|
Name |
Accession |
Description |
Interval |
E-value |
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
38-458 |
0e+00 |
|
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: 776.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 38 DMITWIAGAVTKDFKL---TDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVP 114
Cdd:cd05933 173 DNITWTAKAASQHMDLrpaTVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKGTLVKTLREVRPTAFMGVP 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 115 QIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGLDHCHSFISGTAPL 194
Cdd:cd05933 253 RVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLFYRLAKKLVFKKVRKALGLDRCQKFFTGAAPI 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 195 NQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETE 274
Cdd:cd05933 333 SRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGIGEICFWGRHVFMGYLNMEDK 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 275 TTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKIPIISNAMLVGDKLKFLSMLLTLKC 354
Cdd:cd05933 413 TEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPIISNAMLIGDKRKFLSMLLTLKC 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 355 EMNQMSGEPLDKLNFEAINFCRGLGSQASTVTEIVKQQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGE 434
Cdd:cd05933 493 EVNPETGEPLDELTEEAIEFCRKLGSQATRVSEIAGGKDPKVYEAIEEGIKRVNKKAISNAQKIQKWVILEKDFSVPGGE 572
|
410 420
....*....|....*....|....
gi 768004222 435 LGPMMKLKRHFVAQKYKKQIDHMY 458
Cdd:cd05933 573 LGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
40-458 |
1.03e-117 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 357.10 E-value: 1.03e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 40 ITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVpIKIGALTYFAQADAlkgTLVSTLKEVKPTVFIGVPQIWEK 119
Cdd:COG1022 208 LLSNARALLERLPLGP-GDRTLSFLPLAHVFERTVSYYA-LAAGATVAFAESPD---TLAEDLREVKPTFMLAVPRVWEK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 120 IHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKYNTP---VSYRMAKTLVFSKVKTSLGlDHCHSFISGTAPLNQ 196
Cdd:COG1022 283 VYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARLAGKSPSLllrLKHALADKLVFSKLREALG-GRLRFAVSGGAALGP 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 197 ETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLfqqnkDGIGEICLWGRHIFMGYLESETETT 276
Cdd:COG1022 362 ELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKI-----AEDGEILVRGPNVMKGYYKNPEATA 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 277 EAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVkKKIPIISNAMLVGDKLKFLSMLLTlkcem 356
Cdd:COG1022 437 EAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQPIENAL-KASPLIEQAVVVGDGRPFLAALIV----- 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 357 nqmsgepldkLNFEAI-NFCRGLGSQASTVTEIVkqQDPLVYKAIQQGINAVNQEaMNNAQRIEKWVILEKDFSIYGGEL 435
Cdd:COG1022 511 ----------PDFEALgEWAEENGLPYTSYAELA--QDPEVRALIQEEVDRANAG-LSRAEQIKRFRLLPKEFTIENGEL 577
|
410 420
....*....|....*....|...
gi 768004222 436 GPMMKLKRHFVAQKYKKQIDHMY 458
Cdd:COG1022 578 TPTLKLKRKVILEKYADLIEALY 600
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
54-446 |
4.44e-101 |
|
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: 309.53 E-value: 4.44e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 54 TDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADAlkgTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKnsAKSMG 133
Cdd:cd05907 125 ATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAE---TLLDDLSEVRPTVFLAVPRVWEKVYAAIKV--KAVPG 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 134 LKKKAFVWArnigfkvnskkMLGKyntpvsyrmaktlvfskvktslgldhCHSFISGTAPLNQETAEFFLSLDIPIGELY 213
Cdd:cd05907 200 LKRKLFDLA-----------VGGR--------------------------LRFAASGGAPLPAELLHFFRALGIPVYEGY 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 214 GLSESSGPHTISNQNNYRLLSCGKILTGCKnmlFQQNKDGigEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQL 293
Cdd:cd05907 243 GLTETSAVVTLNPPGDNRIGTVGKPLPGVE---VRIADDG--EILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 294 DGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISNAMLVGDKLKFLSMLLTLKCEMNQMSGEPldklnfeain 373
Cdd:cd05907 318 DEDGFLHITGRKKDLIITSGGKNISPEPIENALKAS-PLISQAVVIGDGRPFLVALIVPDPEALEAWAEE---------- 386
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768004222 374 fcrgLGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEaMNNAQRIEKWVILEKDFSIYGGELGPMMKLKRHFV 446
Cdd:cd05907 387 ----HGIAYTDVAELAA--NPAVRAEIEAAVEAANAR-LSRYEQIKKFLLLPEPFTIENGELTPTLKLKRPVI 452
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
38-458 |
4.86e-54 |
|
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: 189.35 E-value: 4.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 38 DMITWIAGA--VTKDFKLTDKHETVVSYLPLSHIAAQMMdIWVPIKIGALTYFAQADALKgtLVSTLKEVKPTVFIGVPQ 115
Cdd:cd05927 138 NIVSNVAGVfkILEILNKINPTDVYISYLPLAHIFERVV-EALFLYHGAKIGFYSGDIRL--LLDDIKALKPTVFPGVPR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 116 IWEKIHEMVKKNSAKSMGLKKKAFVWARNigFKVNSKKMLGKYNTPVSYRmaktLVFSKVKTSLGLdHCHSFISGTAPLN 195
Cdd:cd05927 215 VLNRIYDKIFNKVQAKGPLKRKLFNFALN--YKLAELRSGVVRASPFWDK----LVFNKIKQALGG-NVRLMLTGSAPLS 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 196 QETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNML--------FQQNKDGIGEICLWGRHIFM 266
Cdd:cd05927 288 PEVLEFLRVaLGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLvdvpemnyDAKDPNPRGEVCIRGPNVFS 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 267 GYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISNAMLVGDKLKfl 346
Cdd:cd05927 368 GYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARS-PFVAQIFVYGDSLK-- 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 347 SMLLTLKCemnqmsgepldkLNFEAI-NFCRGLGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEamNNAQRIE--KWVI 423
Cdd:cd05927 445 SFLVAIVV------------PDPDVLkEWAASKGGGTGSFEELCK--NPEVKKAILEDLVRLGKE--NGLKGFEqvKAIH 508
|
410 420 430
....*....|....*....|....*....|....*.
gi 768004222 424 LEKD-FSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 458
Cdd:cd05927 509 LEPEpFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
39-376 |
3.73e-45 |
|
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: 163.38 E-value: 3.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 39 MITW--IAGAVT--KDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAqaDALKGTLVSTLKEVKPTVFIGVP 114
Cdd:cd05914 108 MLTYrnIVSNVDgvKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFL--DKIPSAKIIALAFAQVTPTLGVP 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 115 QIW--EKIHEMVKKNsaksmglkkkafvwarnigfKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGlDHCHSFISGTA 192
Cdd:cd05914 186 VPLviEKIFKMDIIP--------------------KLTLKKFKFKLAKKINNRKIRKLAFKKVHEAFG-GNIKEFVIGGA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 193 PLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQN-KDGIGEICLWGRHIFMGYLES 271
Cdd:cd05914 245 KINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDpATGEGEIIVRGPNVMKGYYKN 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 272 ETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVET-LVKKKIPIISNAMLVGDKLKFLSML- 349
Cdd:cd05914 325 PEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAkINNMPFVLESLVVVQEKKLVALAYId 404
|
330 340 350
....*....|....*....|....*....|....*
gi 768004222 350 ---LTLKCEMNQ-----MSGEPLDKLNFEAINFCR 376
Cdd:cd05914 405 pdfLDVKALKQRniidaIKWEVRDKVNQKVPNYKK 439
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
44-450 |
1.66e-43 |
|
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: 161.05 E-value: 1.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 44 AGAVTKDFKLTDkhETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADAlkgTLVSTLKEVKPTVFIGVPQIWEKIHEM 123
Cdd:cd17641 188 AAYLAADPLGPG--DEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEEPE---TMMEDLREIGPTFVLLPPRVWEGIAAD 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 124 VKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGK---YNTPVSYRMAKTLVFSKVKTSLGLDHCHSFISGTAPLNQETAE 200
Cdd:cd17641 263 VRARMMDATPFKRFMFELGMKLGLRALDRGKRGRpvsLWLRLASWLADALLFRPLRDRLGFSRLRSAATGGAALGPDTFR 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 201 FFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCknmlfQQNKDGIGEICLWGRHIFMGYLESETETTEAID 280
Cdd:cd17641 343 FFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGT-----EVRIDEVGEILVRSPGVFVGYYKNPEATAEDFD 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 281 DEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISNAMLVGDKLKFLSMLLTLKcemnqms 360
Cdd:cd17641 418 EDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFS-PYIAEAVVLGAGRPYLTAFICID------- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 361 gepldklnFEAI-NFCRGLGSQASTVTEIVKQqdPLVYKAIQQGINAVNQEaMNNAQRIEKWVILEKDFSIYGGELGPMM 439
Cdd:cd17641 490 --------YAIVgKWAEQRGIAFTTYTDLASR--PEVYELIRKEVEKVNAS-LPEAQRIRRFLLLYKELDADDGELTRTR 558
|
410
....*....|.
gi 768004222 440 KLKRHFVAQKY 450
Cdd:cd17641 559 KVRRGVIAEKY 569
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
31-450 |
5.03e-42 |
|
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: 155.70 E-value: 5.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 31 MKTFSlcdMITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQA-DalkgTLVSTLKEVKPTV 109
Cdd:cd05932 156 MLTFG---SFAWAAQAGIEHIGTEE-NDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESlD----TFVEDVQRARPTL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 110 FIGVPQIWEKIHEmvkknsaksmglkkkafvwarNIGFKVNSKKMlgkyNTPVSYRMAKTLVFSKVKTSLGLDHCHSFIS 189
Cdd:cd05932 228 FFSVPRLWTKFQQ---------------------GVQDKIPQQKL----NLLLKIPVVNSLVKRKVLKGLGLDQCRLAGC 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 190 GTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQnkdgiGEICLWGRHIFMGYL 269
Cdd:cd05932 283 GSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISED-----GEILVRSPALMMGYY 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 270 ESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVEtlvkKKI---PIISNAMLVGDKLKFL 346
Cdd:cd05932 358 KDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIE----NKLaehDRVEMVCVIGSGLPAP 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 347 SMLLtlkcemnQMSGEPldklNFEAINFCRGlGSQASTvteivkqqdplvyKAIQQGINAvnqeAMNNAQRIEKWVILEK 426
Cdd:cd05932 434 LALV-------VLSEEA----RLRADAFARA-ELEASL-------------RAHLARVNS----TLDSHEQLAGIVVVKD 484
|
410 420
....*....|....*....|....
gi 768004222 427 DFSIYGGELGPMMKLKRHFVAQKY 450
Cdd:cd05932 485 PWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
39-446 |
1.59e-37 |
|
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: 143.51 E-value: 1.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 39 MITWIAGAVTKDFKLTDKHETVVSYLPLSHI---AAQMmdiwVPIKIGALTYFAQADAL--------KGTLVstlkEVKP 107
Cdd:cd17639 113 LVAGIAGLGDRVPELLGPDDRYLAYLPLAHIfelAAEN----VCLYRGGTIGYGSPRTLtdkskrgcKGDLT----EFKP 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 108 TVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFvwarNIGFKVNSKKMLGKYNTPVsyrmAKTLVFSKVKTSLGlDHCHSF 187
Cdd:cd17639 185 TLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLF----WTAYQSKLKALKEGPGTPL----LDELVFKKVRAALG-GRLRYM 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 188 ISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNML--------FQQNKDGIGEICL 259
Cdd:cd17639 256 LSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLvdweeggySTDKPPPRGEILI 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 260 WGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISNAMLV 339
Cdd:cd17639 336 RGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSN-PLVNNICVY 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 340 GD--KLKFLSMLLTlkcemNQmsgEPLDKlnfeainFCRGLGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEAmnNAQR 417
Cdd:cd17639 415 ADpdKSYPVAIVVP-----NE---KHLTK-------LAEKHGVINSEWEELCE--DKKLQKAVLKSLAETARAA--GLEK 475
|
410 420 430
....*....|....*....|....*....|..
gi 768004222 418 IE---KWVILEKDFSIYGGELGPMMKLKRHFV 446
Cdd:cd17639 476 FEipqGVVLLDEEWTPENGLVTAAQKLKRKEI 507
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
38-458 |
7.42e-37 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 143.32 E-value: 7.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 38 DMITWIAGA-VTKDFKLTDKHetvVSYLPLSHI---AAQMMDIWVPIKIGaltyFAQADALKgtLVSTLKEVKPTVFIGV 113
Cdd:PLN02736 245 NLIANVAGSsLSTKFYPSDVH---ISYLPLAHIyerVNQIVMLHYGVAVG----FYQGDNLK--LMDDLAALRPTIFCSV 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 114 PQIWEKIHEMVKKNSAKSMGLKKKAFvwarNIGFkvNSKK---MLGKYNTPvsyrMAKTLVFSKVKTSLGlDHCHSFISG 190
Cdd:PLN02736 316 PRLYNRIYDGITNAVKESGGLKERLF----NAAY--NAKKqalENGKNPSP----MWDRLVFNKIKAKLG-GRVRFMSSG 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 191 TAPLNQETAEFflsLDIPIG----ELYGLSESSGPHTISNQNNYrllSCGKI----------LTGCKNMLFqQNKDGI-- 254
Cdd:PLN02736 385 ASPLSPDVMEF---LRICFGgrvlEGYGMTETSCVISGMDEGDN---LSGHVgspnpacevkLVDVPEMNY-TSEDQPyp 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 255 -GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQ-LDGlGFLYVTGHIKEILITAGGENVPPIPVETlVKKKIPI 332
Cdd:PLN02736 458 rGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLwLPG-GRLKIIDRKKNIFKLAQGEYIAPEKIEN-VYAKCKF 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 333 ISNAMLVGDKLKflSMLLTLkcemnqMSGEPLDKLNFEAINfcrglGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEAM 412
Cdd:PLN02736 536 VAQCFVYGDSLN--SSLVAV------VVVDPEVLKAWAASE-----GIKYEDLKQLCN--DPRVRAAVLADMDAVGREAQ 600
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 768004222 413 NNAQRIEKWVILEKD-FSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 458
Cdd:PLN02736 601 LRGFEFAKAVTLVPEpFTVENGLLTPTFKVKRPQAKAYFAKAISDMY 647
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
60-446 |
1.44e-32 |
|
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: 129.02 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 60 VVSYLPLSHIAAQmmdiwvpikigALTYFAqadALKG---------TLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAK 130
Cdd:cd17640 132 FLSILPIWHSYER-----------SAEYFI---FACGcsqaytsirTLKDDLKRVKPHYIVSVPRLWESLYSGIQKQVSK 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 131 SMGLKKKAFVWARNIG-FKVNskkmlgkyntpvsyrmaktlvfskvktslgldhchsfISGTAPLNQETAEFFLSLDIPI 209
Cdd:cd17640 198 SSPIKQFLFLFFLSGGiFKFG-------------------------------------ISGGGALPPHVDTFFEAIGIEV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 210 GELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGI------GEICLWGRHIFMGYLESETETTEAIDDEG 283
Cdd:cd17640 241 LNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVlppgekGIVWVRGPQVMKGYYKNPEATSKVLDSDG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 284 WLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVE-TLVKKkiPIISNAMLVGDKLKFLSMLLTlkcemnqmsge 362
Cdd:cd17640 321 WFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEeALMRS--PFIEQIMVVGQDQKRLGALIV----------- 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 363 PldklNFEAINfcRGLGSQASTVTEIVKQ--QDPLVYKAIQQGINAV--NQEAMNNAQRIEKWVILEKDFsIYGGELGPM 438
Cdd:cd17640 388 P----NFEELE--KWAKESGVKLANDRSQllASKKVLKLYKNEIKDEisNRPGFKSFEQIAPFALLEEPF-IENGEMTQT 460
|
....*...
gi 768004222 439 MKLKRHFV 446
Cdd:cd17640 461 MKIKRNVV 468
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
35-312 |
2.02e-32 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 127.43 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 35 SLCDMITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGA-LTYFAQADALKGT-LVSTLKEVKPTVFIG 112
Cdd:pfam00501 179 NLVANVLSIKRVRPRGFGLGP-DDRVLSTLPLFHDFGLSLGLLGPLLAGAtVVLPPGFPALDPAaLLELIERYKVTVLYG 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 113 VPQIWEKIhemvkknsaksmglkkkafvwarnigfkvnskkmlgkyntpVSYRMAKTLVFSKVKTslgldhchsFISGTA 192
Cdd:pfam00501 258 VPTLLNML-----------------------------------------LEAGAPKRALLSSLRL---------VLSGGA 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 193 PLNQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNYRLL---SCGKILTGCK------NMLFQQNKDGIGEICLWGR 262
Cdd:pfam00501 288 PLPPELARRFRElFGGALVNGYGLTETTGVVTTPLPLDEDLRslgSVGRPLPGTEvkivddETGEPVPPGEPGELCVRGP 367
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 768004222 263 HIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITA 312
Cdd:pfam00501 368 GVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
39-340 |
2.04e-32 |
|
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: 128.00 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 39 MITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGA----LTYFAQADALKgtlvsTLKEVKPTVFIGVP 114
Cdd:COG0318 124 NLLANAAAIAAALGLTP-GDVVLVALPLFHVFGLTVGLLAPLLAGAtlvlLPRFDPERVLE-----LIERERVTVLFGVP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 115 QIWekihemvkknsaksmglkkkafvwarnigfkvnskkmlgkyntpvsYRMAKTLVFSKVKTSlgldHCHSFISGTAPL 194
Cdd:COG0318 198 TML----------------------------------------------ARLLRHPEFARYDLS----SLRLVVSGGAPL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 195 NQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNY--RLLSCGKILTGCKNMLFqqNKDG-------IGEICLWGRHI 264
Cdd:COG0318 228 PPELLERFEErFGVRIVEGYGLTETSPVVTVNPEDPGerRPGSVGRPLPGVEVRIV--DEDGrelppgeVGEIVVRGPNV 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768004222 265 FMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVkKKIPIISNAMLVG 340
Cdd:COG0318 306 MKGYWNDPEATAEAFRD-GWLRTGDLGRLDEDGYLYIVGRKKDMIIS-GGENVYPAEVEEVL-AAHPGVAEAAVVG 378
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
55-328 |
1.41e-31 |
|
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: 123.55 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 55 DKHETVVSYLPLSHIAaQMMDIWVPIKIGA----LTYFAQADALKgtlvsTLKEVKPTVFIGVPQIWEKIhemvkknsak 130
Cdd:cd04433 39 TEGDVFLSTLPLFHIG-GLFGLLGALLAGGtvvlLPKFDPEAALE-----LIEREKVTILLGVPTLLARL---------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 131 smglkkkafvwARNIGFKvnskkmlgkyntpvsyrmakTLVFSKVKTslgldhchsFISGTAPLNQETAEFFLSL-DIPI 209
Cdd:cd04433 103 -----------LKAPESA--------------------GYDLSSLRA---------LVSGGAPLPPELLERFEEApGIKL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 210 GELYGLSESSGPHTISN--QNNYRLLSCGKILTGCKNMLFQQNKD-----GIGEICLWGRHIFMGYLESEtETTEAIDDE 282
Cdd:cd04433 143 VNGYGLTETGGTVATGPpdDDARKPGSVGRPVPGVEVRIVDPDGGelppgEIGELVVRGPSVMKGYWNNP-EATAAVDED 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 768004222 283 GWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVKK 328
Cdd:cd04433 222 GWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVEAVLLG 266
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
43-458 |
1.78e-27 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 115.71 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 43 IAGAVTKD--FKLTDK----HETVVSYLPLSHIAAQMMDIWVpIKIGALTYFAQADALkgTLVSTLKEVKPTVFIGVPQI 116
Cdd:PLN02861 246 IAEVLSTDhlLKVTDRvateEDSYFSYLPLAHVYDQVIETYC-ISKGASIGFWQGDIR--YLMEDVQALKPTIFCGVPRV 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 117 WEKIHEMVKKNSAKSMGLKKKAFVWARNigFKV-NSKKMLGKYNTpvSYRMAKtLVFSKVKTSLGlDHCHSFISGTAPLN 195
Cdd:PLN02861 323 YDRIYTGIMQKISSGGMLRKKLFDFAYN--YKLgNLRKGLKQEEA--SPRLDR-LVFDKIKEGLG-GRVRLLLSGAAPLP 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 196 QETAEFFLSLDIP-IGELYGLSESSGPHTISNQNNYRLL-SCGKILTGCKNMLFQQNKDGI--------GEICLWGRHIF 265
Cdd:PLN02861 397 RHVEEFLRVTSCSvLSQGYGLTESCGGCFTSIANVFSMVgTVGVPMTTIEARLESVPEMGYdalsdvprGEICLRGNTLF 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 266 MGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVppiPVETL--VKKKIPIISNAMLVGDkl 343
Cdd:PLN02861 477 SGYHKRQDLTEEVLID-GWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYV---AVENLenTYSRCPLIASIWVYGN-- 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 344 KFLSMLLTLKCEMNQmSGEPLDKLNFEAINF---CrglgsqastvteivkqQDPLVYKAIQQGINAVNQEAMNNAQRIEK 420
Cdd:PLN02861 551 SFESFLVAVVVPDRQ-ALEDWAANNNKTGDFkslC----------------KNLKARKYILDELNSTGKKLQLRGFEMLK 613
|
410 420 430
....*....|....*....|....*....|....*....
gi 768004222 421 WVILEKD-FSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 458
Cdd:PLN02861 614 AIHLEPNpFDIERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
52-458 |
2.92e-27 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 114.91 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 52 KLTdkHETV-VSYLPLSHIAAQMMDIWVPIKIGALTYF-AQADALKgtlvSTLKEVKPTVFIGVPQIWEKIHEMVKKNSA 129
Cdd:PLN02430 262 KMT--HDDVyLSFLPLAHILDRMIEEYFFRKGASVGYYhGDLNALR----DDLMELKPTLLAGVPRVFERIHEGIQKALQ 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 130 KSMGLKKKAFvwarNIGFKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFF-LSLDIP 208
Cdd:PLN02430 336 ELNPRRRLIF----NALYKYKLAWMNRGYSHKKASPMADFLAFRKVKAKLG-GRLRLLISGGAPLSTEIEEFLrVTSCAF 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 209 IGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQ---------NKDGIGEICLWGRHIFMGYLESETETTEAI 279
Cdd:PLN02430 411 VVQGYGLTETLGPTTLGFPDEMCMLGTVGAPAVYNELRLEEvpemgydplGEPPRGEICVRGKCLFSGYYKNPELTEEVM 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 280 DDeGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVppiPVETL--VKKKIPIISNAMLVGDKLKflSMLLTLKCemn 357
Cdd:PLN02430 491 KD-GWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYV---ALEYLenVYGQNPIVEDIWVYGDSFK--SMLVAVVV--- 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 358 qmsgepldkLNFEAINFCRGLGSQASTVTEIVKQqdPLVYKAIQQGINAVnqEAMNNAQRIE--KWVILE-KDFSIYGGE 434
Cdd:PLN02430 562 ---------PNEENTNKWAKDNGFTGSFEELCSL--PELKEHILSELKST--AEKNKLRGFEyiKGVILEtKPFDVERDL 628
|
410 420
....*....|....*....|....
gi 768004222 435 LGPMMKLKRHFVAQKYKKQIDHMY 458
Cdd:PLN02430 629 VTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
185-325 |
5.00e-24 |
|
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: 104.22 E-value: 5.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 185 HSFISGTAPLNQETAEFFLSLDIP--IGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLF------QQNKDGIGE 256
Cdd:cd05911 265 RVILSGGAPLSKELQELLAKRFPNatIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVdddgkdSLGPNEPGE 344
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768004222 257 ICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETL 325
Cdd:cd05911 345 ICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKE-LIKYKGFQVAPAELEAV 412
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
53-323 |
2.02e-23 |
|
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: 102.26 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 53 LTDKHETVVSYLPLSHIAAQMMDIWVPIKIGA----LTYFAQADALKgtlvsTLKEVKPTVFIGVPQIWEKIhemvkkns 128
Cdd:cd05936 164 LLEGDDVVLAALPLFHVFGLTVALLLPLALGAtivlIPRFRPIGVLK-----EIRKHRVTIFPGVPTMYIAL-------- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 129 aksMGLKKKAFVWarnigfkvnskkmlgkyntpvsyrmaktlvFSKVKTSlgldhchsfISGTAPLNQETAEFFLSL-DI 207
Cdd:cd05936 231 ---LNAPEFKKRD------------------------------FSSLRLC---------ISGGAPLPVEVAERFEELtGV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 208 PIGELYGLSESSgPHTISNQ--NNYRLLSCGKILTGCKNMLFqqNKDG-------IGEICLWGRHIFMGYLESETETTEA 278
Cdd:cd05936 269 PIVEGYGLTETS-PVVAVNPldGPRKPGSIGIPLPGTEVKIV--DDDGeelppgeVGELWVRGPQVMKGYWNRPEETAEA 345
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 768004222 279 IDDeGWLHSGDLGQLDGLGFLYVTGHIKEILItAGGENVPPIPVE 323
Cdd:cd05936 346 FVD-GWLRTGDIGYMDEDGYFFIVDRKKDMII-VGGFNVYPREVE 388
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
39-458 |
1.18e-22 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 100.87 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 39 MITWIAGAV----TKDFKLTDKhETVVSYLPLSHIAAQMMDIWVpIKIGALTYFAQADAlkGTLVSTLKEVKPTVFIGVP 114
Cdd:PLN02614 248 IVTLIAGVIrllkSANAALTVK-DVYLSYLPLAHIFDRVIEECF-IQHGAAIGFWRGDV--KLLIEDLGELKPTIFCAVP 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 115 QIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKvNSKKmlGKYNTPVSYRMAKtLVFSKVKTSLGlDHCHSFISGTAPL 194
Cdd:PLN02614 324 RVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFG-NMKK--GQSHVEASPLCDK-LVFNKVKQGLG-GNVRIILSGAAPL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 195 NQETAEFFLSLD-IPIGELYGLSESSGPHTISNQNNYRLLscGKILTGCKNM------LFQQNKDGI-----GEICLWGR 262
Cdd:PLN02614 399 ASHVESFLRVVAcCHVLQGYGLTESCAGTFVSLPDELDML--GTVGPPVPNVdirlesVPEMEYDALastprGEICIRGK 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 263 HIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETlVKKKIPIISNAMLVGDk 342
Cdd:PLN02614 477 TLFSGYYKREDLTKEVLID-GWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGEYVAVENIEN-IYGEVQAVDSVWVYGN- 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 343 lKFLSMLLTLKCEMNQM----SGEPLDKLNFEAInfCRGLGSQASTVTEIVKQQDPLVYKAIQQgINAVNQEAMNnaqri 418
Cdd:PLN02614 554 -SFESFLVAIANPNQQIlerwAAENGVSGDYNAL--CQNEKAKEFILGELVKMAKEKKMKGFEI-IKAIHLDPVP----- 624
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 768004222 419 ekwVILEKDFsiyggeLGPMMKLKRHFVAQKYKKQIDHMY 458
Cdd:PLN02614 625 ---FDMERDL------LTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
43-325 |
1.44e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 100.82 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 43 IAGAVTKDFKLTD------KHETVVSYLPLSHIaaqmMDIWVP---IKIGALTYFAQADalkgTLVST-------LKEVK 106
Cdd:PTZ00216 290 TAGILALEDRLNDligppeEDETYCSYLPLAHI----MEFGVTnifLARGALIGFGSPR----TLTDTfarphgdLTEFR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 107 PTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWArnigFKVNSKKMLGKYNTPvsYRMAKtlVFSKVKTSLGlDHCHS 186
Cdd:PTZ00216 362 PVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHA----YQSRLRALKEGKDTP--YWNEK--VFSAPRAVLG-GRVRA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 187 FISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNK-------DGIGEICL 259
Cdd:PTZ00216 433 MLSGGGPLSAATQEFVNVVFGMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEykhtdtpEPRGEILL 512
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768004222 260 WGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENvppIPVETL 325
Cdd:PTZ00216 513 RGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEY---IALEAL 575
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
187-323 |
1.35e-20 |
|
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: 93.83 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 187 FISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTI--SNQNNYRLLSCGKILTGCKNMLFQQNKD-----GIGEICL 259
Cdd:cd17631 218 VIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFlsPEDHRRKLGSAGRPVFFVEVRIVDPDGRevppgEVGEIVV 297
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768004222 260 WGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 323
Cdd:cd17631 298 RGPHVMAGYWNRPEATAAAFRD-GWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVE 359
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
181-340 |
1.43e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 91.07 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 181 LDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYR--LLSCGKILTGCKNMLFQQNKD-----G 253
Cdd:PRK06839 263 LQSVRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARrkVGSIGKPVLFCDYELIDENKNkvevgE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 254 IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVkKKIPII 333
Cdd:PRK06839 343 VGELLIRGPNVMKEYWNRPDATEETIQD-GWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYPLEVEQVI-NKLSDV 419
|
....*..
gi 768004222 334 SNAMLVG 340
Cdd:PRK06839 420 YEVAVVG 426
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
46-323 |
1.81e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 90.63 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 46 AVTKDFKLTDKhETVVSYLPLSHIAAqmmdiW----VPIKIGA-LTYFAQADAlkGTLVSTLKEVKPTVFIGVPQIWEki 120
Cdd:PRK06187 198 AVCAWLKLSRD-DVYLVIVPMFHVHA-----WglpyLALMAGAkQVIPRRFDP--ENLLDLIETERVTFFFAVPTIWQ-- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 121 hemvkknsaksmglkkkafvwarnigfkvnskkMLGKYntPVSYRMAktlvFSKVKTslgldhchsFISGTAPLNQETAE 200
Cdd:PRK06187 268 ---------------------------------MLLKA--PRAYFVD----FSSLRL---------VIYGGAALPPALLR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 201 FFLS-LDIPIGELYGLSESSG-------PHTISNQNNYRLlSCGKILTGCK------NMLFQQNKDG-IGEICLWGRHIF 265
Cdd:PRK06187 300 EFKEkFGIDLVQGYGMTETSPvvsvlppEDQLPGQWTKRR-SAGRPLPGVEarivddDGDELPPDGGeVGEIIVRGPWLM 378
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 768004222 266 MGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 323
Cdd:PRK06187 379 QGYWNRPEATAETIDG-GWLHTGDVGYIDEDGYLYITDRIKDVIIS-GGENIYPRELE 434
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
185-325 |
6.26e-19 |
|
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: 89.22 E-value: 6.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 185 HSFISGTAPLNQETAEFFLSL--DIPIGELYGLSESSGP-HTISN--QNNYRLLSCGKILTGCKNMLFQQNKDGI----- 254
Cdd:cd05904 278 RQIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVvAMCFApeKDRAKYGSVGRLVPNVEAKIVDPETGESlppnq 357
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768004222 255 -GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETL 325
Cdd:cd05904 358 tGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKE-LIKYKGFQVAPAELEAL 428
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
213-323 |
6.78e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 89.19 E-value: 6.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 213 YGLSESSGPHTISNQNNYRLLSCGKILTGCKNM-------LFQQNKDG-IGEICLWGRHIFMGYLESETETTEAIDDEGW 284
Cdd:PRK07656 314 YGLSEASGVTTFNRLDDDRKTVAGTIGTAIAGVenkivneLGEEVPVGeVGELLVRGPNVMKGYYDDPEATAAAIDADGW 393
|
90 100 110
....*....|....*....|....*....|....*....
gi 768004222 285 LHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 323
Cdd:PRK07656 394 LHTGDLGRLDEEGYLYIVDRKKDMFIV-GGFNVYPAEVE 431
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
38-459 |
1.67e-18 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 88.25 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 38 DMITWIAGAVTKDFKLtDKHETVVSYLPLSHI---AAQ--MMDIWVPIKIG-ALTYFAQADALK-GTL--VSTLKevkPT 108
Cdd:PLN02387 274 NIVATVAGVMTVVPKL-GKNDVYLAYLPLAHIlelAAEsvMAAVGAAIGYGsPLTLTDTSNKIKkGTKgdASALK---PT 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 109 VFIGVPQIWEKIHEMVKKNSAKSMGLKKKAF--VWARNIGFKVNS-------KKMLgkYNTpvsyrmaktLVFSKVKTSL 179
Cdd:PLN02387 350 LMTAVPAILDRVRDGVRKKVDAKGGLAKKLFdiAYKRRLAAIEGSwfgawglEKLL--WDA---------LVFKKIRAVL 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 180 GlDHCHSFISGTAPLNQETAEFF-LSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGI---- 254
Cdd:PLN02387 419 G-GRIRFMLSGGAPLSGDTQRFInICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYlisd 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 255 -----GEICLWGRHIFMGYLESETETTEA--IDDEG--WLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETL 325
Cdd:PLN02387 498 kpmprGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAA 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 326 VKKKiPIISNAMLVGDklKFLSMLLTLKCEMNQMSGEPLDKLNFEAINFCRgLGSQASTVTEivkqqdplvykaIQQGIN 405
Cdd:PLN02387 578 LSVS-PYVDNIMVHAD--PFHSYCVALVVPSQQALEKWAKKAGIDYSNFAE-LCEKEEAVKE------------VQQSLS 641
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 406 AVNQEAmnnaqRIEKWVI------LEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMYH 459
Cdd:PLN02387 642 KAAKAA-----RLEKFEIpakiklLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
190-340 |
3.45e-18 |
|
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: 86.25 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 190 GTAPLNQETAEFFLSLDIPIGELYGLSE-SSGPHTISNQNNY-RLLSCGKILTGCKNMLFQ--QNKDGIGEICLWGRHIF 265
Cdd:cd05912 197 GGGPAPKPLLEQCKEKGIPVYQSYGMTEtCSQIVTLSPEDALnKIGSAGKPLFPVELKIEDdgQPPYEVGEILLKGPNVT 276
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768004222 266 MGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVkKKIPIISNAMLVG 340
Cdd:cd05912 277 KGYLNRPDATEESFEN-GWFKTGDIGYLDEEGFLYVLDRRSD-LIISGGENIYPAEIEEVL-LSHPAIKEAGVVG 348
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
188-323 |
2.70e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 82.91 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 188 ISGTAPLNQET-AEFFLSLDIPIGELYGLSESSGPHTISNQNN-YRLLSCG----------KILTGCKNMLFQQNKDGIG 255
Cdd:cd05944 127 MSGAAPLPVELrARFEDATGLPVVEGYGLTEATCLVAVNPPDGpKRPGSVGlrlpyarvriKVLDGVGRLLRDCAPDEVG 206
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768004222 256 EICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 323
Cdd:cd05944 207 EICVAGPGVFGGYLYTEGNKNAFVAD-GWLNTGDLGRLDADGYLFITGRAKD-LIIRGGHNIDPALIE 272
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
189-340 |
4.95e-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: 81.61 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 189 SGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQnkdgiGEICLWGRHIFMGY 268
Cdd:cd17630 118 LGGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED-----GEIWVGGASLAMGY 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768004222 269 LESETEttEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVkKKIPIISNAMLVG 340
Cdd:cd17630 193 LRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAAL-AAHPAVRDAFVVG 260
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
181-340 |
4.97e-17 |
|
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: 83.35 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 181 LDHCHSFISGTAPLNQETAEFFLS-LDIP-IGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGI---- 254
Cdd:cd17642 300 LSNLHEIASGGAPLSKEVGEAVAKrFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTlgpn 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 255 --GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKiPI 332
Cdd:cd17642 380 erGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKS-LIKYKGYQVPPAELESILLQH-PK 457
|
....*...
gi 768004222 333 ISNAMLVG 340
Cdd:cd17642 458 IFDAGVAG 465
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
213-340 |
9.26e-17 |
|
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: 81.01 E-value: 9.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 213 YGLSE---------SSGPHTISNqnnyrllSCGKILTGcknmlFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEG 283
Cdd:cd17638 148 YGLTEagvatmcrpGDDAETVAT-------TCGRACPG-----FEVRIADDGEVLVRGYNVMQGYLDDPEATAEAIDADG 215
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 768004222 284 WLHSGDLGQLDGLGFLYVTGHIKEILItAGGENVPPIPVETLVkKKIPIISNAMLVG 340
Cdd:cd17638 216 WLHTGDVGELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGAL-AEHPGVAQVAVIG 270
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
42-326 |
2.50e-16 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 81.46 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 42 WIAGAVtkdfKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIh 121
Cdd:PRK08751 243 WLAGTG----KLEEGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGL- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 122 emvkknsaksmglkkkafvwarnigfkvnskkmlgkYNTPvsyrMAKTLVFSKVKTSLGldhchsfisGTAPLNQETAEF 201
Cdd:PRK08751 318 ------------------------------------LNTP----GFDQIDFSSLKMTLG---------GGMAVQRSVAER 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 202 FLSLD-IPIGELYGLSESS-----GPHTISNQNNYRLL------SCGKILTGCKNMLFQqnkdgIGEICLWGRHIFMGYL 269
Cdd:PRK08751 349 WKQVTgLTLVEAYGLTETSpaaciNPLTLKEYNGSIGLpipstdACIKDDAGTVLAIGE-----IGELCIKGPQVMKGYW 423
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 768004222 270 ESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGeNVPPIPVETLV 326
Cdd:PRK08751 424 KRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGF-NVYPNEIEDVI 479
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
154-340 |
2.68e-16 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 81.33 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 154 MLGKynTPVSYRMAKTLVFSKVK-TSLGLdhchsFISGTAPLNQETAEFFLSLDIPIGELYGLSESSgPHTISNQNN--- 229
Cdd:PRK06087 280 MLGA--TPFIYDLLNLLEKQPADlSALRF-----FLCGGTTIPKKVARECQQRGIKLLSVYGSTESS-PHAVVNLDDpls 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 230 YRLLSCGKILTGCKNMLFQQNKDGI-----GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGH 304
Cdd:PRK06087 352 RFMHTDGYAAAGVEIKVVDEARKTLppgceGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGR 431
|
170 180 190
....*....|....*....|....*....|....*.
gi 768004222 305 IKEILITaGGENVPPIPVETLVKKKiPIISNAMLVG 340
Cdd:PRK06087 432 KKDIIVR-GGENISSREVEDILLQH-PKIHDACVVA 465
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
182-323 |
2.78e-16 |
|
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: 80.41 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 182 DHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLF----QQNKDG-IGE 256
Cdd:cd05934 195 AHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVdddgQELPAGePGE 274
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768004222 257 ICL-----WGrhIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 323
Cdd:cd05934 275 LVIrglrgWG--FFKGYYNMPEATAEAMRN-GWFHTGDLGYRDADGFFYFVDRKKD-MIRRRGENISSAEVE 342
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
206-323 |
2.82e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 80.97 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 206 DIPIGelYGLSESSGPHTISNQNN---YRLLSCGKILTGCKNMLFQQN-----KDGIGEICLWGRHIFMGYLESETETTE 277
Cdd:PRK12583 345 EVQIA--YGMTETSPVSLQTTAADdleRRVETVGRTQPHLEVKVVDPDgatvpRGEIGELCTRGYSVMKGYWNNPEATAE 422
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 768004222 278 AIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 323
Cdd:PRK12583 423 SIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIR-GGENIYPREIE 467
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
254-323 |
4.49e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 80.63 E-value: 4.49e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 254 IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 323
Cdd:PRK08315 398 QGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIR-GGENIYPREIE 466
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
187-323 |
1.38e-15 |
|
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: 78.89 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 187 FI-SGTAPLNQETAEFF-LSLDIPIGELYGLSESSGPHTiSNQ---NNYRLLSCGKIlTGCKNMLFQQN----KDG-IGE 256
Cdd:cd05926 269 FIrSCSASLPPAVLEALeATFGAPVLEAYGMTEAAHQMT-SNPlppGPRKPGSVGKP-VGVEVRILDEDgeilPPGvVGE 346
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768004222 257 ICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVE 323
Cdd:cd05926 347 ICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKEL-INRGGEKISPLEVD 412
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
187-323 |
6.57e-15 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 76.92 E-value: 6.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 187 FISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPHTIsnqnNY-----RLLSCG--------KILTGCKNMLFQQN-- 250
Cdd:PRK07529 338 ALCGAAPLPVEVFRRFEAaTGVRIVEGYGLTEATCVSSV----NPpdgerRIGSVGlrlpyqrvRVVILDDAGRYLRDca 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768004222 251 KDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 323
Cdd:PRK07529 414 VDEVGVLCIAGPNVFSGYLEAAHNKGLWLED-GWLNTGDLGRIDADGYFWLTGRAKD-LIIRGGHNIDPAAIE 484
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
213-340 |
7.07e-15 |
|
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: 75.78 E-value: 7.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 213 YGLSESSGPHTISNQNN---YRLLSCGKIL----------TGCKNMLFQQnkdgIGEICLWGRHIFMGYLESETETTEAI 279
Cdd:cd05917 151 YGMTETSPVSTQTRTDDsieKRVNTVGRIMphteakivdpEGGIVPPVGV----PGELCIRGYSVMKGYWNDPEKTAEAI 226
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768004222 280 DDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVKKKiPIISNAMLVG 340
Cdd:cd05917 227 DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIR-GGENIYPREIEEFLHTH-PKVSDVQVVG 285
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
212-340 |
2.51e-14 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 73.84 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 212 LYGLSESSGPHTISNQNNyRLLSCGKILTGCKNMLFQQNKDGI-----GEICLWGRHIFMGYLESETETTEAIDDeGWLH 286
Cdd:cd17637 142 LYGQTETSGLVTLSPYRE-RPGSAGRPGPLVRVRIVDDNDRPVpagetGEIVVRGPLVFQGYWNLPELTAYTFRN-GWHH 219
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 768004222 287 SGDLGQLDGLGFLYVTGHI--KEiLITAGGENVPPIPVETlVKKKIPIISNAMLVG 340
Cdd:cd17637 220 TGDLGRFDEDGYLWYAGRKpeKE-LIKPGGENVYPAEVEK-VILEHPAIAEVCVIG 273
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
208-323 |
3.97e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 74.25 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 208 PI-GELYGLSESsgPHTIS--------NQNNYRLLSCGKILTGCKNMLFQQN-----KDGIGEICLWGRHIFMGYLESET 273
Cdd:PRK06188 307 PIfAQYYGQTEA--PMVITylrkrdhdPDDPKRLTSCGRPTPGLRVALLDEDgrevaQGEVGEICVRGPLVMDGYWNRPE 384
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 768004222 274 ETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 323
Cdd:PRK06188 385 ETAEAFRD-GWLHTGDVAREDEDGFYYIVDRKKDMIVT-GGFNVFPREVE 432
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
213-340 |
4.14e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 74.31 E-value: 4.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 213 YGLSESSG-----P---HTISNQNNYRLLSCGKILTGcknMLFQ-QNKDG-------IGEICLWGRHIFMGYLESETETT 276
Cdd:PRK07470 312 FGLGEVTGnitvlPpalHDAEDGPDARIGTCGFERTG---MEVQiQDDEGrelppgeTGEICVIGPAVFAGYYNNPEANA 388
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768004222 277 EAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVEtlvkKKI---PIISNAMLVG 340
Cdd:PRK07470 389 KAFRD-GWFRTGDLGHLDARGFLYITGRASDMYIS-GGSNVYPREIE----EKLlthPAVSEVAVLG 449
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
254-340 |
1.67e-13 |
|
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: 72.03 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 254 IGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVkKKIPII 333
Cdd:cd05903 288 EGELLSRGPSVFLGYLDRP-DLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIR-GGENIPVLEVEDLL-LGHPGV 364
|
....*..
gi 768004222 334 SNAMLVG 340
Cdd:cd05903 365 IEAAVVA 371
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
179-340 |
3.48e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 71.15 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 179 LGLDHCHS----FISGTAPLNQETAEFFLSLDIPIGELYGLSESSG------PHTISNqnnyRLLSCGKILTGC-----K 243
Cdd:PRK03640 247 LGEGTYPSsfrcMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETASqivtlsPEDALT----KLGSAGKPLFPCelkieK 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 244 NMLFQQNKDgIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 323
Cdd:PRK03640 323 DGVVVPPFE-EGEIVVKGPNVTKGYLNREDATRETFQD-GWFKTGDIGYLDEEGFLYVLDRRSD-LIISGGENIYPAEIE 399
|
170
....*....|....*..
gi 768004222 324 TlVKKKIPIISNAMLVG 340
Cdd:PRK03640 400 E-VLLSHPGVAEAGVVG 415
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
187-340 |
2.21e-12 |
|
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: 68.47 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 187 FISGTAPLNQETAEFFLSLD-IPIGELYGLSESSgpHTISN--QNNYRLLSCGKILTGCKNMLFQQN------KDGIGEI 257
Cdd:cd05941 217 MVSGSAALPVPTLEEWEAITgHTLLERYGMTEIG--MALSNplDGERRPGTVGMPLPGVQARIVDEEtgeplpRGEVGEI 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 258 CLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVkKKIPIISNAM 337
Cdd:cd05941 295 QVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEIERVL-LAHPGVSECA 373
|
...
gi 768004222 338 LVG 340
Cdd:cd05941 374 VIG 376
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
254-323 |
2.90e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 68.42 E-value: 2.90e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 254 IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 323
Cdd:PRK08316 367 VGEIVHRSPQLMLGYWDDPEKTAEAFRG-GWFHSGDLGVMDEEGYITVVDRKKDMIKT-GGENVASREVE 434
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
42-340 |
3.07e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 68.49 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 42 WIAGavtkdfkLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGA-LTYFAQADAlkGTLVSTLKEVKPTVFIGVPQIWEKI 120
Cdd:PRK05605 254 WVPG-------LGDGPERVLAALPMFHAYGLTLCLTLAVSIGGeLVLLPAPDI--DLILDAMKKHPPTWLPGVPPLYEKI 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 121 HEMVKKnsaksmglkkkafvwaRNIGFKvnskkmlgkyntpvSYRMAktlvfskvktslgldhchsfISGTAPLNQETAE 200
Cdd:PRK05605 325 AEAAEE----------------RGVDLS--------------GVRNA--------------------FSGAMALPVSTVE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 201 FFLSLdipIG----ELYGLSESSgPHTISN--QNNYRLLSCG------KILTGCKNMLFQQNKDG-IGEICLWGRHIFMG 267
Cdd:PRK05605 355 LWEKL---TGgllvEGYGLTETS-PIIVGNpmSDDRRPGYVGvpfpdtEVRIVDPEDPDETMPDGeEGELLVRGPQVFKG 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768004222 268 YLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETlVKKKIPIISNAMLVG 340
Cdd:PRK05605 431 YWNRPEETAKSFLD-GWFRTGDVVVMEEDGFIRIVDRIKELIIT-GGFNVYPAEVEE-VLREHPGVEDAAVVG 500
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
169-340 |
3.74e-12 |
|
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: 67.05 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 169 TLVFSKVKTSLGLDHCHSFISGTAPLNQETAEFF--LSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNML 246
Cdd:cd17633 97 TMLQALARTLEPESKIKSIFSSGQKLFESTKKKLknIFPKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEI 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 247 FQQNKDGIGEICLWGRHIFMGYLESEtetteAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLV 326
Cdd:cd17633 177 RNADGGEIGKIFVKSEMVFSGYVRGG-----FSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIII-GGINIFPTEIESVL 250
|
170
....*....|....
gi 768004222 327 kKKIPIISNAMLVG 340
Cdd:cd17633 251 -KAIPGIEEAIVVG 263
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
188-342 |
1.33e-11 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 66.54 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 188 ISGTAPLNQETAEFFLSlDIP---IGELYGLSESsGPhtisnqnnyrLL----------------SCG--------KIL- 239
Cdd:PLN02246 304 LSGAAPLGKELEDAFRA-KLPnavLGQGYGMTEA-GP----------VLamclafakepfpvksgSCGtvvrnaelKIVd 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 240 --TGCKnmlFQQNKDGigEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENV 317
Cdd:PLN02246 372 peTGAS---LPRNQPG--EICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKEL-IKYKGFQV 445
|
170 180
....*....|....*....|....*
gi 768004222 318 PPIPVETLVKKKiPIISNAMLVGDK 342
Cdd:PLN02246 446 APAELEALLISH-PSIADAAVVPMK 469
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
186-326 |
4.06e-11 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 65.00 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 186 SFISGTAPLNQETAEFFLSL--DIPIGELYGLSESS-------GP---HTISNQNnyrllSCGKILTGCKNMLFQQN--- 250
Cdd:PLN02330 307 AIMTAAAPLAPELLTAFEAKfpGVQVQEAYGLTEHScitlthgDPekgHGIAKKN-----SVGFILPNLEVKFIDPDtgr 381
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768004222 251 ---KDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLV 326
Cdd:PLN02330 382 slpKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKE-LIKYKGFQVAPAELEAIL 459
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
213-340 |
4.44e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 64.91 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 213 YGLSESSGPHTISNQNNY--RLLSCGK--------ILTGCKNMLFQQNKdgiGEICLWGRHIFMGYLESETETTEAIDDe 282
Cdd:PRK06145 297 YGLTETCSGDTLMEAGREieKIGSTGRalahveirIADGAGRWLPPNMK---GEICMRGPKVTKGYWKDPEKTAEAFYG- 372
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 768004222 283 GWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVkKKIPIISNAMLVG 340
Cdd:PRK06145 373 DWFRSGDVGYLDEEGFLYLTDRKKDMIIS-GGENIASSEVERVI-YELPEVAEAAVIG 428
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
181-340 |
4.60e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 64.83 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 181 LDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSE-------SSGPHTISNqnnyRLLSCGKILTGCKNMLFQQNKDG 253
Cdd:PRK09088 251 LRHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEagtvfgmSVDCDVIRA----KAGAAGIPTPTVQTRVVDDQGND 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 254 I-----GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVKK 328
Cdd:PRK09088 327 CpagvpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFIS-GGENVYPAEIEAVLAD 405
|
170
....*....|..
gi 768004222 329 KiPIISNAMLVG 340
Cdd:PRK09088 406 H-PGIRECAVVG 416
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
188-326 |
6.43e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 64.28 E-value: 6.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 188 ISGTAPLNQETAEFFLSldIPIGEL---YGLSESSgPHTISN----------------QNNYRLLS--CGKILTGCKnml 246
Cdd:PRK06710 329 ISGSAPLPVEVQEKFET--VTGGKLvegYGLTESS-PVTHSNflwekrvpgsigvpwpDTEAMIMSleTGEALPPGE--- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 247 fqqnkdgIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLV 326
Cdd:PRK06710 403 -------IGEIVVKGPQIMKGYWNKPEETAAVLQD-GWLHTGDVGYMDEDGFFYVKDRKKD-MIVASGFNVYPREVEEVL 473
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
187-323 |
6.60e-11 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 64.14 E-value: 6.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 187 FI-SGTAPLNQETAEF----FLSldiPIGELYGLSE---------------------SSGPHTISNQNNYRLL-SCGKIL 239
Cdd:PRK05852 299 FIrSCSAPLTAETAQAlqteFAA---PVVCAFGMTEathqvtttqiegigqtenpvvSTGLVGRSTGAQIRIVgSDGLPL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 240 TgcknmlfqqnKDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPP 319
Cdd:PRK05852 376 P----------AGAVGEVWLRGTTVVRGYLGDPTITAANFTD-GWLRTGDLGSLSAAGDLSIRGRIKE-LINRGGEKISP 443
|
....
gi 768004222 320 IPVE 323
Cdd:PRK05852 444 ERVE 447
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
213-340 |
9.95e-11 |
|
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: 63.47 E-value: 9.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 213 YGLSESSGPHTI----------SNQNNYRLlscgKILTGCKNMLFQQ------------NKDG--IGEICLWGRHIFMGY 268
Cdd:cd12118 278 YGLTETYGPATVcawkpewdelPTEERARL----KARQGVRYVGLEEvdvldpetmkpvPRDGktIGEIVFRGNIVMKGY 353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768004222 269 LESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETlVKKKIPIISNAMLVG 340
Cdd:cd12118 354 LKNPEATAEAFRG-GWFHSGDLAVIHPDGYIEIKDRSKDIIIS-GGENISSVEVEG-VLYKHPAVLEAAVVA 422
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
54-334 |
1.31e-10 |
|
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: 63.28 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 54 TDKHETVVSYLPLSH----IAAQMmdiwVPIKIGALTYFAqadalkgtlvstlkevkPT-VFIGVPQIW-EKIHEmvkkn 127
Cdd:cd05908 144 WKTKDRILSWMPLTHdmglIAFHL----APLIAGMNQYLM-----------------PTrLFIRRPILWlKKASE----- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 128 saksmglKKKAFVWARNIGFKVnskkMLGKYNTPVSYrmaktlvfskvktSLGLDHCHSFISGTAPLNQETAEFFLSLDI 207
Cdd:cd05908 198 -------HKATIVSSPNFGYKY----FLKTLKPEKAN-------------DWDLSSIRMILNGAEPIDYELCHEFLDHMS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 208 PIG-------ELYGLSESS--------GPHTI--------------------SNQNNYRLLSCGKILTGCK-NMLFQQNK 251
Cdd:cd05908 254 KYGlkrnailPVYGLAEASvgaslpkaQSPFKtitlgrrhvthgepepevdkKDSECLTFVEVGKPIDETDiRICDEDNK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 252 ---DG-IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGlGFLYVTGHIKEILITaGGENVPPIPVETLVK 327
Cdd:cd05908 334 ilpDGyIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIRN-GRLVITGREKDIIFV-NGQNVYPHDIERIAE 411
|
....*..
gi 768004222 328 KKIPIIS 334
Cdd:cd05908 412 ELEGVEL 418
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
202-340 |
3.43e-10 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 62.12 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 202 FLSLDIPIGELYGLSESSGPHTISNQNNYRLLSC-GKILTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAID 280
Cdd:PLN02860 332 FMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCvGKPAPHVELKIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLS 411
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 281 DEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKiPIISNAMLVG 340
Cdd:PLN02860 412 NDGWLDTGDIGWIDKAGNLWLIGRSNDR-IKTGGENVYPEEVEAVLSQH-PGVASVVVVG 469
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
254-340 |
4.16e-10 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 61.61 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 254 IGEICLWGRHIFMGYLESETETteAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVKKKiPII 333
Cdd:PRK13295 392 IGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVIIR-GGENIPVVEIEALLYRH-PAI 467
|
....*..
gi 768004222 334 SNAMLVG 340
Cdd:PRK13295 468 AQVAIVA 474
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
168-326 |
8.59e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 60.93 E-value: 8.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 168 KTLVFSKVKTSLgldhchsfiSGTAPLNQETAEFFLSLD-IPIGELYGLSESSGPHTISNQNNYRLLSCGKIL--TGCKN 244
Cdd:PRK05677 321 RKLDFSALKLTL---------SGGMALQLATAERWKEVTgCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVpsTLCKV 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 245 MlfqqNKDG-------IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGeNV 317
Cdd:PRK05677 392 I----DDDGnelplgeVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGF-NV 466
|
....*....
gi 768004222 318 PPIPVETLV 326
Cdd:PRK05677 467 YPNELEDVL 475
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
168-340 |
8.61e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 60.99 E-value: 8.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 168 KTLVFSKVKTSlgldhchsfISGTAPLNQETAEFFLSLD-IPIGELYGLSESSgphTISNQNNY----RLLSCGKILTGC 242
Cdd:PRK12492 328 KDLDFSALKLT---------NSGGTALVKATAERWEQLTgCTIVEGYGLTETS---PVASTNPYgelaRLGTVGIPVPGT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 243 KNMLFqqNKDGI-------GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGe 315
Cdd:PRK12492 396 ALKVI--DDDGNelplgerGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGF- 472
|
170 180
....*....|....*....|....*
gi 768004222 316 NVPPIPVETLVKKKiPIISNAMLVG 340
Cdd:PRK12492 473 NVYPNEIEDVVMAH-PKVANCAAIG 496
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
189-342 |
1.18e-09 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 60.24 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 189 SGTAPLNQETAEFFLS----LDIPIGelYGLSESS--GPHTISNQNNYRLLSCG--------KIL---TGCknMLFQQNK 251
Cdd:PLN02574 326 CGAAPLSGKFIQDFVQtlphVDFIQG--YGMTESTavGTRGFNTEKLSKYSSVGllapnmqaKVVdwsTGC--LLPPGNC 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 252 dgiGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKIP 331
Cdd:PLN02574 402 ---GELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEI-IKYKGFQIAPADLEAVLISHPE 477
|
170
....*....|..
gi 768004222 332 IISNAML-VGDK 342
Cdd:PLN02574 478 IIDAAVTaVPDK 489
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
158-340 |
2.11e-09 |
|
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: 59.27 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 158 YNTPVSYRM-AKTLVFSKVKTSLgldhcHSFISGTAPLNQETAEFFLS-LDIPIGELYGLSEssgphTISNQNNYRLL-- 233
Cdd:cd05972 177 CGPPTAYRMlIKQDLSSYKFSHL-----RLVVSAGEPLNPEVIEWWRAaTGLPIRDGYGQTE-----TGLTVGNFPDMpv 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 234 ---SCGKILTGCKNMLFQQNKDGI-----GEICL-WGRH-IFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTG 303
Cdd:cd05972 247 kpgSMGRPTPGYDVAIIDDDGRELppgeeGDIAIkLPPPgLFLGYVGDPEKTEASIRG-DYYLTGDRAYRDEDGYFWFVG 325
|
170 180 190
....*....|....*....|....*....|....*...
gi 768004222 304 HIKEIlITAGGENVPPIPVE-TLVKKkiPIISNAMLVG 340
Cdd:cd05972 326 RADDI-IKSSGYRIGPFEVEsALLEH--PAVAEAAVVG 360
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
254-340 |
2.56e-09 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 59.31 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 254 IGEICLWG---RHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETLVKKKi 330
Cdd:PRK08008 366 IGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDR-RCNMIKRGGENVSCVELENIIATH- 443
|
90
....*....|
gi 768004222 331 PIISNAMLVG 340
Cdd:PRK08008 444 PKIQDIVVVG 453
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
252-323 |
2.74e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 59.19 E-value: 2.74e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768004222 252 DG--IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 323
Cdd:PRK08162 384 DGetIGEIMFRGNIVMKGYLKNPKATEEAFAG-GWFHTGDLAVLHPDGYIKIKDRSKDIIIS-GGENISSIEVE 455
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
213-338 |
6.77e-09 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 58.11 E-value: 6.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 213 YGLSESSGP------------------HTISNQNNYRLLSCGKILTGCKNMLFQQNKDG--IGEICLWGRHIFMGYLESE 272
Cdd:PLN03102 331 YGLTEATGPvlfcewqdewnrlpenqqMELKARQGVSILGLADVDVKNKETQESVPRDGktMGEIVIKGSSIMKGYLKNP 410
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768004222 273 TETTEAIDdEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVKKKIPIISNAML 338
Cdd:PLN03102 411 KATSEAFK-HGWLNTGDVGVIHPDGHVEIKDRSKDIIIS-GGENISSVEVENVLYKYPKVLETAVV 474
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
252-319 |
7.48e-09 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 57.63 E-value: 7.48e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768004222 252 DGIGEICLWGRHIFMGYL--ESETETT----EAIDDEGWLHSGDLGQLDGlGFLYVTGHIKEILITAgGENVPP 319
Cdd:cd05931 380 GEVGEIWVRGPSVASGYWgrPEATAETfgalAATDEGGWLRTGDLGFLHD-GELYITGRLKDLIIVR-GRNHYP 451
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
59-435 |
1.12e-08 |
|
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: 57.44 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 59 TVVSYLPLSHIAAQMMDIWVPIKIGALTYFaqaDALK------GTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAksm 132
Cdd:cd05921 210 VLVDWLPWNHTFGGNHNFNLVLYNGGTLYI---DDGKpmpggfEETLRNLREISPTVYFNVPAGWEMLVAALEKDEA--- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 133 gLKKKAFvwarnigfkvnsKKMlgkyntpvsyrmaktlvfskvktslgldhcHSFISGTAPLNQETAEfflSLD------ 206
Cdd:cd05921 284 -LRRRFF------------KRL------------------------------KLMFYAGAGLSQDVWD---RLQalavat 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 207 ----IPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQnkDGIGEICLWGRHIFMGYLESETETTEAIDDE 282
Cdd:cd05921 318 vgerIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVPS--GGKYEVRVKGPNVTPGYWRQPELTAQAFDEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 283 GWLHSGDLGQL----DGLGFLYVTGHIKEILITAGGENVPPIPVET-LVKKKIPIISNAMLVGDKLKFLSMLLtlkcemn 357
Cdd:cd05921 396 GFYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLASGTWVSVGPLRArAVAACAPLVHDAVVAGEDRAEVGALV------- 468
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768004222 358 qmsgepldklnFEAINFCRGL-GSQASTVTEIVKQqdPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGEL 435
Cdd:cd05921 469 -----------FPDLLACRRLvGLQEASDAEVLRH--AKVRAAFRDRLAALNGEATGSSSRIARALLLDEPPSIDKGEI 534
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
190-326 |
1.61e-08 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 56.11 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 190 GTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLL-SCGKILTGCK-----NMLFQQNKDGIGEICLWGRH 263
Cdd:cd17635 126 GSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIEInAVGRPYPGVDvylaaTDGIAGPSASFGTIWIKSPA 205
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768004222 264 IFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLV 326
Cdd:cd17635 206 NMLGYWNNPERTAEVLID-GWVNTGDLGERREDGFLFITGRSSES-INCGGVKIAPDEVERIA 266
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
253-323 |
2.37e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 56.16 E-value: 2.37e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768004222 253 GIGEICLWGRHIFMGYLESETeTTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 323
Cdd:PRK07768 385 GVGVIELRGESVTPGYLTMDG-FIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIM-AGRNIYPTDIE 453
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
255-340 |
3.48e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 55.82 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 255 GEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITAgGENVPPIPVETLVKKKiPIIS 334
Cdd:PRK06178 415 GEIVVRTPSLLKGYWNKPEATAEALRD-GWLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GMSVFPSEVEALLGQH-PAVL 491
|
....*.
gi 768004222 335 NAMLVG 340
Cdd:PRK06178 492 GSAVVG 497
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
188-344 |
4.06e-08 |
|
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: 55.42 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 188 ISGTAPLNQETAEFFLSL-DIPIGELYGLSESSGPHTISNQNNYRLLSC-GKILTGCKNMLFQ---QNKDGIGE---ICL 259
Cdd:cd05909 267 VAGAEKLKDTLRQEFQEKfGIRILEGYGTTECSPVISVNTPQSPNKEGTvGRPLPGMEVKIVSvetHEEVPIGEgglLLV 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 260 WGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKIPIISN--AM 337
Cdd:cd05909 347 RGPNVMLGYLNEPELTSFAFGD-GWYDTGDIGKIDGEGFLTITGRLSR-FAKIAGEMVSLEAIEDILSEILPEDNEvaVV 424
|
....*..
gi 768004222 338 LVGDKLK 344
Cdd:cd05909 425 SVPDGRK 431
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
209-340 |
5.25e-08 |
|
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: 55.08 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 209 IGELYGLSESSGPHTISNQNnyrLL----SCGKILTGCKNMLfqqNKDG-------IGEICLWGRHIFMgYLESETETTE 277
Cdd:cd05929 272 IWEYYGGTEGQGLTIINGEE---WLthpgSVGRAVLGKVHIL---DEDGnevppgeIGEVYFANGPGFE-YTNDPEKTAA 344
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768004222 278 AIDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETLVKKKiPIISNAMLVG 340
Cdd:cd05929 345 ARNEGGWSTLGDVGYLDEDGYLYLTDR-RSDMIISGGVNIYPQEIENALIAH-PKVLDAAVVG 405
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
173-326 |
6.20e-08 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 54.85 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 173 SKVKTSLGLDH-CHSFISGTAPlnqeTAEFFLSLDIP---IGELYGLSESSGPHTISN----------QNNYRLLSCGKI 238
Cdd:PLN02479 301 PKSETILPLPRvVHVMTAGAAP----PPSVLFAMSEKgfrVTHTYGLSETYGPSTVCAwkpewdslppEEQARLNARQGV 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 239 ----LTGCKNMLFQQNK----DG--IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEI 308
Cdd:PLN02479 377 ryigLEGLDVVDTKTMKpvpaDGktMGEIVMRGNMVMKGYLKNPKANEEAFAN-GWFHSGDLGVKHPDGYIEIKDRSKDI 455
|
170
....*....|....*...
gi 768004222 309 LITaGGENVPPIPVETLV 326
Cdd:PLN02479 456 IIS-GGENISSLEVENVV 472
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
187-326 |
6.35e-08 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 54.88 E-value: 6.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 187 FISGTAPLNQET-AEFFLSLDIPIGELYGLSEssgphTISNQNN-Y------------------RLLSC--GKILTgckn 244
Cdd:PRK07514 274 FISGSAPLLAEThREFQERTGHAILERYGMTE-----TNMNTSNpYdgerragtvgfplpgvslRVTDPetGAELP---- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 245 mlfqqnKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVET 324
Cdd:PRK07514 345 ------PGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIIS-GGYNVYPKEVEG 417
|
..
gi 768004222 325 LV 326
Cdd:PRK07514 418 EI 419
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
187-326 |
8.20e-08 |
|
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: 54.60 E-value: 8.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 187 FISGTAPLNQETAEFFLSLDIPIG-------ELYGLSE-------SSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKD 252
Cdd:cd05906 294 LVNAGEAVVAKTIRRLLRLLEPYGlppdairPAFGMTEtcsgviySRSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQ 373
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768004222 253 G-----IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGlGFLYVTGHIKEILITaGGENVPPIPVETLV 326
Cdd:cd05906 374 LlpegeVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDN-GNLTITGRTKDTIIV-NGVNYYSHEIEAAV 450
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
254-340 |
1.63e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 53.63 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 254 IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVKKKiPII 333
Cdd:PRK07786 371 VGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIIS-GGENIYCAEVENVLASH-PDI 447
|
....*..
gi 768004222 334 SNAMLVG 340
Cdd:PRK07786 448 VEVAVIG 454
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
42-326 |
1.65e-07 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 53.52 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 42 WIAGAVtkdfkLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGAltyfaqadalKGTLVSTLKEvkptvfigvpqiwekIH 121
Cdd:PRK08974 240 AAYGPL-----LHPGKELVVTALPLYHIFALTVNCLLFIELGG----------QNLLITNPRD---------------IP 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 122 EMVKKnsaksmgLKKKAFVWARNigfkVNSKkmlgkYNTPVSYRMAKTLVFSKVKTSLGldhchsfisGTAPLNQETAEF 201
Cdd:PRK08974 290 GFVKE-------LKKYPFTAITG----VNTL-----FNALLNNEEFQELDFSSLKLSVG---------GGMAVQQAVAER 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 202 FLSL-DIPIGELYGLSESS-----GPHTISNQNNyrllSCG--------KILTGCKNMLFQqnkDGIGEICLWGRHIFMG 267
Cdd:PRK08974 345 WVKLtGQYLLEGYGLTECSplvsvNPYDLDYYSG----SIGlpvpsteiKLVDDDGNEVPP---GEPGELWVKGPQVMLG 417
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 768004222 268 YLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLV 326
Cdd:PRK08974 418 YWQRPEATDEVIKD-GWLATGDIAVMDEEGFLRIVDRKKDM-ILVSGFNVYPNEIEDVV 474
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
212-313 |
1.83e-07 |
|
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: 53.21 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 212 LYGLSESSG------PHTISNqnnyRLLSCGKILTGCKnmLFQQNKDG-------IGEICLWGRHIFMGYLESETETTEA 278
Cdd:cd05922 263 MYGQTEATRrmtylpPERILE----KPGSIGLAIPGGE--FEILDDDGtptppgePGEIVHRGPNVMKGYWNDPPYRRKE 336
|
90 100 110
....*....|....*....|....*....|....*
gi 768004222 279 IDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAG 313
Cdd:cd05922 337 GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFG 371
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
253-326 |
2.11e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 53.09 E-value: 2.11e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768004222 253 GIGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGlGFLYVTGHIKEiLITAGGENVPPIPVETLV 326
Cdd:PRK09192 410 VVGHICVRGPSLMSGYFRDE-ESQDVLAADGWLDTGDLGYLLD-GYLYITGRAKD-LIIINGRNIWPQDIEWIA 480
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
158-340 |
2.38e-07 |
|
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: 52.85 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 158 YNTPVSYRmakTLVFSKVKTSLGLDHCHSFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSgpHT-ISNQ-NNYRLLS 234
Cdd:cd05919 187 YGVPTFYA---NLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEhFGGPILDGIGATEVG--HIfLSNRpGAWRLGS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 235 CGKILTGCKNMLFqqNKDG-------IGEICLWGRHIFMGYLESeTETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKE 307
Cdd:cd05919 262 TGRPVPGYEIRLV--DEEGhtippgeEGDLLVRGPSAAVGYWNN-PEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADD 338
|
170 180 190
....*....|....*....|....*....|...
gi 768004222 308 ILITaGGENVPPIPVETLVkKKIPIISNAMLVG 340
Cdd:cd05919 339 MLKV-GGQWVSPVEVESLI-IQHPAVAEAAVVA 369
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
251-340 |
3.31e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 52.47 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 251 KDGIGEICLWGRHIFMGYLeSETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETlVKKKI 330
Cdd:PRK07638 330 KGEIGTVYVKSPQFFMGYI-IGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILF-GGINIFPEEIES-VLHEH 406
|
90
....*....|
gi 768004222 331 PIISNAMLVG 340
Cdd:PRK07638 407 PAVDEIVVIG 416
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
60-290 |
4.32e-07 |
|
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: 52.46 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 60 VVSYLPLSHIAAQMmdiwvpIKIGALT-----YFAQADALKgTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGL 134
Cdd:cd17632 268 TLNFMPMSHIAGRI------SLYGTLArggtaYFAAASDMS-TLFDDLALVRPTELFLVPRVCDMLFQRYQAELDRRSVA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 135 KKKAFVWARNIGFKVNSKKMLGKYNTPVsyrmaktlvfskvktslgldhchsfiSGTAPLNQETAEFFLS-LDIPIGELY 213
Cdd:cd17632 341 GADAETLAERVKAELRERVLGGRLLAAV--------------------------CGSAPLSAEMKAFMESlLDLDLHDGY 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 214 GLSEsSGPHTISNQ------NNYRLLSC---GKILTgcknmlfqQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGW 284
Cdd:cd17632 395 GSTE-AGAVILDGVivrppvLDYKLVDVpelGYFRT--------DRPHPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGF 465
|
....*.
gi 768004222 285 LHSGDL 290
Cdd:cd17632 466 YRTGDV 471
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
61-333 |
5.09e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 52.05 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 61 VSYLPLSHIAAQMMdIWVPikigaltyfaqadALKG---TLVStlkevkPTVFIGVPQIWekIHEMVKKNSAKSM--GLK 135
Cdd:PRK12476 239 VSWLPLYHDMGLSM-IGFP-------------AVYGghsTLMS------PTAFVRRPQRW--IKALSEGSRTGRVvtAAP 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 136 KKAFVWARNIGFKVN------SKKMLGKYNTPVSyrMAKTLVFSK-----------VKTSLGLDHCHSFISGTAPLNQET 198
Cdd:PRK12476 297 NFAYEWAAQRGLPAEgddidlSNVVLIIGSEPVS--IDAVTTFNKafapyglprtaFKPSYGIAEATLFVATIAPDAEPS 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 199 AEFFLSLDIPIGELYGLSESSgPHTISNqnnyrlLSCGKIL-----------TGCknmlfqQNKDG-IGEICLWGRHIFM 266
Cdd:PRK12476 375 VVYLDREQLGAGRAVRVAADA-PNAVAH------VSCGQVArsqwavivdpdTGA------ELPDGeVGEIWLHGDNIGR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 267 GYLE--SETETT----------------EAIDDEGWLHSGDLG-QLDGLgfLYVTGHIKEiLITAGGENVPPIPVETLVK 327
Cdd:PRK12476 442 GYWGrpEETERTfgaklqsrlaegshadGAADDGTWLRTGDLGvYLDGE--LYITGRIAD-LIVIDGRNHYPQDIEATVA 518
|
....*.
gi 768004222 328 KKIPII 333
Cdd:PRK12476 519 EASPMV 524
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
256-435 |
5.22e-07 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 52.19 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 256 EICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQL-D----GLGFLYvTGHIKEILITAGGE--NVPPIPVEtLVKK 328
Cdd:PRK08180 413 EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvDpadpERGLMF-DGRIAEDFKLSSGTwvSVGPLRAR-AVSA 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 329 KIPIISNAMLVGDKLKFLSMLLtlkcemnqmsgepldklnFEAINFCRGLGSQASTVTEIVKQQDPLVYKAIQQGINAVN 408
Cdd:PRK08180 491 GAPLVQDVVITGHDRDEIGLLV------------------FPNLDACRRLAGLLADASLAEVLAHPAVRAAFRERLARLN 552
|
170 180
....*....|....*....|....*..
gi 768004222 409 QEAMNNAQRIEKWVILEKDFSIYGGEL 435
Cdd:PRK08180 553 AQATGSSTRVARALLLDEPPSLDAGEI 579
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
205-326 |
1.32e-06 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 50.38 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 205 LDIPIGELYGLSESSG------PHTISNQNNyrllSCGKILTGCKNMLFQQNkdgIGEICLWGRHIFMGYLEsetettEA 278
Cdd:PRK07445 253 LQLRLAPTYGMTETASqiatlkPDDFLAGNN----SSGQVLPHAQITIPANQ---TGNITIQAQSLALGYYP------QI 319
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 768004222 279 IDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLV 326
Cdd:PRK07445 320 LDSQGIFETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAI 366
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
247-323 |
1.45e-06 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 50.53 E-value: 1.45e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768004222 247 FQQNKDG-IGEICLWGRHIFMGYLESETETTEaiddEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 323
Cdd:PRK13382 383 FREVPTGeVGTIFVRNDTQFDGYTSGSTKDFH----DGFMASGDVGYLDENGRLFVVGRDDE-MIVSGGENVYPIEVE 455
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
254-340 |
2.22e-06 |
|
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: 50.02 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 254 IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVkKKIPII 333
Cdd:cd05920 335 EGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKD-QINRGGEKIAAEEVENLL-LRHPAV 412
|
....*..
gi 768004222 334 SNAMLVG 340
Cdd:cd05920 413 HDAAVVA 419
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
254-340 |
2.30e-06 |
|
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: 49.76 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 254 IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKiPII 333
Cdd:COG1021 380 VGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKD-QINRGGEKIAAEEVENLLLAH-PAV 457
|
....*..
gi 768004222 334 SNAMLVG 340
Cdd:COG1021 458 HDAAVVA 464
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
186-340 |
2.45e-06 |
|
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: 49.78 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 186 SFISGTAPLNQETAEFFLSL-DIPIGELYGLSESSgPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGI-------GEI 257
Cdd:cd05935 203 VLTGGGAPMPPAVAEKLLKLtGLRFVEGYGLTETM-SQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRelppnevGEI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 258 CLWGRHIFMGYLESETETTEA-IDDEG--WLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKiPIIS 334
Cdd:cd05935 282 VVRGPQIFKGYWNRPEETEESfIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKR-MINVSGFKVWPAEVEAKLYKH-PAI* 359
|
....*.
gi 768004222 335 NAMLVG 340
Cdd:cd05935 360 EVCVIS 365
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
251-323 |
4.32e-06 |
|
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: 49.17 E-value: 4.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768004222 251 KDG--IGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 323
Cdd:cd12119 365 WDGkaVGELQVRGPWVTKSYYKND-EESEALTEDGWLRTGDVATIDEDGYLTITDRSKD-VIKSGGEWISSVELE 437
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
265-340 |
5.19e-06 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 48.66 E-value: 5.19e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768004222 265 FMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVKKKiPIISNAMLVG 340
Cdd:cd05923 358 FTGYLNQPEATAKKLQD-GWYRTGDVGYVDPSGDVRILGRVDDMIIS-GGENIHPSEIERVLSRH-PGVTEVVVIG 430
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
236-326 |
6.03e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 48.38 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 236 GKILTGCKNMLFQQNKDGI-----GEICLWGRHIFMGYleSETETTEAIDdeGWLHSGDLGQLDGLGFLYVTGHIKEiLI 310
Cdd:PRK07788 379 GRPPKGVTVKILDENGNEVprgvvGRIFVGNGFPFEGY--TDGRDKQIID--GLLSSGDVGYFDEDGLLFVDGRDDD-MI 453
|
90
....*....|....*.
gi 768004222 311 TAGGENVPPIPVETLV 326
Cdd:PRK07788 454 VSGGENVFPAEVEDLL 469
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
158-382 |
1.52e-05 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 47.11 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 158 YNTPVSYRMAKTLVFSKVKtSLGLDHCHSFISGTAPLNQETAEFFLS-LDIPIGELYGLSESsGPHTISNQ--NNYRLLS 234
Cdd:cd05969 184 YTAPTAIRMLMKEGDELAR-KYDLSSLRFIHSVGEPLNPEAIRWGMEvFGVPIHDTWWQTET-GSIMIANYpcMPIKPGS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 235 CGKILTGCKNMLFQQNKDGI-----GEICL---WGRhIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIK 306
Cdd:cd05969 262 MGKPLPGVKAAVVDENGNELppgtkGILALkpgWPS-MFRGIWNDEERYKNSFID-GWYLTGDLAYRDEDGYFWFVGRAD 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 307 EILITAgGENVPPIPVETLVKKKiPIISNAMLVG--DKLK--FLSMLLTLKcemnqmSG-EPLDKLNFEAINFCR-GLGS 380
Cdd:cd05969 340 DIIKTS-GHRVGPFEVESALMEH-PAVAEAGVIGkpDPLRgeIIKAFISLK------EGfEPSDELKEEIINFVRqKLGA 411
|
..
gi 768004222 381 QA 382
Cdd:cd05969 412 HV 413
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
188-331 |
3.63e-05 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 46.46 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 188 ISGTAPLNQETAEFF-LSLDIPIGELYGLSESSGPHTISNQNnyRLLSCGKILTGCKN-----------------MLFQQ 249
Cdd:PRK08633 904 VAGAEKLKPEVADAFeEKFGIRILEGYGATETSPVASVNLPD--VLAADFKRQTGSKEgsvgmplpgvavrivdpETFEE 981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 250 NKDGI-GEICLWGRHIFMGYLESETETTEAI---DDEGWLHSGDLGQLDGLGFLYVTGHIK---EIlitaGGENVPPIPV 322
Cdd:PRK08633 982 LPPGEdGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSrfaKI----GGEMVPLGAV 1057
|
....*....
gi 768004222 323 ETLVKKKIP 331
Cdd:PRK08633 1058 EEELAKALG 1066
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
234-338 |
3.93e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 46.14 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 234 SCGKILTGCKNMLFQQNKDGIGEIcLWGRHIFMGYLESETETT---EAIDDeGWLHSGDLGQLDGLGFLYVTGHiKEILI 310
Cdd:PRK13383 346 TVGKPVAGCPVRILDRNNRPVGPR-VTGRIFVGGELAGTRYTDgggKAVVD-GMTSTGDMGYLDNAGRLFIVGR-EDDMI 422
|
90 100
....*....|....*....|....*...
gi 768004222 311 TAGGENVPPIPVETLVKKKIPIISNAML 338
Cdd:PRK13383 423 ISGGENVYPRAVENALAAHPAVADNAVI 450
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
252-318 |
4.76e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 45.88 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 252 DG-IGEICLWGRHIFMGYLESETETTE-----------------AIDDEGWLHSGDLGQ-LDglGFLYVTGHIKEILITA 312
Cdd:PRK07769 415 DGqIGEIWLHGNNIGTGYWGKPEETAAtfqnilksrlseshaegAPDDALWVRTGDYGVyFD--GELYITGRVKDLVIID 492
|
....*.
gi 768004222 313 GGENVP 318
Cdd:PRK07769 493 GRNHYP 498
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
58-455 |
4.97e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 45.86 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 58 ETVVSYLPLSHI-------AAQMMDIWVPIKIGALTYFAqadalkgtlvSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAK 130
Cdd:PTZ00342 348 KTHLSYLPISHIyerviayLSFMLGGTINIWSKDINYFS----------KDIYNSKGNILAGVPKVFNRIYTNIMTEINN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 131 SMGLKK---KAFVWARNIGFKVNSKKMLGKYnTPVSYRMAktlvfSKVKTSLGLdhchsFISGTAPLNQETA-EFFLSLD 206
Cdd:PTZ00342 418 LPPLKRflvKKILSLRKSNNNGGFSKFLEGI-THISSKIK-----DKVNPNLEV-----ILNGGGKLSPKIAeELSVLLN 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 207 IPIGELYGLSESSGPHTISNQNNYRLLSCGKILtgCKNMLFQ-------QNKDGI--GEICLWGRHIFMGY-LESETeTT 276
Cdd:PTZ00342 487 VNYYQGYGLTETTGPIFVQHADDNNTESIGGPI--SPNTKYKvrtwetyKATDTLpkGELLIKSDSIFSGYfLEKEQ-TK 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 277 EAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENvppIPVETL--VKKKIPIISNAMLVGDK-----LKFLSM- 348
Cdd:PTZ00342 564 NAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEY---IETDMLnnLYSQISFINFCVVYGDDsmdgpLAIISVd 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 349 -LLTLKC----EMNQMSG----EPLDKLNFEAINfcrglgsqASTVTEIVKQQDPLVYKaiQQGINAVNqeAMNNAQRIE 419
Cdd:PTZ00342 641 kYLLFKClkddNMLESTGinekNYLEKLTDETIN--------NNIYVDYVKGKMLEVYK--KTNLNRYN--IINDIYLTS 708
|
410 420 430
....*....|....*....|....*....|....*..
gi 768004222 420 K-WvilekDFSIYggeLGPMMKLKRHFVAQKYKKQID 455
Cdd:PTZ00342 709 KvW-----DTNNY---LTPTFKVKRFYVFKDYAFFID 737
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
253-324 |
5.12e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 45.53 E-value: 5.12e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768004222 253 GIGEICLWGRHIFMGYLESETetteaIDDEGWLHSGDLGQLdGLGFLYVTGHIKEiLITAGGENVPPIPVET 324
Cdd:PRK05851 371 EIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTGDLGYL-VDGGLVVCGRAKE-LITVAGRNIFPTEIER 435
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
168-326 |
5.37e-05 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 45.40 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 168 KTLVFSKVKTSLGldhchsfisGTAPLNQETAEFFLSLD-IPIGELYGLSESSgPHTISNQNNyrllscGKILTGCKNM- 245
Cdd:PRK07059 322 DKLDFSKLIVANG---------GGMAVQRPVAERWLEMTgCPITEGYGLSETS-PVATCNPVD------ATEFSGTIGLp 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 246 -----LFQQNKDG-------IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAG 313
Cdd:PRK07059 386 lpsteVSIRDDDGndlplgePGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKD-MILVS 464
|
170
....*....|...
gi 768004222 314 GENVPPIPVETLV 326
Cdd:PRK07059 465 GFNVYPNEIEEVV 477
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
190-323 |
7.48e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 44.65 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 190 GTAPLNQETAEFFLSLDIPIGELYGLSESSGphtisnqnnyrllSC---GKILTGCKNMLfqqnkdGIGEICLWGRHIFM 266
Cdd:PRK07824 159 GGGPAPAPVLDAAAAAGINVVRTYGMSETSG-------------GCvydGVPLDGVRVRV------EDGRIALGGPTLAK 219
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 768004222 267 GYleSETETTEAIDDEGWLHSGDLGQLDGlGFLYVTGHIKEIlITAGGENVPPIPVE 323
Cdd:PRK07824 220 GY--RNPVDPDPFAEPGWFRTDDLGALDD-GVLTVLGRADDA-ISTGGLTVLPQVVE 272
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
254-305 |
8.38e-05 |
|
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: 44.93 E-value: 8.38e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 768004222 254 IGEICLWGRHIFMGYLESETETTEA---IDDEGWLHSGDLGQLDGLGFLYVTGHI 305
Cdd:cd05945 298 KGELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLVRLEADGLLFYRGRL 352
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
252-314 |
9.48e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 44.60 E-value: 9.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768004222 252 DG--IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGG 314
Cdd:PRK07787 317 DGetVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRESTDLIKSGG 381
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
252-313 |
1.64e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 44.16 E-value: 1.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768004222 252 DGIGEICLWGRHIFMGYLE--SETETT--EAIDD------EG-WLHSGDLGQLDGlGFLYVTGHIKEILITAG 313
Cdd:PRK05850 395 GTVGEIWVHGDNVAAGYWQkpEETERTfgATLVDpspgtpEGpWLRTGDLGFISE-GELFIVGRIKDLLIVDG 466
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
254-340 |
1.73e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 43.96 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 254 IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLG-FLYVT--GHIkeilITAGGENVPPIPVETLVkKKI 330
Cdd:PRK06164 377 SGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGqFVYQTrmGDS----LRLGGFLVNPAEIEHAL-EAL 451
|
90
....*....|
gi 768004222 331 PIISNAMLVG 340
Cdd:PRK06164 452 PGVAAAQVVG 461
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
254-333 |
2.84e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 43.62 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 254 IGEICLWGRHIFMGYL---ESETETTEAIDDEGWLHSGDLGQLDGlGFLYVTGHIKEILITAgGENVPPIPVETLVKKKI 330
Cdd:PRK05691 397 VGEIWASGPSIAHGYWrnpEASAKTFVEHDGRTWLRTGDLGFLRD-GELFVTGRLKDMLIVR-GHNLYPQDIEKTVEREV 474
|
...
gi 768004222 331 PII 333
Cdd:PRK05691 475 EVV 477
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
252-336 |
6.27e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 42.32 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 252 DGIGEIC-LWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETLVKKKI 330
Cdd:PRK13388 349 EAIGELVnTAGAGFFEGYYNNPEATAERMRH-GMYWSGDLAYRDADGWIYFAGR-TADWMRVDGENLSAAPIERILLRHP 426
|
....*.
gi 768004222 331 PIISNA 336
Cdd:PRK13388 427 AINRVA 432
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
158-331 |
6.84e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 42.00 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 158 YNTPVSYRMAKTLVFSK-----VKTSLGLDHCHSF------------ISGTAPLNQETAEFFL-SLDIPIGELYGLSESS 219
Cdd:PRK08043 438 YPSPLHYRIVPELVYDRnctvlFGTSTFLGNYARFanpydfarlryvVAGAEKLQESTKQLWQdKFGLRILEGYGVTECA 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 220 GPHTISNQNNYRLLSCGKILTGCKNMLFqqNKDGI---GEICLWGRHIFMGYLESE---------TETTEAIDDEGWLHS 287
Cdd:PRK08043 518 PVVSINVPMAAKPGTVGRILPGMDARLL--SVPGIeqgGRLQLKGPNIMNGYLRVEkpgvlevptAENARGEMERGWYDT 595
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 768004222 288 GDLGQLDGLGFLYVTGHIKEILITAgGENVPPIPVETLVKKKIP 331
Cdd:PRK08043 596 GDIVRFDEQGFVQIQGRAKRFAKIA-GEMVSLEMVEQLALGVSP 638
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
265-340 |
7.43e-04 |
|
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: 41.65 E-value: 7.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768004222 265 FMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKiPIISNAMLVG 340
Cdd:cd05971 299 FLGYWNNP-SATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDV-ITSSGYRIGPAEIEECLLKH-PAVLMAAVVG 371
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
266-323 |
1.02e-03 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 41.53 E-value: 1.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 768004222 266 MGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 323
Cdd:PRK05857 386 LGYWNNPERTAEVLID-GWVNTGDLLERREDGFFYIKGRSSEMIIC-GGVNIAPDEVD 441
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
254-325 |
1.27e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 41.22 E-value: 1.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768004222 254 IGEICLWGRHIFMgYLESETETTEAID-DEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETL 325
Cdd:PRK13391 353 PGTIWFEGGRPFE-YLNDPAKTAEARHpDGTWSTVGDIGYVDEDGYLYLTDR-AAFMIISGGVNIYPQEAENL 423
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
276-340 |
1.48e-03 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 40.89 E-value: 1.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768004222 276 TEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKiPIISNAMLVG 340
Cdd:PRK06018 403 GEILDDDGFFDTGDVATIDAYGYMRITDRSKDV-IKSGGEWISSIDLENLAVGH-PKVAEAAVIG 465
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
158-326 |
1.71e-03 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 41.10 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 158 YNTPVSYRMAKTLVFSKVKTSL-GLD----------HCHSF------ISGTAPLNQETAEFFLS-LDIPIGELYGLSESS 219
Cdd:PRK06814 866 YPSPLHYRIIPELIYDTNATILfGTDtflngyaryaHPYDFrslryvFAGAEKVKEETRQTWMEkFGIRILEGYGVTETA 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 220 GPHTISNQNNYRLLSCGKILTGCKNMLfqQNKDGI---GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGL 296
Cdd:PRK06814 946 PVIALNTPMHNKAGTVGRLLPGIEYRL--EPVPGIdegGRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEE 1023
|
170 180 190
....*....|....*....|....*....|...
gi 768004222 297 GFLYVTGHIK---EIlitaGGENVPPIPVETLV 326
Cdd:PRK06814 1024 GFITIKGRAKrfaKI----AGEMISLAAVEELA 1052
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
263-323 |
2.40e-03 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 40.13 E-value: 2.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768004222 263 HIFM-GYLESETETTEAIDDEgWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVE 323
Cdd:PRK06155 380 FAFAtGYFGMPEKTVEAWRNL-WFHTGDRVVRDADGWFRFVDRIKDA-IRRRGENISSFEVE 439
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
252-323 |
2.86e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 40.05 E-value: 2.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768004222 252 DGIGEIC-LWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILiTAGGENVPPIPVE 323
Cdd:PRK07867 350 EAIGELVnTAGPGGFEGYYNDPEADAERMRG-GVYWSGDLAYRDADGYAYFAGRLGDWM-RVDGENLGTAPIE 420
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
255-323 |
3.81e-03 |
|
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: 39.21 E-value: 3.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768004222 255 GEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVE 323
Cdd:cd17636 190 GEIVARGPTVMAGYWNRPEVNARRTRG-GWHHTNDLGRREPDGSLSFVGP-KTRMIKSGAENIYPAEVE 256
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
253-340 |
3.82e-03 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 39.37 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768004222 253 GIGEICLWGRHIFMGYLESETETTEA-IDDEG---WLHSGDLGQLDGLGFLYVTGHIKEILITAGGeNVPPIPVETlVKK 328
Cdd:cd05910 297 EIGEITVTGPTVTPTYVNRPVATALAkIDDNSegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGG-TLYTEPVER-VFN 374
|
90
....*....|..
gi 768004222 329 KIPIISNAMLVG 340
Cdd:cd05910 375 THPGVRRSALVG 386
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
268-325 |
4.21e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 39.50 E-value: 4.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 768004222 268 YLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETL 325
Cdd:PRK08276 354 YHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDR-KSDMIISGGVNIYPQEIENL 410
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
274-323 |
7.89e-03 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 38.53 E-value: 7.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 768004222 274 ETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 323
Cdd:PRK12406 370 EKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVIS-GGVNIYPAEIE 418
|
|
| |
