|
Name |
Accession |
Description |
Interval |
E-value |
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
1-370 |
0e+00 |
|
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: 688.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 1 MYEQQLQCVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFG--QANTSLKRWLLDFASKRKEAELR 78
Cdd:cd05927 171 IFERVVEALFLYHGAKIGFYSGDIRLLLDDIKALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 79 SGIVRNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGA 158
Cdd:cd05927 251 SGVVRASPFWDKLVFNKIKQALGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGG 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 159 PMPCNYVKLVDVEEMNYLA--SKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 236
Cdd:cd05927 331 PLPCAEVKLVDVPEMNYDAkdPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIF 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 237 KLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGL-QGSFEELCRNKDINKAILDDLL 315
Cdd:cd05927 411 KLSQGEYVAPEKIENIYARSPFVAQIFVYGDSLKSFLVAIVVPDPDVLKEWAASKGGgTGSFEELCKNPEVKKAILEDLV 490
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907187107 316 KLGKEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYA 370
Cdd:cd05927 491 RLGKENGLKGFEQVKAIHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
1-372 |
4.26e-170 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 489.61 E-value: 4.26e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 1 MYEQQLQCVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTS--LKRWLLDFASKRKEAELR 78
Cdd:PLN02736 274 IYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESggLKERLFNAAYNAKKQALE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 79 SGivRNNS-LWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEctAGCCLSL--PGDWTAGH 155
Cdd:PLN02736 354 NG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTE--TSCVISGmdEGDNLSGH 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 156 VGAPMPCNYVKLVDVEEMNYLASKG---EGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRK 232
Cdd:PLN02736 430 VGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRK 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 233 KHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGLQ-GSFEELCRNKDINKAIL 311
Cdd:PLN02736 510 KNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVL 589
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907187107 312 DDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYATI 372
Cdd:PLN02736 590 ADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
2-370 |
1.04e-119 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 359.03 E-value: 1.04e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 2 YEQQLQCVMLCHGAKIGFfQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTS--LKRWLLDFA---SKRKEAE 76
Cdd:COG1022 237 FERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAggLKRKLFRWAlavGRRYARA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 77 LRSGivRNNSLW--------DKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRtALGCQFYEGYGQTECTAGCCLSLP 148
Cdd:COG1022 316 RLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFR-ALGIPVLEGYGLTETSPVITVNRP 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 149 GDWTAGHVGAPMPCNYVKLVDveemnylaskgEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKI 228
Cdd:COG1022 393 GDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRI 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 229 IDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESlQAFLIAVVVPDVESLPSWAQKRGLQ-GSFEELCRNKDIN 307
Cdd:COG1022 462 TGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSYAELAQDPEVR 540
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907187107 308 KAILDDLLKLgkEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYA 370
Cdd:COG1022 541 ALIQEEVDRA--NAGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
7-357 |
4.52e-118 |
|
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: 349.97 E-value: 4.52e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 7 QCVMLCHGAKIGFFQgDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSLKRWLLDFASkrkeaelrsgivrnns 86
Cdd:cd05907 147 LYVPLLAGARIYFAS-SAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV---------------- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 87 lwdklifhkiqsslGGKVRLMITGAAPVSATVLTFLRtALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVK 166
Cdd:cd05907 210 --------------GGRLRFAASGGAPLPAELLHFFR-ALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVR 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 167 LVDveemnylaskgEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAP 246
Cdd:cd05907 275 IAD-----------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISP 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 247 EKIENIYLRSEAVAQVFVHGESlQAFLIAVVVPDVESLPSWAQKRGL-QGSFEELCRNKDINKAILDDLLKLGkeAGLKP 325
Cdd:cd05907 344 EPIENALKASPLISQAVVIGDG-RPFLVALIVPDPEALEAWAEEHGIaYTDVAELAANPAVRAEIEAAVEAAN--ARLSR 420
|
330 340 350
....*....|....*....|....*....|..
gi 1907187107 326 FEQVKGIAVHPELFSIDNGLLTPTLKAKRPEL 357
Cdd:cd05907 421 YEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
1-373 |
5.49e-117 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 353.76 E-value: 5.49e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 1 MYEQQLQCVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLlnrmFDRIFG------QANTSLKRWLLDFASKRKE 74
Cdd:PLN02861 278 VYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRV----YDRIYTgimqkiSSGGMLRKKLFDFAYNYKL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 75 AELRSGIVRNNS--LWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWT 152
Cdd:PLN02861 354 GNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTSIANVFS 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 153 -AGHVGAPMPCNYVKLVDVEEMNY--LASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKII 229
Cdd:PLN02861 434 mVGTVGVPMTTIEARLESVPEMGYdaLSDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKII 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 230 DRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGLQGSFEELCRNKDINKA 309
Cdd:PLN02861 513 DRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKY 592
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907187107 310 ILDDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYATIK 373
Cdd:PLN02861 593 ILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSEAK 656
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
9-354 |
4.69e-113 |
|
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: 338.81 E-value: 4.69e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 9 VMLCHGAKIGFfqGDIRLLMD--------DLKVLQPTIFPVVPRLLNRMFDRIFGQANTS--LKRWLLDFASKRKEAELR 78
Cdd:cd17639 151 VCLYRGGTIGY--GSPRTLTDkskrgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMggLKRTLFWTAYQSKLKALK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 79 SGIvrNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALgCQFYEGYGQTECTAGCCLSLPGDWTAGHVGA 158
Cdd:cd17639 229 EGP--GTPLLDELVFKKVRAALGGRLRYMLSGGAPLSADTQEFLNIVL-CPVIQGYGLTETCAGGTVQDPGDLETGRVGP 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 159 PMPCNYVKLVDVEEMNYLASKGE--GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 236
Cdd:cd17639 306 PLPCCEIKLVDWEEGGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLV 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 237 KLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGL-QGSFEELCRNKDINKAILDDLL 315
Cdd:cd17639 386 KLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLA 465
|
330 340 350
....*....|....*....|....*....|....*....
gi 1907187107 316 KLGKEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKR 354
Cdd:cd17639 466 ETARAAGLEKFEIPQGVVLLDEEWTPENGLVTAAQKLKR 504
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
1-373 |
1.34e-112 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 342.77 E-value: 1.34e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 1 MYEQQLQCVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIfgQANTS----LKRWLLDFASKRKEAE 76
Cdd:PLN02614 281 IFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGL--QKKLSdggfLKKFVFDSAFSYKFGN 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 77 LRSGI--VRNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDW-TA 153
Cdd:PLN02614 359 MKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELdML 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 154 GHVGAPMPCNYVKLVDVEEMNY--LASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDR 231
Cdd:PLN02614 439 GTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDR 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 232 KKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGLQGSFEELCRNKDINKAIL 311
Cdd:PLN02614 518 KKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFIL 597
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907187107 312 DDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYATIK 373
Cdd:PLN02614 598 GELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTN 659
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
14-372 |
9.50e-103 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 317.14 E-value: 9.50e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 14 GAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFG--QANTSLKRWLLDFASKRKEAELRSGIVRNNS--LWD 89
Cdd:PLN02430 291 GASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYKLAWMNRGYSHKKAspMAD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 90 KLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTA-GHVGAPMPCNYVKLV 168
Cdd:PLN02430 371 FLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMlGTVGAPAVYNELRLE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 169 DVEEMNY--LASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAP 246
Cdd:PLN02430 451 EVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVAL 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 247 EKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGLQGSFEELCRNKDINKAILDDLLKLGKEAGLKPF 326
Cdd:PLN02430 530 EYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGF 609
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907187107 327 EQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYATI 372
Cdd:PLN02430 610 EYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
9-370 |
1.28e-83 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 268.14 E-value: 1.28e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 9 VMLCHGAKIGFfqGDIRLLMD-----------DLKVLQPTIFPVVPRLLNRMFDRIFGQANTS--LKRWLLDFASKRKEA 75
Cdd:PLN02387 312 VMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 76 ELR------SGIVRnnSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPG 149
Cdd:PLN02387 390 AIEgswfgaWGLEK--LLWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWD 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 150 DWTAGHVGAPMPCNYVKLVDVEEMNYLASKG---EGEVCVKGANVFKGYLKDPARTAEA--LDKDG--WLHTGDIGKWLP 222
Cdd:PLN02387 468 DTSVGRVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHP 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 223 NGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGLQ-GSFEELC 301
Cdd:PLN02387 548 DGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELC 627
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907187107 302 RNKDINKAILDDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYA 370
Cdd:PLN02387 628 EKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
9-239 |
4.31e-66 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 215.25 E-value: 4.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 9 VMLCHGAKIGFFQGDIRL----LMDDLKVLQPTIFPVVPRLLNRMFDrifgqantslkrwlldfaSKRKEAELRSGivrn 84
Cdd:pfam00501 221 GPLLAGATVVLPPGFPALdpaaLLELIERYKVTVLYGVPTLLNMLLE------------------AGAPKRALLSS---- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 85 nslwdklifhkiqsslggkVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDW---TAGHVGAPMP 161
Cdd:pfam00501 279 -------------------LRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLP 339
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907187107 162 CNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 239
Cdd:pfam00501 340 GTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
9-370 |
4.71e-65 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 219.08 E-value: 4.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 9 VMLCHGAKIGFfqGDIRLLMD-------DLKVLQPTIFPVVPRLlnrmFDRI----------FGqantSLKRWLLDFASK 71
Cdd:PTZ00216 330 IFLARGALIGF--GSPRTLTDtfarphgDLTEFRPVFLIGVPRI----FDTIkkaveaklppVG----SLKRRVFDHAYQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 72 RKEAELRSGivRNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCqFYEGYGQTECTagCC--LSLPG 149
Cdd:PTZ00216 400 SRLRALKEG--KDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETV--CCggIQRTG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 150 DWTAGHVGAPMPCNYVKLVDVEEMNYlASKGE--GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLK 227
Cdd:PTZ00216 475 DLEPNAVGQLLKGVEMKLLDTEEYKH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLR 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 228 IIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQ----VFVHgeSLQAFLIAVVVPDVESLPSWAQKRGLQGSFEELCRN 303
Cdd:PTZ00216 554 IIGRVKALAKNCLGEYIALEALEALYGQNELVVPngvcVLVH--PARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKD 631
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907187107 304 KDINKAILDDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYA 370
Cdd:PTZ00216 632 PEFQKKATESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELFA 698
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1-355 |
8.19e-63 |
|
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: 207.98 E-value: 8.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 1 MYEQQLQCVMLCHGAKIGFfqGDIRLLMDDLKVLQPTIFPVVPRLlnrmfdrifgqantslkrWlldfaskrkEAeLRSG 80
Cdd:cd17640 141 SYERSAEYFIFACGCSQAY--TSIRTLKDDLKRVKPHYIVSVPRL------------------W---------ES-LYSG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 81 I---VRNNSLWDKLIFHKIQSslGGKVRLMITGAAPVSATVLTFLRtALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVG 157
Cdd:cd17640 191 IqkqVSKSSPIKQFLFLFFLS--GGIFKFGISGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVG 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 158 APMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFK 237
Cdd:cd17640 268 RPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 238 LAQGEYIAPEKIENIYLRSEAVAQVFVHGESlQAFLIAVVVPDVESLPSWAQKRG--LQGSFEELCRNKDINKAILDDLL 315
Cdd:cd17640 348 LSNGENVEPQPIEEALMRSPFIEQIMVVGQD-QKRLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKLYKNEIK 426
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1907187107 316 K-LGKEAGLKPFEQVKGIAVHPELFsIDNGLLTPTLKAKRP 355
Cdd:cd17640 427 DeISNRPGFKSFEQIAPFALLEEPF-IENGEMTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
19-354 |
9.43e-53 |
|
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: 182.28 E-value: 9.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 19 FFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSLKRWLLDFaskrkeaelrsgivrnnSLWDKLIFHKIQS 98
Cdd:cd05932 208 AFAESLDTFVEDVQRARPTLFFSVPRLWTKFQQGVQDKIPQQKLNLLLKI-----------------PVVNSLVKRKVLK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 99 SLG-GKVRLMITGAAPVSATVLTFLRTaLGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDveemnyla 177
Cdd:cd05932 271 GLGlDQCRLAGCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-------- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 178 skgEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSE 257
Cdd:cd05932 342 ---DGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHD 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 258 AVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRG-LQGSFEELCrnKDINKAilddllklgkeagLKPFEQVKGIAVHP 336
Cdd:cd05932 419 RVEMVCVIGSGLPAPLALVVLSEEARLRADAFARAeLEASLRAHL--ARVNST-------------LDSHEQLAGIVVVK 483
|
330
....*....|....*...
gi 1907187107 337 ELFSIDNGLLTPTLKAKR 354
Cdd:cd05932 484 DPWSIDNGILTPTLKIKR 501
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
11-347 |
1.18e-51 |
|
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: 181.11 E-value: 1.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 11 LCHGAkIGFFQG--DIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIfgQAntSLKRWLLDFA-----SKRKEAELRsgivr 83
Cdd:cd17632 287 LARGG-TAYFAAasDMSTLFDDLALVRPTELFLVPRVCDMLFQRY--QA--ELDRRSVAGAdaetlAERVKAELR----- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 84 nnslwdklifhkiQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEctAGCCLSLpgdwtaGHVGAPMPCN 163
Cdd:cd17632 357 -------------ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVILD------GVIVRPPVLD 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 164 YvKLVDVEEMNYLASKG---EGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQ 240
Cdd:cd17632 416 Y-KLVDVPELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQ 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 241 GEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPdveslpswAQKRGLQGSFEELcrnkdiNKAILDDLLKLGKE 320
Cdd:cd17632 495 GEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVP--------TQDALAGEDTARL------RAALAESLQRIARE 560
|
330 340
....*....|....*....|....*..
gi 1907187107 321 AGLKPFEQVKGIAVHPELFSIDNGLLT 347
Cdd:cd17632 561 AGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
10-291 |
4.83e-48 |
|
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: 165.54 E-value: 4.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 10 MLCHGAKI----GFFQGDIRLLMDDLKVlqpTIFPVVPRLLNRMFDRIfgqantslkrwlldfasKRKEAELRSgivrnn 85
Cdd:cd04433 62 ALLAGGTVvllpKFDPEAALELIEREKV---TILLGVPTLLARLLKAP-----------------ESAGYDLSS------ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 86 slwdklifhkiqsslggkVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWT--AGHVGAPMPCN 163
Cdd:cd04433 116 ------------------LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 164 YVKLVDVEEmNYLASKGEGEVCVKGANVFKGYLKDPARTAEAlDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEY 243
Cdd:cd04433 178 EVRIVDPDG-GELPPGEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGEN 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907187107 244 IAPEKIENIYLRSEAVAQVFVHG---ESLQAFLIAVVVP------DVESLPSWAQKR 291
Cdd:cd04433 255 VYPAEVEAVLLGHPGVAEAAVVGvpdPEWGERVVAVVVLrpgadlDAEELRAHVRER 311
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
104-291 |
9.19e-47 |
|
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: 165.37 E-value: 9.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTA--GHVGAPMPCNYVKLVDvEEMNYLASKGE 181
Cdd:COG0318 217 LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRELPPGEV 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 182 GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQ 261
Cdd:COG0318 296 GEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAHPGVAE 373
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907187107 262 VFV-------HGESLQAFLIAV--VVPDVESLPSWAQKR 291
Cdd:COG0318 374 AAVvgvpdekWGERVVAFVVLRpgAELDAEELRAFLRER 412
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
13-369 |
2.09e-45 |
|
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: 164.07 E-value: 2.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 13 HGAKIGFFQGDIR--LLMDDLKVLQPTIFPVVPRLLNRMFDRI--FGQANTSLKRWLLDFAsKRKEAE-------LRSGI 81
Cdd:cd05933 220 VGGQVYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkaVGAKSGTLKRKIASWA-KGVGLEtnlklmgGESPS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 82 VRNNSLWDKLIFHKIQSSLG-GKVRLMITGAAPVSATVLTFLrTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPM 160
Cdd:cd05933 299 PLFYRLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKAL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 161 PCNYVKLVDVEemnylaSKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQ 240
Cdd:cd05933 378 PGCKTKIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAG 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 241 GEYIAPEKIEN-IYLRSEAVAQVFVHGESLQaFLIAVVVPDVESLPswaqKRGLQG---SFE--ELCRNKDINKAILDDL 314
Cdd:cd05933 452 GENVPPVPIEDaVKKELPIISNAMLIGDKRK-FLSMLLTLKCEVNP----ETGEPLdelTEEaiEFCRKLGSQATRVSEI 526
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 315 LKLGKEAGLKPFEQ---------------VKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELY 369
Cdd:cd05933 527 AGGKDPKVYEAIEEgikrvnkkaisnaqkIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
90-354 |
1.09e-39 |
|
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: 146.43 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 90 KLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTaLGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPmpcnyVKLVD 169
Cdd:cd05914 222 KLAFKKVHEAFGGNIKEFVIGGAKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVE 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 170 VEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKI 249
Cdd:cd05914 296 VRIDSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEI 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 250 ENIYLRSEAVA--QVFV-HGEslqafLIAVVVPDveslPSWAQKRGLQgsfeelcrNKDINKAILDDLL-KLGKEagLKP 325
Cdd:cd05914 376 EAKINNMPFVLesLVVVqEKK-----LVALAYID----PDFLDVKALK--------QRNIIDAIKWEVRdKVNQK--VPN 436
|
250 260
....*....|....*....|....*....
gi 1907187107 326 FEQVKGIAVHPELFSidnglLTPTLKAKR 354
Cdd:cd05914 437 YKKISKVKIVKEEFE-----KTPKGKIKR 460
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
23-284 |
5.18e-39 |
|
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: 144.63 E-value: 5.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 23 DIRLLMDDLKVLQPTIFPVVPRLLNRMFDrifgqantslkrwlldfASKRKEAELRSgivrnnslwdklifhkiqsslgg 102
Cdd:cd05936 204 RPIGVLKEIRKHRVTIFPGVPTMYIALLN-----------------APEFKKRDFSS----------------------- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 kVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECT-AGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGE 181
Cdd:cd05936 244 -LRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVD-DDGEELPPGEV 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 182 GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQ 261
Cdd:cd05936 322 GELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAE 399
|
250 260 270
....*....|....*....|....*....|
gi 1907187107 262 VFV-------HGESLQAFliaVVVPDVESL 284
Cdd:cd05936 400 AAVvgvpdpySGEAVKAF---VVLKEGASL 426
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
104-266 |
4.68e-38 |
|
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: 142.35 E-value: 4.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFLRTALG-CQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPcNY-VKLVDVEEMNYLASKGE 181
Cdd:cd05911 264 LRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLP-NVeAKIVDDDGKDSLGPNEP 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 182 GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQ 261
Cdd:cd05911 343 GEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVAD 421
|
....*
gi 1907187107 262 VFVHG 266
Cdd:cd05911 422 AAVIG 426
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
27-354 |
4.69e-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: 141.02 E-value: 4.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 27 LMDDLKVLQPTIFPVVPRLLNRM--FDRIFGQANTSLKRWLLDF--------ASKRKEAELRSGIVRNNS-LWDKLIFHK 95
Cdd:cd17641 237 MMEDLREIGPTFVLLPPRVWEGIaaDVRARMMDATPFKRFMFELgmklglraLDRGKRGRPVSLWLRLASwLADALLFRP 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 96 IQSSLG-GKVRLMITGAAPVSATVLTFLRtALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVeemn 174
Cdd:cd17641 317 LRDRLGfSRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV---- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 175 ylaskgeGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIEN--- 251
Cdd:cd17641 392 -------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENklk 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 252 --IYLRsEAVaqVFVHGeslQAFLIAVVVPDVESLPSWAQKRGLQ-GSFEELCRNKDINKAILDDLLKLGKEagLKPFEQ 328
Cdd:cd17641 465 fsPYIA-EAV--VLGAG---RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS--LPEAQR 536
|
330 340
....*....|....*....|....*.
gi 1907187107 329 VKGIAVHPELFSIDNGLLTPTLKAKR 354
Cdd:cd17641 537 IRRFLLLYKELDADDGELTRTRKVRR 562
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
35-291 |
4.80e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 140.04 E-value: 4.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 35 QPTIFPVVPRLLNRMFDrifgqantslkrwlldfASKRKEAELRSgivrnnslwdklifhkiqsslggkVRLMITGAAPV 114
Cdd:PRK07656 255 RITVLPGPPTMYNSLLQ-----------------HPDRSAEDLSS------------------------LRLAVTGAASM 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 115 SATVLTFLRTALGCQ-FYEGYGQTECTAGCCLSLPGD---WTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGAN 190
Cdd:PRK07656 294 PVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVN-ELGEEVPVGEVGELLVRGPN 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 191 VFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV------ 264
Cdd:PRK07656 373 VMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHPAVAEAAVigvpde 451
|
250 260 270
....*....|....*....|....*....|
gi 1907187107 265 -HGESLQAFLIAVVVPDV--ESLPSWAQKR 291
Cdd:PRK07656 452 rLGEVGKAYVVLKPGAELteEELIAYCREH 481
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
103-280 |
1.23e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 130.69 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 KVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECT-AGCCL----SLPGDWT-AGHVGAPMPCNYVKLVDvEEMNYL 176
Cdd:PRK06187 282 SLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLppedQLPGQWTkRRSAGRPLPGVEARIVD-DDGDEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 177 ASKGE--GEVCVKGANVFKGYLKDPARTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYL 254
Cdd:PRK06187 361 PPDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDALY 438
|
170 180
....*....|....*....|....*..
gi 1907187107 255 RSEAVAQVfvhgeslqafliAVV-VPD 280
Cdd:PRK06187 439 GHPAVAEV------------AVIgVPD 453
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
98-280 |
2.63e-31 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 123.10 E-value: 2.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 98 SSLggkvRLMITGAAPVSATVLTFLRtALGCQFYEGYGQTECTAGCCLSLPGDW--TAGHVGAPMPCNYVKLVDvEEMNY 175
Cdd:cd17631 213 SSL----RAVIYGGAPMPERLLRALQ-ARGVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIVD-PDGRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 176 LASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLR 255
Cdd:cd17631 287 VPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLYE 364
|
170 180 190
....*....|....*....|....*....|..
gi 1907187107 256 SEAVAQVFV-------HGESlqafLIAVVVPD 280
Cdd:cd17631 365 HPAVAEVAVigvpdekWGEA----VVAVVVPR 392
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
104-291 |
4.80e-29 |
|
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: 114.91 E-value: 4.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFLRTALGCQ-FYEGYGQTECTAGCcLSLPGD---WTAGHVGAPMPCNYVKLVDveemnylask 179
Cdd:cd17638 117 LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVAT-MCRPGDdaeTVATTCGRACPGFEVRIAD---------- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 180 gEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAV 259
Cdd:cd17638 186 -DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEHPGV 263
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907187107 260 AQVFV-------HGESLQAFLIAV--VVPDVESLPSWAQKR 291
Cdd:cd17638 264 AQVAVigvpderMGEVGKAFVVARpgVTLTEEDVIAWCRER 304
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
103-291 |
6.24e-29 |
|
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: 116.62 E-value: 6.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 KVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEctAGCCLSLP--GDWTAGHVGAPMPCNYVKLVDVEEMNYLASKG 180
Cdd:cd05941 213 RLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRGE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 181 EGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIAPEKIENIYLRSEAV 259
Cdd:cd05941 291 VGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERVLLAHPGV 369
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907187107 260 AQVFVHGESLQAF---LIAVVVP-------DVESLPSWAQKR 291
Cdd:cd05941 370 SECAVIGVPDPDWgerVVAVVVLragaaalSLEELKEWAKQR 411
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
102-274 |
6.52e-28 |
|
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: 111.99 E-value: 6.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 102 GKVRLMITGAAPVSATVLTFLRTALGC-QFYEGYGQTECTAGCCLSLPGDWT---AGHVGAPMPCNYVKLVDvEEMNYLA 177
Cdd:cd05917 118 SSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIekrVNTVGRIMPHTEAKIVD-PEGGIVP 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 178 SKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRS 256
Cdd:cd05917 197 PVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPREIEEFLHTH 275
|
170 180
....*....|....*....|....*
gi 1907187107 257 EAVAQVFV-------HGESLQAFLI 274
Cdd:cd05917 276 PKVSDVQVvgvpderYGEEVCAWIR 300
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
2-367 |
2.14e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 113.66 E-value: 2.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 2 YEQQLQCVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQAN--TSLKRWLLdfaskRKEAELRS 79
Cdd:PTZ00342 360 YERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPPLKRFLV-----KKILSLRK 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 80 GivRNNSLWDKL---IFH---KIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTA 153
Cdd:PTZ00342 435 S--NNNGGFSKFlegITHissKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNNT 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 154 GHVGAPM-PCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRK 232
Cdd:PTZ00342 513 ESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRS 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 233 KHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGL---QGSFEELCRNK----D 305
Cdd:PTZ00342 593 KGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKDDNMlesTGINEKNYLEKltdeT 672
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907187107 306 INKAILDD-----LLKLGKEAGLKPFEQVKGIAVHPELFSIDNgLLTPTLKAKRPELRNYFRSQIDE 367
Cdd:PTZ00342 673 INNNIYVDyvkgkMLEVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVFKDYAFFIDQ 738
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
85-284 |
2.15e-27 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 113.23 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 85 NSLWDKLI----FHKIQSSlggKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECT---AGCCLSLPGdwTAGHVG 157
Cdd:PRK08974 307 NTLFNALLnneeFQELDFS---SLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 158 APMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFk 237
Cdd:PRK08974 382 LPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI- 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907187107 238 LAQGEYIAPEKIENIYLRSEAVAQVF-------VHGESLQAFliavVVPDVESL 284
Cdd:PRK08974 459 LVSGFNVYPNEIEDVVMLHPKVLEVAavgvpseVSGEAVKIF----VVKKDPSL 508
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
105-319 |
6.57e-27 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 110.62 E-value: 6.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 105 RLMITGAAPVSATVLTFLRTaLGCQFYEGYGQTE-CTAGCCLSLPGDWTAGHVGAPMPCNYVKL-VDVEEmnylaskGEG 182
Cdd:TIGR01923 222 RKILLGGSAIPAPLIEEAQQ-YGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 183 EVCVKGANVFKGYLkDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQV 262
Cdd:TIGR01923 294 EIMVKGANLMKGYL-YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEA 371
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907187107 263 FVhgeslqafliaVVVPDVEslpsWAQKRGLQGSFeelcrNKDINKAILDDLL--KLGK 319
Cdd:TIGR01923 372 VV-----------VPKPDAE----WGQVPVAYIVS-----ESDISQAKLIAYLteKLAK 410
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
102-291 |
1.02e-25 |
|
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: 106.99 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 102 GKVRLmITGAAPVSATVLTFLRtALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGE 181
Cdd:cd05934 196 HRLRA-AYGAPNPPELHEEFEE-RFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD-DDGQELPAGEP 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 182 GEVCVKGAN---VFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEA 258
Cdd:cd05934 273 GELVIRGLRgwgFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPA 350
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907187107 259 VAQVFVHG----ESLQAFLIAVVVP-----DVESLPSWAQKR 291
Cdd:cd05934 351 VREAAVVAvpdeVGEDEVKAVVVLRpgetlDPEELFAFCEGQ 392
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
103-291 |
1.24e-25 |
|
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: 107.78 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 KVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTE-CTAGCCLSLPGDW-TAGHVGAPmpcNYVKLVDV-EEMNYLASK 179
Cdd:cd05926 266 KLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEaAHQMTSNPLPPGPrKPGSVGKP---VGVEVRILdEDGEILPPG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 180 GEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAV 259
Cdd:cd05926 343 VVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHPAV 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907187107 260 AQ--VF-----VHGESLQafliAVVVP------DVESLPSWAQKR 291
Cdd:cd05926 422 LEavAFgvpdeKYGEEVA----AAVVLregasvTEEELRAFCRKH 462
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
107-266 |
2.86e-25 |
|
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: 106.84 E-value: 2.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 107 MITGAAPVSATVLTFLRTALGCQFY-EGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGEGEVC 185
Cdd:cd17642 306 IASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELC 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 186 VKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVH 265
Cdd:cd17642 386 VKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAGVA 464
|
.
gi 1907187107 266 G 266
Cdd:cd17642 465 G 465
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
84-284 |
3.07e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 107.16 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 84 NNSLWDKLIFHKIQSSLGGkvrlmitGAAPVSATVLTFLRTAlGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCN 163
Cdd:PRK05677 316 NNEAFRKLDFSALKLTLSG-------GMALQLATAERWKEVT-GCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPST 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 164 YVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEY 243
Cdd:PRK05677 388 LCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFN 465
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907187107 244 IAPEKIENIYLRSEAVAQVFV-------HGESLQAFliaVVVPDVESL 284
Cdd:PRK05677 466 VYPNELEDVLAALPGVLQCAAigvpdekSGEAIKVF---VVVKPGETL 510
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
103-264 |
3.41e-25 |
|
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: 106.55 E-value: 3.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 KVRLMITGAAPVSATVL-TFLRTALGCQFYEGYGQTECTAG---CCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNYLAS 178
Cdd:cd05904 276 SLRQIMSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVvamCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESLPP 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 179 KGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEA 258
Cdd:cd05904 356 NQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEALLLSHPE 434
|
....*.
gi 1907187107 259 VAQVFV 264
Cdd:cd05904 435 ILDAAV 440
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
110-275 |
4.38e-25 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 106.44 E-value: 4.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 110 GAAPVSATVLTFlRTALGCQFYEGYGQTECTAGCCLSLPGDWTA-GHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKG 188
Cdd:PRK12492 342 GTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPGTALKVID-DDGNELPLGERGELCIKG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 189 ANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV---- 264
Cdd:PRK12492 420 PQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAigvp 498
|
170
....*....|....
gi 1907187107 265 ---HGESLQAFLIA 275
Cdd:PRK12492 499 derSGEAVKLFVVA 512
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
102-279 |
2.02e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 101.22 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 102 GKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGE 181
Cdd:PRK07787 241 RGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVD-EDGGPVPHDGE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 182 --GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDR------KKHIFKLAQGEyiapekIENIY 253
Cdd:PRK07787 320 tvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIGAGE------IETAL 393
|
170 180
....*....|....*....|....*....
gi 1907187107 254 LRSEAVAQVFVHGE---SLQAFLIAVVVP 279
Cdd:PRK07787 394 LGHPGVREAAVVGVpddDLGQRIVAYVVG 422
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
103-264 |
2.81e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 101.21 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 KVRLMITGAAPVSATVLT-FLRTALGCQFYEGYGQTECTagcCLSLP-GDWTAGH-------VGAPMPCNYVKLVDVEEM 173
Cdd:PLN02330 304 KLQAIMTAAAPLAPELLTaFEAKFPGVQVQEAYGLTEHS---CITLThGDPEKGHgiakknsVGFILPNLEVKFIDPDTG 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 174 NYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIY 253
Cdd:PLN02330 381 RSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAIL 459
|
170
....*....|.
gi 1907187107 254 LRSEAVAQVFV 264
Cdd:PLN02330 460 LTHPSVEDAAV 470
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
105-252 |
4.81e-23 |
|
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: 100.10 E-value: 4.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 105 RLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPG-DWTAGHVGAPMPCNYVKLVDVEEMNYLASKGEGE 183
Cdd:cd05909 264 RLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGL 343
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907187107 184 VCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 252
Cdd:cd05909 344 LLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDI 410
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
84-283 |
4.85e-23 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 100.34 E-value: 4.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 84 NNSLWDKLIFHKIQSSLGGkvrlmitGAApVSATVLTFLRTALGCQFYEGYGQTECTAGCCLS-LPGDWTAGHVGAPMPC 162
Cdd:PRK08751 319 NTPGFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSPAACINpLTLKEYNGSIGLPIPS 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 163 NYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 242
Cdd:PRK08751 391 TDACIKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSGF 468
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907187107 243 YIAPEKIENIYLRSEAVAQVfvhgeslqaflIAVVVPDVES 283
Cdd:PRK08751 469 NVYPNEIEDVIAMMPGVLEV-----------AAVGVPDEKS 498
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
86-286 |
1.27e-22 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 98.37 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 86 SLWdKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTECTAGCCL--SLPGDWTAGHV--GAPM 160
Cdd:cd05930 193 SLL-RLLLQELELAALPSLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATVDATYyrVPPDDEEDGRVpiGRPI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 161 PCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEA-----LDKDGWLH-TGDIGKWLPNGTLKIIDRKKH 234
Cdd:cd05930 272 PNTRVYVLD-ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDD 350
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907187107 235 IFKLAqGEYIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAVVVPDVESLPS 286
Cdd:cd05930 351 QVKIR-GYRIELGEIEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGGELD 404
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
133-274 |
1.50e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 99.11 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 133 GYGQTECTAGCCLSLPGD------WTaghVGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEAL 206
Cdd:PRK08315 347 AYGMTETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAI 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907187107 207 DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAV--AQVF-V----HGESLQAFLI 274
Cdd:PRK08315 424 DADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIqdVQVVgVpdekYGEEVCAWII 497
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
100-287 |
2.38e-22 |
|
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: 98.09 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 100 LGGKVRLMITGAAPVSATVLTFLRtaLGCQFYEGYGQTE-CTAGCCLSLPGDWTAGHV----------GAPMPCNYVKLV 168
Cdd:cd12119 279 LSSLRRVVIGGSAVPRSLIEAFEE--RGVRVIHAWGMTEtSPLGTVARPPSEHSNLSEdeqlalrakqGRPVPGVELRIV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 169 DvEEMNYLASKGE--GEVCVKGANVFKGYLKDPaRTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAP 246
Cdd:cd12119 357 D-DDGRELPWDGKavGELQVRGPWVTKSYYKND-EESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSG-GEWISS 433
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907187107 247 EKIENIYLRSEAVAQVfvhgeslqafliAVV-VPDveslPSW 287
Cdd:cd12119 434 VELENAIMAHPAVAEA------------AVIgVPH----PKW 459
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
103-334 |
2.80e-22 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 98.84 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 KVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLP-----GDWT-----AGHVGAPMPCNYVKLVDVEE 172
Cdd:PRK08633 899 SLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPET 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 173 MNYLASKGEGEVCVKGANVFKGYLKDPARTAEAL---DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKI 249
Cdd:PRK08633 979 FEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAV 1057
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 250 EniylrsEAVAQVFvHGESLQafLIAVVVPDveslpswaQKRG---------LQGSFEELCR---NKDINKA-------I 310
Cdd:PRK08633 1058 E------EELAKAL-GGEEVV--FAVTAVPD--------EKKGeklvvlhtcGAEDVEELKRaikESGLPNLwkpsryfK 1120
|
250 260
....*....|....*....|....
gi 1907187107 311 LDDLLKLGkeAGLKPFEQVKGIAV 334
Cdd:PRK08633 1121 VEALPLLG--SGKLDLKGLKELAL 1142
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
105-302 |
4.00e-22 |
|
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: 97.07 E-value: 4.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 105 RLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEC--TAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEG 182
Cdd:cd05903 211 RTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECpgAVTSITPAPEDRRLYTDGRPLPGVEIKVVD-DTGATLAPGVEG 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 183 EVCVKGANVFKGYLKDPARTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQV 262
Cdd:cd05903 290 ELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEA 367
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907187107 263 FVHG---ESLQAFLIAVVVPdveslpswaqKRGLQGSFEELCR 302
Cdd:cd05903 368 AVVAlpdERLGERACAVVVT----------KSGALLTFDELVA 400
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
104-267 |
6.71e-22 |
|
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: 96.26 E-value: 6.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFLRTaLGCQFYEGYGQTE-CTAGCCLSlPGDWTA--GHVGAPMPCNYVKLVDVEEmnylASKG 180
Cdd:cd05912 191 LRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIEDDGQ----PPYE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 181 EGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVA 260
Cdd:cd05912 265 VGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPAIK 342
|
....*..
gi 1907187107 261 QVFVHGE 267
Cdd:cd05912 343 EAGVVGI 349
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
133-304 |
1.23e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 96.38 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 133 GYGQTECTAGCCLSLPGD---WTAGHVGAPMPCNYVKLVDVEEmNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKD 209
Cdd:PRK12583 349 AYGMTETSPVSLQTTAADdleRRVETVGRTQPHLEVKVVDPDG-ATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 210 GWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHGeslqafliavvVPDV---ESLPS 286
Cdd:PRK12583 428 GWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG-----------VPDEkygEEIVA 495
|
170 180
....*....|....*....|..
gi 1907187107 287 WAQKR-GLQGSFEEL---CRNK 304
Cdd:PRK12583 496 WVRLHpGHAASEEELrefCKAR 517
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
98-279 |
1.71e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 95.82 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 98 SSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHV------GAPMPCNYVKLVDvE 171
Cdd:PRK06188 281 SSL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD-E 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 172 EMNYLASkGE-GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 250
Cdd:PRK06188 356 DGREVAQ-GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVE 432
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907187107 251 NIYLRSEAVAQVFV-------HGESLQafliAVVVP 279
Cdd:PRK06188 433 DVLAEHPAVAQVAVigvpdekWGEAVT----AVVVL 464
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
97-304 |
2.22e-21 |
|
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: 95.06 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 97 QSSLGGKVRLMITGAAPvSATVLtFLRTALGCQFYEGYGQTEcTAG---CCL------SLPGDWTA--------GHVGAp 159
Cdd:cd12118 243 ARPLPHRVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatVCAwkpewdELPTEERArlkarqgvRYVGL- 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 160 mpcNYVKLVDVEEMNYLASKGE--GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFk 237
Cdd:cd12118 319 ---EEVDVLDPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII- 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907187107 238 LAQGEYIAPEKIENIYLRSEAVAQVFVhgeslqafliaVVVPDveslPSWAQ--------KRGLQGSFEEL---CRNK 304
Cdd:cd12118 394 ISGGENISSVEVEGVLYKHPAVLEAAV-----------VARPD----EKWGEvpcafvelKEGAKVTEEEIiafCREH 456
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
104-291 |
3.26e-21 |
|
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: 94.30 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTflRTALGCQFYEGYGQTECTAGCCLS--LPGDWTagHVGAPMPCNYVKLVDVEEMnyLASKGE 181
Cdd:cd17653 211 LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILDADLQ--PVPEGV 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 182 -GEVCVKGANVFKGYLKDPARTAEAL----DKDGWLH--TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYL 254
Cdd:cd17653 285 vGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEVVL 363
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907187107 255 RSEAVAQ---VFVHGESLQAFliavVVP---DVESLPSWAQKR 291
Cdd:cd17653 364 QSQPEVTqaaAIVVNGRLVAF----VTPetvDVDGLRSELAKH 402
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
6-250 |
5.57e-21 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 94.28 E-value: 5.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 6 LQCVMLCH---GAKIGFFQG-DIRLLMDDLKVLQPTIFPVVPRLLnrmfdrifgqantslkrwlLDFAskrkeaelRSGI 81
Cdd:PLN02246 239 LNSVLLCGlrvGAAILIMPKfEIGALLELIQRHKVTIAPFVPPIV-------------------LAIA--------KSPV 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 82 VRNNSLwdklifhkiqSSlggkVRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTEctAGCCLSL-------PGDWTA 153
Cdd:PLN02246 292 VEKYDL----------SS----IRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTE--AGPVLAMclafakePFPVKS 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 154 GHVGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 233
Cdd:PLN02246 356 GSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLK 435
|
250
....*....|....*..
gi 1907187107 234 HIFKLaQGEYIAPEKIE 250
Cdd:PLN02246 436 ELIKY-KGFQVAPAELE 451
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
116-282 |
5.87e-21 |
|
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: 92.33 E-value: 5.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 116 ATVLTFLRTAlGCQFYEGYGQTECTAGCCLSlPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGY 195
Cdd:cd17637 126 ETIQRFEETT-GATFWSLYGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGY 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 196 LKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENIYLRSEAVAQVFVHGeslqafl 273
Cdd:cd17637 203 WNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHPAIAEVCVIG------- 273
|
....*....
gi 1907187107 274 iavvVPDVE 282
Cdd:cd17637 274 ----VPDPK 278
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
98-260 |
1.54e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 93.10 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 98 SSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLP-GDWTAGHVGAPMPCNYVKLVDVEEM-NY 175
Cdd:PRK07529 333 SSL----RYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRY 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 176 L--ASKGE-GEVCVKGANVFKGYLkDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENI 252
Cdd:PRK07529 409 LrdCAVDEvGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLI-IRGGHNIDPAAIEEA 486
|
....*...
gi 1907187107 253 YLRSEAVA 260
Cdd:PRK07529 487 LLRHPAVA 494
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
107-266 |
3.82e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 91.41 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 107 MITGAAP-VSATVLTFLrtALGCQFYEGYGQTEctAGCCLSLPGDWT-----AGHVGAPMPCNYVKLVDVEEMNYLAskG 180
Cdd:PRK09088 257 LFTGGAPhAAEDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGNDCPA--G 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 181 E-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAV 259
Cdd:PRK09088 331 VpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGI 409
|
....*..
gi 1907187107 260 AQVFVHG 266
Cdd:PRK09088 410 RECAVVG 416
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
104-264 |
4.61e-20 |
|
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: 90.79 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGA-APVSATVLTFLRTALGCQFYEGYGQTECTAGC-CLSLPGDWTAGHV----GAPMPCNYVKLVDvEEMNYLA 177
Cdd:TIGR01733 237 LRLVILGGeALTPALVDRWRARGPGARLINLYGPTETTVWStATLVDPDDAPRESpvpiGRPLANTRLYVLD-DDLRPVP 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 178 SKGEGEVCVKGANVFKGYLKDPARTAE--------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 249
Cdd:TIGR01733 316 VGVVGELYIGGPGVARGYLNRPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEI 394
|
170
....*....|....*
gi 1907187107 250 ENIYLRSEAVAQVFV 264
Cdd:TIGR01733 395 EAALLRHPGVREAVV 409
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
104-274 |
5.02e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 91.63 E-value: 5.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLS-LPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGEG 182
Cdd:PRK06710 325 IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNfLWEKRVPGSIGVPWPDTEAMIMSLETGEALPPGEIG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 183 EVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQV 262
Cdd:PRK06710 405 EIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVLYEHEKVQEV 482
|
170
....*....|....*....
gi 1907187107 263 FV-------HGESLQAFLI 274
Cdd:PRK06710 483 VTigvpdpyRGETVKAFVV 501
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
102-267 |
1.16e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 89.08 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 102 GKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLP-GDWTAGHVGAPMPCNYVKLVDVE-EMNYL--A 177
Cdd:cd05944 121 SSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKVLDgVGRLLrdC 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 178 SKGE-GEVCVKGANVFKGYLKDpARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRS 256
Cdd:cd05944 201 APDEvGEICVAGPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRH 278
|
170
....*....|.
gi 1907187107 257 EAVAQVFVHGE 267
Cdd:cd05944 279 PAVAFAGAVGQ 289
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
104-284 |
1.87e-19 |
|
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: 89.52 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTflRTALGCQFYEGYGQTECTAGCCLSLPG-DWTAGHVGAPMPCN-YVklVDVEEMNYLASKGE 181
Cdd:cd05918 217 LRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGATcWV--VDPDNHDRLVPIGA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 182 -GEVCVKGANVFKGYLKDPARTAEALDKD-GWLH------------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 247
Cdd:cd05918 293 vGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKI-RGQRVELG 371
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907187107 248 KIENIYLRS-----EAVAQVFVH-GESLQAFLIAVVVPDVESL 284
Cdd:cd05918 372 EIEHHLRQSlpgakEVVVEVVKPkDGSSSPQLVAFVVLDGSSS 414
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
23-320 |
3.10e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 89.29 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 23 DIRLLMDDLKVLQPTIFPVVPRLlnrmFDRIfgqantslkrwlldfaskRKEAELRsGIvrnnslwdklifhkiqsSLGG 102
Cdd:PRK05605 298 DIDLILDAMKKHPPTWLPGVPPL----YEKI------------------AEAAEER-GV-----------------DLSG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 kVRLMITGAA--PVSaTVLTFlRTALGCQFYEGYGQTECTA-GCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASK 179
Cdd:PRK05605 338 -VRNAFSGAMalPVS-TVELW-EKLTGGLLVEGYGLTETSPiIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEDPDETMPD 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 180 GE-GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEA 258
Cdd:PRK05605 415 GEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITGGFNVYPAEVEEVLREHPG 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 259 VAQVFVHG-------ESLQAfliAVV-----VPDVESLPSWAQKRgLQG--------SFEELCRN---KDINKAILDDLL 315
Cdd:PRK05605 493 VEDAAVVGlpredgsEEVVA---AVVlepgaALDPEGLRAYCREH-LTRykvprrfyHVDELPRDqlgKVRRREVREELL 568
|
....*
gi 1907187107 316 KLGKE 320
Cdd:PRK05605 569 EKLGA 573
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
103-286 |
9.64e-19 |
|
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: 85.85 E-value: 9.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 KVRLMITGAAPVSAtVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDveemnylaskgEG 182
Cdd:cd17630 112 SLRAVLLGGAPIPP-ELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-----------DG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 183 EVCVKGANVFKGYLKdpARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQV 262
Cdd:cd17630 180 EIWVGGASLAMGYLR--GQLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDA 256
|
170 180
....*....|....*....|....*..
gi 1907187107 263 FVHG---ESLQAFLIAVVVPDVESLPS 286
Cdd:cd17630 257 FVVGvpdEELGQRPVAVIVGRGPADPA 283
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
104-291 |
1.66e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 86.55 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTflrtalGCQ-----FYEGYGQTEcTAGCCLSLPGDWTA---GHVGAPM-PCNyVKLVDveEMN 174
Cdd:PRK03640 256 FRCMLLGGGPAPKPLLE------QCKekgipVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGV 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 175 YLASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYL 254
Cdd:PRK03640 326 VVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLL 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907187107 255 RSEAVAQVFVHGESLQ-------AFLIAVVVPDVESLPSWAQKR 291
Cdd:PRK03640 404 SHPGVAEAGVVGVPDDkwgqvpvAFVVKSGEVTEEELRHFCEEK 447
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
103-291 |
1.76e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 86.75 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 KVRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTECTAGCCLSLPGDWTA--GHVGAPMPCNYVKLVDvEEMNYLASK 179
Cdd:PRK07786 291 ALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSPVTCMLLGEDAIRklGSVGKVIPTVAARVVD-ENMNDVPVG 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 180 GEGEVCVKGANVFKGYLKDPARTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAV 259
Cdd:PRK07786 370 EVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDI 447
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907187107 260 AQVFVHGESLQAF---LIAVVVPD-------VESLPSWAQKR 291
Cdd:PRK07786 448 VEVAVIGRADEKWgevPVAVAAVRnddaaltLEDLAEFLTDR 489
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
102-252 |
2.26e-18 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 86.43 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 102 GKVRLMITGAAPVSA-TVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGH--VGAPMPCNYVKLVDVEEMNYLAS 178
Cdd:PLN02574 319 KSLKQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTEKLSKYssVGLLAPNMQAKVVDWSTGCLLPP 398
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907187107 179 KGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 252
Cdd:PLN02574 399 GNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPADLEAV 471
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
84-283 |
2.89e-18 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 86.23 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 84 NNSLWDKLIFHKIQSSLGGkvrlmitGAAPVSATVLTFLRTAlGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHVGAPMP 161
Cdd:PRK07059 317 NNPDFDKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGLSE-TSPVATCNPVDATEfsGTIGLPLP 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 162 CNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQG 241
Cdd:PRK07059 388 STEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI-LVSG 465
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907187107 242 EYIAPEKIEniylrsEAVAQvfvHGESLQAflIAVVVPDVES 283
Cdd:PRK07059 466 FNVYPNEIE------EVVAS---HPGVLEV--AAVGVPDEHS 496
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
105-254 |
6.51e-18 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 85.18 E-value: 6.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 105 RLMITGAAPVSATVLtflRTAL--GCQFYEGYGQTECTAGCCLSL--PGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKG 180
Cdd:PRK06087 305 RFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSPHAVVNLddPLSRFMHTDGYAAAGVEIKVVD-EARKTLPPGC 380
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907187107 181 EGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYL 254
Cdd:PRK06087 381 EGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDILL 453
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
105-279 |
7.20e-18 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 85.10 E-value: 7.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 105 RLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTA--GCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEG 182
Cdd:PRK13295 315 RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAvtLTKLDDPDERASTTDGCPLPGVEVRVVD-ADGAPLPAGQIG 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 183 EVCVKGANVFKGYLKDPARTAEalDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQV 262
Cdd:PRK13295 394 RLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAIAQV 470
|
170 180
....*....|....*....|
gi 1907187107 263 FVHG---ESLQAFLIAVVVP 279
Cdd:PRK13295 471 AIVAypdERLGERACAFVVP 490
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
104-358 |
7.47e-18 |
|
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: 84.31 E-value: 7.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGE 183
Cdd:cd05972 199 LRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEGD 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 184 VCVKGANV--FKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQ 261
Cdd:cd05972 278 IAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 262 VFV-------HGESLQAFLiaVVVPDVESLPSWAQkrglqgsfeelcrnkdinkaildDLLKLGKEAgLKPFEQVKGIAV 334
Cdd:cd05972 356 AAVvgspdpvRGEVVKAFV--VLTSGYEPSEELAE-----------------------ELQGHVKKV-LAPYKYPREIEF 409
|
250 260
....*....|....*....|....
gi 1907187107 335 HPELfsidngLLTPTLKAKRPELR 358
Cdd:cd05972 410 VEEL------PKTISGKIRRVELR 427
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
127-274 |
9.23e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 84.35 E-value: 9.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 127 GCQFYEGYGQTECTAGCCLSLPGD---WTAghVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGA---NVFKGYLKDPA 200
Cdd:PRK08008 312 GVRLLTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRD-DHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 201 RTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFVHG-------ESLQAFL 273
Cdd:PRK08008 389 ATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVGikdsirdEAIKAFV 467
|
.
gi 1907187107 274 I 274
Cdd:PRK08008 468 V 468
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
98-280 |
1.09e-17 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 84.43 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 98 SSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEctaG--CCLSL--PGDWTAGHVGAPM-PCNYVKLVDvEE 172
Cdd:COG1021 300 SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlvNYTRLddPEEVILTTQGRPIsPDDEVRIVD-ED 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 173 MNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlaQGEYIAPEKIEN 251
Cdd:COG1021 372 GNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQINR--GGEKIAAEEVEN 449
|
170 180 190
....*....|....*....|....*....|
gi 1907187107 252 IYLRSEAVAQVfvhgeslqafliAVV-VPD 280
Cdd:COG1021 450 LLLAHPAVHDA------------AVVaMPD 467
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
133-220 |
1.11e-17 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 84.55 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 133 GYGQTEcTAGCCLSL--PGDwTAGHVGAPMPCNYVKLVDVEemnylaskGEGEVCVKGANVFKGYLKDPARTAEALDKDG 210
Cdd:PRK08180 371 GLGMTE-TAPSATFTtgPLS-RAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEG 440
|
90
....*....|
gi 1907187107 211 WLHTGDIGKW 220
Cdd:PRK08180 441 YYRSGDAVRF 450
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
103-347 |
1.18e-17 |
|
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: 84.41 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 KVRLMITGAAPVSATVLTFLrTALGCQ-------FYEGYGQTEcTAGCCLSLPGDWT-AGHVGAPMPCNYVKLVdveemn 174
Cdd:cd05921 291 RLKLMFYAGAGLSQDVWDRL-QALAVAtvgeripMMAGLGATE-TAPTATFTHWPTErSGLIGLPAPGTELKLV------ 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 175 ylASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWL----PNGTLKIIDRKKHIFKLAQGEYIA--Pek 248
Cdd:cd05921 363 --PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLVFDGRVAEDFKLASGTWVSvgP-- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 249 ieniyLRSEAVAQ-------VFVHGESlQAFLIAVVVPDVESLpswaqkRGLQG----SFEELCRNKDINKAILDDLLKL 317
Cdd:cd05921 439 -----LRARAVAAcaplvhdAVVAGED-RAEVGALVFPDLLAC------RRLVGlqeaSDAEVLRHAKVRAAFRDRLAAL 506
|
250 260 270
....*....|....*....|....*....|
gi 1907187107 318 GKEAGLKPfEQVKGIAVHPELFSIDNGLLT 347
Cdd:cd05921 507 NGEATGSS-SRIARALLLDEPPSIDKGEIT 535
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
104-266 |
1.80e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 83.76 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFLRTAlGCQFYEGYGQTECTAGCCLSLPGDW--TAGHVGAPMPCNYVKLVDvEEMNYLASKGE 181
Cdd:PRK06839 266 VRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELID-ENKNKVEVGEV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 182 GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQ 261
Cdd:PRK06839 344 GELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKLSDVYE 421
|
....*
gi 1907187107 262 VFVHG 266
Cdd:PRK06839 422 VAVVG 426
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
98-280 |
2.20e-17 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 83.62 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 98 SSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWT-AGHVGAPMPCNYVKLVDvEEMNYL 176
Cdd:COG0365 306 SSL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSMGKPVPGYDVAVVD-EDGNPV 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 177 ASKGEGEVCVKGAN--VFKGYLKDPARTAEAL--DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 252
Cdd:COG0365 381 PPGEEGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIESA 459
|
170 180
....*....|....*....|....*....
gi 1907187107 253 YLRSEAVAqvfvhgESlqafliAVV-VPD 280
Cdd:COG0365 460 LVSHPAVA------EA------AVVgVPD 476
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
110-279 |
2.66e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 83.06 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 110 GAAPVSATVLTFLRTAL-GCQFYEGYGQTEcTAGCCLSLPGDWTAGHVG-APMPCNYV--KLVDvEEMNYLASKGEGEVC 185
Cdd:PRK08316 294 GASIMPVEVLKELRERLpGLRFYNCYGQTE-IAPLATVLGPEEHLRRPGsAGRPVLNVetRVVD-DDGNDVAPGEVGEIV 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 186 VKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFV- 264
Cdd:PRK08316 372 HRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEALYTHPAVAEVAVi 449
|
170
....*....|....*...
gi 1907187107 265 ---HGESLQAfLIAVVVP 279
Cdd:PRK08316 450 glpDPKWIEA-VTAVVVP 466
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
104-233 |
3.40e-17 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 82.62 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATvlTFL----RTalGCQFYEGYGQTEctAGCCLSLP--GDWTAGHVGAPMPCNYVKLVDVEEMNYLA 177
Cdd:PRK07514 271 MRLFISGSAPLLAE--THRefqeRT--GHAILERYGMTE--TNMNTSNPydGERRAGTVGFPLPGVSLRVTDPETGAELP 344
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907187107 178 SKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 233
Cdd:PRK07514 345 PGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
95-291 |
3.47e-17 |
|
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: 82.53 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 95 KIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMN 174
Cdd:cd05935 192 EFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGR 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 175 YLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDG---WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 251
Cdd:cd05935 272 ELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEA 350
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907187107 252 IYLRSEAVAQVFV-------HGESLQAFLiaVVVP------DVESLPSWAQKR 291
Cdd:cd05935 351 KLYKHPAI*EVCVisvpderVGEEVKAFI--VLRPeyrgkvTEEDIIEWAREQ 401
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
122-282 |
5.22e-17 |
|
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: 81.91 E-value: 5.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 122 LRTAL-GCQFYEGYGQTECTAGCCL------------SLPgdwtaghVGAPMPCnyVKLVDVEEMNYLASKGE-GEVCVK 187
Cdd:cd05945 234 LQQRFpDARIYNTYGPTEATVAVTYievtpevldgydRLP-------IGYAKPG--AKLVILDEDGRPVPPGEkGELVIS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 188 GANVFKGYLKDPARTAEALDKD---GWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV 264
Cdd:cd05945 305 GPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQVPGVKEAVV 383
|
170 180
....*....|....*....|..
gi 1907187107 265 ----HGESLQAfLIAVVVPDVE 282
Cdd:cd05945 384 vpkyKGEKVTE-LIAFVVPKPG 404
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
97-279 |
5.37e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 82.37 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 97 QSSLGGKVRLMITGAAPVSATVLTFLRtaLGCQFYEGYGQTECTAGCCL--------SLPGDWTAgHVGAPMPCNYVKL- 167
Cdd:PLN03102 296 LSPRSGPVHVLTGGSPPPAALVKKVQR--LGFQVMHAYGLTEATGPVLFcewqdewnRLPENQQM-ELKARQGVSILGLa 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 168 -VDVEEMNYLAS-----KGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQG 241
Cdd:PLN03102 373 dVDVKNKETQESvprdgKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGG 450
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907187107 242 EYIAPEKIENIylrseavaqVFVHGESLQAFLIAVVVP 279
Cdd:PLN03102 451 ENISSVEVENV---------LYKYPKVLETAVVAMPHP 479
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
103-294 |
6.15e-17 |
|
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: 81.71 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 KVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTA--GCCLSLpGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKG 180
Cdd:cd05971 208 KLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLviGNCSAL-FPIKPGSMGKPIPGHRVAIVD-DNGTPLPPGE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 181 EGEVCVK--GANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEA 258
Cdd:cd05971 286 VGEIAVElpDPVAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLKHPA 363
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907187107 259 VAQVFV-------HGESLQAFLiaVVVPDVEslPSWAQKRGLQ 294
Cdd:cd05971 364 VLMAAVvgipdpiRGEIVKAFV--VLNPGET--PSDALAREIQ 402
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
95-286 |
7.84e-17 |
|
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: 81.61 E-value: 7.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 95 KIQSSLGGKVRLMITGAAPVSATVLTFL--RTALGCQFYEGYGQTECTAGCCLSL--PGDWTAGHV--GAPMPCNYVKLV 168
Cdd:cd17655 244 AADDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASIYQyePETDQQVSVpiGKPLGNTRIYIL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 169 DvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 242
Cdd:cd17655 324 D-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGY 401
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907187107 243 YIAPEKIENIYLRSEAVAQ--VFVH-GESLQAFLIAVVVPDvESLPS 286
Cdd:cd17655 402 RIELGEIEARLLQHPDIKEavVIARkDEQGQNYLCAYIVSE-KELPV 447
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
97-302 |
1.74e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 80.76 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 97 QSSLGGKVRLMITGAAPVSAtVLTFLRtALGCQFYEGYGQTEC--TAGCCLSLPGdWTA----------GHVGAPMPC-N 163
Cdd:PRK08162 292 RAGIDHPVHAMVAGAAPPAA-VIAKME-EIGFDLTHVYGLTETygPATVCAWQPE-WDAlplderaqlkARQGVRYPLqE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 164 YVKLVDVEEMNYLASKGE--GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQG 241
Cdd:PRK08162 369 GVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDII-ISGG 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907187107 242 EYIAPEKIENIYLRSEAVaqvfvhgeslqafLIAVVV--PDveslPSWAQ--------KRGLQGSFEEL---CR 302
Cdd:PRK08162 447 ENISSIEVEDVLYRHPAV-------------LVAAVVakPD----PKWGEvpcafvelKDGASATEEEIiahCR 503
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
111-289 |
1.87e-16 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 79.27 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 111 AAPVSATVLTFLRTALGCQFYeGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASkGE-GEVCVKGA 189
Cdd:cd17636 121 AAPEWNDMATVDTSPWGRKPG-GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDGREVPD-GEvGEIVARGP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 190 NVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFVHGesl 269
Cdd:cd17636 198 TVMAGYWNRPEVNARRT-RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERCLRQHPAVADAAVIG--- 272
|
170 180
....*....|....*....|
gi 1907187107 270 qafliavvVPDveslPSWAQ 289
Cdd:cd17636 273 --------VPD----PRWAQ 280
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
103-266 |
4.45e-16 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 79.46 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 KVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAgCCLSLPG-DWTAGHVGAPMPCNYVKLVDVEEMNYLASKgE 181
Cdd:cd05970 302 SLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-E 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 182 GEVCVKGAN-----VFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRS 256
Cdd:cd05970 380 GEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQH 457
|
170
....*....|
gi 1907187107 257 EAVAQVFVHG 266
Cdd:cd05970 458 PAVLECAVTG 467
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
104-291 |
1.62e-15 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 78.36 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITG--AAPVsATVLTFLRTALGCQFYEGYGQTECTAGCCLSL--PGDWTAGHV--GAPMPCNYVKLVDvEEMNyLA 177
Cdd:COG1020 733 LRLVLVGgeALPP-ELVRRWRARLPGARLVNLYGPTETTVDSTYYEvtPPDADGGSVpiGRPIANTRVYVLD-AHLQ-PV 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 178 SKG-EGEVCVKGANVFKGYLKDPARTAEA-----LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 249
Cdd:COG1020 810 PVGvPGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKI-RGFRIELGEI 888
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907187107 250 ENIYLRSEAVAQ--VFVHGESLQA-FLIAVVVPDVESLPSWAQKR 291
Cdd:COG1020 889 EAALLQHPGVREavVVAREDAPGDkRLVAYVVPEAGAAAAAALLR 933
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
104-233 |
2.12e-15 |
|
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: 77.32 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFLRTAL---GCQ---FYEGYGQTECTAGC--CLSLP-GDWTAGH----VGAPMPCNYVKLVDV 170
Cdd:cd05906 291 LRYLVNAGEAVVAKTIRRLLRLLepyGLPpdaIRPAFGMTETCSGViySRSFPtYDHSQALefvsLGRPIPGVSMRIVDD 370
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907187107 171 EemNYLASKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKK 233
Cdd:cd05906 371 E--GQLLPEGEvGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
156-291 |
2.23e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 77.39 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 156 VGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHI 235
Cdd:PRK06178 389 VGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEM 467
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907187107 236 FKLaQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFLiaVVVP----DVESLPSWAQKR 291
Cdd:PRK06178 468 LKV-NGMSVFPSEVEALLGQHPAVLGSAVvgrpdpdKGQVPVAFV--QLKPgadlTAAALQAWCREN 531
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
97-292 |
3.66e-15 |
|
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: 76.61 E-value: 3.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 97 QSSLGGKVRLMITGAAPVSATVLT--FLRTALGCQFYEGYGQTECTAGCCLSLPGD---WTA-GHVGAPMPCNYVKLVDv 170
Cdd:cd17651 248 LGVRLAALRYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 171 EEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 244
Cdd:cd17651 327 AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRI 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907187107 245 APEKIENIYLRSEAVAQ--VFVHGE-SLQAFLIAVVVPDVESLPSWAQKRG 292
Cdd:cd17651 406 ELGEIEAALARHPGVREavVLAREDrPGEKRLVAYVVGDPEAPVDAAELRA 456
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
98-291 |
3.97e-15 |
|
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: 76.47 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 98 SSLGGkVRLMITGAAPVS-ATVLTFLRTALGCQFYEGYGQTECT--AGCCLSLPGDWTAGHV--GAPMPCNYVKLVDveE 172
Cdd:cd12117 246 ECFAG-LRELLTGGEVVSpPHVRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIANTRVYVLD--E 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 173 MNYLASKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 245
Cdd:cd12117 323 DGRPVPPGVpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIE 401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907187107 246 PEKIENIYLRSEAVAQVFV------HGE-SLQAFLIAVVVPDVESLPSWAQKR 291
Cdd:cd12117 402 LGEIEAALRAHPGVREAVVvvredaGGDkRLVAYVVAEGALDAAELRAFLRER 454
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
104-304 |
6.83e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 76.04 E-value: 6.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPvSATVLtFLRTALGCQFYEGYGQTEcTAG----CCL-----SLPGDwTAGHVGAPMPCNYVKL-----VD 169
Cdd:PLN02479 313 VHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWkpewdSLPPE-EQARLNARQGVRYIGLegldvVD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 170 VEEMNYLASKGE--GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 247
Cdd:PLN02479 389 TKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSL 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907187107 248 KIENIYLRSEAVAQVFV-------HGESLQAFLiaVVVPDVESlpswAQKRGLQGSFEELCRNK 304
Cdd:PLN02479 467 EVENVVYTHPAVLEASVvarpderWGESPCAFV--TLKPGVDK----SDEAALAEDIMKFCRER 524
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
110-282 |
8.89e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 75.29 E-value: 8.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 110 GAA-PVSatvLTFLRTALGCQFYEGYGQTECTAGCCL----SLPGdwtaghVGAPMPCNYVKLVDveemnylaskgeGEV 184
Cdd:PRK09029 249 GAAiPVE---LTEQAEQQGIRCWCGYGLTEMASTVCAkradGLAG------VGSPLPGREVKLVD------------GEI 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 185 CVKGANVFKGYLKDPARTAeALDKDGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFV 264
Cdd:PRK09029 308 WLRGASLALGYWRQGQLVP-LVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV 384
|
170
....*....|....*...
gi 1907187107 265 hgeslqafliaVVVPDVE 282
Cdd:PRK09029 385 -----------VPVADAE 391
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
105-275 |
1.17e-14 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 75.06 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 105 RLMITGAAPVSATVLTFLRTALGCQFYEGYGQTE----CTAgccLSLPGDWTAGHVGAPM-PCNYVKLVDvEEMNYLASK 179
Cdd:cd05920 258 RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEgllnYTR---LDDPDEVIIHTQGRPMsPDDEIRVVD-EEGNPVPPG 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 180 GEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAV 259
Cdd:cd05920 334 EEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVENLLLRHPAV 412
|
170 180
....*....|....*....|...
gi 1907187107 260 AQVFV-------HGESLQAFLIA 275
Cdd:cd05920 413 HDAAVvampdelLGERSCAFVVL 435
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
121-266 |
1.40e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 74.92 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 121 FLRTALGCQFYEGYGQTECTAGCCLSLPGDWTA--GHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKD 198
Cdd:PRK06145 284 FTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKD 362
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907187107 199 PARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 266
Cdd:PRK06145 363 PEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
103-286 |
1.59e-14 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 74.92 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 KVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGccLSLPGDWTAGHVGAP-MPCNYVKLVDVEEMNYLASKGE 181
Cdd:PRK05852 296 ALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQ--VTTTQIEGIGQTENPvVSTGLVGRSTGAQIRIVGSDGL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 182 -------GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYL 254
Cdd:PRK05852 374 plpagavGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGVLA 451
|
170 180 190
....*....|....*....|....*....|....*
gi 1907187107 255 RSEAVAQVFVHGESLQAF---LIAVVVPDVESLPS 286
Cdd:PRK05852 452 SHPNVMEAAVFGVPDQLYgeaVAAVIVPRESAPPT 486
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
98-287 |
1.64e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 74.69 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 98 SSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTaGCCLSLP------GDWTAGHVGapmPCNY------V 165
Cdd:PRK07470 280 SSL----RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVT-GNITVLPpalhdaEDGPDARIG---TCGFertgmeV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 166 KLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 245
Cdd:PRK07470 352 QIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVY 428
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907187107 246 PEKIENIYLRSEAVAQVFVHGeslqafliavvVPDveslPSW 287
Cdd:PRK07470 429 PREIEEKLLTHPAVSEVAVLG-----------VPD----PVW 455
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
96-264 |
1.84e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 74.14 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 96 IQSSLGG---KVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSlPGD-WTAGHVGAPMPCNYVKLVDVE 171
Cdd:cd05974 191 IQQDLASfdvKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNS-PGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 172 EmnylASKGEGEVCV-----KGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAP 246
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 1907187107 247 EKIENIYLRSEAVAQVFV 264
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
104-304 |
2.60e-14 |
|
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: 73.94 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGE 183
Cdd:cd05959 282 LRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 184 VCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVF 263
Cdd:cd05959 361 LYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLEAA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907187107 264 VHGESLQAFLI---AVVVPDVESLPSWAQKRGLQgsfeELCRNK 304
Cdd:cd05959 439 VVGVEDEDGLTkpkAFVVLRPGYEDSEALEEELK----EFVKDR 478
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
108-283 |
2.91e-14 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 74.04 E-value: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 108 ITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCV- 186
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIr 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 187 ----KGANVFKGYLKDPARTAEALDKDGWLhTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQV 262
Cdd:cd05928 376 vkpiRPFGLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHPAVVES 453
|
170 180
....*....|....*....|....*...
gi 1907187107 263 FV-------HGESLQAFLiaVVVPDVES 283
Cdd:cd05928 454 AVvsspdpiRGEVVKAFV--VLAPQFLS 479
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
104-275 |
4.30e-14 |
|
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: 73.26 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGE 183
Cdd:cd05919 210 LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEGHTIPPGEEGD 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 184 VCVKGANVFKGYLKDPaRTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVF 263
Cdd:cd05919 289 LLVRGPSAAVGYWNNP-EKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAA 366
|
170
....*....|....*....
gi 1907187107 264 V------HGES-LQAFLIA 275
Cdd:cd05919 367 VvavpesTGLSrLTAFVVL 385
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
8-369 |
4.70e-14 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 73.74 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 8 CV--MLCHGAKIGffQGDIRLLMDDLKVLQPTIFPVVPRLlnrmfdriFGQANTSLKR----------WLLDfaskrKEA 75
Cdd:PTZ00297 662 FVlgLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysWLFE-----RAF 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 76 ELRSGIV----RNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATV-----LTFLRTALGCQ-FYegygqTECTAGCCL 145
Cdd:PTZ00297 727 QLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTSFsllehISVCYVPCLREvFF-----LPSEGVFCV 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 146 SlpgdwtaghvGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGanvfkgylkDPARTAEAldkdgwlhtgdIGKWLPNGT 225
Cdd:PTZ00297 802 D----------GTPAPSLQVDLEPFDEPSDGAGIGQLVLAKKG---------EPRRTLPI-----------AAQWKRDRT 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 226 LKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAfLIAVVVPDVESLP-SWAQKRG--------LQGS 296
Cdd:PTZ00297 852 LRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHCmgegggpaRQLG 930
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907187107 297 FEELCRNKdiNKAILDDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELY 369
Cdd:PTZ00297 931 WTELVAYA--SSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFY 1001
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
109-293 |
2.89e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 70.55 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 109 TGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLsLPGDWTA---GHVGAPMPCNYVKLVDVEEMnyLASKGE-GEV 184
Cdd:cd05922 239 AGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTY-LPPERILekpGSIGLAIPGGEFEILDDDGT--PTPPGEpGEI 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 185 CVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyLRSEAVAQVFV 264
Cdd:cd05922 316 VHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEAA-ARSIGLIIEAA 393
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907187107 265 -------HGESLQAFLIAVVVPDVESLPSWAQKRGL 293
Cdd:cd05922 394 avglpdpLGEKLALFVTAPDKIDPKDVLRSLAERLP 429
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
130-347 |
8.28e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 69.69 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 130 FYEGYGQTEcTAGccLSLPGDWTA---GHVGAPMPCNYVKLVDVEEmNYlaskgegEVCVKGANVFKGYLKDPARTAEAL 206
Cdd:PRK12582 380 FYTGYGATE-TAP--TTTGTHWDTervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAF 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 207 DKDGWLHTGDIGKWL----PNGTLKIIDRKKHIFKLAQGEYIAPEKieniyLRSEAVA-------QVFVHGESlQAFLIA 275
Cdd:PRK12582 449 DEEGFYRLGDAARFVdpddPEKGLIFDGRVAEDFKLSTGTWVSVGT-----LRPDAVAacspvihDAVVAGQD-RAFIGL 522
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907187107 276 VVVPDVESLPSWAQKRGlqGSFEELCRNKDINKAILDDLLKLGKEAGlKPFEQVKGIAVHPELFSIDNGLLT 347
Cdd:PRK12582 523 LAWPNPAACRQLAGDPD--AAPEDVVKHPAVLAILREGLSAHNAEAG-GSSSRIARALLMTEPPSIDAGEIT 591
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
131-279 |
8.62e-13 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 69.33 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 131 YEGYGQTECTAGCCLSlPGDWTA--GHVGAPMPCNyVKLVDvEEMNYLASKGEGEVCVKGANVFKgYLKDPARTAEALDK 208
Cdd:cd05929 273 WEYYGGTEGQGLTIIN-GEEWLThpGSVGRAVLGK-VHILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNE 348
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907187107 209 DGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG---ESLQAFLIAVVVP 279
Cdd:cd05929 349 GGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVGvpdEELGQRVHAVVQP 421
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
104-252 |
1.25e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 69.22 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNylasKGeGE 183
Cdd:PRK06814 909 LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID----EG-GR 983
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 184 VCVKGANVFKGYLK-DPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 252
Cdd:PRK06814 984 LFVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
124-296 |
1.42e-12 |
|
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: 68.47 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 124 TALGCQFYEGYGQTECT--AGCCLSLPGDwTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPAR 201
Cdd:cd12116 260 LSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPAL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 202 TAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQ--VFVHGESLQAF 272
Cdd:cd12116 338 TAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAHPGVAQaaVVVREDGGDRR 416
|
170 180
....*....|....*....|....*
gi 1907187107 273 LIAVVVPDVESLPSWAQ-KRGLQGS 296
Cdd:cd12116 417 LVAYVVLKAGAAPDAAAlRAHLRAT 441
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
86-306 |
3.41e-12 |
|
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: 66.90 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 86 SLWDKLI-FHKIQSSLGGKVRLMITGAA-PVSATVLTFLRTALgCQFYEGYGQTECTAGCCLSLPGDWT-AGHVGAPMPC 162
Cdd:cd17635 100 TLLSKLVsELKSANATVPSLRLIGYGGSrAIAADVRFIEATGL-TNTAQVYGLSETGTALCLPTDDDSIeINAVGRPYPG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 163 NYVKLVDVEEMNyLASKGEGEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGE 242
Cdd:cd17635 179 VDVYLAATDGIA-GPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GV 255
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907187107 243 YIAPEKIENIYLRSEAVAQVFVH-------GESLQAFLIAVVVPDvESLPSwAQKRGLQGSFEELCRNKDI 306
Cdd:cd17635 256 KIAPDEVERIAEGVSGVQECACYeisdeefGELVGLAVVASAELD-ENAIR-ALKHTIRRELEPYARPSTI 324
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
182-280 |
4.17e-12 |
|
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: 67.30 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 182 GEVCVKGANVFKGYLKDPARTAEAL--DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSE 257
Cdd:cd12114 327 GELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIELGEIEAALQAHP 405
|
90 100
....*....|....*....|....*
gi 1907187107 258 AVAQ--VFVHGESLQAFLIAVVVPD 280
Cdd:cd12114 406 GVARavVVVLGDPGGKRLAAFVVPD 430
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
130-291 |
4.90e-12 |
|
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: 66.72 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 130 FYEGYGQTECTAGcclSLPgdwtaghVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKD 209
Cdd:cd17650 256 YYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVEN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 210 GW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAVVVPD 280
Cdd:cd17650 325 PFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAA 403
|
170
....*....|.
gi 1907187107 281 veSLPSWAQKR 291
Cdd:cd17650 404 --ATLNTAELR 412
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
86-291 |
6.41e-12 |
|
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: 66.69 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 86 SLWDKLIFHKIQSSLGG--KVRLMITGAAPVSATVLTFLRTALG--CQFYEGYGQTECTAGCCLSLPGDWTAGH-----V 156
Cdd:cd17644 206 AYWHLLVLELLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpI 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 157 GAPMPC-------NYVKLVDVEEMnylaskgeGEVCVKGANVFKGYLKDPARTAEALDKDGWLH--------TGDIGKWL 221
Cdd:cd17644 286 GRPIANtqvyildENLQPVPVGVP--------GELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYL 357
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907187107 222 PNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAVVVPDVESLPSWAQKR 291
Cdd:cd17644 358 PDGNIEYLGRIDNQVKI-RGFRIELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPHYEESPSTVELR 429
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
86-284 |
7.22e-12 |
|
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: 66.38 E-value: 7.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 86 SLWDKLIFHKIQSSLGGK-VRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEctAGCCLSLPgDWTAGHVGAPMPCNY 164
Cdd:cd05923 250 THLDALAAAAEFAGLKLSsLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTE--AMNSLYMR-DARTGTEMRPGFFSE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 165 VKLVDV-EEMNYLASKG-EGEVCVK--GANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQ 240
Cdd:cd05923 327 VRIVRIgGSPDEALANGeEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISG 404
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907187107 241 GEYIAPEKIENIYLRSEAVAQVFVHG---ESLQAFLIAVVVPDVESL 284
Cdd:cd05923 405 GENIHPSEIERVLSRHPGVTEVVVIGvadERWGQSVTACVVPREGTL 451
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
104-280 |
9.62e-12 |
|
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: 66.14 E-value: 9.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEC----TAGCClslPGDWTAGHV--GAPMPCNYVKLVDvEEMNYLA 177
Cdd:cd17646 255 LRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAaidvTHWPV---RGPAETPSVpiGRPVPNTRLYVLD-DALRPVP 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 178 SKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLH------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIEN 251
Cdd:cd17646 331 VGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEA 409
|
170 180 190
....*....|....*....|....*....|..
gi 1907187107 252 IYLRSEAVAQVFV---HGESLQAFLIAVVVPD 280
Cdd:cd17646 410 ALAAHPAVTHAVVvarAAPAGAARLVGYVVPA 441
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
151-291 |
1.12e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 65.92 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 151 WTAGhvGAPM-PCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKII 229
Cdd:PRK06164 348 IEGG--GRPAsPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQ 425
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 230 DRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFVHGESLQ------AFLIAV--VVPDVESLPSWAQKR 291
Cdd:PRK06164 426 TRMGDSLRLG-GFLVNPAEIEHALEALPGVAAAQVVGATRDgktvpvAFVIPTdgASPDEAGLMAACREA 494
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
105-275 |
1.22e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 65.78 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 105 RLMITGAAPVSATVLTFLRTALGCQFYEGYGQTE----CTAgccLSLPGDWTAGHVGAPM-PCNYVKLVDvEEMNYLASK 179
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEglvnYTR---LDDSDERIFTTQGRPMsPDDEVWVAD-ADGNPLPQG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 180 GEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----GEYIAPEKIENIYLR 255
Cdd:PRK10946 379 EVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEKIAAEEIENLLLR 453
|
170 180
....*....|....*....|....*..
gi 1907187107 256 SEAVAQVF-------VHGESLQAFLIA 275
Cdd:PRK10946 454 HPAVIHAAlvsmedeLMGEKSCAFLVV 480
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
106-291 |
1.36e-11 |
|
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: 65.35 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 106 LMITGAAPVSATVLtflRTALGCQFYEGYGQTECTAGCCLSLP-GDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEV 184
Cdd:cd17652 209 LVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLD-ARLRPVPPGVPGEL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 185 CVKGANVFKGYLKDPARTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSE 257
Cdd:cd17652 285 YIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGEVEAALTEHP 363
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907187107 258 AVAQ--VFVHGESL-QAFLIAVVVPDVESLPSWAQKR 291
Cdd:cd17652 364 GVAEavVVVRDDRPgDKRLVAYVVPAPGAAPTAAELR 400
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
127-290 |
2.27e-11 |
|
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: 64.88 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 127 GCQFYEGYGQTECTAgCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKG-EGEVCVKGANVFKGYLKDPARTAEA 205
Cdd:cd17645 234 GYKLVNNYGPTENTV-VATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGvAGELCIAGEGLARGYLNRPELTAEK 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 206 LDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAF 272
Cdd:cd17645 313 FIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPFLMNHPLIELAAVlakedadGRKYLVAY 391
|
170
....*....|....*...
gi 1907187107 273 LIAVVVPDVESLPSWAQK 290
Cdd:cd17645 392 VTAPEEIPHEELREWLKN 409
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
152-291 |
2.68e-11 |
|
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: 64.64 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 152 TAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAE-------ALDKDGWLHTGDIGKWLPNG 224
Cdd:cd17643 268 AASPIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDG 346
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 225 TLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFV---HGESLQAFLIAVVVPDVESLPSWAQKR 291
Cdd:cd17643 347 ELEYLGRADEQVKI-RGFRIELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDGAAADIAELR 415
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
102-289 |
2.97e-11 |
|
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: 64.31 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 102 GKVRLMITGAAPVSATVLTFLRTAlGCQFYEGYGQTEC--TAGCCLSLPGDWTAGH---VGAPMPcNYVKLVDVEEMNYL 176
Cdd:cd17649 212 PSLRLYIFGGEALSPELLRRWLKA-PVRLFNAYGPTEAtvTPLVWKCEAGAARAGAsmpIGRPLG-GRSAYILDADLNPV 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 177 ASKGEGEVCVKGANVFKGYLKDPARTAEAL--DKDG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 249
Cdd:cd17649 290 PVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RGFRIELGEI 368
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907187107 250 ENIYLRSEAVAQVFVHGES--LQAFLIAVVVP-DVESLPSWAQ 289
Cdd:cd17649 369 EAALLEHPGVREAAVVALDgaGGKQLVAYVVLrAAAAQPELRA 411
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
98-282 |
3.02e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 64.54 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 98 SSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHVGAPMPCNyVKLVDvEEMNY 175
Cdd:PRK08276 262 SSL----RVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-EDGNE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 176 LASKGEGEVCVK-GANVFKgYLKDPARTAEALDKDGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 253
Cdd:PRK08276 335 LPPGEIGTVYFEmDGYPFE-YHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIENLL 411
|
170 180
....*....|....*....|....*....
gi 1907187107 254 LRSEAVAQVFVHGeslqafliavvVPDVE 282
Cdd:PRK08276 412 VTHPKVADVAVFG-----------VPDEE 429
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
134-280 |
3.43e-11 |
|
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: 64.26 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 134 YGQTECT--AGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGW 211
Cdd:cd12115 246 YGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPF 324
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907187107 212 L------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQ--VFVHGESL-QAFLIAVVVPD 280
Cdd:cd12115 325 GpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRSIPGVREavVVAIGDAAgERRLVAYIVAE 401
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
98-279 |
7.27e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 63.56 E-value: 7.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 98 SSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHVGAPMpcnYVKLVDVEEMNY 175
Cdd:PRK13391 275 SSL----EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLAhpGTVGRAM---FGDLHILDDDGA 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 176 LASKGE-GEVCVKGANVFKgYLKDPARTAEALDKDG-WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 253
Cdd:PRK13391 347 ELPPGEpGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAENLL 424
|
170 180
....*....|....*....|....*....
gi 1907187107 254 LRSEAVAQVFVHG---ESLQAFLIAVVVP 279
Cdd:PRK13391 425 ITHPKVADAAVFGvpnEDLGEEVKAVVQP 453
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
159-314 |
1.20e-10 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 62.61 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 159 PMPCNYVK-----LVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEAL-DKDGW--LHTGDIGKwLPNGTLKIID 230
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY-LEDGLLFYQG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 231 RKKHIFKLAqGEYIAPEKIENiYLR-----SEAVAQVFVHGESLQAfLIAVVVPDveslpswaqkrglQGSFEelcRNKD 305
Cdd:PRK04813 396 RIDFQIKLN-GYRIELEEIEQ-NLRqssyvESAVVVPYNKDHKVQY-LIAYVVPK-------------EEDFE---REFE 456
|
....*....
gi 1907187107 306 INKAILDDL 314
Cdd:PRK04813 457 LTKAIKKEL 465
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
104-250 |
2.00e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 61.94 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVS-ATVLTFL---------RTALGCqfyeGYGQTECTAGCCLSLPGD--------------------WTA 153
Cdd:PRK07768 278 LRFALNGAEPIDpADVEDLLdagarfglrPEAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATK 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 154 GHV------GAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLkDPARTAEALDKDGWLHTGDIGKWLPNGTLK 227
Cdd:PRK07768 354 GNTrrlatlGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVV 431
|
170 180
....*....|....*....|...
gi 1907187107 228 IIDRKKHIFKLAqGEYIAPEKIE 250
Cdd:PRK07768 432 VCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
105-284 |
3.27e-10 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 61.31 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 105 RLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDwTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEV 184
Cdd:PRK06155 295 RVRVALGPGVPAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLAPGFEARVVD-EHDQELPDGEPGEL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 185 CVKGANVF---KGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQ 261
Cdd:PRK06155 373 LLRADEPFafaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQVLLSHPAVAA 450
|
170 180
....*....|....*....|....*....
gi 1907187107 262 VFVH------GESlqAFLIAVVVPDVESL 284
Cdd:PRK06155 451 AAVFpvpselGED--EVMAAVVLRDGTAL 477
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
98-282 |
4.83e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 60.74 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 98 SSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAG-----------CCLSLPgdwTAGhVGApmpcnyvK 166
Cdd:PRK08314 305 SSL----RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQthsnppdrpklQCLGIP---TFG-VDA-------R 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 167 LVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEA---LDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEY 243
Cdd:PRK08314 370 VIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFK 448
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907187107 244 IAPEKIENIYLRSEAVAQVFV-------HGESLQafliAVVVPDVE 282
Cdd:PRK08314 449 VWPAEVENLLYKHPAIQEACViatpdprRGETVK----AVVVLRPE 490
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
86-281 |
5.21e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 61.33 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 86 SLWDKLIFHKIQSSLGGKVRLMITGAA-PVSATVLTFlRTALGCQFYEGYGQTECTAGC----CLSLPGDWTAGHVGAPM 160
Cdd:PRK12467 756 SHLQALLQASRVALPRPQRALVCGGEAlQVDLLARVR-ALGPGARLINHYGPTETTVGVstyeLSDEERDFGNVPIGQPL 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 161 PCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKK 233
Cdd:PRK12467 835 ANLGLYILD-HYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMD 913
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907187107 234 HIFKLaQGEYIAPEKIENIYLRSEAVAQVFV--HGESLQAFLIAVVVPDV 281
Cdd:PRK12467 914 HQVKI-RGFRIELGEIEARLLAQPGVREAVVlaQPGDAGLQLVAYLVPAA 962
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
98-274 |
8.97e-10 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 59.84 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 98 SSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCC--LSLPGDWTAGHVGAPMPCNYVKLVDvEEMNY 175
Cdd:cd05973 201 ARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLAnhHALEHPVHAGSAGRAMPGWRVAVLD-DDGDE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 176 LASKGEGEVCVKGANV----FKGYLKDPARTAEAldkdGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 251
Cdd:cd05973 280 LGPGEPGRLAIDIANSplmwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVES 354
|
170 180 190
....*....|....*....|....*....|
gi 1907187107 252 IYLRSEAVAQVFV-------HGESLQAFLI 274
Cdd:cd05973 355 ALIEHPAVAEAAVigvpdpeRTEVVKAFVV 384
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
119-358 |
1.64e-09 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 59.43 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 119 LTFLRtaLGCQFYEGYGQTECTAGCCLSLPGDWTAGH-VGAPMPcnYVKLvdveEMNYLASKGEGEVCVKGANVFKGYLK 197
Cdd:PLN02860 330 LTFMT--LHDPTLESPKQTLQTVNQTKSSSVHQPQGVcVGKPAP--HVEL----KIGLDESSRVGRILTRGPHVMLGYWG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 198 DPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFVHGeSLQAFLIAVV 277
Cdd:PLN02860 402 QNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVG-VPDSRLTEMV 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 278 VPDVESLPSW--------AQKRGLQGSFEEL---CRNKdinkailddllklgkeaGLKPFEQVKGIAVHPELFSidnglL 346
Cdd:PLN02860 480 VACVRLRDGWiwsdnekeNAKKNLTLSSETLrhhCREK-----------------NLSRFKIPKLFVQWRKPFP-----L 537
|
250
....*....|..
gi 1907187107 347 TPTLKAKRPELR 358
Cdd:PLN02860 538 TTTGKIRRDEVR 549
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
103-261 |
1.75e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 59.34 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 KVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMnylaSKGeG 182
Cdd:PRK08043 480 RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGI----EQG-G 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 183 EVCVKGANVFKGYLK--DP-------ARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 253
Cdd:PRK08043 555 RLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSLEMVEQLA 633
|
....*...
gi 1907187107 254 LRSEAVAQ 261
Cdd:PRK08043 634 LGVSPDKQ 641
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
156-363 |
2.60e-09 |
|
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: 58.65 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 156 VGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKKHI 235
Cdd:cd05908 316 VGKPIDETDIRICD-EDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGREKDI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 236 FkLAQGEYIAPEKIENiylrseavaqvfvhgeslqaflIAVVVPDVESlpswaQKRGLQGSFEELCRNKDI-----NKAI 310
Cdd:cd05908 394 I-FVNGQNVYPHDIER----------------------IAEELEGVEL-----GRVVACGVNNSNTRNEEIfcfieHRKS 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907187107 311 LDDLLKLGKEAGlKPFEQVKGIAVHpELFSIDNGLLTPTLKAKRPELRNYFRS 363
Cdd:cd05908 446 EDDFYPLGKKIK-KHLNKRGGWQIN-EVLPIRRIPKTTSGKVKRYELAQRYQS 496
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
104-251 |
5.29e-09 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 57.60 E-value: 5.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFLRTAL--GCQFYEGYGQTEC------TAGCCLSLPGDWT---AGH-VGAPMPCNYVKLVDV- 170
Cdd:PRK09274 290 LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEAlpissiESREILFATRAATdngAGIcVGRPVDGVEVRIIAIs 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 171 -------EEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEA--LDKDG--WLHTGDIGkWL-PNGTLKIIDRKKHIFKL 238
Cdd:PRK09274 370 dapipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVET 448
|
170
....*....|....*
gi 1907187107 239 AQGEY--IAPEKIEN 251
Cdd:PRK09274 449 AGGTLytIPCERIFN 463
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
127-282 |
6.97e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 57.38 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 127 GCQFYEGYGQTEctAGCCLSLPGDWTAGHVGAPMPCnyVKLVDVE--------------EMNYLASKGEgEVCVKGANVF 192
Cdd:PRK07867 290 GCVVVDGFGSTE--GGVAITRTPDTPPGALGPLPPG--VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNTAGPGGF 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 193 KGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHGeslqaf 272
Cdd:PRK07867 365 EGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA------ 436
|
170
....*....|
gi 1907187107 273 liavvVPDVE 282
Cdd:PRK07867 437 -----VPDPV 441
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
98-280 |
8.17e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 57.02 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 98 SSLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTE------CTAGCCLSLPGDwtaghVGAPMPCNYVKLVDvE 171
Cdd:PRK12406 271 SSL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTEsgavtfATSEDALSHPGT-----VGKAAPGAELRFVD-E 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 172 EMNYLASKGEGEVCVK--GANVFKgYLKDPARTAEaLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKI 249
Cdd:PRK12406 341 DGRPLPQGEIGEIYSRiaGNPDFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEI 417
|
170 180 190
....*....|....*....|....*....|....
gi 1907187107 250 ENIYLRSEAVAQVFVHG---ESLQAFLIAVVVPD 280
Cdd:PRK12406 418 EAVLHAVPGVHDCAVFGipdAEFGEALMAVVEPQ 451
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
102-274 |
8.24e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 57.08 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 102 GKVRLMITGAAPVSATVLTFLRTALG-CQFYEG-----YGQTECTAGCCLSLPG-----------DWTAGH----VGAPM 160
Cdd:PRK05851 272 GALRVALNGGEPVDCDGFERFATAMApFGFDAGaaapsYGLAESTCAVTVPVPGiglrvdevttdDGSGARrhavLGNPI 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 161 PCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPartaeALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFKLAq 240
Cdd:PRK05851 352 PGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVA- 424
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907187107 241 GEYIAPEKIENIY-----LRSEAVAQVFVHGESLQAFLI 274
Cdd:PRK05851 425 GRNIFPTEIERVAaqvrgVREGAVVAVGTGEGSARPGLV 463
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
157-250 |
8.52e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 56.94 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 157 GAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPArTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIF 236
Cdd:PRK09192 388 GKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLG-YLLDGYLYITGRAKDLI 464
|
90
....*....|....
gi 1907187107 237 kLAQGEYIAPEKIE 250
Cdd:PRK09192 465 -IINGRNIWPQDIE 477
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
127-284 |
8.98e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 56.96 E-value: 8.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 127 GCQFYEGYGQTEctAGCCLSLPGDWTAGHVGAPMPCnyVKLVDVE-----------EMNYLASKGE--GE-VCVKGANVF 192
Cdd:PRK13388 288 GCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGAPG--VAIYNPEtltecavarfdAHGALLNADEaiGElVNTAGAGFF 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 193 KGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHG----ES 268
Cdd:PRK13388 364 EGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYAvpdeRV 441
|
170
....*....|....*.
gi 1907187107 269 LQAFLIAVVVPDVESL 284
Cdd:PRK13388 442 GDQVMAALVLRDGATF 457
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
102-280 |
2.58e-08 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 55.32 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 102 GKVRLMITGAAPVSATVLT-FLRTALGCQF-----YEGYGQTECT----------AGCCLSLPGDWTAGHV--------- 156
Cdd:cd05931 271 SSWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATlfvsggppgtGPVVLRVDRDALAGRAvavaaddpa 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 157 -------GAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAE------ALDKDGWLHTGDIGkWLPN 223
Cdd:cd05931 351 arelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTGDLG-FLHD 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907187107 224 GTLKIIDRKKHIFKLAqGEYIAPEKIENiylrseAVAQvfVHGESLQAFLIAVVVPD 280
Cdd:cd05931 430 GELYITGRLKDLIIVR-GRNHYPQDIEA------TAEE--AHPALRPGCVAAFSVPD 477
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
104-262 |
3.19e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 55.40 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFL-----RTAlgcQFYeGYGQTECTAGCclsLPGD------WTAGHVGAPMPCNYVKLVDVEE 172
Cdd:PRK05857 288 LRLVGYGGSRAIAADVRFIeatgvRTA---QVY-GLSETGCTALC---LPTDdgsivkIEAGAVGRPYPGVDVYLAATDG 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 173 MNYLASKGE-----GEVCVKGANVFKGYLKDPARTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 247
Cdd:PRK05857 361 IGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPD 438
|
170
....*....|....*
gi 1907187107 248 KIENIylrSEAVAQV 262
Cdd:PRK05857 439 EVDRI---AEGVSGV 450
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
156-282 |
4.37e-08 |
|
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: 54.79 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 156 VGAPMPCNYVKLVDVEEMnyLASKGE-GEVCVKGANVFKGYLKDPARTAEALDKDGW------LHTGDIGKWLPNGTLKI 228
Cdd:cd17656 303 IGKPISNTWIYILDQEQQ--LQPQGIvGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEF 380
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907187107 229 IDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQ--VFVHGESL-QAFLIAVVVPDVE 282
Cdd:cd17656 381 LGRADHQVKI-RGYRIELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVMEQE 436
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
103-280 |
4.50e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 55.35 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 KVRLMITGAAPVSATVLTFLRTALGCQF-YEGYGQTECTA-----GCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYL 176
Cdd:PRK12316 2262 AVRVYCFGGEAVPAASLRLAWEALRPVYlFNGYGPTEAVVtpllwKCRPQDPCGAAYVPIGRALGNRRAYILD-ADLNLL 2340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 177 ASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 249
Cdd:PRK12316 2341 APGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEI 2419
|
170 180 190
....*....|....*....|....*....|....
gi 1907187107 250 ENIYLRSEAVAQVFV---HGESLQAfLIAVVVPD 280
Cdd:PRK12316 2420 EARLQAHPAVREAVVvaqDGASGKQ-LVAYVVPD 2452
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
129-252 |
5.48e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 54.44 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 129 QFYEGYGQTECTAgcCLSLPGDWTAGH---VGAPMPCNYVKLVDvEEMNYLASKGE-GEVCVKGANVFKGYL-KDPARTA 203
Cdd:PRK06334 327 QLRQGYGTTECSP--VITINTVNSPKHescVGMPIRGMDVLIVS-EETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGF 403
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907187107 204 EALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 252
Cdd:PRK06334 404 VELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEALESI 451
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
86-266 |
5.65e-08 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 54.40 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 86 SLWDKLIFHKIQS-----SLggkvRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGA-- 158
Cdd:PRK05620 281 TLWIQLMVHYLKNppermSL----QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWay 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 159 -------PMPCNYvKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPART----------------AEALDKDGWLHTG 215
Cdd:PRK05620 357 rvsqgrfPASLEY-RIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADGWLRTG 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907187107 216 DIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEAVAQVFVHG 266
Cdd:PRK05620 436 DVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
165-266 |
1.05e-07 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 53.60 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 165 VKLVDvEEMNYLASKGE--GEVCVKGANVFKGYLKDparTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGE 242
Cdd:PRK06018 367 MKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYYRV---DGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIK-SGGE 441
|
90 100
....*....|....*....|....
gi 1907187107 243 YIAPEKIENIYLRSEAVAQVFVHG 266
Cdd:PRK06018 442 WISSIDLENLAVGHPKVAEAAVIG 465
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
104-275 |
1.41e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 53.63 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTE----CTAGCCLSLPGDWTAghVGAPMPCNYVKLVDvEEMNYLAS 178
Cdd:PRK05691 1390 LRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTEtainVTHWQCQAEDGERSP--IGRPLGNVLCRVLD-AELNLLPP 1466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 179 KGEGEVCVKGANVFKGYLKDPARTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIEN 251
Cdd:PRK05691 1467 GVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVEPEEIQA 1545
|
170 180
....*....|....*....|....*.
gi 1907187107 252 IYLRSEAVAQ--VFVHGESLQAFLIA 275
Cdd:PRK05691 1546 RLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
179-260 |
2.97e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 52.02 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 179 KGEGEVCVKGANVFKGYLKdpaRTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEA 258
Cdd:PRK07008 382 KAFGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIENVAVAHPA 456
|
..
gi 1907187107 259 VA 260
Cdd:PRK07008 457 VA 458
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
103-292 |
4.93e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 52.09 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 KVRLMITG--AAPVSATVLTFLRtaLG-CQFYEGYGQTECTAG-----CCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMN 174
Cdd:PRK12467 1835 SLRRVVCGgeALEVEALRPWLER--LPdTGLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIANLSTYILD-ASLN 1911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 175 YLASKGEGEVCVKGANVFKGYLKDPARTAEAL------DKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 247
Cdd:PRK12467 1912 PVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELG 1990
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907187107 248 KIENIYLRSEAVAQ--VFVHGESLQAFLIAVVVPDVESLPSWAQKRG 292
Cdd:PRK12467 1991 EIEARLREQGGVREavVIAQDGANGKQLVAYVVPTDPGLVDDDEAQV 2037
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
103-268 |
5.24e-07 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 50.87 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 103 KVRLMITGAAPVSATVLTFLRTAL-GCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCnyvklVDVEEMNYlASKGE 181
Cdd:cd17633 111 KIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPN-----VEIEIRNA-DGGEI 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 182 GEVCVKGANVFKGYLKdpartAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQ 261
Cdd:cd17633 185 GKIFVKSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEE 258
|
....*..
gi 1907187107 262 VFVHGES 268
Cdd:cd17633 259 AIVVGIP 265
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
100-294 |
1.25e-06 |
|
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: 50.17 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 100 LGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASK 179
Cdd:cd05958 211 DLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDG 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 180 GEGEVCVKGANVFKgYLKDPARTAEAldKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAV 259
Cdd:cd05958 290 TIGRLAVRGPTGCR-YLADKRQRTYV--QGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAV 365
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907187107 260 AQVFVHGESLQAFLI---AVVVPDVESLPSWAQKRGLQ 294
Cdd:cd05958 366 AECAVVGHPDESRGVvvkAFVVLRPGVIPGPVLARELQ 403
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
131-302 |
1.30e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 50.73 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 131 YEGYGQTECTAG-CCLSLPGDWTAG----HVGAPMPCNYVKLVDVEeMNYLASKGEGEVCVKGANVFKGYLKDPARTAE- 204
Cdd:PRK12316 4839 FNGYGPTETTVTvLLWKARDGDACGaaymPIGTPLGNRSGYVLDGQ-LNPLPVGVAGELYLGGEGVARGYLERPALTAEr 4917
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 205 ----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVHGE--SLQAFLIAV 276
Cdd:PRK12316 4918 fvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKI-RGFRIELGEIEARLREHPAVREAVVIAQegAVGKQLVGY 4996
|
170 180
....*....|....*....|....*..
gi 1907187107 277 VVPDVESL-PSWAQKRGLQGSFEELCR 302
Cdd:PRK12316 4997 VVPQDPALaDADEAQAELRDELKAALR 5023
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
129-266 |
1.91e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 49.39 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 129 QFYEGYGQTECTAGCCLSlPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGE-GEVCVKGANVFKGYLKDpARTAEALD 207
Cdd:PRK07638 281 KLYEFYGASELSFVTALV-DEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEiGTVYVKSPQFFMGYIIG-GVLARELN 358
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907187107 208 KDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAVAQVFVHG 266
Cdd:PRK07638 359 ADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVDEIVVIG 416
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
104-261 |
2.10e-06 |
|
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: 49.38 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFLRTAL--GCQFYEGYGQTECTAGCC------LSLPGDWTAGH----VGAPMPCNYVKLVDVE 171
Cdd:cd05910 201 LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVRIIEID 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 172 EMNY--------LASKGEGEVCVKGANVFKGYLKDPARTAEALDKDG----WLHTGDIGKWLPNGTLKIIDRKKHIFKLA 239
Cdd:cd05910 281 DEPIaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITT 360
|
170 180
....*....|....*....|..
gi 1907187107 240 QGEYIApEKIENIYLRSEAVAQ 261
Cdd:cd05910 361 GGTLYT-EPVERVFNTHPGVRR 381
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
115-285 |
3.22e-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: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 115 SATVLTFLRTALGCQFYEGYGQTEC--TAGCCLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVF 192
Cdd:cd17648 220 TAPVFEKLRSRFAGLIINAYGPTETtvTNHKRFFPGDQRFDKSLGRPVRNTKCYVLN-DAMKRVPVGAVGELYLGGDGVA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 193 KGYLKDPARTAE-------------ALDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEA 258
Cdd:cd17648 299 RGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQVKI-RGQRIEPGEVEAALASYPG 377
|
170 180 190
....*....|....*....|....*....|....*
gi 1907187107 259 VAQVFV--------HGESLQAFLIAVVVPDVESLP 285
Cdd:cd17648 378 VRECAVvakedasqAQSRIQKYLVGYYLPEPGHVP 412
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
104-282 |
1.04e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTEcTAGCCLSLPGDWTA--GHVGAPMpCNYVKLVDvEEMNYLASKGE 181
Cdd:PRK13390 272 LRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSV-LGDLHICD-DDGNELPAGRI 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 182 GEVCVKGANVFKGYLKDPARTAEALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEAV 259
Cdd:PRK13390 349 GTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMHPAV 427
|
170 180
....*....|....*....|...
gi 1907187107 260 AQVFVHGeslqafliavvVPDVE 282
Cdd:PRK13390 428 HDVAVIG-----------VPDPE 439
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
127-277 |
1.33e-05 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 46.95 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 127 GCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVdVEEMNYLASKGEGEVCVKGANVFKGYLKDPArtaEAL 206
Cdd:PRK06060 286 GIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVV-APDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---SPV 361
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907187107 207 DKDGWLHTGDIGKWLPNGTLKIIDRKKHIfKLAQGEYIAPEKIENIYLRSEAVAQVFVHG-------ESLQAFLIAVV 277
Cdd:PRK06060 362 ANEGWLDTRDRVCIDSDGWVTYRCRADDT-EVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLVATS 438
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
156-275 |
1.46e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.47 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 156 VGAPMPCNYVKLVDvEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGW-------LHTGDIGKWLPNGTLKI 228
Cdd:PRK05691 4042 IGSPTDNNRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEY 4120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907187107 229 IDRKKHI-----FKLAQGEyIAPEKIENIYLRSEAVA-QVFVHGESLQAFLIA 275
Cdd:PRK05691 4121 VGRIDHQvkirgYRIELGE-IEARLHEQAEVREAAVAvQEGVNGKHLVGYLVP 4172
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
105-299 |
4.12e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 45.72 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 105 RLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHV--GAPMPCNYVKLVDVEeMNYLASKGEG 182
Cdd:PRK12316 774 RIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIANLACYILDAN-LEPVPVGVLG 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 183 EVCVKGANVFKGYLKDPARTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRS 256
Cdd:PRK12316 853 ELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEH 931
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907187107 257 EAVAQVFVHGESLQAfLIAVVVPDVE--SLPSwAQKRGLQGSFEE 299
Cdd:PRK12316 932 PWVREAAVLAVDGKQ-LVGYVVLESEggDWRE-ALKAHLAASLPE 974
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
110-291 |
4.24e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 45.04 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 110 GAAPVSATVLTfLRTALGCQFYEGYGQTEcTAGCCLslpgdwtagHVGAPMPCNYVKLVDveemnylaskgeGEVCVKGA 189
Cdd:PRK07824 159 GGGPAPAPVLD-AAAAAGINVVRTYGMSE-TSGGCV---------YDGVPLDGVRVRVED------------GRIALGGP 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 190 NVFKGY--LKDPARTAEaldkDGWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEAVAQVFVHG- 266
Cdd:PRK07824 216 TLAKGYrnPVDPDPFAE----PGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLPQVVEAALATHPAVADCAVFGl 289
|
170 180
....*....|....*....|....*..
gi 1907187107 267 --ESLQAFLIAVVVPDVESLPSWAQKR 291
Cdd:PRK07824 290 pdDRLGQRVVAAVVGDGGPAPTLEALR 316
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
157-250 |
8.04e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.77 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 157 GAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEA-LDKDG--WLHTGDIGkWLPNGTLKIIDRKK 233
Cdd:PRK05691 373 GRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfVEHDGrtWLRTGDLG-FLRDGELFVTGRLK 451
|
90
....*....|....*..
gi 1907187107 234 HIFkLAQGEYIAPEKIE 250
Cdd:PRK05691 452 DML-IVRGHNLYPQDIE 467
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
163-273 |
8.21e-05 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 44.34 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 163 NYVKLVDVEEMNYLASKGEGE----VCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKL 238
Cdd:cd05915 338 IPLVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKS 417
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1907187107 239 AqGEYIAPEKIENIYLRSEAVAQVFV-------HGESLQAFL 273
Cdd:cd05915 418 G-GEWISSVDLENALMGHPKVKEAAVvaiphpkWQERPLAVV 458
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
182-265 |
8.87e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 44.65 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 182 GEVCVKGANVFKGYLKDPARTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLR 255
Cdd:PRK10252 803 GDLYLTGIQLAQGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRAMQA 881
|
90
....*....|
gi 1907187107 256 SEAVAQVFVH 265
Cdd:PRK10252 882 LPDVEQAVTH 891
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-290 |
1.17e-04 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 43.52 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 177 ASKGEGEVCVKGaNVFKGYLKDPARTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 253
Cdd:cd05924 210 GSGGVGWIARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTG-GEKVFPEEVEEAL 287
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907187107 254 LRSEAVAQVFVHGeslqafliavvVPDveslPSWAQK 290
Cdd:cd05924 288 KSHPAVYDVLVVG-----------RPD----ERWGQE 309
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
9-283 |
1.47e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.18 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 9 VMLCHGAKIGFFQG--DIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSLKRWLLDFASKRKEAELRSGIVRNNS 86
Cdd:PRK12316 3214 VGIRHSALSNHLCWmqQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHA 3293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 87 LWDKL--IFHKIQSSLGGKVRLMITGAAPVSATVLTflRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGH--VGAPMPC 162
Cdd:PRK12316 3294 YPSMLqaFLEEEDAHRCTSLKRIVCGGEALPADLQQ--QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIAN 3371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 163 NYVKLVDVEeMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIF 236
Cdd:PRK12316 3372 RACYILDGS-LEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQV 3450
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907187107 237 KLaQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAfLIAVVVPDVES 283
Cdd:PRK12316 3451 KI-RGFRIELGEIEARLLEHPWVREAVVLAVDGRQ-LVAYVVPEDEA 3495
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
104-289 |
1.88e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.54 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 104 VRLMITGAAPVSATVLTFLRTALGCQ-FYEGYGQTE-------CTAGccLSLPGDWTAGHVGAPMPCNYVKLVDvEEMNY 175
Cdd:PRK05691 2450 VRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTEtvvmplaCLAP--EQLEEGAASVPIGRVVGARVAYILD-ADLAL 2526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 176 LASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 248
Cdd:PRK05691 2527 VPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQVKI-RGFRIELGE 2605
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907187107 249 IENIYLRSEAV--AQVFVHGESLQAFLIAVVVPDVESLPSWAQ 289
Cdd:PRK05691 2606 IESRLLEHPAVreAVVLALDTPSGKQLAGYLVSAVAGQDDEAQ 2648
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
129-282 |
3.76e-03 |
|
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: 39.26 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 129 QFYEGYGQTECTAGCcLSLPG-DWTAGHVGA----PMPCNYVKlVDVEEMNYL---------ASKGEGEVCVKGAN---V 191
Cdd:cd05940 222 RIAEFYAATEGNSGF-INFFGkPGAIGRNPSllrkVAPLALVK-YDLESGEPIrdaegrcikVPRGEPGLLISRINpleP 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907187107 192 FKGYLkDPARTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEAVAQVFVH 265
Cdd:cd05940 300 FDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANVY 377
|
170
....*....|....*..
gi 1907187107 266 GeslqafliaVVVPDVE 282
Cdd:cd05940 378 G---------VQVPGTD 385
|
|
| |
