRLRAAGVGPGDVVGVLAERSPE-LVVAL--------LAVLKA---------G-----AAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 208 LESKLKAALLDINCVkhIIYVDNKTINRAEYPEGLEIHsmqsveELGSKPENSSIPPSRPTPSDMAIVMYTSGSTGRPKG 287
Cdd:cd12117 82 PAERLAFMLADAGAK--VLLTDRSLAGRAGGLEVAVVI------DEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKG 153
|
170 180 190
....*....|....*....|....*....|....*
gi 1958806453 288 VMMHHSNLIAGMTGQCERipGLGPKDTYIGYLPLA 322
Cdd:cd12117 154 VAVTHRGVVRLVKNTNYV--TLGPDDRVLQTSPLA 186
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
77-313 |
3.94e-10 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 62.52 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 77 DTLDKLFDHAVAKFGKKDSLGTREilseenemqpngkvfkklilGNYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIF 156
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRD--------------------QGLRW-TYREFNEEVDALAKGLLALGIEKGDRVGIW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 157 CETRAEWmiaaqtcfkynfpLVTLYAT--LGkeAVV-------------HGLNESEASYLITS--------VELLES--- 210
Cdd:PRK08315 75 APNVPEW-------------VLTQFATakIG--AILvtinpayrlseleYALNQSGCKALIAAdgfkdsdyVAMLYElap 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 211 --------KLKAALLDinCVKHIIYVDnktinrAEYPEGLeiHSMQSVEELGSKPENSSIPPSRPT--PSDmAIVM-YTS 279
Cdd:PRK08315 140 elatcepgQLQSARLP--ELRRVIFLG------DEKHPGM--LNFDELLALGRAVDDAELAARQATldPDD-PINIqYTS 208
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958806453 280 GSTGRPKGVMMHHSNLI--AGMTGQCERipgLGPKD 313
Cdd:PRK08315 209 GTTGFPKGATLTHRNILnnGYFIGEAMK---LTEED 241
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
126-327 |
4.42e-10 |
|
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: 62.11 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ELlesklkaalldincvkhiiyvdnktinraeypegleihsmqsveelgskpenssippsrptpSDMAIVMYTSGSTGRP 285
Cdd:cd05935 82 EL--------------------------------------------------------------DDLALIPYTSGTTGLP 99
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958806453 286 KGVMMHHSNLIAGMTGQCeRIPGLGPKDTYIGYLPLAHVLEL 327
Cdd:cd05935 100 KGCMHTHFSAAANALQSA-VWTGLTPSDVILACLPLFHVTGF 140
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
63-437 |
4.45e-10 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 62.95 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 63 THFDSLAvidipGADTLDKLFDHAVAKFGKKDSLGtreilsEENEmqpngkvfkkliLGNYKWINYLEVNCRVNNFGSGL 142
Cdd:PTZ00297 418 REYNPLA-----GVRSLGEMWERSVTRHSTFRCLG------QTSE------------SGESEWLTYGTVDARARELGSGL 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 143 TALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLyatLGKEAVVHGLneseasylitsveLLESKLKAALLDINCV 222
Cdd:PTZ00297 475 LALGVRPGDVIGVDCEASRNIVILEVACALYGFTTLPL---VGKGSTMRTL-------------IDEHKIKVVFADRNSV 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 223 KHIIYVDNKTINRAEYpegleIHS----------------MQSVEELGSKPENSSIPPSRPTPSDMAIVMY----TSGST 282
Cdd:PTZ00297 539 AAILTCRSRKLETVVY-----THSfydeddhavardlnitLIPYEFVEQKGRLCPVPLKEHVTTDTVFTYVvdntTSASG 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 283 GRPKGVMMHHSNLIAG-----MTGQcerIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIGYSSPLTLSDQSSKIkk 357
Cdd:PTZ00297 614 DGLAVVRVTHADVLRDistlvMTGV---LPSSFKKHLMVHFTPFAMLFNRVFVLGLFAHGSAVATVDAAHLQRAFVKF-- 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 358 gskgdctvlKPTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKIGYDYKLEQIK-KGYDAPLCNLILFKKVKALLGGNV 436
Cdd:PTZ00297 689 ---------QPTILVAAPSLFSTSRLQLSRANERYSAVYSWLFERAFQLRSRLINiHRRDSSLLRFIFFRATQELLGGCV 759
|
.
gi 1958806453 437 R 437
Cdd:PTZ00297 760 E 760
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
126-323 |
5.87e-10 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 62.20 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAqtcfkynFPLVTLYATLG-------KEAVVHGLNESEA 198
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAW-------LGLAKLGAVVAllntqqrGAVLAHSLNLVDA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 199 SYLITSVELLE--SKLKAALLdincVKHIIYVDNKTINRAeyPEGL-EIHSMQSveelGSKPENssiPPSRP--TPSDMA 273
Cdd:PRK08279 136 KHLIVGEELVEafEEARADLA----RPPRLWVAGGDTLDD--PEGYeDLAAAAA----GAPTTN---PASRSgvTAKDTA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958806453 274 IVMYTSGSTGRPKGVMMHHSNLI---AGMTGQCeripGLGPKDTYIGYLPLAH 323
Cdd:PRK08279 203 FYIYTSGTTGLPKAAVMSHMRWLkamGGFGGLL----RLTPDDVLYCCLPLYH 251
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
128-482 |
6.78e-10 |
|
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: 61.47 E-value: 6.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 128 YLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLItsvel 207
Cdd:cd17631 23 YAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 208 lesklkaalldincvkhiiyvdnktinraeypegleihsmqsveelgskpenssippsrptpSDMAIVMYTSGSTGRPKG 287
Cdd:cd17631 98 --------------------------------------------------------------DDLALLMYTSGTTGRPKG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 288 VMMHHSNL-----IAGMTGqceripGLGPKDTYIGYLPLAHVleltAEISCFTygcrigysSPLTLSDQSSKIKKGSKGD 362
Cdd:cd17631 116 AMLTHRNLlwnavNALAAL------DLGPDDVLLVVAPLFHI----GGLGVFT--------LPTLLRGGTVVILRKFDPE 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 363 cTVL------KPTLMAAVPEIMDRIyknvmskvqemnyIQKTLFkigydykleqikKGYDAPlcnlilfkkvkallggNV 436
Cdd:cd17631 178 -TVLdlierhRVTSFFLVPTMIQAL-------------LQHPRF------------ATTDLS----------------SL 215
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958806453 437 RMMLSGGAPLSPQTHRFMNVcFCCPIGQGYGLTESCGAGTVTEGKH 482
Cdd:cd17631 216 RAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSPGVTFLSPED 260
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
128-348 |
9.21e-10 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 61.22 E-value: 9.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 128 YLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFK----YNfPLVTLYAtlgKEAVVHGLNESEASYLIT 203
Cdd:PRK13295 58 YRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRigavLN-PLMPIFR---ERELSFMLKHAESKVLVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 204 -------SVELLESKLKAALLDIncvKHIIYVDNKTINraeypegleihsmqSVEELGSKPENSSIP-------PSRPTP 269
Cdd:PRK13295 134 pktfrgfDHAAMARRLRPELPAL---RHVVVVGGDGAD--------------SFEALLITPAWEQEPdapailaRLRPGP 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958806453 270 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHvleLTAeiscFTYGCRIgyssPLTL 348
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERL-GLGADDVILMASPMAH---QTG----FMYGLMM----PVML 263
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
124-315 |
9.85e-10 |
|
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: 61.44 E-value: 9.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 124 KWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLIT 203
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 204 ---------SVELLESKLKAALLDINCVKHIIYVDnKTINRAEYPEGLEIHSMQSVEElgSKPENSsipPSRPTPSDMAI 274
Cdd:cd17634 163 adggvragrSVPLKKNVDDALNPNVTSVEHVIVLK-RTGSDIDWQEGRDLWWRDLIAK--ASPEHQ---PEAMNAEDPLF 236
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958806453 275 VMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTY 315
Cdd:cd17634 237 ILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIY 277
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
268-307 |
1.29e-09 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 60.63 E-value: 1.29e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1958806453 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIP 307
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALG 143
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-314 |
1.46e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.51 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ELLEsklkaaLLDINCVKHIIYVDNKTINRAEYPEGleihsmqsveelgskpenssIPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:PRK12316 617 HLGR------KLPLAAGVQVLDLDRPAAWLEGYSEE--------------------NPGTELNPENLAYVIYTSGSTGKP 670
|
170 180
....*....|....*....|....*....
gi 1958806453 286 KGVMMHHSNLIAGMTGQCERIpGLGPKDT 314
Cdd:PRK12316 671 KGAGNRHRALSNRLCWMQQAY-GLGVGDT 698
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
128-323 |
1.79e-09 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 60.53 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 128 YLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLI----- 202
Cdd:PRK06087 52 YSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFaptlf 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 203 --TSVELLESKLKAallDINCVKHIIYVDNktinraEYPEgleiHSMQSVEELGSKPENSSIPPsrPTPSD-MAIVMYTS 279
Cdd:PRK06087 132 kqTRPVDLILPLQN---QLPQLQQIVGVDK------LAPA----TSSLSLSQIIADYEPLTTAI--TTHGDeLAAVLFTS 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1958806453 280 GSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAH 323
Cdd:PRK06087 197 GTEGLPKGVMLTHNNILASERAYCARL-NLTWQDVFMMPAPLGH 239
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
127-324 |
1.90e-09 |
|
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: 60.34 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 127 NYLEVNCRVNNFGSGLTALGLKPKNTIAIFCetraeWmiaaqTCFKYnfpLVTLYATLGKEAVVHGLN------------ 194
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLA-----W-----NTHRH---LELYYAVPGMGAVLHTINprlfpeqiayii 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 195 -ESEASYLITSVELLesKLKAALLD-INCVKHIIYVDNKTINRAEYPEGLE-----IHSMQSVEELGSKPENssippsrp 267
Cdd:cd12119 94 nHAEDRVVFVDRDFL--PLLEAIAPrLPTVEHVVVMTDDAAMPEPAGVGVLayeelLAAESPEYDWPDFDEN-------- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958806453 268 tpsDMAIVMYTSGSTGRPKGVMM-HHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHV 324
Cdd:cd12119 164 ---TAAAICYTSGTTGNPKGVVYsHRSLVLHAMAALLTDGLGLSESDVVLPVVPMFHV 218
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
121-322 |
2.51e-09 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 59.95 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASY 200
Cdd:TIGR02188 84 GEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 201 LITSVELLE----SKLKA----ALLDINC-VKHIIYVDNKTINRAEYPEGLEI--HSMQsveelgsKPENSSIPPSRPTP 269
Cdd:TIGR02188 164 VITADEGLRggkvIPLKAivdeALEKCPVsVEHVLVVRRTGNPVVPWVEGRDVwwHDLM-------AKASAYCEPEPMDS 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958806453 270 SDMAIVMYTSGSTGRPKGVMmhHS----NLIAGMTgqCERIPGLGPKD--------------TYIGYLPLA 322
Cdd:TIGR02188 237 EDPLFILYTSGSTGKPKGVL--HTtggyLLYAAMT--MKYVFDIKDGDifwctadvgwitghSYIVYGPLA 303
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
134-321 |
2.58e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 59.76 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 134 RVNNFGSGLTALGLKPKNTIAI-------FCETRAEWMIAAQTCFKYnfpLVTLYATLgKEAVVHGLNESEASYLITSVE 206
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLilpnrftYIELSFAVAYAGGRLGLV---FVPLNPTL-KESVLRYLVADAGGRIVLADA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 207 LLESKLKAALldincvkhIIYVDNKTINRAEypegleihsmqsveelGSKPENSSIPPSRPTPSDMAIVMYTSGSTGRPK 286
Cdd:cd05922 78 GAADRLRDAL--------PASPDPGTVLDAD----------------GIRAARASAPAHEVSHEDLALLLYTSGSTGSPK 133
|
170 180 190
....*....|....*....|....*....|....*
gi 1958806453 287 GVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPL 321
Cdd:cd05922 134 LVRLSHQNLLANARSIAEYL-GITADDRALTVLPL 167
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
263-313 |
3.08e-09 |
|
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: 59.60 E-value: 3.08e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1958806453 263 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKD 313
Cdd:cd17646 131 PLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYP-LGPGD 180
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-322 |
4.09e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 59.79 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ELLesklkaALLDIncvkhiiyvdnktinraeyPEGLEIHSMQSVEEL--GSKPENssiPPSRPTPSDMAIVMYTSGSTG 283
Cdd:PRK12467 618 HLL------AQLPV-------------------PAGLRSLCLDEPADLlcGYSGHN---PEVALDPDNLAYVIYTSGSTG 669
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958806453 284 RPKGVMMHHSNLiAGMTGQCERIPGLGPKDTYIGYLPLA 322
Cdd:PRK12467 670 QPKGVAISHGAL-ANYVCVIAERLQLAADDSMLMVSTFA 707
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
268-313 |
5.09e-09 |
|
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: 58.86 E-value: 5.09e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1958806453 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKD 313
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA-TQRWFGFNEDD 135
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
183-328 |
5.20e-09 |
|
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: 58.88 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 183 TLGKEAVVHGLNESEASYLITSVELLEsklKAALLDINCV---KHIIYVDN--KTINRAE----YPEGLeIHSMQSVEEL 253
Cdd:cd05909 64 TAGLRELRACIKLAGIKTVLTSKQFIE---KLKLHHLFDVeydARIVYLEDlrAKISKADkckaFLAGK-FPPKWLLRIF 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806453 254 GSKPENssippsrptPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYLPLAHVLELT 328
Cdd:cd05909 140 GVAPVQ---------PDDPAVILFTSGSEGLPKGVVLSHKNLLANVE-QITAIFDPNPEDVVFGALPFFHSFGLT 204
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
255-482 |
6.65e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 58.62 E-value: 6.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 255 SKPENSSIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPG--LGP-KDTYIGYLPLAHvleltaeI 331
Cdd:PRK05677 192 AKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANML-QCRALMGsnLNEgCEILIAPLPLYH-------I 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 332 SCFTYGCRIgysspLTLSdqsskikkgskGDCTVLKPTlmaavPEIMDRIYKnVMSKVQEMNYIQ-KTLFkigydykleq 410
Cdd:PRK05677 264 YAFTFHCMA-----MMLI-----------GNHNILISN-----PRDLPAMVK-ELGKWKFSGFVGlNTLF---------- 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958806453 411 ikkgydAPLCNLILFKKV--KALlggnvRMMLSGGAPLSPQTHRFMNVCFCCPIGQGYGLTESCGAGTVTEGKH 482
Cdd:PRK05677 312 ------VALCNNEAFRKLdfSAL-----KLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQA 374
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
128-472 |
8.43e-09 |
|
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: 57.74 E-value: 8.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 128 YLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKynfplvtlyatLGKEAVvhglneseasylitsveL 207
Cdd:cd05912 4 FAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWL-----------LGAEAV-----------------L 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 208 LESKLKAALLdincvkhiiyvdnktinraeypegleihsMQSVEELGSKPEnssippsrptpsDMAIVMYTSGSTGRPKG 287
Cdd:cd05912 56 LNTRLTPNEL-----------------------------AFQLKDSDVKLD------------DIATIMYTSGTTGKPKG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 288 VMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVLELTAEISCFTYGCRIgyssplTLSDQ--SSKIKKGSKGDctv 365
Cdd:cd05912 95 VQQTFGNHWWSAIGSALNL-GLTEDDNWLCALPLFHISGLSILMRSVIYGMTV------YLVDKfdAEQVLHLINSG--- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 366 lKPTLMAAVPEIMDRIyknvmskvqemnyiqktlfkigydykLEQIKKGYDAplcnlilfkkvkallggNVRMMLSGGAP 445
Cdd:cd05912 165 -KVTIISVVPTMLQRL--------------------------LEILGEGYPN-----------------NLRCILLGGGP 200
|
330 340
....*....|....*....|....*....
gi 1958806453 446 LSPQThrfMNVC--FCCPIGQGYGLTESC 472
Cdd:cd05912 201 APKPL---LEQCkeKGIPVYQSYGMTETC 226
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
126-288 |
9.74e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 57.99 E-value: 9.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ELLESKLKAAlldincvkhiiyvdnktinrAEYPEGLEIHSM--------QSVEELGSkpENSSIPPSRPTP-SDMAivm 276
Cdd:PRK08276 92 ALADTAAELA--------------------AELPAGVPLLLVvagpvpgfRSYEEALA--AQPDTPIADETAgADML--- 146
|
170
....*....|..
gi 1958806453 277 YTSGSTGRPKGV 288
Cdd:PRK08276 147 YSSGTTGRPKGI 158
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
121-293 |
1.08e-08 |
|
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: 57.96 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASY 200
Cdd:cd05966 80 DQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 201 LITSVEL--------LESKLKAALLDINCVKHIIYVDNkTINRAEYPEGLEI--HsmqsvEELGSKPENssIPPSRPTPS 270
Cdd:cd05966 160 VITADGGyrggkvipLKEIVDEALEKCPSVEKVLVVKR-TGGEVPMTEGRDLwwH-----DLMAKQSPE--CEPEWMDSE 231
|
170 180
....*....|....*....|...
gi 1958806453 271 DMAIVMYTSGSTGRPKGVMmhHS 293
Cdd:cd05966 232 DPLFILYTSGSTGKPKGVV--HT 252
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
255-477 |
1.17e-08 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 57.68 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 255 SKPENSSIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCE-RIPGLG--PKDTYIGYLPLAHVLELTAEI 331
Cdd:PLN02246 164 TQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDgENPNLYfhSDDVILCVLPMFHIYSLNSVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 332 SCftyGCRIGysspltlsdqsSKIKKGSKGDCTVL-------KPTLMAAVPEIMDRIYKNVMSKvqemnyiqktlfkigy 404
Cdd:PLN02246 244 LC---GLRVG-----------AAILIMPKFEIGALleliqrhKVTIAPFVPPIVLAIAKSPVVE---------------- 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958806453 405 DYKLEQIkkgydaplcnlilfkkvkallggnvRMMLSGGAPLSPQTH-----RFMNVCfccpIGQGYGLTEscgAGTV 477
Cdd:PLN02246 294 KYDLSSI-------------------------RMVLSGAAPLGKELEdafraKLPNAV----LGQGYGMTE---AGPV 339
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
269-346 |
2.10e-08 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 57.03 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYLPLAHVLELTaeISCFT---YGCRIG-YSS 344
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVE-QIKTIADFTPNDRFMSALPLFHSFGLT--VGLFTpllTGAEVFlYPS 440
|
..
gi 1958806453 345 PL 346
Cdd:PRK08043 441 PL 442
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
121-292 |
2.55e-08 |
|
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: 56.73 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 121 GNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASY 200
Cdd:cd05968 87 GTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 201 LITS---------VELLESKLKAALLDINcVKHIIYVdnktiNRAEYPEGleihsMQSVEELGSKPENSSIPP--SRPTP 269
Cdd:cd05968 167 LITAdgftrrgreVNLKEEADKACAQCPT-VEKVVVV-----RHLGNDFT-----PAKGRDLSYDEEKETAGDgaERTES 235
|
170 180
....*....|....*....|...
gi 1958806453 270 SDMAIVMYTSGSTGRPKGVMMHH 292
Cdd:cd05968 236 EDPLMIIYTSGTTGKPKGTVHVH 258
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
269-472 |
2.57e-08 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that 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: 341234 [Multi-domain] Cd Length: 499 Bit Score: 56.73 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTAeiscftygcriGYSSPLTl 348
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTE-WKTKDRILSWMPLTHDMGLIA-----------FHLAPLI- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 349 sdqsskikkgsKGDCTVLKPTLMAAVPEImdriykNVMSKVQEMNYIQKTLFKIGYDYKLEQIK--KGYDAPLcnlilfk 426
Cdd:cd05908 172 -----------AGMNQYLMPTRLFIRRPI------LWLKKASEHKATIVSSPNFGYKYFLKTLKpeKANDWDL------- 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958806453 427 kvkallgGNVRMMLSGGAPLSPQ-THRFMNVCfccpigQGYGLTESC 472
Cdd:cd05908 228 -------SSIRMILNGAEPIDYElCHEFLDHM------SKYGLKRNA 261
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
268-313 |
2.78e-08 |
|
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: 56.49 E-value: 2.78e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1958806453 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKD 313
Cdd:cd17652 91 TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAF-DVGPGS 135
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
271-323 |
2.96e-08 |
|
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: 56.15 E-value: 2.96e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1958806453 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAH 323
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRF-GLGEDDVYLTVLPLFH 133
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
136-315 |
3.70e-08 |
|
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: 55.97 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 136 NNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLEsklkaa 215
Cdd:cd05969 11 ARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEELYE------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 216 lldincvkhiiyvdnktinraeypegleihsmqsveelgskpenssippsRPTPSDMAIVMYTSGSTGRPKGVMMHHSNL 295
Cdd:cd05969 85 --------------------------------------------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAM 114
|
170 180
....*....|....*....|.
gi 1958806453 296 IA-GMTGQceRIPGLGPKDTY 315
Cdd:cd05969 115 IFyYFTGK--YVLDLHPDDIY 133
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
263-313 |
4.41e-08 |
|
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: 55.81 E-value: 4.41e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1958806453 263 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKD 313
Cdd:cd17651 129 PDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASS-LGPGA 178
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
126-323 |
5.08e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 55.85 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRA---EWMIAAQTCFKYnFPLVTLYATLGKEAVVhgLNESEASYLI 202
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLrylEVCWAAERSGLY-YTCVNSHLTPAEAAYI--VDDSGARALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 203 TSVELLESkLKAALLDINCVKHIIYVDNKtinrAEYP--EGLEihsmQSVEELGSKPEnssipPSRPTPSDMaivMYTSG 280
Cdd:PRK13391 102 TSAAKLDV-ARALLKQCPGVRHRLVLDGD----GELEgfVGYA----EAVAGLPATPI-----ADESLGTDM---LYSSG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1958806453 281 STGRPKGVM--MHHSNLIA--GMTGQCERIPGLGPKDTYIGYLPLAH 323
Cdd:PRK13391 165 TTGRPKGIKrpLPEQPPDTplPLTAFLQRLWGFRSDMVYLSPAPLYH 211
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
142-324 |
1.27e-07 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 54.58 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 142 LTALGLKPKNTIAifcetraewmiaaqtcfkYNFPLV--TLYATLGKEA---------------VVHGLNESEASYLITS 204
Cdd:PRK07529 75 LHSLGVGPGDVVA------------------FLLPNLpeTHFALWGGEAagianpinpllepeqIAELLRAAGAKVLVTL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 205 VELLES----KLKAALLDINCVKHIIYVDnktINRAEYPEGLEIHSMQSV----------EELGSKPENSSIPPSRPTPS 270
Cdd:PRK07529 137 GPFPGTdiwqKVAEVLAALPELRTVVEVD---LARYLPGPKRLAVPLIRRkaharildfdAELARQPGDRLFSGRPIGPD 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958806453 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHV 324
Cdd:PRK07529 214 DVAAYFHTGGTTGMPKLAQHTHGNEVA-NAWLGALLLGLGPGDTVFCGLPLFHV 266
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
135-373 |
1.65e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 54.01 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 135 VNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKA 214
Cdd:PRK12583 55 VDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAFKTSDYHA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 215 ALLDIncVKHIIYVDNKTINRAEYPE--------GLEIHSMQSVEELGSKPENSSIP-----PSRPTPSDMAIVMYTSGS 281
Cdd:PRK12583 135 MLQEL--LPGLAEGQPGALACERLPElrgvvslaPAPPPGFLAWHELQARGETVSREalaerQASLDRDDPINIQYTSGT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 282 TGRPKGVMMHHSNLI--AGMTGqcERIpGLGPKDTYIGYLPLAHVLELT-AEISCFTYGCRIGYssPLTLSDQSSKIKKG 358
Cdd:PRK12583 213 TGFPKGATLSHHNILnnGYFVA--ESL-GLTEHDRLCVPVPLYHCFGMVlANLGCMTVGACLVY--PNEAFDPLATLQAV 287
|
250
....*....|....*..
gi 1958806453 359 SKGDCTVLK--PTLMAA 373
Cdd:PRK12583 288 EEERCTALYgvPTMFIA 304
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
142-324 |
1.82e-07 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 53.73 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 142 LTALGLKPKNTIAIFCETRAEWMIaaqtcfkynfplvtLY-ATLGKEAVVHGLN----ESEASYLITSVEllesklkAAL 216
Cdd:PRK07514 45 LVALGVKPGDRVAVQVEKSPEALA--------------LYlATLRAGAVFLPLNtaytLAELDYFIGDAE-------PAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 217 ldincvkhiIYVDNKtiNRAEYPEGLEIHSMQSVEELGSKPENSSI------PPSRPT----PSDMAIVMYTSGSTGRPK 286
Cdd:PRK07514 104 ---------VVCDPA--NFAWLSKIAAAAGAPHVETLDADGTGSLLeaaaaaPDDFETvprgADDLAAILYTSGTTGRSK 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958806453 287 GVMMHHSNLIA-GMTgqCERIPGLGPKDTYIGYLPLAHV 324
Cdd:PRK07514 173 GAMLSHGNLLSnALT--LVDYWRFTPDDVLIHALPIFHT 209
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
271-324 |
2.33e-07 |
|
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: 53.10 E-value: 2.33e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958806453 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHV 324
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLG-FGGGDSWLLSLPLYHV 53
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
247-297 |
2.98e-07 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 53.36 E-value: 2.98e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1958806453 247 MQSVEELGSKPENSSIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIA 297
Cdd:PRK09274 151 GTTLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEA 201
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
122-296 |
3.00e-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: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 122 NYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYL 201
Cdd:cd17656 11 NQKL-TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 202 ITSVELlESKLKaalldincvkhiiyvDNKTINRAEYPegleIHSMQSVEELGSKPENSsippsrptpsDMAIVMYTSGS 281
Cdd:cd17656 90 LTQRHL-KSKLS---------------FNKSTILLEDP----SISQEDTSNIDYINNSD----------DLLYIIYTSGT 139
|
170
....*....|....*
gi 1958806453 282 TGRPKGVMMHHSNLI 296
Cdd:cd17656 140 TGKPKGVQLEHKNMV 154
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
259-346 |
3.78e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 53.02 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 259 NSSIPPSRPTPSdMAIVMYTSGSTGRPKGVMMHHSNLIA----GMTGQCERIPGLGPKD-TYIGYLPLAH----VLELTA 329
Cdd:PRK05850 150 RGSDARPRDLPS-TAYLQYTSGSTRTPAGVMVSHRNVIAnfeqLMSDYFGDTGGVPPPDtTVVSWLPFYHdmglVLGVCA 228
|
90
....*....|....*..
gi 1958806453 330 EISCftyGCRIGYSSPL 346
Cdd:PRK05850 229 PILG---GCPAVLTSPV 242
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-295 |
4.04e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.42 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITsv 205
Cdd:PRK12316 3083 LSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS-- 3160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ellESKLKAALLDincvkhiiYVDNKTINRAeyPEGLEIHSmqsveelgskpenssiPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:PRK12316 3161 ---QSHLRLPLAQ--------GVQVLDLDRG--DENYAEAN----------------PAIRTMPENLAYVIYTSGSTGKP 3211
|
170
....*....|
gi 1958806453 286 KGVMMHHSNL 295
Cdd:PRK12316 3212 KGVGIRHSAL 3221
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
249-323 |
4.12e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 53.25 E-value: 4.12e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958806453 249 SVEELGSKPENSSIPPSRPtPSDMAIVMYTSGSTGRPKGVMMHHSNLIAG--MTGQCERIPgLGPKDTYIGYLPLAH 323
Cdd:PRK05691 146 CVDTLDPALAEAWQEPALQ-PDDIAFLQYTSGSTALPKGVQVSHGNLVANeqLIRHGFGID-LNPDDVIVSWLPLYH 220
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
263-329 |
4.41e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 53.05 E-value: 4.41e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958806453 263 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHVLELTA 329
Cdd:PRK06814 786 YFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARID-FSPEDKVFNALPVFHSFGLTG 851
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
72-337 |
4.47e-07 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 52.76 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 72 DIPGADTLDKLFDHAVAKFGKKDSLgtreilseenemqpngkVFKKLIlGNYKWINYLEVNCRVNNFGSGLTALGLKPKN 151
Cdd:PRK08008 2 DIVGGQHLRQMWDDLADVYGHKTAL-----------------IFESSG-GVVRRYSYLELNEEINRTANLFYSLGIRKGD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 152 TIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVELLESKLKAALLDINCVKHIIyvdnk 231
Cdd:PRK08008 64 KVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHIC----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 232 tINRAEYPEGLEIHSMQSVEELGSKPENSSIPPSrptPSDMAIVMYTSGSTGRPKGVMMHHSNLI-AGMTG--QCeripG 308
Cdd:PRK08008 139 -LTRVALPADDGVSSFTQLKAQQPATLCYAPPLS---TDDTAEILFTSGTTSRPKGVVITHYNLRfAGYYSawQC----A 210
|
250 260 270
....*....|....*....|....*....|
gi 1958806453 309 LGPKDTYIGYLPLAHV-LELTAEISCFTYG 337
Cdd:PRK08008 211 LRDDDVYLTVMPAFHIdCQCTAAMAAFSAG 240
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
126-297 |
5.54e-07 |
|
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: 52.32 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEwMIAAqtcfkynfplvtLYATLGkeavvhglneSEASYLItsv 205
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPD-LVVA------------LLAVLK----------AGAAYVP--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ellesklkaalLDincvkhiiyvdnktinrAEYPEgleihsmqsvEELGSKPENSSIPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:cd12115 79 -----------LD-----------------PAYPP----------ERLRFILEDAQARLVLTDPDDLAYVIYTSGSTGRP 120
|
170
....*....|..
gi 1958806453 286 KGVMMHHSNLIA 297
Cdd:cd12115 121 KGVAIEHRNAAA 132
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
178-329 |
6.40e-07 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 52.62 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 178 VTLYATLGKEAVVHGLNESEASYLITSVELLEsKLKAALLDincvkhiiyvdnktinrAEYPEGLEIHSMqsvEELGSKP 257
Cdd:PRK08633 693 VNLNYTASEAALKSAIEQAQIKTVITSRKFLE-KLKNKGFD-----------------LELPENVKVIYL---EDLKAKI 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 258 ENS---------SIPPSR---------PTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERIPGLGPKDTYIGYL 319
Cdd:PRK08633 752 SKVdkltallaaRLLPARllkrlygptFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIE-QISDVFNLRNDDVILSSL 830
|
170
....*....|
gi 1958806453 320 PLAHVLELTA 329
Cdd:PRK08633 831 PFFHSFGLTV 840
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
263-292 |
6.74e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 52.74 E-value: 6.74e-07
10 20 30
....*....|....*....|....*....|
gi 1958806453 263 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHH 292
Cdd:PRK10252 591 PLQLSQPHHTAYIIFTSGSTGRPKGVMVGQ 620
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
271-477 |
9.86e-07 |
|
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: 51.52 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAgmtgQCERIP---GLGPKDTYIGYLPLAHVLELTAEISCFTYgCRigySSPLT 347
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAA----NVRALVdawRWTEDDVLLHVLPLHHVHGLVNALLCPLF-AG---ASVEF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 348 LSDQSSKIKKGSKGDCTVlkpTLMAAVPEIMDRIYKNVMSKVQEMNYIQKTLFKigydykleqikkgydaplcnlilfkk 427
Cdd:cd05941 162 LPKFDPKEVAISRLMPSI---TVFMGVPTIYTRLLQYYEAHFTDPQFARAAAAE-------------------------- 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806453 428 vkallggNVRMMLSGGAPLSPQTHRfmnvCFCCPIGQG----YGLTE-----SCG------AGTV 477
Cdd:cd05941 213 -------RLRLMVSGSAALPVPTLE----EWEAITGHTllerYGMTEigmalSNPldgerrPGTV 266
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-471 |
9.91e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 51.40 E-value: 9.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 119 ILGNYKWINYLEVNCRVNNFGSGLT-ALGLKPKNTIAIFcetraewmiaAQTCFKYnfpLVTLYATLGKEAVVHGLN--- 194
Cdd:PRK06839 21 IITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAIL----------SQNSLEY---IVLLFAIAKVECIAVPLNirl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 195 -ESEASYLI----TSVELLESKLKAALLDIncvKHIIYVDNKTinRAEYPEGLEIHSMQSVEElgskpenssippsrPTP 269
Cdd:PRK06839 88 tENELIFQLkdsgTTVLFVEKTFQNMALSM---QKVSYVQRVI--SITSLKEIEDRKIDNFVE--------------KNE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 270 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHVleltAEISCFTY-----GCRIGYSS 344
Cdd:PRK06839 149 SASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAI-DLTMHDRSIVLLPLFHI----GGIGLFAFptlfaGGVIIVPR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 345 PLTLSDQSSKIKKGskgdctvlKPTLMAAVPEIMDRiyknvmskvqemnyiqktlfkigydykleqikkgydapLCNLIL 424
Cdd:PRK06839 224 KFEPTKALSMIEKH--------KVTVVMGVPTIHQA--------------------------------------LINCSK 257
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958806453 425 FKKVKAllgGNVRMMLSGGAPLS-PQTHRFMNVCFccPIGQGYGLTES 471
Cdd:PRK06839 258 FETTNL---QSVRWFYNGGAPCPeELMREFIDRGF--LFGQGFGMTET 300
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
142-323 |
1.08e-06 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 51.54 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 142 LTALGLKPKNTIAIFCETRAEWMIAAQTCfKYN----FPLVTLYATLGKEAVVHGLN----ESEASYLITSVELLESKLK 213
Cdd:PRK09192 66 LLALGLKPGDRVALIAETDGDFVEAFFAC-QYAglvpVPLPLPMGFGGRESYIAQLRgmlaSAQPAAIITPDELLPWVNE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 214 AAlldincvkhiiyvdnktiNRAEYPEGLeihsmqSVEELGSKPEnSSIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHS 293
Cdd:PRK09192 145 AT------------------HGNPLLHVL------SHAWFKALPE-ADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHR 199
|
170 180 190
....*....|....*....|....*....|
gi 1958806453 294 NLIAGMTGQCERIPGLGPKDTYIGYLPLAH 323
Cdd:PRK09192 200 ALMANLRAISHDGLKVRPGDRCVSWLPFYH 229
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
257-297 |
1.28e-06 |
|
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: 51.09 E-value: 1.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958806453 257 PENSSIPPSR---------PT-----PSDMAIVMYTSGSTGRPKGVMMHHSNLIA 297
Cdd:cd05945 70 PLDASSPAERireildaakPAlliadGDDNAYIIFTSGSTGRPKGVQISHDNLVS 124
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
260-333 |
1.28e-06 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 51.36 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 260 SSIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGP---------KDTYIGYLPLAHVLELTAE 330
Cdd:PRK12492 197 LSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPdgqplmkegQEVMIAPLPLYHIYAFTAN 276
|
...
gi 1958806453 331 ISC 333
Cdd:PRK12492 277 CMC 279
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
124-335 |
1.50e-06 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 51.13 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 124 KWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEW------MIAAQTCFKYNFPlVTLYATLGKEAvvhglnESE 197
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYgivalgIMAAGGVFSGANP-TALESEIKKQA------EAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 198 ASYLITSVELLESKLKAALLDIncvkhIIYVDNKTINRAEYPEGLEihsmqSVEELGSKPENSSIppsrpTPSDMAIVMY 277
Cdd:PLN02330 127 GAKLIVTNDTNYGKVKGLGLPV-----IVLGEEKIEGAVNWKELLE-----AADRAGDTSDNEEI-----LQTDLCALPF 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806453 278 TSGSTGRPKGVMMHHSNLIAGMtgqCERIPGLGP----KDTYIGYLPLAHVLELTAeISCFT 335
Cdd:PLN02330 192 SSGTTGISKGVMLTHRNLVANL---CSSLFSVGPemigQVVTLGLIPFFHIYGITG-ICCAT 249
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
263-323 |
1.94e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 50.76 E-value: 1.94e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958806453 263 PPSRP---TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAH 323
Cdd:PRK07768 142 DPIDPvetGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFH 205
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
126-300 |
2.25e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 50.52 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCfkynfplvtlyATLG-KEAVVHG----------LN 194
Cdd:PRK00174 99 ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLAC-----------ARIGaVHSVVFGgfsaealadrII 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 195 ESEASYLITSVELLE----SKLKA----ALLDINCVKHIIYVdNKTINRAEYPEGLEI--HSMQsveelgsKPENSSIPP 264
Cdd:PRK00174 168 DAGAKLVITADEGVRggkpIPLKAnvdeALANCPSVEKVIVV-RRTGGDVDWVEGRDLwwHELV-------AGASDECEP 239
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1958806453 265 SRPTPSDMAIVMYTSGSTGRPKGVMmhHS----NLIAGMT 300
Cdd:PRK00174 240 EPMDAEDPLFILYTSGSTGKPKGVL--HTtggyLVYAAMT 277
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
269-296 |
2.52e-06 |
|
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: 50.25 E-value: 2.52e-06
10 20
....*....|....*....|....*...
gi 1958806453 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLI 296
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLV 130
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
269-324 |
2.58e-06 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 50.18 E-value: 2.58e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806453 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCErIPGLGPKDTYIGYLPLAHV 324
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIA-IVGYGEDDVYLHTAPLCHI 225
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-295 |
2.87e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 50.54 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:PRK12467 3121 LSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQA 3200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ELLESklkaalLDINCVKHIIYVDNktinraeypegleihsmqsvEELGSKPENSsiPPSRPTPSDMAIVMYTSGSTGRP 285
Cdd:PRK12467 3201 HLLEQ------LPAPAGDTALTLDR--------------------LDLNGYSENN--PSTRVMGENLAYVIYTSGSTGKP 3252
|
170
....*....|
gi 1958806453 286 KGVMMHHSNL 295
Cdd:PRK12467 3253 KGVGVRHGAL 3262
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
267-295 |
2.92e-06 |
|
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: 50.00 E-value: 2.92e-06
10 20
....*....|....*....|....*....
gi 1958806453 267 PTPSDMAIVMYTSGSTGRPKGVMMHHSNL 295
Cdd:cd17653 102 DSPDDLAYIIFTSGSTGIPKGVMVPHRGV 130
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
126-296 |
3.82e-06 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 49.74 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITsv 205
Cdd:cd17644 26 LTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLLT-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ellesklkaalldincvkhiiyvdnktinraeypegleihsmqsveelgsKPENssippsrptpsdMAIVMYTSGSTGRP 285
Cdd:cd17644 104 --------------------------------------------------QPEN------------LAYVIYTSGSTGKP 121
|
170
....*....|.
gi 1958806453 286 KGVMMHHSNLI 296
Cdd:cd17644 122 KGVMIEHQSLV 132
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
130-320 |
4.23e-06 |
|
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: 49.35 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 130 EVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSVelle 209
Cdd:cd05971 11 ELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 210 sklkaalldincvkhiiyvdnktinraeypegleihsmqsveelgskpenssippsrptPSDMAIVMYTSGSTGRPKGVM 289
Cdd:cd05971 87 -----------------------------------------------------------SDDPALIIYTSGTTGPPKGAL 107
|
170 180 190
....*....|....*....|....*....|.
gi 1958806453 290 MHHSNLIaGMTGQCERIPGLGPKDTYIGYLP 320
Cdd:cd05971 108 HAHRVLL-GHLPGVQFPFNLFPRDGDLYWTP 137
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
186-313 |
5.84e-06 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 48.94 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 186 KEAVVHG--------LNESE---ASYLITSVELLESKLKAALLDincvkhiiyvdnKTInraeypegLEIHSMQSVEELG 254
Cdd:cd17648 3 RVAVVYGdkrltyreLNERAnrlAHYLLSVAEIRPDDLVGLVLD------------KSE--------LMIIAILAVWKAG 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806453 255 SK--PENSSIPPSR--------------PTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKD 313
Cdd:cd17648 63 AAyvPIDPSYPDERiqfiledtgarvviTNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGD 137
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
118-300 |
5.89e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 49.21 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 118 LILGNYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAE-W--MIAAQTC-FKYnfplVTLYATLGKEAVVHGL 193
Cdd:PRK06188 31 LVLGDTRL-TYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEvLmaIGAAQLAgLRR----TALHPLGSLDDHAYVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 194 NESEASYLITSVELLESKLKAALLDINCVKHIIyvdnkTINRAEYPEGLeihsMQSVEELGSKPenssiPPSRPTPSDMA 273
Cdd:PRK06188 106 EDAGISTLIVDPAPFVERALALLARVPSLKHVL-----TLGPVPDGVDL----LAAAAKFGPAP-----LVAAALPPDIA 171
|
170 180
....*....|....*....|....*..
gi 1958806453 274 IVMYTSGSTGRPKGVMMHHSNlIAGMT 300
Cdd:PRK06188 172 GLAYTGGTTGKPKGVMGTHRS-IATMA 197
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
124-329 |
7.10e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 48.88 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 124 KWINYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASyLIT 203
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAK-VIL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 204 SVELLESKLkAALLDINCVKHII-----------------YVDNKTINR-AEYPEGLEIHSMQSVEelgsKPENSSIPPS 265
Cdd:PRK06710 127 CLDLVFPRV-TNVQSATKIEHVIvtriadflpfpknllypFVQKKQSNLvVKVSESETIHLWNSVE----KEVNTGVEVP 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806453 266 RPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAG-MTGQCERIPGLGPKDTYIGYLPLAHVLELTA 329
Cdd:PRK06710 202 CDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNtLMGVQWLYNCKEGEEVVLGVLPFFHVYGMTA 266
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
250-324 |
7.18e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 49.01 E-value: 7.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958806453 250 VEELGSKPENSSIPPSRPtpsdmAIVMYTSGSTGRPKGVMMHHSNLiAGMTGQCERIPGLGPKDTyIGYL--PLAHV 324
Cdd:PRK07786 159 LAEAGPAHAPVDIPNDSP-----ALIMYTSGTTGRPKGAVLTHANL-TGQAMTCLRTNGADINSD-VGFVgvPLFHI 228
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
269-296 |
7.49e-06 |
|
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: 48.62 E-value: 7.49e-06
10 20
....*....|....*....|....*...
gi 1958806453 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLI 296
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVA 119
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
271-337 |
1.01e-05 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 48.03 E-value: 1.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958806453 271 DMAIVMYTSGSTGRPKGVMMHHSNLI-AGMtgQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYG 337
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIaANL--QLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAG 66
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
271-476 |
1.07e-05 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 48.30 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTG----QCERIPGLGPKDTYIGYLPLAHVLELtaeiSCFTYGcrigysspl 346
Cdd:PLN02574 199 DVAAIMYSSGTTGASKGVVLTHRNLIAMVELfvrfEASQYEYPGSDNVYLAALPMFHIYGL----SLFVVG--------- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 347 TLSDQSSKIkkgskgdctvlkptlmaavpeIMDRIYKNVMSKVQEMNYIqkTLFKIgydykleqikkgydAPLCNLILFK 426
Cdd:PLN02574 266 LLSLGSTIV---------------------VMRRFDASDMVKVIDRFKV--THFPV--------------VPPILMALTK 308
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958806453 427 KVKALLG---GNVRMMLSGGAPLSPQT-HRFMNVCFCCPIGQGYGLTESCGAGT 476
Cdd:PLN02574 309 KAKGVCGevlKSLKQVSCGAAPLSGKFiQDFVQTLPHVDFIQGYGMTESTAVGT 362
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
242-295 |
1.20e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 47.96 E-value: 1.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958806453 242 LEIHSMQSVEELGSKPEnsSIPPSRPT-PSDMAIVMYTSGSTGRPKGVMMHHSNL 295
Cdd:PRK06145 122 IDAAAQADSRRLAQGGL--EIPPQAAVaPTDLVRLMYTSGTTDRPKGVMHSYGNL 174
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
268-322 |
1.46e-05 |
|
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: 47.75 E-value: 1.46e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958806453 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgmtgQCE---RIPGLGPKDTYIGYLPLA 322
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPLAA----HCQataERYGLTPGDRELQFASFN 145
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
264-341 |
1.97e-05 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 47.32 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 264 PSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCE-------RIPGLGPKDTYIGYLPLAHVLELTAeisCFTY 336
Cdd:PRK07059 198 PVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVL-QMEawlqpafEKKPRPDQLNFVCALPLYHIFALTV---CGLL 273
|
....*
gi 1958806453 337 GCRIG 341
Cdd:PRK07059 274 GMRTG 278
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
260-324 |
1.97e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 47.29 E-value: 1.97e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806453 260 SSIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAHV 324
Cdd:PRK07787 118 SWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAW-QWTADDVLVHGLPLFHV 181
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
271-337 |
2.16e-05 |
|
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: 47.09 E-value: 2.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958806453 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAhvleltaeiscFTYG 337
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLA-----------FTFG 153
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
252-323 |
3.75e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 46.60 E-value: 3.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958806453 252 ELGSKPENSSIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNL-IAGMTgQCERIpGLGPKDTYIGYLPLAH 323
Cdd:PRK07867 134 DELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVaSAGVM-LAQRF-GLGPDDVCYVSMPLFH 204
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
269-374 |
4.11e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 46.12 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLI--AGMTGqcERIpGLGPKDTYIGYLPLAHVLELT-AEISCFTYGCRIGYSSP 345
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIG--ERL-GLTEQDRLCIPVPLFHCFGSVlGVLACLTHGATMVFPSP 77
|
90 100 110
....*....|....*....|....*....|.
gi 1958806453 346 LTlsDQSSKIKKGSKGDCTVLK--PTLMAAV 374
Cdd:cd05917 78 SF--DPLAVLEAIEKEKCTALHgvPTMFIAE 106
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
264-310 |
4.25e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 45.81 E-value: 4.25e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1958806453 264 PSRPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLG 310
Cdd:PRK07824 29 VGEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGPG 75
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
270-315 |
5.08e-05 |
|
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: 45.79 E-value: 5.08e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1958806453 270 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTY 315
Cdd:cd05972 81 EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPT-AAYWLGLRPDDIH 125
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
271-323 |
6.88e-05 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 45.65 E-value: 6.88e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1958806453 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIpGLGPKDTYIGYLPLAH 323
Cdd:PRK05852 177 DDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGY-RLSPRDATVAVMPLYH 228
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
250-337 |
7.10e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 45.53 E-value: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 250 VEELGSKPENSSIPPsrPTPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTA 329
Cdd:PRK05851 134 LATAAHTNRSASLTP--PDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSWLPLYHDMGLAF 211
|
....*...
gi 1958806453 330 EISCFTYG 337
Cdd:PRK05851 212 LLTAALAG 219
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
259-323 |
8.54e-05 |
|
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: 45.37 E-value: 8.54e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958806453 259 NSSIPPSRPTPSDMAIVM-YTSGSTGRPKGVMMHH--------SNLIAGmtgqceripGLGPKDTYIGYLPLAH 323
Cdd:cd12118 121 DPDFEWIPPADEWDPIALnYTSGTTGRPKGVVYHHrgaylnalANILEW---------EMKQHPVYLWTLPMFH 185
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
126-337 |
1.24e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 44.73 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCfkynfplvtlyATLGkeAVVHGLN----ESEASYL 201
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLAC-----------ARLG--ATVIAVNtryrSHEVAHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 202 ITS-----------------VELLESKLKAALLDincVKHIIYVDNKTinrAEYPEGLEIHSMQSVEELGSKPENSSIPP 264
Cdd:PRK06164 103 LGRgrarwlvvwpgfkgidfAAILAAVPPDALPP---LRAIAVVDDAA---DATPAPAPGARVQLFALPDPAPPAAAGER 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958806453 265 SRPtPSDMAIVMYTSGSTGRPKGVMMHHSNLIAgMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYG 337
Cdd:PRK06164 177 AAD-PDAGALLFTTSGTTSGPKLVLHRQATLLR-HARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGG 247
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
78-323 |
1.24e-04 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 44.74 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 78 TLDKLFDHAVAKFGKkdslgtREILSEENEmqpngkvfkklilGNYKWINYLEVNCRVNNFGSGLTALGLKPKNTIAifc 157
Cdd:PRK06018 11 LCHRIIDHAARIHGN------REVVTRSVE-------------GPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVA--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 158 eTRAeWMIAAQtcfkynfpLVTLYATLGKEAVVHGLN---------------ESEASYL-ITSVELLEsKLKAALLDINc 221
Cdd:PRK06018 69 -TIA-WNTWRH--------LEAWYGIMGIGAICHTVNprlfpeqiawiinhaEDRVVITdLTFVPILE-KIADKLPSVE- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 222 vKHIIYVDNKTI------NRAEYPEGLEIHSMQSVeeLGSKPENSSippsrptpsdmAIVMYTSGSTGRPKGVMM-HHSN 294
Cdd:PRK06018 137 -RYVVLTDAAHMpqttlkNAVAYEEWIAEADGDFA--WKTFDENTA-----------AGMCYTSGTTGDPKGVLYsHRSN 202
|
250 260
....*....|....*....|....*....
gi 1958806453 295 LIAGMTGQCERIPGLGPKDTYIGYLPLAH 323
Cdd:PRK06018 203 VLHALMANNGDALGTSAADTMLPVVPLFH 231
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
118-324 |
1.31e-04 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 44.86 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 118 LILGNYKWiNYLEVNCRVNNFGSGLTALGLKPKNTIAIfcetraewmiaaqtCFKYNFPLVTLY-ATLGKEAVVHGLNES 196
Cdd:PRK09029 22 LRLNDEVL-TWQQLCARIDQLAAGFAQQGVVEGSGVAL--------------RGKNSPETLLAYlALLQCGARVLPLNPQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 197 easylitsveLLESKLkAALLDINCVKHIIYvdnktINRAEYPEGLEIHSMQSVEElgskpenssIPPSRPTPSDMAIVM 276
Cdd:PRK09029 87 ----------LPQPLL-EELLPSLTLDFALV-----LEGENTFSALTSLHLQLVEG---------AHAVAWQPQRLATMT 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1958806453 277 YTSGSTGRPKGVMMHHSNLIAGMTGQCERIPgLGPKDTYIGYLPLAHV 324
Cdd:PRK09029 142 LTSGSTGLPKAAVHTAQAHLASAEGVLSLMP-FTAQDSWLLSLPLFHV 188
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
184-352 |
1.36e-04 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 44.77 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 184 LGKEAVVHGLNESEASYLITSVELLEsKLKAALLDINCVKHIIYV--DNKTINRAEYPEGLEIHSMQSveELGSKPENSS 261
Cdd:PRK05620 98 LMNDQIVHIINHAEDEVIVADPRLAE-QLGEILKECPCVRAVVFIgpSDADSAAAHMPEGIKVYSYEA--LLDGRSTVYD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 262 IPPSRPTpsDMAIVMYTSGSTGRPKGVMMHHSNL-IAGMTGQCERIPGLGPKDTYIGYLPLAHVLELTAEISCFTYGcri 340
Cdd:PRK05620 175 WPELDET--TAAAICYSTGTTGAPKGVVYSHRSLyLQSLSLRTTDSLAVTHGESFLCCVPIYHVLSWGVPLAAFMSG--- 249
|
170
....*....|..
gi 1958806453 341 gysSPLTLSDQS 352
Cdd:PRK05620 250 ---TPLVFPGPD 258
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
270-395 |
1.39e-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: 44.17 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 270 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPLAHVLE-------LTAEISCFTYGCRIGY 342
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGlwwiltcLIHGGLCVTGGENTTY 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958806453 343 SSPLtlsdqssKIKKGSKGDCTVLKPTLMAAVPEimdrIYKNVMSKVQEMNYI 395
Cdd:cd17635 81 KSLF-------KILTTNAVTTTCLVPTLLSKLVS----ELKSANATVPSLRLI 122
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
126-323 |
1.39e-04 |
|
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: 44.65 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEAsylitsv 205
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSA------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ellesklkaalldincvKHIIYvdnktinraeypegleihsmqsveelgskpenssippsrptpsDMAIVMYTSGSTGRP 285
Cdd:cd05940 77 -----------------KHLVV-------------------------------------------DAALYIYTSGTTGLP 96
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958806453 286 KGVMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAH 323
Cdd:cd05940 97 KAAIISHRRAWRGGAF-FAGSGGALPSDVLYTCLPLYH 133
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
266-328 |
1.85e-04 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 44.27 E-value: 1.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958806453 266 RP--TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTgQCERI--PGLGP-KDTYIGYLPLAHVLELT 328
Cdd:PRK08974 200 KPelVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLE-QAKAAygPLLHPgKELVVTALPLYHIFALT 266
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
248-295 |
2.27e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 44.03 E-value: 2.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1958806453 248 QSVEELGSKPeNSSIPPSRPTpsdmaIVMYTSGSTGRPKGVMMHHSNL 295
Cdd:PRK09088 119 ASADALEPAD-TPSIPPERVS-----LILFTSGTSGQPKGVMLSERNL 160
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
128-324 |
2.43e-04 |
|
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: 43.82 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 128 YLEVNCRVNNFGSGL-TALGLKPKNTIAIFC--ETRAEWM---IAAQTCfkynfPLVTLYATLGKEAVVHGLNESEASYL 201
Cdd:cd05938 8 YRDVDRRSNQAARALlAHAGLRPGDTVALLLgnEPAFLWIwlgLAKLGC-----PVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 202 ITSVELLES------KLKAALLdincvkHIIYVDNKTInraeyPEGleihsmqsVEELGSKPENSS---IPPS---RPTP 269
Cdd:cd05938 83 VVAPELQEAveevlpALRADGV------SVWYLSHTSN-----TEG--------VISLLDKVDAASdepVPASlraHVTI 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1958806453 270 SDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQceRIPGLGPKDTYIGYLPLAHV 324
Cdd:cd05938 144 KSPALYIYTSGTTGLPKAARISHLRVLQCSGFL--SLCGVTADDVIYITLPLYHS 196
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
271-314 |
2.83e-04 |
|
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: 43.60 E-value: 2.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1958806453 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDT 314
Cdd:cd05919 92 DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDR 135
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
271-323 |
2.84e-04 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 43.26 E-value: 2.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1958806453 271 DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCErIPGLGPKDTYIGYLPLAH 323
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWAD-CADLTEDDRYLIINPFFH 52
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
126-345 |
3.04e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKYNFPLVTLYATLGKEAVVHGLNESEASYLITSV 205
Cdd:PRK05691 1157 LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQS 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ELLEsklkaalldincvkhiiyvdnktinRAEYPEGLEIHSMQSVEeLGSKPensSIPPSRPTPSD-MAIVMYTSGSTGR 284
Cdd:PRK05691 1237 HLLE-------------------------RLPQAEGVSAIALDSLH-LDSWP---SQAPGLHLHGDnLAYVIYTSGSTGQ 1287
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958806453 285 PKGVMMHHSNLIagmtgqcERIPGLgpKDTYIgyLPLAHVLELTAEIS-------CF---TYGCRIGYSSP 345
Cdd:PRK05691 1288 PKGVGNTHAALA-------ERLQWM--QATYA--LDDSDVLMQKAPISfdvsvweCFwplITGCRLVLAGP 1347
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
251-310 |
3.09e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 3.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958806453 251 EELGSKPENSSIPPSRPTPSDMAIVMYTSGSTGRPKGVMMHHsnliAGM-TGQCERIPGLG 310
Cdd:PRK05691 3850 EEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQ----RGMlNNQLSKVPYLA 3906
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
233-296 |
5.71e-04 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 42.57 E-value: 5.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958806453 233 INRAEYP---EGLEIHSMQSVEELGSKPEnsSIPPSRP-TPSDMAIVMYTSGSTGRPKGVMMHHSNLI 296
Cdd:PRK04813 104 IATEELPleiLGIPVITLDELKDIFATGN--PYDFDHAvKGDDNYYIIFTSGTTGKPKGVQISHDNLV 169
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
126-325 |
5.93e-04 |
|
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: 42.50 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 126 INYLEVNCRVNNFGSGLTALGLKPKNTIAIFCETRAEWMIAAQTCFKynfplvtlyatLGkeAVVhglneseasylitsv 205
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHR-----------LG--AVP--------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 206 ELLESKLKAALLDiNCVKH-----IIYVDNKTINRAEYPEGLEIHSMQSVEELGSkPENSS--IPPSRPTPSDMAIVMYT 278
Cdd:cd05923 81 ALINPRLKAAELA-ELIERgemtaAVIAVDAQVMDAIFQSGVRVLALSDLVGLGE-PESAGplIEDPPREPEQPAFVFYT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958806453 279 SGSTGRPKGVMM---HHSNLIAGMTGQCeripGL--GPKDTYIGYLPLAHVL 325
Cdd:cd05923 159 SGTTGLPKGAVIpqrAAESRVLFMSTQA----GLrhGRHNVVLGLMPLYHVI 206
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
249-325 |
7.65e-04 |
|
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: 42.42 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 249 SVEELGSKPENSSIPPSRP--TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKD-TYIGYLPLAHVL 325
Cdd:cd05921 142 SFAELAATPPTAAVDAAFAavGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPpVLVDWLPWNHTF 221
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
252-321 |
8.28e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 42.34 E-value: 8.28e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806453 252 ELGSKPENSSIPPSRPTPS--DMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGQCERIPGLGPKDTYIGYLPL 321
Cdd:PRK06178 189 DLLPALRACTAPVPLPPPAldALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPE 260
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
263-292 |
3.72e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.54 E-value: 3.72e-03
10 20 30
....*....|....*....|....*....|
gi 1958806453 263 PPSRPTPSDMAIVMYTSGSTGRPKGVMMHH 292
Cdd:PRK05691 2326 LPFLSLPQHQAYLIYTSGSTGKPKGVVVSH 2355
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-297 |
4.94e-03 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 39.75 E-value: 4.94e-03
10 20 30
....*....|....*....|....*....|.
gi 1958806453 267 PTPSDMAIVMYTSGSTGRPKGVMMHHSNLIA 297
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAA 112
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
268-325 |
6.06e-03 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 39.48 E-value: 6.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806453 268 TPSDMAIVMYTSGSTGRPKGVMMHHSNLIAG--MTGQCERIPGLGPKdTYIGYLPLAHVL 325
Cdd:PRK08180 207 GPDTIAKFLFTSGSTGLPKAVINTHRMLCANqqMLAQTFPFLAEEPP-VLVDWLPWNHTF 265
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
239-295 |
6.23e-03 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 39.66 E-value: 6.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958806453 239 PEGLEIHSMQSVEELGSKPENSSI-PPSRPTPSdmaivmYTSGSTGRPKGVMMHHSNL 295
Cdd:TIGR03443 389 LEGGETDVLAPYQALKDTPTGVVVgPDSNPTLS------FTSGSEGIPKGVLGRHFSL 440
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
277-323 |
7.08e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 39.25 E-value: 7.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1958806453 277 YTSGSTGRPKGVMMHHSNLIAGMTGQ-CERIPGLGPKDTYIGYLPLAH 323
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQMAFVITNHlADLMPGTTEQDASLVVAPLSH 217
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
269-323 |
7.85e-03 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 39.03 E-value: 7.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958806453 269 PSDMAIVMYTSGSTGRPKGVMMHHSNLIAGMTGqCERIPGLGPKDTYIGYLPLAH 323
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRA-CLKFFSPKEDDVMMSFLPPFH 235
|
|
| |
