|
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 ... |
1-369 |
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: 661.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 1 MFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFH--QADTSLKRWLLEFAAKRKQAEVR 78
Cdd:cd05927 171 IFERVVEALFLYHGAKIGFYSGDIRLLLDDIKALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 79 SGIIRNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGA 158
Cdd:cd05927 251 SGVVRASPFWDKLVFNKIKQALGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGG 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 159 PLPCNHIKLVDAEELNYW--TCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIF 236
Cdd:cd05927 331 PLPCAEVKLVDVPEMNYDakDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIF 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 237 KLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKK-GIEGTYQELCMKKELKKAILDDMV 315
Cdd:cd05927 411 KLSQGEYVAPEKIENIYARSPFVAQIFVYGDSLKSFLVAIVVPDPDVLKEWAASKgGGTGSFEELCKNPEVKKAILEDLV 490
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1907081048 316 MLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 369
Cdd:cd05927 491 RLGKENGLKGFEQVKAIHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
1-369 |
8.01e-171 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 491.15 E-value: 8.01e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 1 MFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLLEFAAKRKQAEVR 78
Cdd:PLN02736 274 IYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESggLKERLFNAAYNAKKQALE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 79 SGiiRNNS-IWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVG 157
Cdd:PLN02736 354 NG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 158 APLPCNHIKLVDAEELNYwTCKGE----GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK 233
Cdd:PLN02736 432 SPNPACEVKLVDVPEMNY-TSEDQpyprGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKK 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 234 HIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKKGIE-GTYQELCMKKELKKAILD 312
Cdd:PLN02736 511 NIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVLA 590
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081048 313 DMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 369
Cdd:PLN02736 591 DMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMY 647
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
2-369 |
1.95e-115 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 347.86 E-value: 1.95e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 2 FERVIQSVVYCHGGRVGFfQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLLEFA---AKRKQAE 76
Cdd:COG1022 237 FERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAggLKRKLFRWAlavGRRYARA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 77 VRSGiiRNNSIW--------DELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTP 148
Cdd:COG1022 316 RLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVITVNRP 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 149 GDWTSGHVGAPLPCNHIKLvdAEElnywtckgeGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKI 228
Cdd:COG1022 393 GDNRIGTVGPPLPGVEVKI--AED---------GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRI 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 229 IDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKaFLVGIVVPDPEVMPSWAQKKGIE-GTYQELCMKKELK 307
Cdd:COG1022 462 TGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDGRP-FLAALIVPDFEALGEWAEENGLPyTSYAELAQDPEVR 540
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081048 308 KAILDDMVMLGKesGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 369
Cdd:COG1022 541 ALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALY 600
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1-357 |
6.78e-115 |
|
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: 341.50 E-value: 6.78e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 1 MFERV-IQSVVYCHGGRVGFFQgDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLKRWLLEFAAkrkqaevrs 79
Cdd:cd05907 140 VFERRaGLYVPLLAGARIYFAS-SAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV--------- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 80 giirnnsiwdelffnkiqaslGGHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAP 159
Cdd:cd05907 210 ---------------------GGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKP 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 160 LPCNHIKLVDaeelnywtckgEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLA 239
Cdd:cd05907 268 LPGVEVRIAD-----------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITS 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 240 QGEYVAPEKIENIYIRSEPVAQIYVHGDSLKaFLVGIVVPDPEVMPSWAQKKGIEG-TYQELCMKKELKKAILDDMVMLG 318
Cdd:cd05907 337 GGKNISPEPIENALKASPLISQAVVIGDGRP-FLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAAN 415
|
330 340 350
....*....|....*....|....*....|....*....
gi 1907081048 319 KEsgLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPEL 357
Cdd:cd05907 416 AR--LSRYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
2-354 |
5.97e-111 |
|
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: 333.41 E-value: 5.97e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 2 FERVIQSVVYCHGGRVGFfqGDIRLLSD--------DMKALRPTIFPVVPRLLNRMYDKIFHQADT--SLKRWLLEFAAK 71
Cdd:cd17639 144 FELAAENVCLYRGGTIGY--GSPRTLTDkskrgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPmgGLKRTLFWTAYQ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 72 RKQAEVRSGIirNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDW 151
Cdd:cd17639 222 SKLKALKEGP--GTPLLDELVFKKVRAALGGRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 152 TSGHVGAPLPCNHIKLVDAEELNYWTCKGE--GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKII 229
Cdd:cd17639 299 ETGRVGPPLPCCEIKLVDWEEGGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKII 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 230 DRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKKG-IEGTYQELCMKKELKK 308
Cdd:cd17639 379 DRKKDLVKLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGvINSEWEELCEDKKLQK 458
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907081048 309 AILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKR 354
Cdd:cd17639 459 AVLKSLAETARAAGLEKFEIPQGVVLLDEEWTPENGLVTAAQKLKR 504
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
1-369 |
1.71e-107 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 329.67 E-value: 1.71e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 1 MFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLLEFAAKRKQAEVR 78
Cdd:PLN02614 281 IFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYKFGNMK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 79 SGI--IRNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GH 155
Cdd:PLN02614 361 KGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMlGT 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 156 VGAPLPCNHIKLVDAEELNY--WTCKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKK 233
Cdd:PLN02614 441 VGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKK 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 234 HIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKKGIEGTYQELCMKKELKKAILDD 313
Cdd:PLN02614 520 NIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGE 599
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081048 314 MVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 369
Cdd:PLN02614 600 LVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
1-369 |
1.44e-104 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 321.79 E-value: 1.44e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 1 MFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFH--QADTSLKRWLLEFAAKRKQAEVR 78
Cdd:PLN02861 278 VYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQkiSSGGMLRKKLFDFAYNYKLGNLR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 79 SGIIRNNS--IWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTS--G 154
Cdd:PLN02861 358 KGLKQEEAspRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGC-FTSIANVFSmvG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 155 HVGAPLPCNHIKLVDAEELNY--WTCKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRK 232
Cdd:PLN02861 437 TVGVPMTTIEARLESVPEMGYdaLSDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRK 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 233 KHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKKGIEGTYQELCMKKELKKAILD 312
Cdd:PLN02861 516 KNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILD 595
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081048 313 DMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 369
Cdd:PLN02861 596 ELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
1-369 |
2.50e-95 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 297.88 E-value: 2.50e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 1 MFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFH--QADTSLKRWLLEFAAKRKQAEVR 78
Cdd:PLN02430 278 ILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYKLAWMN 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 79 SGIIRNNS--IWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GH 155
Cdd:PLN02430 358 RGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMlGT 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 156 VGAPLPCNHIKLVDAEELNYwTCKGE---GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRK 232
Cdd:PLN02430 438 VGAPAVYNELRLEEVPEMGY-DPLGEpprGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRK 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 233 KHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKKGIEGTYQELCMKKELKKAILD 312
Cdd:PLN02430 516 KNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILS 595
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081048 313 DMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 369
Cdd:PLN02430 596 ELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
30-369 |
1.08e-85 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 273.53 E-value: 1.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 30 DMKALRPTIFPVVPRLLNRMYDKIFHQADTS--LKRWLLEFAAKRKQAEVR------SGIIRnnSIWDELFFNKIQASLG 101
Cdd:PLN02387 342 DASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIRAVLG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 102 GHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTCKG- 180
Cdd:PLN02387 420 GRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKp 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 181 --EGEICVKGPNVFKGYLKDEDRTKEA--LDSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYI 254
Cdd:PLN02387 500 mpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALS 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 255 RSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKKGIE-GTYQELCMKKELKKAILDDMVMLGKESGLHSFEQVKAIY 333
Cdd:PLN02387 580 VSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIK 659
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907081048 334 IHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 369
Cdd:PLN02387 660 LLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
2-369 |
9.68e-67 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 223.70 E-value: 9.68e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 2 FERVIQSVVYCHGGRVGFfqGDIRLLSD-------DMKALRPTIFPVVPRllnrmydkIFhqaDT-------------SL 61
Cdd:PTZ00216 323 MEFGVTNIFLARGALIGF--GSPRTLTDtfarphgDLTEFRPVFLIGVPR--------IF---DTikkaveaklppvgSL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 62 KRWLLEFAAKRKQAEVRSGiiRNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCqVYEGYGQTE--C 139
Cdd:PTZ00216 390 KRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTEtvC 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 140 TAGCTFTtpGDWTSGHVGAPLPCNHIKLVDAEELNYwTCKGE--GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDI 217
Cdd:PTZ00216 467 CGGIQRT--GDLEPNAVGQLLKGVEMKLLDTEEYKH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDV 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 218 GKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQ----IYVHGDslKAFLVGIVVPDPEVMPSWAQKKGI 293
Cdd:PTZ00216 544 GSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNELVVPngvcVLVHPA--RSYICALVLTDEAKAMAFAKEHGI 621
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081048 294 EGTYQELCMKKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELY 369
Cdd:PTZ00216 622 EGEYPAILKDPEFQKKATESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
9-239 |
2.03e-64 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 210.63 E-value: 2.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 9 VVYCHGGRVGFFQGDIRL----LSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwllefaakrkqaevrsgIIRN 84
Cdd:pfam00501 221 GPLLAGATVVLPPGFPALdpaaLLELIERYKVTVLYGVPTLLNM--------------------------------LLEA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 85 NSIWDELFfnkiqaslgGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDW---TSGHVGAPLP 161
Cdd:pfam00501 269 GAPKRALL---------SSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLP 339
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081048 162 CNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLA 239
Cdd:pfam00501 340 GTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1-355 |
1.02e-53 |
|
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: 184.10 E-value: 1.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 1 MFERVIQSVVYCHGGRVGFfqGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQadtslkrwllefaaKRKQAEVRSG 80
Cdd:cd17640 141 SYERSAEYFIFACGCSQAY--TSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQ--------------VSKSSPIKQF 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 81 IIrnnsiwdeLFFnkiqaSLGGHVRMIVTGAAPASPTVLGFLRaALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPL 160
Cdd:cd17640 205 LF--------LFF-----LSGGIFKFGISGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 161 PCNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQ 240
Cdd:cd17640 271 PGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSN 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 241 GEYVAPEKIENIYIRSEPVAQIYVHGDSLKaFLVGIVVPDPEVMPSWAQKKGI---EGTYQELCMKKELKKAILDDMVML 317
Cdd:cd17640 351 GENVEPQPIEEALMRSPFIEQIMVVGQDQK-RLGALIVPNFEELEKWAKESGVklaNDRSQLLASKKVLKLYKNEIKDEI 429
|
330 340 350
....*....|....*....|....*....|....*...
gi 1907081048 318 GKESGLHSFEQVKAIYIHCDMFsVQNGLLTPTLKAKRP 355
Cdd:cd17640 430 SNRPGFKSFEQIAPFALLEEPF-IENGEMTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
1-354 |
5.56e-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: 183.05 E-value: 5.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 1 MFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLL----NRMYDKIFHQadtSLKRWLlefaakrkQAE 76
Cdd:cd05932 190 VTERVFVEGGSLYGGVLVAFAESLDTFVEDVQRARPTLFFSVPRLWtkfqQGVQDKIPQQ---KLNLLL--------KIP 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 77 VRSGIIRNnsiwdelffnKIQASLG-GHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGH 155
Cdd:cd05932 259 VVNSLVKR----------KVLKGLGlDQCRLAGCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGT 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 156 VGAPLPCNHIKLVDaeelnywtckgEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHI 235
Cdd:cd05932 328 VGNAGPGVEVRISE-----------DGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 236 FKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAfLVGIVVPDPEvmpswAQKKGIEGTYQELcmkKELKKAILDDMv 315
Cdd:cd05932 397 FKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPA-PLALVVLSEE-----ARLRADAFARAEL---EASLRAHLARV- 466
|
330 340 350
....*....|....*....|....*....|....*....
gi 1907081048 316 mlgkESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKR 354
Cdd:cd05932 467 ----NSTLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKR 501
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
1-347 |
8.89e-48 |
|
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: 170.71 E-value: 8.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 1 MFERVIQSVVYCHGGrVGFFQG--DIRLLSDDMKALRPTIFPVVPRLLNRMYDKifHQADtsLKRWL-----LEFAAKRK 73
Cdd:cd17632 277 IAGRISLYGTLARGG-TAYFAAasDMSTLFDDLALVRPTELFLVPRVCDMLFQR--YQAE--LDRRSvagadAETLAERV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 74 QAEVRsgiirnnsiwdelffnkiQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTtpgdwtS 153
Cdd:cd17632 352 KAELR------------------ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL------D 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 154 GHVGAPlPCNHIKLVDAEELNYWTCKG---EGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIID 230
Cdd:cd17632 406 GVIVRP-PVLDYKLVDVPELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVD 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 231 RKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSwaqkkgiEGTyqelcmkKELKKAI 310
Cdd:cd17632 485 RRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALAG-------EDT-------ARLRAAL 550
|
330 340 350
....*....|....*....|....*....|....*..
gi 1907081048 311 LDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLT 347
Cdd:cd17632 551 AESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
13-369 |
2.86e-46 |
|
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: 166.76 E-value: 2.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 13 HGGRVGFFQGDIR--LLSDDMKALRPTIFPVVPRLLNRMYDKI---FHQAdTSLKRWLLEFAaKRKQAEV-------RSG 80
Cdd:cd05933 220 VGGQVYFAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkavGAKS-GTLKRKIASWA-KGVGLETnlklmggESP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 81 IIRNNSIWDELFFNKIQASLG-GHVRMIVTGAAPASPTVLGFLrAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAP 159
Cdd:cd05933 298 SPLFYRLAKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKA 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 160 LPCNHIKLVDAEelnywtCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLA 239
Cdd:cd05933 377 LPGCKTKIHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 240 QGEYVAPEKIENIYIRSEP-VAQIYVHGDSLKaFLVGIVV------PD---------PEVMpSWAQKKGIEGTY-QELCM 302
Cdd:cd05933 451 GGENVPPVPIEDAVKKELPiISNAMLIGDKRK-FLSMLLTlkcevnPEtgepldeltEEAI-EFCRKLGSQATRvSEIAG 528
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081048 303 KKELK--KAILDDMVMLGKESGLHSFEQVKAIYIHCDmFSVQNGLLTPTLKAKRPELREYFKKQIEELY 369
Cdd:cd05933 529 GKDPKvyEAIEEGIKRVNKKAISNAQKIQKWVILEKD-FSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
23-281 |
3.63e-44 |
|
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: 158.44 E-value: 3.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 23 DIRLLSDDMKALRPTIFPVVPRLLNRMYDKI-FHQADTSlkrwllefaakrkqaevrsgiirnnsiwdelffnkiqaslg 101
Cdd:COG0318 177 DPERVLELIERERVTVLFGVPTMLARLLRHPeFARYDLS----------------------------------------- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 102 gHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDAE--ELNywt 177
Cdd:COG0318 216 -SLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVDEDgrELP--- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 178 cKGE-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRS 256
Cdd:COG0318 292 -PGEvGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAAH 368
|
250 260 270
....*....|....*....|....*....|..
gi 1907081048 257 EPVAQIYV-------HGDSLKAFlvgiVVPDP 281
Cdd:COG0318 369 PGVAEAAVvgvpdekWGERVVAF----VVLRP 396
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
12-282 |
1.81e-42 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 150.90 E-value: 1.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 12 CHGGRVGFFQG-DIRLLSDDMKALRPTIFPVVPRLLNRmydkifhqadtslkrwLLEFAAKRKQAevrsgiirnnsiwde 90
Cdd:cd04433 64 LAGGTVVLLPKfDPEAALELIEREKVTILLGVPTLLAR----------------LLKAPESAGYD--------------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 91 lffnkiQASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT--SGHVGAPLPCNHIKLV 168
Cdd:cd04433 113 ------LSSL----RALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 169 DAE--ELNYWtckGEGEICVKGPNVFKGYLKDEDRTkEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAP 246
Cdd:cd04433 183 DPDggELPPG---EIGELVVRGPSVMKGYWNNPEAT-AAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYP 257
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907081048 247 EKIENIYIRSEPVAQIYVHGdslkaflvgivVPDPE 282
Cdd:cd04433 258 AEVEAVLLGHPGVAEAAVVG-----------VPDPE 282
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
30-320 |
1.71e-36 |
|
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: 139.09 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 30 DMKALRPTIFPVVPRLLN--------RMYDKifhqadTSLKRWL--------LEFAAKRKQAEVRSGIIRNNS-IWDELF 92
Cdd:cd17641 240 DLREIGPTFVLLPPRVWEgiaadvraRMMDA------TPFKRFMfelgmklgLRALDRGKRGRPVSLWLRLASwLADALL 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 93 FNKIQASLG-GHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTEcTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDa 170
Cdd:cd17641 314 FRPLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTE-LAGAYTVHRdGDVDPDTVGVPFPGTEVRIDE- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 171 eelnywtckgEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIE 250
Cdd:cd17641 391 ----------VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIE 460
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081048 251 NIYIRSEPVAQIYVHGDSlKAFLVGIVVPDPEVMPSWAQKKGIE-GTYQELCMKKELKKAILDDMVMLGKE 320
Cdd:cd17641 461 NKLKFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS 530
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
23-274 |
1.78e-36 |
|
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: 137.69 E-value: 1.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 23 DIRLLsDDMKALRPTIFPVVPRllnrMYDKIFHQADtslkrwllefaakrkqaevrsgiirnnsiwdelfFNKIQASlgg 102
Cdd:cd05936 205 PIGVL-KEIRKHRVTIFPGVPT----MYIALLNAPE----------------------------------FKKRDFS--- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDaEELNYWTCKGE 181
Cdd:cd05936 243 SLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLPGTEVKIVD-DDGEELPPGEV 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 182 GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQ 261
Cdd:cd05936 322 GELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHPAVAE 399
|
250 260
....*....|....*....|
gi 1907081048 262 IYV-------HGDSLKAFLV 274
Cdd:cd05936 400 AAVvgvpdpySGEAVKAFVV 419
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
103-274 |
2.15e-36 |
|
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: 137.73 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTCKGE 181
Cdd:cd05911 263 SLRVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEP 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 182 GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIyIRSEP--- 258
Cdd:cd05911 343 GEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAV-LLEHPgva 420
|
170 180
....*....|....*....|.
gi 1907081048 259 ---VAQIY--VHGDSLKAFLV 274
Cdd:cd05911 421 daaVIGIPdeVSGELPRAYVV 441
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
81-282 |
5.24e-36 |
|
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: 136.42 E-value: 5.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 81 IIRNNSIWdELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPL 160
Cdd:cd05914 214 KINNRKIR-KLAFKKVHEAFGGNIKEFVIGGAKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVI 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 161 PCNHIKLVDAEELNywtckGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQ 240
Cdd:cd05914 292 DGVEVRIDSPDPAT-----GEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSS 366
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907081048 241 GEYVAPEKIENIYIRSEPVAQ--IYVHGDSLKAflvgIVVPDPE 282
Cdd:cd05914 367 GKNIYPEEIEAKINNMPFVLEslVVVQEKKLVA----LAYIDPD 406
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
103-274 |
3.30e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 132.34 E-value: 3.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDaeELNYWTC 178
Cdd:PRK07656 282 SLRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAGVENKIVN--ELGEEVP 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 179 KGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSE 257
Cdd:PRK07656 360 VGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGFNVYPAEVEEVLYEHP 438
|
170 180
....*....|....*....|....
gi 1907081048 258 PVAQIYV-------HGDSLKAFLV 274
Cdd:PRK07656 439 AVAEAAVigvpderLGEVGKAYVV 462
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
2-369 |
4.30e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 121.75 E-value: 4.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 2 FERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQAD--TSLKRWLLE--FAAKRkqaev 77
Cdd:PTZ00342 360 YERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPPLKRFLVKkiLSLRK----- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 78 rsgiiRNNSIWDELFF-------NKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPG- 149
Cdd:PTZ00342 435 -----SNNNGGFSKFLegithisSKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTE-TTGPIFVQHAd 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 150 DWTSGHVGAPL-PCNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKI 228
Cdd:PTZ00342 509 DNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTF 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 229 IDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHG-DSLKAFLvGIVVPDPEVM------PSWAQKKGI-EGTYQEL 300
Cdd:PTZ00342 589 LDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGdDSMDGPL-AIISVDKYLLfkclkdDNMLESTGInEKNYLEK 667
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081048 301 CMKKELKKAILDDMV---MLG--KESGLHSFEQVKAIYIHCDMFSVQNgLLTPTLKAKRPEL-REY--FKKQIEELY 369
Cdd:PTZ00342 668 LTDETINNNIYVDYVkgkMLEvyKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVfKDYafFIDQVKKIY 743
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
103-281 |
1.68e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 119.14 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGH------VGAPLPCNHIKLVDAEELNYW 176
Cdd:PRK06187 282 SLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPEDQLPGQwtkrrsAGRPLPGVEARIVDDDGDELP 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 177 TCKGE-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyir 255
Cdd:PRK06187 362 PDGGEvGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDA--- 436
|
170 180
....*....|....*....|....*.
gi 1907081048 256 sepvaqIYVHGDSLKAFLVGivVPDP 281
Cdd:PRK06187 437 ------LYGHPAVAEVAVIG--VPDE 454
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
104-275 |
6.28e-28 |
|
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: 111.82 E-value: 6.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDAeelnywtck 179
Cdd:cd17638 117 LRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIADD--------- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 180 geGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPV 259
Cdd:cd17638 187 --GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEHPGV 263
|
170 180
....*....|....*....|...
gi 1907081048 260 AQIYV-------HGDSLKAFLVG 275
Cdd:cd17638 264 AQVAVigvpderMGEVGKAFVVA 286
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
104-252 |
1.65e-27 |
|
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: 113.10 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTP---GDWTSGHVGAPLPCNHIKLVDAEELNYWTCK 179
Cdd:cd05904 277 LRQIMSGAAPLGKELIeAFRAKFPNVDLGQGYGMTESTGVVAMCFApekDRAKYGSVGRLVPNVEAKIVDPETGESLPPN 356
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081048 180 GEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENI 252
Cdd:cd05904 357 QTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
104-281 |
2.88e-27 |
|
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: 111.55 E-value: 2.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDAE--ELNywtcK 179
Cdd:cd17631 215 LRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVFFVEVRIVDPDgrEVP----P 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 180 GE-GEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIyirsep 258
Cdd:cd17631 290 GEvGEIVVRGPHVMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDV------ 361
|
170 180
....*....|....*....|...
gi 1907081048 259 vaqIYVHGDSLKAFLVGivVPDP 281
Cdd:cd17631 362 ---LYEHPAVAEVAVIG--VPDE 379
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
103-285 |
4.94e-27 |
|
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: 111.23 E-value: 4.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTP--GDWTSGHVGAPLPCNHIKLVDAEELNYWTCKG 180
Cdd:cd05941 213 RLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEETGEPLPRGE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 181 EGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK-HIFKlAQGEYVAPEKIENIYIRSEPV 259
Cdd:cd05941 291 VGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIERVLLAHPGV 369
|
170 180
....*....|....*....|....*....
gi 1907081048 260 AQIYVHGDSLKAF---LVGIVVPDPEVMP 285
Cdd:cd05941 370 SECAVIGVPDPDWgerVVAVVVLRAGAAA 398
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
127-274 |
9.96e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 111.39 E-value: 9.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 127 GCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVD--AEELNYwtckGE-GEICVKGPNVFKGYLKDEDRTK 203
Cdd:PRK05677 351 GCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDddGNELPL----GEvGELCVKGPQVMKGYWQRPEATD 426
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081048 204 EALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQ---IYV----HGDSLKAFLV 274
Cdd:PRK05677 427 EILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGFNVYPNELEDVLAALPGVLQcaaIGVpdekSGEAIKVFVV 503
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
105-291 |
1.53e-26 |
|
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: 109.85 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 105 RMIVTGAAPASPTVLgflRAAL--GCQVYEGYGQTE-CTAGCTFTTPGDWTSGHVGAPLPCNHIKL-VDAEElnywtckG 180
Cdd:TIGR01923 222 RKILLGGSAIPAPLI---EEAQqyGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVDNKE-------G 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 181 EGEICVKGPNVFKGYLKDEDRTkEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVA 260
Cdd:TIGR01923 292 HGEIMVKGANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQ 369
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907081048 261 QIYV--HGDSL-----KAFLVGIVVPDPEVMPSWAQKK 291
Cdd:TIGR01923 370 EAVVvpKPDAEwgqvpVAYIVSESDISQAKLIAYLTEK 407
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
103-289 |
2.59e-26 |
|
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: 108.59 E-value: 2.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTE-CTAGCTFTtPGDWTS--GHVGAPLPCNHIKLVDAEELNYwtck 179
Cdd:cd05912 190 NLRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIEDDGQPPY---- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 180 GEGEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPV 259
Cdd:cd05912 264 EVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPAI 341
|
170 180 190
....*....|....*....|....*....|
gi 1907081048 260 AQIYVhgdslkaflVGIvvPDPEvmpsWAQ 289
Cdd:cd05912 342 KEAGV---------VGI--PDDK----WGQ 356
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
103-282 |
1.45e-24 |
|
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: 104.92 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAALGCQ-VYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTCKGE 181
Cdd:cd17642 302 NLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNER 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 182 GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQ 261
Cdd:cd17642 382 GELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFD 460
|
170 180
....*....|....*....|.
gi 1907081048 262 IYVHGdslkaflvgivVPDPE 282
Cdd:cd17642 461 AGVAG-----------IPDED 470
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
102-281 |
3.83e-24 |
|
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: 101.59 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 102 GHVRMIVTGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGDWTS---GHVGAPLPCNHIKLVDAEelnywT 177
Cdd:cd05917 118 SSLRTGIMAGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIEkrvNTVGRIMPHTEAKIVDPE-----G 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 178 CK----GE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENI 252
Cdd:cd05917 193 GIvppvGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIYPREIEEF 271
|
170 180
....*....|....*....|....*....
gi 1907081048 253 yirsepvaqIYVHGDSLKAFLVGivVPDP 281
Cdd:cd05917 272 ---------LHTHPKVSDVQVVG--VPDE 289
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
84-274 |
4.31e-24 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 103.60 E-value: 4.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 84 NNSIWDELFFNKIQASLGGhvrmivtgAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTPGdwTSGHVGAPL 160
Cdd:PRK08974 315 NNEEFQELDFSSLKLSVGG--------GMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 161 PCNHIKLVDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQ 240
Cdd:PRK08974 385 PSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVS 461
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907081048 241 GEYVAPEKIENIYIRSEPVAQIY-------VHGDSLKAFLV 274
Cdd:PRK08974 462 GFNVYPNEIEDVVMLHPKVLEVAavgvpseVSGEAVKIFVV 502
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
103-359 |
4.63e-24 |
|
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: 103.16 E-value: 4.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTP---GDWTSGHVGAPLPcNHIKLVDAEELnywTCK 179
Cdd:cd05926 266 KLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTE-AAHQMTSNPlppGPRKPGSVGKPVG-VEVRILDEDGE---ILP 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 180 --GEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSE 257
Cdd:cd05926 341 pgVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVLLSHP 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 258 PVAQIYVHGdslkaflvgivVPDP----EVMPSWAQKKGIEGTYQELcmKKELKKailddmvmlgkesGLHSFEQVKAIY 333
Cdd:cd05926 420 AVLEAVAFG-----------VPDEkygeEVAAAVVLREGASVTEEEL--RAFCRK-------------HLAAFKVPKKVY 473
|
250 260
....*....|....*....|....*.
gi 1907081048 334 IhcdmfsVQNGLLTPTLKAKRPELRE 359
Cdd:cd05926 474 F------VDELPKTATGKIQRRKVAE 493
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
98-282 |
5.21e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 102.96 E-value: 5.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 98 ASLGGHVRMIVTGAAP-ASPTVLGFLraALGCQVYEGYGQTEctAGCTFTTPGDWT-----SGHVGAPLPCNHIKLVDAE 171
Cdd:PRK09088 248 AAALRHLTALFTGGAPhAAEDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQ 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 172 ELNywtCK-GE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKI 249
Cdd:PRK09088 324 GND---CPaGVpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEI 399
|
170 180 190
....*....|....*....|....*....|...
gi 1907081048 250 EniyirsepvAQIYVHGDSLKAFLVGivVPDPE 282
Cdd:PRK09088 400 E---------AVLADHPGIRECAVVG--MADAQ 421
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
85-264 |
1.03e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 102.36 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 85 NSIWDELFFNKIQaslgghVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTagCTFTTPGDWTSGH-------V 156
Cdd:PLN02330 292 NPIVEEFDLSKLK------LQAIMTAAAPLAPELLtAFEAKFPGVQVQEAYGLTEHS--CITLTHGDPEKGHgiakknsV 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 157 GAPLPCNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIF 236
Cdd:PLN02330 364 GFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELI 443
|
170 180
....*....|....*....|....*...
gi 1907081048 237 KLaQGEYVAPEKIENIYIRSEPVAQIYV 264
Cdd:PLN02330 444 KY-KGFQVAPAELEAILLTHPSVEDAAV 470
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
127-274 |
1.24e-23 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 102.21 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 127 GCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDAE--ELNYwtckGE-GEICVKGPNVFKGYLKDEDRT 202
Cdd:PRK12492 358 GCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPGTALKVIDDDgnELPL----GErGELCIKGPQVMKGYWQQPEAT 433
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081048 203 KEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYV-------HGDSLKAFLV 274
Cdd:PRK12492 434 AEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVV 511
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
108-282 |
1.99e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 100.44 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 108 VTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEelNYWTCKGE-GEICV 186
Cdd:cd05934 200 AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD--GQELPAGEpGELVI 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 187 K---GPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVAQIY 263
Cdd:cd05934 278 RglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAVREAA 355
|
170 180
....*....|....*....|....*.
gi 1907081048 264 VHG-------DSLKAFlvgIVVPDPE 282
Cdd:cd05934 356 VVAvpdevgeDEVKAV---VVLRPGE 378
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
105-252 |
2.44e-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: 100.87 E-value: 2.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 105 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPCNHIKLVDAEELNYWTCKGEGE 183
Cdd:cd05909 264 RLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGL 343
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081048 184 ICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 252
Cdd:cd05909 344 LLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDI 410
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
23-280 |
2.54e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 98.53 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 23 DIRLLSDDMKALRPTIFPVVPRLlnrmYDKIfhqadtslkrwlLEFAAKRkqaevrsGIirnnsiwdelffnkiqaSLGG 102
Cdd:PRK05605 298 DIDLILDAMKKHPPTWLPGVPPL----YEKI------------AEAAEER-------GV-----------------DLSG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 hVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECT---AGCTFTTpgDWTSGHVGAPLPCNHIKLVDAEELNYWTCK 179
Cdd:PRK05605 338 -VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpiiVGNPMSD--DRRPGYVGVPFPDTEVRIVDPEDPDETMPD 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 180 GE-GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEniyirsEP 258
Cdd:PRK05605 415 GEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITGGFNVYPAEVE------EV 486
|
250 260
....*....|....*....|..
gi 1907081048 259 VAQiyvHGDSLKAFLVGIVVPD 280
Cdd:PRK05605 487 LRE---HPGVEDAAVVGLPRED 505
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
115-282 |
1.06e-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: 94.64 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 115 SPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaeELNYWTCKGE-GEICVKGPNVFK 193
Cdd:cd17637 124 APETIQRFEETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD--DNDRPVPAGEtGEIVVRGPLVFQ 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 194 GYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRK--KHIFKlAQGEYVAPEKIENIYIRSEPVAQIYVHGdslka 271
Cdd:cd17637 201 GYWNLPELTAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHPAIAEVCVIG----- 273
|
170
....*....|.
gi 1907081048 272 flvgivVPDPE 282
Cdd:cd17637 274 ------VPDPK 278
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
105-286 |
1.93e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 95.44 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 105 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaEELNYWTCKGE--G 182
Cdd:PRK07787 244 RLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVD-EDGGPVPHDGEtvG 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 183 EICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDR------KKHIFKLAQGEyvapekIENIYIRS 256
Cdd:PRK07787 323 ELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGGYRIGAGE------IETALLGH 396
|
170 180 190
....*....|....*....|....*....|...
gi 1907081048 257 EPVAQIYVHG---DSLKAFLVGIVVPDPEVMPS 286
Cdd:PRK07787 397 PGVREAAVVGvpdDDLGQRIVAYVVGADDVAAD 429
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
103-286 |
2.44e-21 |
|
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: 94.90 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFT--TPGDWTSGHV--GAPLPCNHIKLVDaEELNYWT 177
Cdd:cd05930 209 SLRLVLVGGEALPPDLVrRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVP 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 178 CKGEGEICVKGPNVFKGYLKDEDRTKEA-----LDSDGWLH-TGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIEN 251
Cdd:cd05930 288 PGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEA 366
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907081048 252 IYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPEVMPS 286
Cdd:cd05930 367 ALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGGELD 404
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
84-283 |
3.22e-21 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 95.09 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 84 NNSIWDELFFNKIQASLGGhvrmivtGAAPASPTVLGFLRAAlGCQVYEGYG--QTECTAGCTFTTPGDWTsGHVGAPLP 161
Cdd:PRK07059 317 NNPDFDKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGlsETSPVATCNPVDATEFS-GTIGLPLP 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 162 CNHIKLVDAE--ELNYwtckGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkL 238
Cdd:PRK07059 388 STEVSIRDDDgnDLPL----GEpGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMI-L 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907081048 239 AQGEYVAPEKIENIyIRSEP----VAQIYVH----GDSLKAFlvgIVVPDPEV 283
Cdd:PRK07059 463 VSGFNVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLF---VVKKDPAL 511
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
104-280 |
4.40e-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: 93.91 E-value: 4.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFT--TPGDWTsgHVGAPLPCNHIKLVDAEELNYwTCKGE 181
Cdd:cd17653 211 LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILDADLQPV-PEGVV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 182 GEICVKGPNVFKGYLKDEDRTKEALDSDGWLH------TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIR 255
Cdd:cd17653 286 GEICISGVQVARGYLGNPALTASKFVPDPFWPgsrmyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEIEEVVLQ 364
|
170 180
....*....|....*....|....*...
gi 1907081048 256 SEPVAQ---IYVHGDSLKAFlvgiVVPD 280
Cdd:cd17653 365 SQPEVTqaaAIVVNGRLVAF----VTPE 388
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
102-274 |
4.85e-21 |
|
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: 93.94 E-value: 4.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 102 GHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAE--ELNYWTck 179
Cdd:cd05972 197 SHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDgrELPPGE-- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 180 gEGEICVKGPNV--FKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSE 257
Cdd:cd05972 275 -EGDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHP 351
|
170 180
....*....|....*....|....
gi 1907081048 258 PVAQIYV-------HGDSLKAFLV 274
Cdd:cd05972 352 AVAEAAVvgspdpvRGEVVKAFVV 375
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
102-260 |
7.44e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 92.54 E-value: 7.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 102 GHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLV--DAEELNYWTC 178
Cdd:cd05944 121 SSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKvlDGVGRLLRDC 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 179 KGE--GEICVKGPNVFKGYLKDEDRtKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRS 256
Cdd:cd05944 201 APDevGEICVAGPGVFGGYLYTEGN-KNAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRH 278
|
....
gi 1907081048 257 EPVA 260
Cdd:cd05944 279 PAVA 282
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
84-281 |
8.03e-21 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 93.79 E-value: 8.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 84 NNSIWDELFFNKIQASLGGHvrMIVTGAapasptVLGFLRAALGCQVYEGYGQTECT-AGCTFTTPGDWTSGHVGAPLPC 162
Cdd:PRK08751 319 NTPGFDQIDFSSLKMTLGGG--MAVQRS------VAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPS 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 163 NHIKLVDaeELNYWTCKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQG 241
Cdd:PRK08751 391 TDACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-LVSG 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907081048 242 EYVAPEKIENIYIRSEPVAQIYVHG----DSLKAFLVGIVVPDP 281
Cdd:PRK08751 468 FNVYPNEIEDVIAMMPGVLEVAAVGvpdeKSGEIVKVVIVKKDP 511
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
103-264 |
8.26e-21 |
|
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: 93.21 E-value: 8.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD----WTSGhvGAPLPCNHIKLVDAEELNYwTC 178
Cdd:cd05903 209 RLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrLYTD--GRPLPGVEIKVVDDTGATL-AP 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 179 KGEGEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEP 258
Cdd:cd05903 286 GVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPG 363
|
....*.
gi 1907081048 259 VAQIYV 264
Cdd:cd05903 364 VIEAAV 369
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
103-281 |
9.34e-21 |
|
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: 93.46 E-value: 9.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAaLGCQVYEGYGQTECTAGCTFTTPgdwTSGHV--------------GAPLPCNHIKLV 168
Cdd:cd12119 281 SLRRVVIGGSAVPRSLIEAFEE-RGVRVIHAWGMTETSPLGTVARP---PSEHSnlsedeqlalrakqGRPVPGVELRIV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 169 DAE--ELNyWTCKGEGEICVKGPNVFKGYLKDeDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAP 246
Cdd:cd12119 357 DDDgrELP-WDGKAVGELQVRGPWVTKSYYKN-DEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSG-GEWISS 433
|
170 180 190
....*....|....*....|....*....|....*
gi 1907081048 247 EKIENIYIRSEPVAQIYVhgdslkaflvgIVVPDP 281
Cdd:cd12119 434 VELENAIMAHPAVAEAAV-----------IGVPHP 457
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
103-266 |
2.38e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 91.95 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAAlGCQVYEGYGQTEcTAGCTFTTPGDWTS---GHVGAPL-PCNhIKLVDaeELNYWTC 178
Cdd:PRK03640 255 SFRCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPP 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 179 KGEGEICVKGPNVFKGYLKDEDRTKEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEP 258
Cdd:PRK03640 330 FEEGEIVVKGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPG 407
|
....*...
gi 1907081048 259 VAQIYVHG 266
Cdd:PRK03640 408 VAEAGVVG 415
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
104-266 |
3.00e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 92.14 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAALGC-QVYEGYGQTECTAGCTFTTPGD-----WTSghVGAPLPCNHIKLVDAEELNywT 177
Cdd:PRK12583 319 LRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdlerrVET--VGRTQPHLEVKVVDPDGAT--V 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 178 CKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRS 256
Cdd:PRK12583 395 PRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTH 473
|
170
....*....|
gi 1907081048 257 EPVAQIYVHG 266
Cdd:PRK12583 474 PAVADVQVFG 483
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
82-250 |
5.18e-20 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 91.91 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 82 IRNNSIWDELFfnkiqASLgghvRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-----GDWT---- 152
Cdd:PRK08633 887 LRNKKLHPLMF-----ASL----RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaaDFKRqtgs 957
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 153 -SGHVGAPLPCNHIKLVDAEelNYWTCKG--EGEICVKGPNVFKGYLKDEDRTKEAL---DSDGWLHTGDIGKWLPEGTL 226
Cdd:PRK08633 958 kEGSVGMPLPGVAVRIVDPE--TFEELPPgeDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFL 1035
|
170 180
....*....|....*....|....
gi 1907081048 227 KIIDRKKHIFKLAqGEYVAPEKIE 250
Cdd:PRK08633 1036 TITDRYSRFAKIG-GEMVPLGAVE 1058
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
104-254 |
5.68e-20 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 91.20 E-value: 5.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAALGCQVY-EGYGQTE-------CTAgctFT-TPGDWTSGHVGAPLPCNHIKLVDAE--- 171
Cdd:PLN02246 300 IRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEagpvlamCLA---FAkEPFPVKSGSCGTVVRNAELKIVDPEtga 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 172 ELNYWTCkgeGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIEN 251
Cdd:PLN02246 377 SLPRNQP---GEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEA 452
|
...
gi 1907081048 252 IYI 254
Cdd:PLN02246 453 LLI 455
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
104-233 |
6.04e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 91.17 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDAEEL-NYWT-C-K 179
Cdd:PRK07529 335 LRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLRdCaV 414
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081048 180 GE-GEICVKGPNVFKGYLkDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK 233
Cdd:PRK07529 415 DEvGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAK 468
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
133-245 |
1.52e-19 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 89.94 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 133 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEelnywtckGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWL 212
Cdd:PRK08180 371 GLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYY 442
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907081048 213 HTGDIGKWL----PEGTLKIIDRKKHIFKLAQGEYVA 245
Cdd:PRK08180 443 RSGDAVRFVdpadPERGLMFDGRIAEDFKLSSGTWVS 479
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
106-289 |
1.71e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 89.66 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 106 MIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHV------GAPLPCNHIKLVDAEELNYWTck 179
Cdd:PRK06188 285 TVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLDEDGREVAQ-- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 180 GE-GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEP 258
Cdd:PRK06188 363 GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNVFPREVEDVLAEHPA 440
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907081048 259 VAQIYV-------HGDSLKAflvgIVVPDPEVMPSWAQ 289
Cdd:PRK06188 441 VAQVAVigvpdekWGEAVTA----VVVLRPGAAVDAAE 474
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
102-254 |
1.30e-18 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 87.20 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 102 GHVRMIVTGAAPAS-PTVLGFLRAALGCQVYEGYGQTECTAGCT--FTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTC 178
Cdd:PLN02574 319 KSLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYSSVGLLAPNMQAKVVDWSTGCLLPP 398
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081048 179 KGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 254
Cdd:PLN02574 399 GNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIAPADLEAVLI 473
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
133-284 |
2.76e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 86.02 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 133 GYGQTECTAGCTFTTPGD------WTsghVGAPLPCNHIKLVDAEelnywTCK----GE-GEICVKGPNVFKGYLKDEDR 201
Cdd:PRK08315 347 AYGMTETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVDPE-----TGEtvprGEqGELCTRGYSVMKGYWNDPEK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 202 TKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP 281
Cdd:PRK08315 419 TAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEF---------LYTHPKIQDVQVVG--VPDE 486
|
....*..
gi 1907081048 282 ----EVM 284
Cdd:PRK08315 487 kygeEVC 493
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
97-300 |
3.69e-18 |
|
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: 85.43 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 97 QASLGGHVRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPC----NHIKLV 168
Cdd:cd12118 243 ARPLPHRVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatvCAWKPEWDELPTEERARLKArqgvRYVGLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 169 DAEELNYWTCK-----GE--GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQG 241
Cdd:cd12118 320 EVDVLDPETMKpvprdGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGG 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081048 242 EYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP---EVMPSW-AQKKGIEGTYQEL 300
Cdd:cd12118 398 ENISSVEVEGV---------LYKHPAVLEAAVVA--RPDEkwgEVPCAFvELKEGAKVTEEEI 449
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
123-282 |
5.85e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 85.09 E-value: 5.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 123 RAALGCQVYEG-YGQTECTAGCTFTTpGDWTSGH--------VGAPLPCNHIKLVDAEELNYWTCKGEGEICVKGPNVFK 193
Cdd:PRK06178 348 RALTGSVLAEAaWGMTETHTCDTFTA-GFQDDDFdllsqpvfVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLK 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 194 GYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRsepvaqiyvHGDSLKAFL 273
Cdd:PRK06178 427 GYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NGMSVFPSEVEALLGQ---------HPAVLGSAV 495
|
....*....
gi 1907081048 274 VGivVPDPE 282
Cdd:PRK06178 496 VG--RPDPD 502
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
122-315 |
5.92e-18 |
|
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: 84.99 E-value: 5.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 122 LRAAL-GCQVYEGYGQTECTAGCTFT--TP---GDWTSGHVGAPLPCNHIKLVDaEELNYWTCKGEGEICVKGPNVFKGY 195
Cdd:cd05945 234 LQQRFpDARIYNTYGPTEATVAVTYIevTPevlDGYDRLPIGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGY 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 196 LKDEDRTKEALDSD---GWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYV----HGDS 268
Cdd:cd05945 313 LNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIELEEIEAALRQVPGVKEAVVvpkyKGEK 391
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907081048 269 lKAFLVGIVVPDPEVMPswAQKKGIegtyqelcmKKELKKAILDDMV 315
Cdd:cd05945 392 -VTELIAFVVPKPGAEA--GLTKAI---------KAELAERLPPYMI 426
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
95-282 |
7.15e-18 |
|
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: 84.45 E-value: 7.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 95 KIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELN 174
Cdd:cd05935 192 EFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGR 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 175 YWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDG---WLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIEN 251
Cdd:cd05935 272 ELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEA 350
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907081048 252 IYIRSEPVAQIYV-------HGDSLKAFlvgiVVPDPE 282
Cdd:cd05935 351 KLYKHPAI*EVCVisvpderVGEEVKAF----IVLRPE 384
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
104-361 |
1.36e-17 |
|
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: 82.76 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPtvlGFLRAA--LGCQVYEGYGQTEcTAGCTFT-TPGDWTSGHVGAPLPCNHIKLVDaeelnywtckg 180
Cdd:cd17630 113 LRAVLLGGAPIPP---ELLERAadRGIPLYTTYGMTE-TASQVATkRPDGFGRGGVGVLLPGRELRIVE----------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 181 EGEICVKGPNVFKGYLKDedRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEniyirsepvA 260
Cdd:cd17630 178 DGEIWVGGASLAMGYLRG--QLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIE---------A 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 261 QIYVHGDSLKAFLVGivVPDPEV--MPSWAQKKGIEGTYQEL--CMKKELKKailddmvmlgkesglhsFEQVKAIYIhc 336
Cdd:cd17630 246 ALAAHPAVRDAFVVG--VPDEELgqRPVAVIVGRGPADPAELraWLKDKLAR-----------------FKLPKRIYP-- 304
|
250 260
....*....|....*....|....*
gi 1907081048 337 dmfsVQNGLLTPTLKAKRPELREYF 361
Cdd:cd17630 305 ----VPELPRTGGGKVDRRALRAWL 325
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
105-281 |
1.65e-17 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 83.95 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 105 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKLVDAE--ELNYWTck 179
Cdd:PRK13295 315 RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVDADgaPLPAGQ-- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 180 gEGEICVKGPNVFKGYLKDEDRTkeALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPV 259
Cdd:PRK13295 392 -IGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAI 467
|
170 180
....*....|....*....|...
gi 1907081048 260 AQiyvhgdslkaflVGIV-VPDP 281
Cdd:PRK13295 468 AQ------------VAIVaYPDE 478
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
127-274 |
2.01e-17 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 83.58 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 127 GCQVYEGYGQTECTAGCTFTTPGD---WTSghVGAPLPCNHIKLVDAEelNYWTCKGE-GEICVKG---PNVFKGYLKDE 199
Cdd:PRK08008 312 GVRLLTSYGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRDDH--NRPLPAGEiGEICIKGvpgKTIFKEYYLDP 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 200 DRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyIRSEP-VAQIYVHG--DSL-----KA 271
Cdd:PRK08008 388 KATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENI-IATHPkIQDIVVVGikDSIrdeaiKA 465
|
...
gi 1907081048 272 FLV 274
Cdd:PRK08008 466 FVV 468
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
103-264 |
3.11e-17 |
|
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: 82.31 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTECTAGCT-FTTPGDWTSGHV----GAPLPCNHIKLVDA--EELN 174
Cdd:TIGR01733 236 SLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTaTLVDPDDAPRESpvpiGRPLANTRLYVLDDdlRPVP 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 175 YWtckGEGEICVKGPNVFKGYLKDEDRTKEA-LDSDGWL-------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAP 246
Cdd:TIGR01733 316 VG---VVGELYIGGPGVARGYLNRPELTAERfVPDPFAGgdgarlyRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIEL 391
|
170
....*....|....*...
gi 1907081048 247 EKIENIYIRSEPVAQIYV 264
Cdd:TIGR01733 392 GEIEAALLRHPGVREAVV 409
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
103-282 |
3.33e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 82.60 E-value: 3.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPAS-PTVLGFLRAalGCQVYEGYGQTEcTAGCTFTTPGD---WTSGHVGAPLPCNHIKLVDaEELNYWTC 178
Cdd:PRK06839 265 SVRWFYNGGAPCPeELMREFIDR--GFLFGQGFGMTE-TSPTVFMLSEEdarRKVGSIGKPVLFCDYELID-ENKNKVEV 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 179 KGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIyirsep 258
Cdd:PRK06839 341 GEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV------ 412
|
170 180
....*....|....*....|....
gi 1907081048 259 vaqIYVHGDSLKAFLVGivVPDPE 282
Cdd:PRK06839 413 ---INKLSDVYEVAVVG--RQHVK 431
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
104-274 |
3.44e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 82.77 E-value: 3.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgctfTTPGDW-----TSGHVGAPLPCNHIKLVDAEELNYWTC 178
Cdd:PRK06710 325 IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSP----VTHSNFlwekrVPGSIGVPWPDTEAMIMSLETGEALPP 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 179 KGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEP 258
Cdd:PRK06710 401 GEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVLYEHEK 478
|
170 180
....*....|....*....|...
gi 1907081048 259 VAQIYV-------HGDSLKAFLV 274
Cdd:PRK06710 479 VQEVVTigvpdpyRGETVKAFVV 501
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
103-281 |
3.65e-17 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 82.62 E-value: 3.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTfTTP--GDWTSGHVGAPLPCNHIKLVDAE---ELNywt 177
Cdd:PRK07514 270 HMRLFISGSAPLLAETHREFQERTGHAILERYGMTE-TNMNT-SNPydGERRAGTVGFPLPGVSLRVTDPEtgaELP--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 178 cKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIfkLAQGEY-VAPEKIENiYIR 255
Cdd:PRK07514 345 -PGEiGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDL--IISGGYnVYPKEVEG-EID 420
|
170 180 190
....*....|....*....|....*....|
gi 1907081048 256 SEP-VAQIYVHGDSLKAF---LVGIVVPDP 281
Cdd:PRK07514 421 ELPgVVESAVIGVPHPDFgegVTAVVVPKP 450
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
107-286 |
6.83e-17 |
|
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: 81.74 E-value: 6.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 107 IVTGAAPASPTVLG-FLRAALGCQVYEGYGQTEctAGCTFTT--PGDWTSGHVGAPLPCNHIKLVDaEELNYWTCKGEGE 183
Cdd:cd05919 212 LCVSAGEALPRGLGeRWMEHFGGPILDGIGATE--VGHIFLSnrPGAWRLGSTGRPVPGYEIRLVD-EEGHTIPPGEEGD 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 184 ICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIY 263
Cdd:cd05919 289 LLVRGPSAAVGYWNNPEKSRATF-NGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLIIQHPAVAEAA 366
|
170 180 190
....*....|....*....|....*....|
gi 1907081048 264 V----HGDSL---KAFlvgiVVPDPEVMPS 286
Cdd:cd05919 367 VvavpESTGLsrlTAF----VVLKSPAAPQ 392
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
103-291 |
6.92e-17 |
|
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: 81.72 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFTTPG--DWTSGHVGAPLPCNHIKLVDAEELNYWTck 179
Cdd:cd05922 232 SLRYLTQAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTYLPPEriLEKPGSIGLAIPGGEFEILDDDGTPTPP-- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 180 GE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyIRSEP 258
Cdd:cd05922 310 GEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIEAA-ARSIG 387
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907081048 259 ---VAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKK 291
Cdd:cd05922 388 liiEAAAVGLPDPLGEKLALFVTAPDKIDPKDVLRS 423
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
103-282 |
8.36e-17 |
|
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: 81.43 E-value: 8.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGflRAALGCQVYEGYGQTECTAGCTFTTPG-DWTSGHVGAPLPC--------NHIKLVDaeel 173
Cdd:cd05918 216 SLRTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGAtcwvvdpdNHDRLVP---- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 174 nywtcKGE-GEICVKGPNVFKGYLKDEDRTKEA-LDSDGWLH------------TGDIGKWLPEGTLKIIDRKKHIFKLa 239
Cdd:cd05918 290 -----IGAvGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKI- 363
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907081048 240 QGEYVAPEKIENIYIRSEP-----VAQIYVH-GDSLKAFLVGIVVPDPE 282
Cdd:cd05918 364 RGQRVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLDGS 412
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
104-281 |
8.62e-17 |
|
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: 81.77 E-value: 8.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPG-DWTSGHVGAPLPCNHIKLVDAEELnywTCKG-- 180
Cdd:cd05970 303 LRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLIDREGR---SCEAge 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 181 EGEICV---KGPNV--FKGYLKDEDRTKEALdSDGWLHTGDIGkWLPE-GTLKIIDRKKHIFKlAQGEYVAPEKIENIYI 254
Cdd:cd05970 379 EGEIVIrtsKGKPVglFGGYYKDAEKTAEVW-HDGYYHTGDAA-WMDEdGYLWFVGRTDDLIK-SSGYRIGPFEVESALI 455
|
170 180
....*....|....*....|....*..
gi 1907081048 255 RSEPVAQIYVHGdslkaflvgivVPDP 281
Cdd:cd05970 456 QHPAVLECAVTG-----------VPDP 471
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
127-252 |
8.95e-17 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 81.72 E-value: 8.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 127 GCQVYEGYGQTECTAGcTFTTPGD---WTSGHVGAPLPCNHIKLVDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTK 203
Cdd:PRK06087 326 GIKLLSVYGSTESSPH-AVVNLDDplsRFMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTA 403
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907081048 204 EALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENI 252
Cdd:PRK06087 404 RALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDI 451
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
121-281 |
2.03e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 80.32 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 121 FLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS--GHVGAPLPcnHIKLVDAEELNYWTCKG-EGEICVKGPNVFKGYLK 197
Cdd:PRK06145 284 FTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALA--HVEIRIADGAGRWLPPNmKGEICMRGPKVTKGYWK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 198 DEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEN-IYIRSE--PVAQIYVHGDSLKAFLV 274
Cdd:PRK06145 362 DPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERvIYELPEvaEAAVIGVHDDRWGERIT 439
|
....*..
gi 1907081048 275 GIVVPDP 281
Cdd:PRK06145 440 AVVVLNP 446
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
97-281 |
2.71e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 80.06 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 97 QASLGGHVRMIVTGAAPasPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGD-WTSghvgapLPCN------------ 163
Cdd:PLN03102 296 LSPRSGPVHVLTGGSPP--PAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDeWNR------LPENqqmelkarqgvs 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 164 HIKLVDAEELNYWTC-------KGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIF 236
Cdd:PLN03102 368 ILGLADVDVKNKETQesvprdgKTMGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII 446
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907081048 237 kLAQGEYVAPEKIENIyirsepvaqIYVHGDSLKAFLVGIvvPDP 281
Cdd:PLN03102 447 -ISGGENISSVEVENV---------LYKYPKVLETAVVAM--PHP 479
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
103-310 |
5.19e-16 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 79.39 E-value: 5.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtaGCTFTTPGDWTS---GHVGAPLPCNHIKLVDAEelnywtck 179
Cdd:COG0365 307 SLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTET--GGIFISNLPGLPvkpGSMGKPVPGYDVAVVDED-------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 180 G-------EGEICVKG--PNVFKGYLKDEDRTKEAL--DSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEK 248
Cdd:COG0365 377 GnpvppgeEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAE 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081048 249 IENIYIRSEPVAQIYV----H---GDSLKAFlvgiVVPDPEVMPSwaqkkgiegtyQELcmKKELKKAI 310
Cdd:COG0365 456 IESALVSHPAVAEAAVvgvpDeirGQVVKAF----VVLKPGVEPS-----------DEL--AKELQAHV 507
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
105-307 |
7.25e-16 |
|
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: 78.63 E-value: 7.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 105 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC---TAGCTFTTPGDwtSGHVGAPLPCNHIKLVDAeelnywtcKGE 181
Cdd:cd05971 210 RAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVDD--------NGT 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 182 -------GEICVKGPN--VFKGYLKDEDRTKEALDSDgWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 252
Cdd:cd05971 280 plppgevGEIAVELPDpvAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEEC 357
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907081048 253 YIRsepvaqiyvHGDSLKAFLVGIvvPDP---EVMPSWAQKKGIEGTYQELcmKKELK 307
Cdd:cd05971 358 LLK---------HPAVLMAAVVGI--PDPirgEIVKAFVVLNPGETPSDAL--AREIQ 402
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
133-289 |
2.73e-15 |
|
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: 75.80 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 133 GYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAE--ELNywtcKGE-GEICVKGPNVFKGYLkDEDRTKEALDSD 209
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDgrEVP----DGEvGEIVARGPTVMAGYW-NRPEVNARRTRG 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 210 GWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqgeyvapekIENIY-------IRSEP-VAQIYVhgdslkaflvgIVVPDp 281
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSG---------AENIYpaevercLRQHPaVADAAV-----------IGVPD- 275
|
....*...
gi 1907081048 282 evmPSWAQ 289
Cdd:cd17636 276 ---PRWAQ 280
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
131-281 |
3.11e-15 |
|
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: 77.09 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 131 YEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVdaeelnywTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDG 210
Cdd:cd05921 325 MAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEG 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 211 WLHTGDIGKWL----PEGTLKIIDRKKHIFKLAQGEYVA--PekieniyIRSEPVAQI--YVHgDSL-----KAFLVGIV 277
Cdd:cd05921 397 FYCLGDAAKLAdpddPAKGLVFDGRVAEDFKLASGTWVSvgP-------LRARAVAACapLVH-DAVvagedRAEVGALV 468
|
....
gi 1907081048 278 VPDP 281
Cdd:cd05921 469 FPDL 472
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
96-264 |
7.17e-15 |
|
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: 75.30 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 96 IQASLGG---HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGD-WTSGHVGAPLPCNHIKLVDAE 171
Cdd:cd05974 191 IQQDLASfdvKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG-NSPGQpVKAGSMGRPLPGYRVALLDPD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 172 ElnywTCKGEGEICV-----KGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAP 246
Cdd:cd05974 270 G----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISP 343
|
170
....*....|....*...
gi 1907081048 247 EKIENIYIRSEPVAQIYV 264
Cdd:cd05974 344 FELESVLIEHPAVAEAAV 361
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
104-252 |
7.34e-15 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 76.16 E-value: 7.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNywtcKGeGE 183
Cdd:PRK06814 909 LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID----EG-GR 983
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 184 ICVKGPNVFKGYLKDED-RTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 252
Cdd:PRK06814 984 LFVRGPNVMLGYLRAENpGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
104-266 |
1.04e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 75.20 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAgCTFTTPGD---WTSGHVGAPLPCNHIKLVDaEELNYwTCK 179
Cdd:PRK07786 292 LRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSP-VTCMLLGEdaiRKLGSVGKVIPTVAARVVD-ENMND-VPV 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 180 GE-GEICVKGPNVFKGYLKDEDRTKEALDSdGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEP 258
Cdd:PRK07786 369 GEvGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPD 446
|
....*...
gi 1907081048 259 VAQIYVHG 266
Cdd:PRK07786 447 IVEVAVIG 454
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
110-281 |
1.40e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 74.97 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 110 GAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFTTPGDwtsgHVGAP----LPCNHI--KLVDA--EELnywtCKG 180
Cdd:PRK08316 294 GASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE----HLRRPgsagRPVLNVetRVVDDdgNDV----APG 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 181 E-GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIyirsepv 259
Cdd:PRK08316 366 EvGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEA------- 436
|
170 180
....*....|....*....|..
gi 1907081048 260 aqIYVHGDSLKAFLVGivVPDP 281
Cdd:PRK08316 437 --LYTHPAVAEVAVIG--LPDP 454
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
105-233 |
1.74e-14 |
|
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: 74.63 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 105 RMIVTGAAPASPTVLGFLRAALGCQVYE-----GYGQTECTAGCTFTTP---GDWTSGH----VGAPLPCNHIKLVDAEE 172
Cdd:cd05906 293 YLVNAGEAVVAKTIRRLLRLLEPYGLPPdairpAFGMTETCSGVIYSRSfptYDHSQALefvsLGRPIPGVSMRIVDDEG 372
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081048 173 lnywTCKGEGEIC---VKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGkWLPEGTLKIIDRKK 233
Cdd:cd05906 373 ----QLLPEGEVGrlqVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
94-264 |
6.26e-14 |
|
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: 72.75 E-value: 6.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 94 NKIQASLGGHVRMIVTGAAPASPTVLGFL--RAALGCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIKL 167
Cdd:cd17655 243 DAADDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASIyqYEPETDQQVSVpiGKPLGNTRIYI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 168 VDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQG 241
Cdd:cd17655 323 LD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RG 400
|
170 180
....*....|....*....|...
gi 1907081048 242 EYVAPEKIENIYIRSEPVAQIYV 264
Cdd:cd17655 401 YRIELGEIEARLLQHPDIKEAVV 423
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
105-282 |
1.43e-13 |
|
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: 71.72 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 105 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctaG-CTFTTPGD--WTSGH-VGAPL-PCNHIKLVDAEelnywtck 179
Cdd:COG1021 303 RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeEVILTtQGRPIsPDDEVRIVDED-------- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 180 GE-------GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKK-HIFKlaQGEYVAPEKIEN 251
Cdd:COG1021 372 GNpvppgevGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQINR--GGEKIAAEEVEN 449
|
170 180 190
....*....|....*....|....*....|.
gi 1907081048 252 iyirsepvaQIYVHGDSLKAFLVGivVPDPE 282
Cdd:COG1021 450 ---------LLLAHPAVHDAAVVA--MPDEY 469
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
104-286 |
2.83e-13 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 71.07 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTfTTPGDWtSGHVGAPLPCN---------HIKLV--DAEE 172
Cdd:PRK05852 297 LRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVT-TTQIEG-IGQTENPVVSTglvgrstgaQIRIVgsDGLP 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 173 LnywTCKGEGEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 252
Cdd:PRK05852 375 L---PAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEGV 449
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907081048 253 YIRSEPVAQIYVHGDSLKAF---LVGIVVPDPEVMPS 286
Cdd:PRK05852 450 LASHPNVMEAAVFGVPDQLYgeaVAAVIVPRESAPPT 486
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
105-282 |
3.97e-13 |
|
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: 70.43 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 105 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPL-PCNHIKLVDAEELNywTCKGE- 181
Cdd:cd05920 258 RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrLDDPDEVIIHTQGRPMsPDDEIRVVDEEGNP--VPPGEe 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 182 GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENiyirsepvaQ 261
Cdd:cd05920 336 GELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVEN---------L 405
|
170 180
....*....|....*....|.
gi 1907081048 262 IYVHGDSLKAFLVGivVPDPE 282
Cdd:cd05920 406 LLRHPAVHDAAVVA--MPDEL 424
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
103-226 |
4.40e-13 |
|
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: 70.66 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTF--TTPGDWTSGHV--GAPLPCNHIKLVDAEelnywt 177
Cdd:COG1020 732 SLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYyeVTPPDADGGSVpiGRPIANTRVYVLDAH------ 805
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081048 178 ckGE-------GEICVKGPNVFKGYLKDEDRTKEA-----LDSDG--WLHTGDIGKWLPEGTL 226
Cdd:COG1020 806 --LQpvpvgvpGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNL 866
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
103-274 |
5.18e-13 |
|
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: 70.19 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDaEELNYWTCKGEG 182
Cdd:cd05928 292 SLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 183 EICVK-GPN----VFKGYLKDEDRTKEALDSDGWLhTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSE 257
Cdd:cd05928 371 DIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHP 448
|
170 180
....*....|....*....|....
gi 1907081048 258 PVAQIYV-------HGDSLKAFLV 274
Cdd:cd05928 449 AVVESAVvsspdpiRGEVVKAFVV 472
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
97-235 |
8.25e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 69.59 E-value: 8.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 97 QASLGGHVRMIVTGAAPAsPTVLGFLRAAlGCQVYEGYGQTEcTAG----CTFTtpGDWTS----------GHVGAPLPC 162
Cdd:PRK08162 292 RAGIDHPVHAMVAGAAPP-AAVIAKMEEI-GFDLTHVYGLTE-TYGpatvCAWQ--PEWDAlplderaqlkARQGVRYPL 366
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081048 163 -NHIKLVDAEELNYWTCKGE--GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHI 235
Cdd:PRK08162 367 qEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDI 441
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
116-264 |
1.09e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 68.74 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 116 PTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTSGhVGAPLPCNHIKLVDaeelnywtckgeGEICVKGPNVFKGY 195
Cdd:PRK09029 253 PVELTEQAEQQGIRCWCGYGLTE-MASTVCAKRADGLAG-VGSPLPGREVKLVD------------GEIWLRGASLALGY 318
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081048 196 LKDeDRTKEALDSDGWLHTGDIGKWLpEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQIYV 264
Cdd:PRK09029 319 WRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQHPLVQQVFV 384
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
104-282 |
1.58e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 68.45 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWT-SGHVGAPLPCNHIKLVDAEELNYWTCKGEG 182
Cdd:PRK08314 307 LRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPDRPkLQCLGIPTFGVDARVIDPETLEELPPGEVG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 183 EICVKGPNVFKGYLKDEDRTKEA---LDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPV 259
Cdd:PRK08314 386 EIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAI 464
|
170 180 190
....*....|....*....|....*....|
gi 1907081048 260 AQIYV-------HGDSLKAFlvgiVVPDPE 282
Cdd:PRK08314 465 QEACViatpdprRGETVKAV----VVLRPE 490
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
1-369 |
1.67e-12 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 69.11 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 1 MFERVIQSVVYCHGGRVGffQGDIRLLSDDMKALRPTIFPVVPRLlnrmydkiFHQADTSLKR----------WLLEfaa 70
Cdd:PTZ00297 657 LFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysWLFE--- 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 71 krKQAEVRSGII----RNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTvlgflraalgcqvyegYGQTECTAGCTft 146
Cdd:PTZ00297 724 --RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTS----------------FSLLEHISVCY-- 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 147 tpgdwtsghvgAPLPCnhiklvdaeELNYWTCkgEGEICVKG---PNVFKGYLKDEDRTKEA------LDSDGWL-HTGD 216
Cdd:PTZ00297 784 -----------VPCLR---------EVFFLPS--EGVFCVDGtpaPSLQVDLEPFDEPSDGAgigqlvLAKKGEPrRTLP 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 217 IG-KWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAfLVGIVVPDPEVMP-SWAQKKGIE 294
Cdd:PTZ00297 842 IAaQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHCMG 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 295 ---GTYQELCMKKELKKA---ILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEEL 368
Cdd:PTZ00297 921 eggGPARQLGWTELVAYAsslLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERF 1000
|
.
gi 1907081048 369 Y 369
Cdd:PTZ00297 1001 Y 1001
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
130-244 |
5.20e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 66.99 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 130 VYEGYGQTEcTAGCTFTTpgDWTS---GHVGAPLPCNHIKLVDAEElNYwtckgegEICVKGPNVFKGYLKDEDRTKEAL 206
Cdd:PRK12582 380 FYTGYGATE-TAPTTTGT--HWDTervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAF 448
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1907081048 207 DSDGWLHTGDIGKWL----PEGTLKIIDRKKHIFKLAQGEYV 244
Cdd:PRK12582 449 DEEGFYRLGDAARFVdpddPEKGLIFDGRVAEDFKLSTGTWV 490
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
98-283 |
1.09e-11 |
|
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: 65.69 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 98 ASLGGhVRMIVTGAAPASPT-VLGFLRAALGCQVYEGYGQTECTagcTFTT-----PGDWTSGHV--GAPLPCNHIKLVD 169
Cdd:cd12117 246 ECFAG-LRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENT---TFTTshvvtELDEVAGSIpiGRPIANTRVYVLD 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 170 AeelnywtcKG-------EGEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIF 236
Cdd:cd12117 322 E--------DGrpvppgvPGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQV 393
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907081048 237 KLaQGEYVAPEKIENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPEV 283
Cdd:cd12117 394 KI-RGFRIELGEIEAALRAHPGVREAVVvvrEDAGGDKRLVAYVVAEGAL 442
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
105-286 |
1.31e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 65.88 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 105 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCNHIKLVDAE--ELNywtcKG 180
Cdd:PRK12406 274 RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGKAAPGAELRFVDEDgrPLP----QG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 181 E-GEICVKGPNV--FKGYLKDEDRTkeALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSE 257
Cdd:PRK12406 349 EiGEIYSRIAGNpdFTYHNKPEKRA--EIDRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVP 425
|
170 180 190
....*....|....*....|....*....|..
gi 1907081048 258 PVAQIYVHGDSLKAF---LVGIVVPDPEVMPS 286
Cdd:PRK12406 426 GVHDCAVFGIPDAEFgeaLMAVVEPQPGATLD 457
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
104-270 |
1.36e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 65.89 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCnhiklVDAEELNYWTCKGEGE 183
Cdd:PRK08043 481 LRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPG-----MDARLLSVPGIEQGGR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 184 ICVKGPNVFKGYLKDEDRTK-EALDSD--------GWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYI 254
Cdd:PRK08043 556 LQLKGPNIMNGYLRVEKPGVlEVPTAEnargemerGWYDTGDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSLEMVEQLAL 634
|
170
....*....|....*.
gi 1907081048 255 RSEPVAQiyvHGDSLK 270
Cdd:PRK08043 635 GVSPDKQ---HATAIK 647
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
104-279 |
2.35e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 64.79 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT------FTTPGDWTSGH----VGAPLPCNHIKLV--D 169
Cdd:cd05910 201 LRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVRIIeiD 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 170 AEELNYWTCKGE------GEICVKGPNVFKGYLKDEDRTKEALDSDG----WLHTGDIGKWLPEGTLKIIDRKKHIFKLA 239
Cdd:cd05910 281 DEPIAEWDDTLElprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITT 360
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907081048 240 QGEYVapekieniyirSEPVAQIY-VHGDSLKAFLVGIVVP 279
Cdd:cd05910 361 GGTLY-----------TEPVERVFnTHPGVRRSALVGVGKP 390
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
123-281 |
2.88e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 64.68 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 123 RAALGCQVYEGYGQTECTAGCTFTTP-----GDWTSGHVGaplPCNH------IKLVDAE--ELNywtcKGE-GEICVKG 188
Cdd:PRK07470 301 LAKLGKVLVQYFGLGEVTGNITVLPPalhdaEDGPDARIG---TCGFertgmeVQIQDDEgrELP----PGEtGEICVIG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 189 PNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENiyirsepvaQIYVHGDS 268
Cdd:PRK07470 374 PAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMY-ISGGSNVYPREIEE---------KLLTHPAV 442
|
170
....*....|...
gi 1907081048 269 LKAFLVGivVPDP 281
Cdd:PRK07470 443 SEVAVLG--VPDP 453
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
104-286 |
3.45e-11 |
|
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: 64.31 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTF--TTPGDWTSGHVGAPLPCNHIKLVDaEELNYWTCKGE 181
Cdd:cd05959 282 LRLCVSAGEALPAEVGERWKARFGLDILDGIGSTE--MLHIFlsNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEP 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 182 GEICVKGPNVFKGYLKDEDRTKEALDSdGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIYIRSEPVAQ 261
Cdd:cd05959 359 GELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLE 436
|
170 180 190
....*....|....*....|....*....|..
gi 1907081048 262 IYVHG-------DSLKAFlvgiVVPDPEVMPS 286
Cdd:cd05959 437 AAVVGvededglTKPKAF----VVLRPGYEDS 464
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
134-280 |
3.61e-11 |
|
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: 64.03 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 134 YGQTECTAGCTFTTPGDWTSGH-----VGAPLPCNHIKLVDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDS 208
Cdd:cd17650 245 YGVTEATIDSTYYEEGRDPLGDsanvpIGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 209 DGW------LHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYV---HGDSLKAFLVGIVVP 279
Cdd:cd17650 324 NPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELGEIESQLARHPAIDEAVVavrEDKGGEARLCAYVVA 402
|
.
gi 1907081048 280 D 280
Cdd:cd17650 403 A 403
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
111-282 |
3.64e-11 |
|
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: 64.32 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 111 AAPASPTVLGFLRAALGCQVYEGYGQTECTaGCTFTTPGDWTS--GHVGAPLPCN-HIKLVDAEELNYWTckgEGEICVK 187
Cdd:cd05929 253 AAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-GLTIINGEEWLThpGSVGRAVLGKvHILDEDGNEVPPGE---IGEVYFA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 188 GPNVFKgYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRsepvaqiyvHGD 267
Cdd:cd05929 329 NGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIA---------HPK 397
|
170
....*....|....*
gi 1907081048 268 SLKAFLVGivVPDPE 282
Cdd:cd05929 398 VLDAAVVG--VPDEE 410
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
105-362 |
4.50e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 63.96 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 105 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPgdwTSGHVGAPLPCNH--------------IKLVDA 170
Cdd:PRK07008 296 RRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKL---KWKHSQLPLDEQRkllekqgrviygvdMKIVGD 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 171 E--ELNyWTCKGEGEICVKGPNVFKGYLKDEDrtkEALDsDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEK 248
Cdd:PRK07008 373 DgrELP-WDGKAFGDLQVRGPWVIDRYFRGDA---SPLV-DGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSID 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 249 IENIYIRSEPVAQIYVhgdslkaflvgIVVPDPEvmpsW--------AQKKGIEGTYQELCMKKELKKA---ILDDMVMl 317
Cdd:PRK07008 447 IENVAVAHPAVAEAAC-----------IACAHPK----WderpllvvVKRPGAEVTREELLAFYEGKVAkwwIPDDVVF- 510
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907081048 318 gkesglhsfeqVKAIyihcdmfsvqngLLTPTLKAKRPELREYFK 362
Cdd:PRK07008 511 -----------VDAI------------PHTATGKLQKLKLREQFR 532
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
182-285 |
4.59e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 63.99 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 182 GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQ 261
Cdd:PRK06164 378 GEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIEHALEALPGVAA 456
|
90 100
....*....|....*....|....*.
gi 1907081048 262 IYVHGDSL--KAFLVGIVVPDPEVMP 285
Cdd:PRK06164 457 AQVVGATRdgKTVPVAFVIPTDGASP 482
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
104-282 |
4.74e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 63.94 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCN-HIKLVDAEELNywtcKG 180
Cdd:PRK13391 277 LEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLAhpGTVGRAMFGDlHILDDDGAELP----PG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 181 E-GEICVKGPNVFKgYLKDEDRTKEALDSDG-WLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEP 258
Cdd:PRK13391 352 EpGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGVNIYPQEAENLLITHPK 429
|
170 180
....*....|....*....|....
gi 1907081048 259 VAQIYVHGdslkaflvgivVPDPE 282
Cdd:PRK13391 430 VADAAVFG-----------VPNED 442
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
103-280 |
5.80e-11 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 63.46 E-value: 5.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAApaSPTVLGFLRAALGCQVYEGYGQTECT--AGCTFTTPGDwTSGHVGAPLPCNHIKLVDAEelnywtckG 180
Cdd:cd12116 241 GLTALCGGEA--LPPDLAARLLSRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLDAA--------L 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 181 E-------GEICVKGPNVFKGYLKDEDRTKEALDSDGWLH-------TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAP 246
Cdd:cd12116 310 RpvppgvpGELYIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIEL 388
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907081048 247 EKIENIYIRSEPVAQ--IYVHGDSLKAFLVGIVVPD 280
Cdd:cd12116 389 GEIEAALAAHPGVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
104-274 |
8.55e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 63.32 E-value: 8.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPaSPTVLgFLRAALGCQVYEGYGQTEcTAG----CTFTTPGDWTSGHVGAPLPCNH---------IKLVDA 170
Cdd:PLN02479 313 VHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstvCAWKPEWDSLPPEEQARLNARQgvryiglegLDVVDT 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 171 EELNYWTCKGE--GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEK 248
Cdd:PLN02479 390 KTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSLE 467
|
170 180
....*....|....*....|....*.
gi 1907081048 249 IENIyirsepvaqIYVHGDSLKAFLV 274
Cdd:PLN02479 468 VENV---------VYTHPAVLEASVV 484
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
104-300 |
1.03e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 62.99 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAAL--GCQVYEGYGQTECTAGCT-------FTTPGDWTSGH---VGAPLPCNHIKLV--D 169
Cdd:PRK09274 290 LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEALPISSiesreilFATRAATDNGAgicVGRPVDGVEVRIIaiS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 170 AEELNYWT-----CKGE-GEICVKGPNVFKGYLKDEDRTKEA--LDSDG--WLHTGDIGkWL-PEGTLKIIDRKKHIFKL 238
Cdd:PRK09274 370 DAPIPEWDdalrlATGEiGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVET 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 239 AQGEYVapekieniyirSEPVAQIY-VHGDSLKAFLVGIVVPD---P----EVMPSWAQKKgiEGTYQEL 300
Cdd:PRK09274 449 AGGTLY-----------TIPCERIFnTHPGVKRSALVGVGVPGaqrPvlcvELEPGVACSK--SALYQEL 505
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
104-250 |
1.05e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 63.09 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVL----------GFLRAALGCqvyeGYGQTECTAGCTFTTPGD--------------------WTS 153
Cdd:PRK07768 278 LRFALNGAEPIDPADVedlldagarfGLRPEAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATK 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 154 GHV------GAPLPCNHIKLVDaEELNYWTCKGEGEICVKGPNVFKGYLkDEDRTKEALDSDGWLHTGDIGKWLPEGTLK 227
Cdd:PRK07768 354 GNTrrlatlGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVV 431
|
170 180
....*....|....*....|...
gi 1907081048 228 IIDRKKHIFKLAqGEYVAPEKIE 250
Cdd:PRK07768 432 VCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
102-233 |
1.22e-10 |
|
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: 62.64 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 102 GHVRMIVTGAAPASPTVL----------GFLRAAlgcqVYEGYGQTECTAGCTFTTPG----------DWTSGHV----- 156
Cdd:cd05931 271 SSWRVALNGAEPVRPATLrrfaeafapfGFRPEA----FRPSYGLAEATLFVSGGPPGtgpvvlrvdrDALAGRAvavaa 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 157 -----------GAPLPCNHIKLVDAEelnywTCK-----GEGEICVKGPNVFKGYLKDEDRTKE------ALDSDGWLHT 214
Cdd:cd05931 347 ddpaarelvscGRPLPDQEVRIVDPE-----TGRelpdgEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRT 421
|
170
....*....|....*....
gi 1907081048 215 GDIGkWLPEGTLKIIDRKK 233
Cdd:cd05931 422 GDLG-FLHDGELYITGRLK 439
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
104-286 |
4.18e-10 |
|
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: 60.82 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTG--AAPASPTVLGFLRAALGCQVYEGYGQTE---CTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDAeelnywt 177
Cdd:cd17651 255 LRYLLTGgeQLVLTEDLREFCAGLPGLRLHNHYGPTEthvVTALSLPGDPAAWPApPPIGRPIDNTRVYVLDA------- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 178 cKGE-------GEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYV 244
Cdd:cd17651 328 -ALRpvppgvpGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRI 405
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907081048 245 APEKIENIYIRSEPVAQIYV------HGDslkAFLVGIVVPDPEVMPS 286
Cdd:cd17651 406 ELGEIEAALARHPGVREAVVlaredrPGE---KRLVAYVVGDPEAPVD 450
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
103-266 |
4.41e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 60.92 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAApASPTvlGFLRA--ALGCQVYEGYGQTECTAGCTFTT--------PGDWTSGHV---GAPLPCNHIKLVD 169
Cdd:PRK06018 295 HLKMVVCGGS-AMPR--SMIKAfeDMGVEVRHAWGMTEMSPLGTLAAlkppfsklPGDARLDVLqkqGYPPFGVEMKITD 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 170 --AEELNyWTCKGEGEICVKGPNVFKGYLKDEDrtkEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPE 247
Cdd:PRK06018 372 daGKELP-WDGKTFGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRSKDVIK-SGGEWISSI 446
|
170
....*....|....*....
gi 1907081048 248 KIENIYIRSEPVAQIYVHG 266
Cdd:PRK06018 447 DLENLAVGHPKVAEAAVIG 465
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
127-290 |
7.25e-10 |
|
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: 60.26 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 127 GCQVYEGYGQTECTAGCT-FTTPGDWTSGHVGAPLPCNHIKLVDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEA 205
Cdd:cd17645 234 GYKLVNNYGPTENTVVATsFEIDKPYANIPIGKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLARGYLNRPELTAEK 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 206 LDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPV---AQIYVHGDSLKAFLVGI 276
Cdd:cd17645 313 FIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIEPFLMNHPLIelaAVLAKEDADGRKYLVAY 391
|
170
....*....|....*...
gi 1907081048 277 VVP----DPEVMPSWAQK 290
Cdd:cd17645 392 VTApeeiPHEELREWLKN 409
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
147-285 |
7.29e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 60.36 E-value: 7.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 147 TPGDWTSGHVGAPLPCNHIKLVDA--EELNYWTckgEGEICVKGPNVFKGYLKDEDRTKEAL--DSDG--WLHTGDIGKW 220
Cdd:cd12114 293 VPPDWRSIPYGRPLANQRYRVLDPrgRDCPDWV---PGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRY 369
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081048 221 LPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQ--IYVHGDSLKAFLVGIVVPDPEVMP 285
Cdd:cd12114 370 RPDGTLEFLGRRDGQVKV-RGYRIELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPDNDGTP 435
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
104-252 |
7.42e-10 |
|
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: 59.58 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDAEELNYWTcKGEG 182
Cdd:cd17635 119 LRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPS-ASFG 197
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 183 EICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 252
Cdd:cd17635 198 TIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
104-285 |
8.07e-10 |
|
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: 60.02 E-value: 8.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTFT--TPGDWTSGHVGAPLPCNHIKLVDaEELNYWTCKG 180
Cdd:cd12115 215 VRVVNLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTTYSTVApvPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGV 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 181 EGEICVKGPNVFKGYLKDEDRTKEALDSDGWL------HTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYI 254
Cdd:cd12115 294 PGELYIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALR 372
|
170 180 190
....*....|....*....|....*....|....
gi 1907081048 255 RSEPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMP 285
Cdd:cd12115 373 SIPGVREavVVAIGDAAgERRLVAYIVAEPGAAG 406
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
104-266 |
8.67e-10 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 60.20 E-value: 8.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASP-----TVLGFLRAALgcqvYEGYGQTECTAGCTFTTPGDWT-----------------SGH------ 155
Cdd:PLN02860 290 VRKILNGGGSLSSrllpdAKKLFPNAKL----FSAYGMTEACSSLTFMTLHDPTlespkqtlqtvnqtkssSVHqpqgvc 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 156 VGAPLPcnHIKL-VDAEELNYwtckgEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKH 234
Cdd:PLN02860 366 VGKPAP--HVELkIGLDESSR-----VGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSND 438
|
170 180 190
....*....|....*....|....*....|..
gi 1907081048 235 IFKlAQGEYVAPEKIENIYIRSEPVAQIYVHG 266
Cdd:PLN02860 439 RIK-TGGENVYPEEVEAVLSQHPGVASVVVVG 469
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
104-282 |
1.35e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 59.53 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLgflRAAL---GCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVGAPLPCN-HIKLVDAEELNywt 177
Cdd:PRK08276 264 LRVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGEvRILDEDGNELP--- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 178 cKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGkWLPE-GTLKIIDRKKHIFkLAQGEYVAPEKIENIYIR 255
Cdd:PRK08276 337 -PGEiGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLDEdGYLYLTDRKSDMI-ISGGVNIYPQEIENLLVT 413
|
170 180
....*....|....*....|....*..
gi 1907081048 256 SEPVAQIYVHGdslkaflvgivVPDPE 282
Cdd:PRK08276 414 HPKVADVAVFG-----------VPDEE 429
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
114-283 |
2.02e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 58.92 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 114 ASPTVLGFLRAALGCQVYEGYGQTEctAGCTFTTPGDWTSGHVGaPLPCNhIKLVDAE--------------ELNYWTCK 179
Cdd:PRK07867 277 GAPGDIARFARRFGCVVVDGFGSTE--GGVAITRTPDTPPGALG-PLPPG-VAIVDPDtgtecppaedadgrLLNADEAI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 180 GEgEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPV 259
Cdd:PRK07867 353 GE-LVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDA 429
|
170 180
....*....|....*....|....
gi 1907081048 260 AQIYVHGdslkaflvgivVPDPEV 283
Cdd:PRK07867 430 TEVAVYA-----------VPDPVV 442
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
103-259 |
2.34e-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: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASP----------TVLGFLRAAlgcqVYEGYGQTECTAGCTF--------------------------- 145
Cdd:cd05908 229 SIRMILNGAEPIDYelchefldhmSKYGLKRNA----ILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepevd 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 146 -TTPGDWTSGHVGAPLPCNHIKLVDaeELNYWTCKGE-GEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGkWLPE 223
Cdd:cd05908 305 kKDSECLTFVEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRN 381
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907081048 224 GTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPV 259
Cdd:cd05908 382 GRLVITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
157-233 |
2.51e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 58.86 E-value: 2.51e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081048 157 GAPLPCNHIKLVDA--EELNYwtcKGEGEICVKGPNVFKGYLKDEDRTKeALDSDGWLHTGDIGkWLPEGTLKIIDRKK 233
Cdd:PRK09192 388 GKALPGHEIEIRNEagMPLPE---RVVGHICVRGPSLMSGYFRDEESQD-VLAADGWLDTGDLG-YLLDGYLYITGRAK 461
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
103-266 |
5.59e-09 |
|
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: 57.03 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTEcTAGCTFTTPGD-WTSGHVGAPLPCNHIKLVDAEElnywtcKG 180
Cdd:cd17633 111 KIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSE-LSFITYNFNQEsRPPNSVGRPFPNVEIEIRNADG------GE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 181 EGEICVKGPNVFKGYLKDEDRTKealdsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVA 260
Cdd:cd17633 184 IGKIFVKSEMVFSGYVRGGFSNP-----DGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIE 257
|
....*.
gi 1907081048 261 QIYVHG 266
Cdd:cd17633 258 EAIVVG 263
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
107-289 |
5.83e-09 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 57.26 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 107 IVTGAAPASPTVLgflRAALGCQVYEGYGQTECTAGCTFTTP-GDWTSGHVGAPLPCNHIKLVDAeELNYWTCKGEGEIC 185
Cdd:cd17652 210 VVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLDA-RLRPVPPGVPGELY 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 186 VKGPNVFKGYLKDEDRTKEALDSD------GWLH-TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEP 258
Cdd:cd17652 286 IAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIELGEVEAALTEHPG 364
|
170 180 190
....*....|....*....|....*....|....
gi 1907081048 259 VAQ--IYVHGDSL-KAFLVGIVVPDPEVMPSWAQ 289
Cdd:cd17652 365 VAEavVVVRDDRPgDKRLVAYVVPAPGAAPTAAE 398
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
104-290 |
6.92e-09 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 57.33 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAA--LGCQVYeGYGQTECTAGCTFTTPGDWT---SGHVGAPLPCNHIKLVDAEELNYWTC 178
Cdd:PRK05857 288 LRLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVYLAATDGIGPTAP 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 179 KGE-----GEICVKGPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIy 253
Cdd:PRK05857 367 GAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGGVNIAPDEVDRI- 443
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907081048 254 irSEPVAQI-----YVHGDSLKAFLVGI-VVPDPEVMPSWAQK 290
Cdd:PRK05857 444 --AEGVSGVreaacYEIPDEEFGALVGLaVVASAELDESAARA 484
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
104-290 |
1.00e-08 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 56.71 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGA---------PLPCNHiKLVDAEELN 174
Cdd:PRK05620 300 LQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWayrvsqgrfPASLEY-RIVNDGQVM 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 175 YWTCKGEGEICVKGPNVFKGYLKDE----------------DRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKl 238
Cdd:PRK05620 379 ESTDRNEGEIQVRGNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR- 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907081048 239 AQGEYVAPEKIENIYIRSEPVaqiyvhgdsLKAFLVGIvvPDPEvmpsWAQK 290
Cdd:PRK05620 458 SGGEWIYSAQLENYIMAAPEV---------VECAVIGY--PDDK----WGER 494
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
129-282 |
1.11e-08 |
|
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: 56.55 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 129 QVYEGYGQTECTAGCTFT--TPGDW---TSGHVGAPLPCNHIKLVDAEeLNYWTCKGEGEICVKGPNVFKGYLKDEDRTK 203
Cdd:cd17643 240 QLVNMYGITETTVHVTFRplDAADLpaaAASPIGRPLPGLRVYVLDAD-GRPVPPGVVGELYVSGAGVARGYLGRPELTA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 204 E-------ALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYV---HGDSLKAFL 273
Cdd:cd17643 319 ErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RGFRIELGEIEAALATHPSVRDAAVivrEDEPGDTRL 397
|
....*....
gi 1907081048 274 VGIVVPDPE 282
Cdd:cd17643 398 VAYVVADDG 406
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
90-282 |
3.45e-08 |
|
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: 54.97 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 90 ELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSGHV--GAPLPCNHIK 166
Cdd:cd17646 241 RVFLAEPAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVThWPVRGPAETPSVpiGRPVPNTRLY 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 167 LVDAEeLNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLH------TGDIGKWLPEGTLKIIDRKKHIFKLaQ 240
Cdd:cd17646 321 VLDDA-LRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-R 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907081048 241 GEYVAPEKIENIYIRSEPVAQIYV---HGDSLKAFLVGIVVPDPE 282
Cdd:cd17646 399 GFRVEPGEIEAALAAHPAVTHAVVvarAAPAGAARLVGYVVPAAG 443
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
129-254 |
4.52e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 54.82 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 129 QVYEGYGQTECTAGCTFTT---PGDwtSGHVGAPLPCNHIKLVdAEELNYWTCKGE-GEICVKGPNVFKGYL-KDEDRTK 203
Cdd:PRK06334 327 QLRQGYGTTECSPVITINTvnsPKH--ESCVGMPIRGMDVLIV-SEETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGF 403
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907081048 204 EALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYI 254
Cdd:PRK06334 404 VELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEALESILM 453
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
108-266 |
4.60e-08 |
|
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: 54.82 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 108 VTGAAPASP-TVLGFLRAALGCQVYEGYGQTECTagcTFTTPGDWTSGHVGAPLPCNHIKLVD-AEELNYWTCKG-EGEI 184
Cdd:cd05923 272 VTFAGATMPdAVLERVNQHLPGEKVNIYGTTEAM---NSLYMRDARTGTEMRPGFFSEVRIVRiGGSPDEALANGeEGEL 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 185 CVK--GPNVFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEPVAQI 262
Cdd:cd05923 349 IVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEV 426
|
....
gi 1907081048 263 YVHG 266
Cdd:cd05923 427 VVIG 430
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
105-289 |
6.19e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 54.23 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 105 RMIVTGAAPASPTVLGF-----LRAALGcqvyegYGQTEcTAG--CTFTtPGDWTSG--HVGAPLPCNHIKLvdaeelny 175
Cdd:PRK07445 233 RTILLGGAPAWPSLLEQarqlqLRLAPT------YGMTE-TASqiATLK-PDDFLAGnnSSGQVLPHAQITI-------- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 176 wTCKGEGEICVKGPNVFKGYLkdedrtKEALDSDGWLHTGDIGKWLPEGTLKIIDR--KKHIfklAQGEYVAPEKIENIY 253
Cdd:PRK07445 297 -PANQTGNITIQAQSLALGYY------PQILDSQGIFETDDLGYLDAQGYLHILGRnsQKII---TGGENVYPAEVEAAI 366
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907081048 254 IRSEPVAQIYVHGdslkaflvgivVPDPEvmpsWAQ 289
Cdd:PRK07445 367 LATGLVQDVCVLG-----------LPDPH----WGE 387
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
105-281 |
6.34e-08 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 54.23 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 105 RMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCT---------FTT------PGD--WTSGHVGAPLPCNHIkl 167
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTrlddsderiFTTqgrpmsPDDevWVADADGNPLPQGEV-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 168 vdaeelnywtckgeGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHifklaQ----GEY 243
Cdd:PRK10946 381 --------------GRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEK 441
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907081048 244 VAPEKIENIYIRsepvaqiyvHGDSLKAFLVGIvvPDP 281
Cdd:PRK10946 442 IAAEEIENLLLR---------HPAVIHAALVSM--EDE 468
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
100-286 |
9.38e-08 |
|
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: 53.64 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 100 LGGHVRMIVTgAAPASPTVLGFL-RAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNywTC 178
Cdd:cd05958 211 DLSSLRKCVS-AGEALPAALHRAwKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEGNP--VP 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 179 KGE-GEICVKGPNvfkGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSE 257
Cdd:cd05958 288 DGTiGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHP 363
|
170 180 190
....*....|....*....|....*....|..
gi 1907081048 258 PVAQIYVHGDSLKAFLV---GIVVPDPEVMPS 286
Cdd:cd05958 364 AVAECAVVGHPDESRGVvvkAFVVLRPGVIPG 395
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
104-283 |
1.31e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 53.09 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEcTAGCTFTTPGDWTS--GHVG-APLPCNHIKLVDAEELNywtcKG 180
Cdd:PRK13390 272 LRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGrSVLGDLHICDDDGNELP----AG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 181 E-GEICVKGPNVFKGYLKDEDRTKEALDSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSE 257
Cdd:PRK13390 347 RiGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALTMHP 425
|
170 180
....*....|....*....|....*.
gi 1907081048 258 PVAQIYVHGdslkaflvgivVPDPEV 283
Cdd:PRK13390 426 AVHDVAVIG-----------VPDPEM 440
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
104-274 |
1.68e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 53.11 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAALG-CQVYEGYGQTEctAGCTFT--TPGDWTSGHVGAPLPCNHIKLVdAEELNYWTCKG 180
Cdd:PRK06060 262 LRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTE--VGQTFVsnRVDEWRLGTLGRVLPPYEIRVV-APDGTTAGPGV 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 181 EGEICVKGPNVFKGYLkdeDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIfKLAQGEYVAPEKIENIYIRSEPVA 260
Cdd:PRK06060 339 EGDLWVRGPAIAKGYW---NRPDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDT-EVIGGVNVDPREVERLIIEDEAVA 414
|
170 180
....*....|....*....|.
gi 1907081048 261 QIYVHG-------DSLKAFLV 274
Cdd:PRK06060 415 EAAVVAvrestgaSTLQAFLV 435
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
86-286 |
1.82e-07 |
|
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: 52.82 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 86 SIWDELFFNKIQASLGG--HVRMIVTGAAPASPTVLGFLRAALG--CQVYEGYGQTECTAGCTFTTPGDWTSGH-----V 156
Cdd:cd17644 206 AYWHLLVLELLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpI 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 157 GAPLPCNHIKLVDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLH--------TGDIGKWLPEGTLKI 228
Cdd:cd17644 286 GRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEY 364
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907081048 229 IDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQ--IYVHGDSL-KAFLVGIVVPDPEVMPS 286
Cdd:cd17644 365 LGRIDNQVKI-RGFRIELGEIEAVLSQHNDVKTavVIVREDQPgNKRLVAYIVPHYEESPS 424
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
127-283 |
2.79e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 52.34 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 127 GCQVYEGYGQTEctAGCTFTTPGDWTSGHVGAPLPcnHIKLVDAEELNywTC---------------KGEGEICVK-GPN 190
Cdd:PRK13388 288 GCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGAP--GVAIYNPETLT--ECavarfdahgallnadEAIGELVNTaGAG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 191 VFKGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYVHGdslk 270
Cdd:PRK13388 362 FFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYA---- 435
|
170
....*....|...
gi 1907081048 271 aflvgivVPDPEV 283
Cdd:PRK13388 436 -------VPDERV 441
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
127-268 |
5.19e-07 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 51.32 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 127 GCQVYEGYG--QTECTAGCTFTTPGDWTS-GHVGAPLPCNHIKLVDaEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTK 203
Cdd:cd17656 271 NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD-QEQQLQPQGIVGELYISGASVARGYLNRQELTA 349
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081048 204 EALDSDGW------LHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQ--IYVHGDS 268
Cdd:cd17656 350 EKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIEAQLLNHPGVSEavVLDKADD 421
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
134-252 |
8.00e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 50.92 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 134 YGQTECTAGCTFTTPG-----------DWTSGH----VGAPLPCNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKD 198
Cdd:PRK05851 310 YGLAESTCAVTVPVPGiglrvdevttdDGSGARrhavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQ 389
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1907081048 199 EdrtkeALDSDGWLHTGDIGkWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENI 252
Cdd:PRK05851 390 A-----PIDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV 436
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
103-285 |
8.28e-07 |
|
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: 50.48 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 103 HVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEC--TAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEeLNYWTCKG 180
Cdd:cd17648 208 HLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETtvTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDA-MKRVPVGA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 181 EGEICVKGPNVFKGYLKDEDRTKE-------------ALDSDGWLH-TGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAP 246
Cdd:cd17648 287 VGELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQVKI-RGQRIEP 365
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907081048 247 EKIENIY-----IRSEPVAQIYVHGDSLKA---FLVGIVVPDPEVMP 285
Cdd:cd17648 366 GEVEAALasypgVRECAVVAKEDASQAQSRiqkYLVGYYLPEPGHVP 412
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
93-281 |
8.31e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 50.55 E-value: 8.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 93 FNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAgCTFTTPGDWTSGHVGAPLPCNHIKLVDAEE 172
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF-VTALVDEESERRPNSVGRPFHNVQVRICNE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 173 LNYWTCKGE-GEICVKGPNVFKGYLKDEDRTKEaLDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIEN 251
Cdd:PRK07638 324 AGEEVQKGEiGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIES 401
|
170 180 190
....*....|....*....|....*....|
gi 1907081048 252 IYIRSEPVAQIYVHGdslkaflvgivVPDP 281
Cdd:PRK07638 402 VLHEHPAVDEIVVIG-----------VPDS 420
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
104-282 |
1.71e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 49.93 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 104 VRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECtAGCTFTTPGDWT--SGHVGAPLPCNHIKLVDAE--ELNywtcK 179
Cdd:PRK07788 325 LKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAeaPGTVGRPPKGVTVKILDENgnEVP----R 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 180 GE-GEICVKGPNVFKGYLkdEDRTKEALdsDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYIRSEP 258
Cdd:PRK07788 400 GVvGRIFVGNGFPFEGYT--DGRDKQII--DGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDLLAGHPD 474
|
170 180
....*....|....*....|....
gi 1907081048 259 VAQIYVHGdslkaflvgivVPDPE 282
Cdd:PRK07788 475 VVEAAVIG-----------VDDEE 487
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
102-264 |
1.94e-06 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 49.76 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 102 GH-VRMIVTGAAPASptVLGFLRAALGCQVYEGYGQTECTAGCtFTTPGDWTSGHVGAPLPCNHIKLVDAE--ELNywtc 178
Cdd:PRK06155 293 AHrVRVALGPGVPAA--LHAAFRERFGVDLLDGYGSTETNFVI-AVTHGSQRPGSMGRLAPGFEARVVDEHdqELP---- 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 179 KGE-GEICVKG--PNVF-KGYLKDEDRTKEALdSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKlAQGEYVAPEKIENIyI 254
Cdd:PRK06155 366 DGEpGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIR-RRGENISSFEVEQV-L 442
|
170
....*....|.
gi 1907081048 255 RSEP-VAQIYV 264
Cdd:PRK06155 443 LSHPaVAAAAV 453
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
159-226 |
4.11e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 48.35 E-value: 4.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081048 159 PLPCNHIK-----LVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEAL-DSDGW--LHTGDIGKwLPEGTL 226
Cdd:PRK04813 317 RLPIGYAKpdsplLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY-LEDGLL 391
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
94-319 |
1.18e-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: 47.04 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 94 NKIQASLGGHVRMIVTGAAPASPTV----LGFLRA--ALGCQVYEGYGqTECTAGCTFTTPGDWTSGHVGAPLPCNHI-K 166
Cdd:cd05915 263 ESTGHRLKTLRRLVVGGSAAPRSLIarfeRMGVEVrqGYGLTETSPVV-VQNFVKSHLESLSEEEKLTLKAKTGLPIPlV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 167 LVDAEELNYWTCKGEGE----ICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGE 242
Cdd:cd05915 342 RLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG-GE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 243 YVAPEKIENIyirsepvaqIYVHGDSLKAFLVGivVPDP---EVMPSWAQKKGIEGTYQELCmkkELKKAILDDMVMLGK 319
Cdd:cd05915 421 WISSVDLENA---------LMGHPKVKEAAVVA--IPHPkwqERPLAVVVPRGEKPTPEELN---EHLLKAGFAKWQLPD 486
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
107-289 |
2.48e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 45.81 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 107 IVTGAAPASPTVLgflRAA--LGCQVYEGYGQTECTAGCTFTtpgdwtsghvGAPLPCNHIKLVDaeelnywtckgeGEI 184
Cdd:PRK07824 156 VLVGGGPAPAPVL---DAAaaAGINVVRTYGMSETSGGCVYD----------GVPLDGVRVRVED------------GRI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 185 CVKGPNVFKGYLKDEDrtKEALDSDGWLHTGDIGKwLPEGTLKIIDRKKHIFKLAqGEYVAPEKIENIYIRSEPVAQIYV 264
Cdd:PRK07824 211 ALGGPTLAKGYRNPVD--PDPFAEPGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLPQVVEAALATHPAVADCAV 286
|
170 180
....*....|....*....|....*...
gi 1907081048 265 HG---DSLKAFLVGIVVPDPEVMPSWAQ 289
Cdd:PRK07824 287 FGlpdDRLGQRVVAAVVGDGGPAPTLEA 314
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
122-315 |
3.86e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 46.10 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 122 LRAALGCQVYEGYGQTECTAGCT-FTTPGDWTSG----HVGAPLPCNHIKLVDaEELNYWTCKGEGEICVKGPNVFKGYL 196
Cdd:PRK12316 4830 WRALKPVYLFNGYGPTETTVTVLlWKARDGDACGaaymPIGTPLGNRSGYVLD-GQLNPLPVGVAGELYLGGEGVARGYL 4908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 197 KDEDRTKEALDSD------GWLH-TGDIGKWLPEGTLKIIDRKKHI-----FKLAQGEYVAPEKiENIYIRSEPVaqIYV 264
Cdd:PRK12316 4909 ERPALTAERFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVDHQvkirgFRIELGEIEARLR-EHPAVREAVV--IAQ 4985
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907081048 265 HGdSLKAFLVGIVVP-DPEVMPSWAQKKGIEGTyqelcMKKELKKAILDDMV 315
Cdd:PRK12316 4986 EG-AVGKQLVGYVVPqDPALADADEAQAELRDE-----LKAALRERLPEYMV 5031
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
105-290 |
6.76e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 44.30 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 105 RMIVTGAAPASPTVL-GFLRAALGCQVYEGYGQTECTAGCTFTTPGdwtSGHVGAPL-PCNHIKLVDAEELNYWTCK--G 180
Cdd:cd05924 137 FAISSGGALLSPEVKqGLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGPFtRANPDTVVLDDDGRVVPPGsgG 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 181 EGEICVKGpNVFKGYLKDEDRTKEA---LDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAqGEYVAPEKIEniyirse 257
Cdd:cd05924 214 VGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTG-GEKVFPEEVE------- 284
|
170 180 190
....*....|....*....|....*....|...
gi 1907081048 258 pvAQIYVHGDSLKAFLVGivVPDPEvmpsWAQK 290
Cdd:cd05924 285 --EALKSHPAVYDVLVVG--RPDER----WGQE 309
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
130-266 |
1.15e-04 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 43.96 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 130 VYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKL--------VDAEELNYWT------CK----GE-GEICVKGPN 190
Cdd:cd05937 229 IGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFenqvvlvkMDPETDDPIRdpktgfCVrapvGEpGEMLGRVPF 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 191 V----FKGYLKDEDRTKEAL------DSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVA 260
Cdd:cd05937 309 KnreaFQGYLHNEDATESKLvrdvfrKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIA 387
|
....*.
gi 1907081048 261 QIYVHG 266
Cdd:cd05937 388 EANVYG 393
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
101-283 |
2.00e-04 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 43.21 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 101 GGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTEctAGCTFT-TPGDWTSG--HVGAPLPCNHIKLVDAE--ELNy 175
Cdd:PRK13382 311 GRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATE--AGMIATaTPADLRAApdTAGRPAEGTEIRILDQDfrEVP- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 176 wtcKGE-GEICVKGPNVFKGYlkDEDRTKEAldSDGWLHTGDIGKWLPEGTLKIIDRKKHIFkLAQGEYVAPEKIENIYI 254
Cdd:PRK13382 388 ---TGEvGTIFVRNDTQFDGY--TSGSTKDF--HDGFMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIEVEKTLA 459
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907081048 255 RSEPVAQIYV-------HGDSLKAFlvgiVVPDPEV 283
Cdd:PRK13382 460 THPDVAEAAVigvddeqYGQRLAAF----VVLKPGA 491
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
129-282 |
5.44e-04 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 41.96 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 129 QVYEGYGQTECTAGCT--FTTPGdwTSGHVGAPLPCNH-IKLV--DAEELNYWT-----C----KGE-----GEICVKGP 189
Cdd:cd05940 222 RIAEFYAATEGNSGFInfFGKPG--AIGRNPSLLRKVApLALVkyDLESGEPIRdaegrCikvpRGEpglliSRINPLEP 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 190 nvFKGYLKDEDRTKEAL-----DSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLaQGEYVAPEKIENIYIRSEPVAQIYV 264
Cdd:cd05940 300 --FDGYTDPAATEKKILrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRW-KGENVSTTEVAAVLGAFPGVEEANV 376
|
170 180
....*....|....*....|...
gi 1907081048 265 HGDSL-----KAFLVGIVVPDPE 282
Cdd:cd05940 377 YGVQVpgtdgRAGMAAIVLQPNE 399
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
90-275 |
8.55e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 41.69 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 90 ELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAAL-GCQVYEGYGQTECTAGCTF--TTPGDWTSGHVGAPLPCNHIK 166
Cdd:PRK05691 1376 QLFIDEPLAAACTSLRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTETAINVTHwqCQAEDGERSPIGRPLGNVLCR 1455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 167 LVDAEeLNYWTCKGEGEICVKGPNVFKGYLKDEDRTKE-----ALDSDG--WLHTGDIGKWLPEGTLKIIDRKKHIFKLa 239
Cdd:PRK05691 1456 VLDAE-LNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL- 1533
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907081048 240 QGEYVAPEKIENIYIRSEPVAQ--IYVHGDSLKAFLVG 275
Cdd:PRK05691 1534 RGFRVEPEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
157-261 |
1.81e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.54 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 157 GAPLPCNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEA---LDSDGWLHTGDIGkWLPEGTLKIIDRKK 233
Cdd:PRK05691 373 GRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLG-FLRDGELFVTGRLK 451
|
90 100
....*....|....*....|....*...
gi 1907081048 234 HIFkLAQGEYVAPEKIENIYIRSEPVAQ 261
Cdd:PRK05691 452 DML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
97-274 |
2.17e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 40.15 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 97 QASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTF------TTPGDWTSghVGAPLPCNHIKLVDa 170
Cdd:PRK05691 3979 RQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfrvdlaSTRGSYLP--IGSPTDNNRLYLLD- 4055
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081048 171 EELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEAL-------DSDGWLHTGDIGKWLPEGTLKIIDRKKHI-----FKL 238
Cdd:PRK05691 4056 EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDHQvkirgYRI 4135
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907081048 239 AQGEYVApEKIENIYIRSEPVA-QIYVHGDSLKAFLV 274
Cdd:PRK05691 4136 ELGEIEA-RLHEQAEVREAAVAvQEGVNGKHLVGYLV 4171
|
|
| |
