|
Name |
Accession |
Description |
Interval |
E-value |
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
23-615 |
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: 1107.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 23 KNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAK 102
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 103 VNILLVENDQQLQKILSIpQSSLEPLKAIIQYRLPMK-KNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTS 181
Cdd:cd05933 81 ANILVVENQKQLQKILQI-QDKLPHLKAIIQYKEPLKeKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 182 GTTGIPKGVMLSHDNITWIAGAVTKDFKL---TDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVST 258
Cdd:cd05933 160 GTTGMPKGVMLSHDNITWTAKAASQHMDLrpaTVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKGTLVKT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 259 LKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGL 338
Cdd:cd05933 240 LREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLFYRLAKKLVFKKVRKALGL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 339 DHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGIGEICLWG 418
Cdd:cd05933 320 DRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGIGEICFWG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 419 RHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKIPIISNAMLVGD 498
Cdd:cd05933 400 RHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPIISNAMLIGD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 499 KLKFLSMLLTLKCEMNQMSGEPLDKLNFEAINFCRGLGSQASTVTEIVKQQDPLVYKAIQQGINAVNQEAMNNAQRIEKW 578
Cdd:cd05933 480 KRKFLSMLLTLKCEVNPETGEPLDELTEEAIEFCRKLGSQATRVSEIAGGKDPKVYEAIEEGIKRVNKKAISNAQKIQKW 559
|
570 580 590
....*....|....*....|....*....|....*..
gi 1008909320 579 VILEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 615
Cdd:cd05933 560 VILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1-615 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 548.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 1 MTIPEFFRESVNRFGTYPALASKNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGG 80
Cdd:COG1022 11 DTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 81 LCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKILSIpQSSLEPLKAIIQY-RLPMKKNNNLYSWDDFMELGRSI-P 158
Cdd:COG1022 91 VTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV-RDELPSLRHIVVLdPRGLRDDPRLLSLDELLALGREVaD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 159 DTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVpIK 238
Cdd:COG1022 170 PAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGP-GDRTLSFLPLAHVFERTVSYYA-LA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 239 IGALTYFAQADAlkgTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKYNTP 318
Cdd:COG1022 248 AGATVAFAESPD---TLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARLAGKSPSL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 319 ---VSYRMAKTLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKI 395
Cdd:COG1022 325 llrLKHALADKLVFSKLREALG-GRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 396 LTGCKNMLfqqnkDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVP 475
Cdd:COG1022 404 LPGVEVKI-----AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 476 PIPVETLVkKKIPIISNAMLVGDKLKFLSMLLTlkcemnqmsgepldkLNFEAI-NFCRGLGSQASTVTEIVkqQDPLVY 554
Cdd:COG1022 479 PQPIENAL-KASPLIEQAVVVGDGRPFLAALIV---------------PDFEALgEWAEENGLPYTSYAELA--QDPEVR 540
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1008909320 555 KAIQQGINAVNQEaMNNAQRIEKWVILEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 615
Cdd:COG1022 541 ALIQEEVDRANAG-LSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALY 600
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
28-603 |
2.72e-140 |
|
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: 415.46 E-value: 2.72e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 28 WEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILL 107
Cdd:cd05907 3 WQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 108 VENdqqlqkilsipqssleplkaiiqyrlpmkknnnlyswddfmelgrsiPDtqleqviesqkanQCAVLIYTSGTTGIP 187
Cdd:cd05907 83 VED-----------------------------------------------PD-------------DLATIIYTSGTTGRP 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 188 KGVMLSHDNITWIAGAVTkDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADAlkgTLVSTLKEVKPTVF 267
Cdd:cd05907 103 KGVMLSHRNILSNALALA-ERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAE---TLLDDLSEVRPTVF 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 268 IGVPQIWEKIHEMVKKnsAKSMGLKKKAFVWArnigfkvnskkMLGKyntpvsyrmaktlvfskvktslgldhCHSFISG 347
Cdd:cd05907 179 LAVPRVWEKVYAAIKV--KAVPGLKRKLFDLA-----------VGGR--------------------------LRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 348 TAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKnmlFQQNKDGigEICLWGRHIFMGYLE 427
Cdd:cd05907 220 GAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVE---VRIADDG--EILVRGPNVMLGYYK 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 428 SETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISNAMLVGDKLKFLSMLL 507
Cdd:cd05907 295 NPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKAS-PLISQAVVIGDGRPFLVALI 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 508 TLKCEMNQMSGEPldklnfeainfcrgLGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEaMNNAQRIEKWVILEKDFSI 587
Cdd:cd05907 374 VPDPEALEAWAEE--------------HGIAYTDVAELAA--NPAVRAEIEAAVEAANAR-LSRYEQIKKFLLLPEPFTI 436
|
570
....*....|....*.
gi 1008909320 588 YGGELGPMMKLKRHFV 603
Cdd:cd05907 437 ENGELTPTLKLKRPVI 452
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
27-615 |
5.74e-87 |
|
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: 281.03 E-value: 5.74e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 27 KWEILNFNQYYEACRKAAKSLIKLGLERFHG--VGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVN 104
Cdd:cd05927 2 PYEWISYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 105 ILLVENDQqlqkilsipqssleplkaiiqyrlpmkknnNLYSWDDFMELGRSIPdtqlEQVIESqKANQCAVLIYTSGTT 184
Cdd:cd05927 82 IVFCDAGV------------------------------KVYSLEEFEKLGKKNK----VPPPPP-KPEDLATICYTSGTT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 185 GIPKGVMLSHDNI-TWIAGA--VTKDFKLTDKHETVVSYLPLSHIAAQMMdIWVPIKIGALTYFAQADALKgtLVSTLKE 261
Cdd:cd05927 127 GNPKGVMLTHGNIvSNVAGVfkILEILNKINPTDVYISYLPLAHIFERVV-EALFLYHGAKIGFYSGDIRL--LLDDIKA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 262 VKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNigFKVNSKKMLGKYNTPVSYRmaktLVFSKVKTSLGLdHC 341
Cdd:cd05927 204 LKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALN--YKLAELRSGVVRASPFWDK----LVFNKIKQALGG-NV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 342 HSFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNML--------FQQNKDGIG 412
Cdd:cd05927 277 RLMLTGSAPLSPEVLEFLRVaLGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLvdvpemnyDAKDPNPRG 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 413 EICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISN 492
Cdd:cd05927 357 EVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARS-PFVAQ 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 493 AMLVGDKLKflSMLLTLKCemnqmsgepldkLNFEAI-NFCRGLGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEamNN 571
Cdd:cd05927 436 IFVYGDSLK--SFLVAIVV------------PDPDVLkEWAASKGGGTGSFEELCK--NPEVKKAILEDLVRLGKE--NG 497
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1008909320 572 AQRIE--KWVILEKD-FSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 615
Cdd:cd05927 498 LKGFEqvKAIHLEPEpFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
7-469 |
5.05e-78 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 253.39 E-value: 5.05e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 7 FRESVNRFGTYPALaskNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIY 86
Cdd:pfam00501 1 LERQAARTPDKTAL---EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 87 ATNSAEVCQYVITHAKVNILLVENDQQLQKILSIPQSSLEPLKAIIQYRLPMKKNNNLYSWDDfmelgrsiPDTQLEQVI 166
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAK--------PADVPPPPP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 167 ESQKANQCAVLIYTSGTTGIPKGVMLSHDNI----TWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGA- 241
Cdd:pfam00501 150 PPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLvanvLSIKRVRPRGFGLGP-DDRVLSTLPLFHDFGLSLGLLGPLLAGAt 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 242 LTYFAQADALKGT-LVSTLKEVKPTVFIGVPQIWEKIhemvkknsaksmglkkkafvwarnigfkvnskkmlgkyntpVS 320
Cdd:pfam00501 229 VVLPPGFPALDPAaLLELIERYKVTVLYGVPTLLNML-----------------------------------------LE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 321 YRMAKTLVFSKVKTslgldhchsFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNYRLL---SCGKIL 396
Cdd:pfam00501 268 AGAPKRALLSSLRL---------VLSGGAPLPPELARRFRElFGGALVNGYGLTETTGVVTTPLPLDEDLRslgSVGRPL 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1008909320 397 TGCK------NMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITA 469
Cdd:pfam00501 339 PGTEvkivddETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
28-607 |
2.11e-76 |
|
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: 253.88 E-value: 2.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 28 WEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILL 107
Cdd:cd17641 9 WQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 108 VENDQQLQKILSIpQSSLEPLKAIIqYRLP--MKKNNN--LYSWDDFMELGRSI----PDtQLEQVIESQKANQCAVLIY 179
Cdd:cd17641 89 AEDEEQVDKLLEI-ADRIPSVRYVI-YCDPrgMRKYDDprLISFEDVVALGRALdrrdPG-LYEREVAAGKGEDVAVLCT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 180 TSGTTGIPKGVMLSHDN-ITWIAGAVTKDFKLTDkhETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADAlkgTLVST 258
Cdd:cd17641 166 TSGTTGKPKLAMLSHGNfLGHCAAYLAADPLGPG--DEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEEPE---TMMED 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 259 LKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGK---YNTPVSYRMAKTLVFSKVKTS 335
Cdd:cd17641 241 LREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLRALDRGKRGRpvsLWLRLASWLADALLFRPLRDR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 336 LGLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCknmlfQQNKDGIGEIC 415
Cdd:cd17641 321 LGFSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGT-----EVRIDEVGEIL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 416 LWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISNAML 495
Cdd:cd17641 396 VRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFS-PYIAEAVV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 496 VGDKLKFLSMLLTLKcemnqmsgepldklnFEAI-NFCRGLGSQASTVTEIVKQqdPLVYKAIQQGINAVNQEaMNNAQR 574
Cdd:cd17641 475 LGAGRPYLTAFICID---------------YAIVgKWAEQRGIAFTTYTDLASR--PEVYELIRKEVEKVNAS-LPEAQR 536
|
570 580 590
....*....|....*....|....*....|...
gi 1008909320 575 IEKWVILEKDFSIYGGELGPMMKLKRHFVAQKY 607
Cdd:cd17641 537 IRRFLLLYKELDADDGELTRTRKVRRGVIAEKY 569
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
25-607 |
6.74e-70 |
|
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: 235.06 E-value: 6.74e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 25 GKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVN 104
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 105 ILLV----ENDQQLQKILSIPQSSLEPlkaiiqyrlPMKKNNNLYSWDDFMELGrsipdtQLEQVIESQKANQCAVLIYT 180
Cdd:cd05932 81 ALFVgkldDWKAMAPGVPEGLISISLP---------PPSAANCQYQWDDLIAQH------PPLEERPTRFPEQLATLIYT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 181 SGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQA-DalkgTLVSTL 259
Cdd:cd05932 146 SGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEE-NDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESlD----TFVEDV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 260 KEVKPTVFIGVPQIWEKIHEmvkknsaksmglkkkafvwarNIGFKVNSKKMlgkyNTPVSYRMAKTLVFSKVKTSLGLD 339
Cdd:cd05932 221 QRARPTLFFSVPRLWTKFQQ---------------------GVQDKIPQQKL----NLLLKIPVVNSLVKRKVLKGLGLD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 340 HCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQnkdgiGEICLWGR 419
Cdd:cd05932 276 QCRLAGCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISED-----GEILVRSP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 420 HIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVEtlvkKKI---PIISNAMLV 496
Cdd:cd05932 351 ALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIE----NKLaehDRVEMVCVI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 497 GDKLKFLSMLLtlkcemnQMSGEPldklNFEAINFCRGlGSQASTvteivkqqdplvyKAIQQGINAvnqeAMNNAQRIE 576
Cdd:cd05932 427 GSGLPAPLALV-------VLSEEA----RLRADAFARA-ELEASL-------------RAHLARVNS----TLDSHEQLA 477
|
570 580 590
....*....|....*....|....*....|.
gi 1008909320 577 KWVILEKDFSIYGGELGPMMKLKRHFVAQKY 607
Cdd:cd05932 478 GIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
35-533 |
8.79e-63 |
|
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: 214.61 E-value: 8.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 35 QYYEACRKAAKSLIKL---GLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEND 111
Cdd:cd05914 9 TYKDLADNIAKFALLLkinGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 112 QQLqkilsipqssleplkaiiqyrlpmkknnnlyswddfmelgrsipdtqleqviesqkanqcAVLIYTSGTTGIPKGVM 191
Cdd:cd05914 89 DDV------------------------------------------------------------ALINYTSGTTGNSKGVM 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 192 LSHDNITWIAGAVtKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAqaDALKGTLVSTLKEVKPTVFIGVP 271
Cdd:cd05914 109 LTYRNIVSNVDGV-KEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFL--DKIPSAKIIALAFAQVTPTLGVP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 272 QIW--EKIHEMVKKNsaksmglkkkafvwarnigfKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGlDHCHSFISGTA 349
Cdd:cd05914 186 VPLviEKIFKMDIIP--------------------KLTLKKFKFKLAKKINNRKIRKLAFKKVHEAFG-GNIKEFVIGGA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 350 PLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQN-KDGIGEICLWGRHIFMGYLES 428
Cdd:cd05914 245 KINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDpATGEGEIIVRGPNVMKGYYKN 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 429 ETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVET-LVKKKIPIISNAMLVGDKLKFLSML- 506
Cdd:cd05914 325 PEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAkINNMPFVLESLVVVQEKKLVALAYId 404
|
490 500 510
....*....|....*....|....*....|....*
gi 1008909320 507 ---LTLKCEMNQ-----MSGEPLDKLNFEAINFCR 533
Cdd:cd05914 405 pdfLDVKALKQRniidaIKWEVRDKVNQKVPNYKK 439
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
3-497 |
5.18e-58 |
|
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: 201.58 E-value: 5.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 3 IPEFFRESVNRFGTYPALASKngkkWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLC 82
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG----GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 83 VGIYATNSAEVCQYVITHAKVNILLvendqqlqkilsipqssleplkaiiqyrlpmkknnnlyswddfmelgrsipdtql 162
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALV------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 163 eqviesqkanqCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGA- 241
Cdd:COG0318 102 -----------TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTP-GDVVLVALPLFHVFGLTVGLLAPLLAGAt 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 242 ---LTYFAQADALKgtlvsTLKEVKPTVFIGVPQIWekihemvkknsaksmglkkkafvwarnigfkvnskkmlgkyntp 318
Cdd:COG0318 170 lvlLPRFDPERVLE-----LIERERVTVLFGVPTML-------------------------------------------- 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 319 vsYRMAKTLVFSKVKTSlgldHCHSFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNY--RLLSCGKI 395
Cdd:COG0318 201 --ARLLRHPEFARYDLS----SLRLVVSGGAPLPPELLERFEErFGVRIVEGYGLTETSPVVTVNPEDPGerRPGSVGRP 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 396 LTGCKNMLFqqNKDG-------IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILIT 468
Cdd:COG0318 275 LPGVEVRIV--DEDGrelppgeVGEIVVRGPNVMKGYWNDPEATAEAFRD-GWLRTGDLGRLDEDGYLYIVGRKKDMIIS 351
|
490 500
....*....|....*....|....*....
gi 1008909320 469 aGGENVPPIPVETLVkKKIPIISNAMLVG 497
Cdd:COG0318 352 -GGENVYPAEVEEVL-AAHPGVAEAAVVG 378
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
2-615 |
3.89e-57 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 203.79 E-value: 3.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 2 TIPEFFRESVNRFGTYPALASK---NGK----KWeiLNFNQYYEAcRKAAKS-LIKLGLERFHGVGILGFNSAEWFITAV 73
Cdd:PLN02736 45 TLHDNFVYAVETFRDYKYLGTRirvDGTvgeyKW--MTYGEAGTA-RTAIGSgLVQHGIPKGACVGLYFINRPEWLIVDH 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 74 GAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVeNDQQLQKILSIpQSSLEPLKAIIQY--------RLPMKKNNNLY 145
Cdd:PLN02736 122 ACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSC-LSEIPSVRLIVVVggadeplpSLPSGTGVEIV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 146 SWDDFMELGRSIPdtqleQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDN-ITWIAGA-VTKDFKLTDKHetvVSYLPL 223
Cdd:PLN02736 200 TYSKLLAQGRSSP-----QPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNlIANVAGSsLSTKFYPSDVH---ISYLPL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 224 SHI---AAQMMDIWVPIKIGaltyFAQADALKgtLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFvwar 300
Cdd:PLN02736 272 AHIyerVNQIVMLHYGVAVG----FYQGDNLK--LMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLF---- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 301 NIGFkvNSKK---MLGKYNTPvsyrMAKTLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFflsLDIPIG----ELYGLS 373
Cdd:PLN02736 342 NAAY--NAKKqalENGKNPSP----MWDRLVFNKIKAKLG-GRVRFMSSGASPLSPDVMEF---LRICFGgrvlEGYGMT 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 374 ESSGPHTISNQNNYrllSCGKI----------LTGCKNMLFqQNKDGI---GEICLWGRHIFMGYLESETETTEAIDDEG 440
Cdd:PLN02736 412 ETSCVISGMDEGDN---LSGHVgspnpacevkLVDVPEMNY-TSEDQPyprGEICVRGPIIFKGYYKDEVQTREVIDEDG 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 441 WLHSGDLGQ-LDGlGFLYVTGHIKEILITAGGENVPPIPVETlVKKKIPIISNAMLVGDKLKflSMLLTLkcemnqMSGE 519
Cdd:PLN02736 488 WLHTGDIGLwLPG-GRLKIIDRKKNIFKLAQGEYIAPEKIEN-VYAKCKFVAQCFVYGDSLN--SSLVAV------VVVD 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 520 PLDKLNFEAINfcrglGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKD-FSIYGGELGPMMKL 598
Cdd:PLN02736 558 PEVLKAWAASE-----GIKYEDLKQLCN--DPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEpFTVENGLLTPTFKV 630
|
650
....*....|....*..
gi 1008909320 599 KRHFVAQKYKKQIDHMY 615
Cdd:PLN02736 631 KRPQAKAYFAKAISDMY 647
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
31-603 |
9.89e-55 |
|
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: 193.97 E-value: 9.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 31 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYvithakvnillven 110
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIH-------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 111 dqqlqkilsipqssleplkaiiqyrlpmkknnnlyswddfmelgrSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGV 190
Cdd:cd17639 72 ---------------------------------------------SLNETECSAIFTDGKPDDLACIMYTSGSTGNPKGV 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 191 MLSHDNITW-IAGAVTKDFKLTDKHETVVSYLPLSHI---AAQMmdiwVPIKIGALTYFAQADAL--------KGTLVst 258
Cdd:cd17639 107 MLTHGNLVAgIAGLGDRVPELLGPDDRYLAYLPLAHIfelAAEN----VCLYRGGTIGYGSPRTLtdkskrgcKGDLT-- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 259 lkEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFvwarNIGFKVNSKKMLGKYNTPVsyrmAKTLVFSKVKTSLGl 338
Cdd:cd17639 181 --EFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLF----WTAYQSKLKALKEGPGTPL----LDELVFKKVRAALG- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 339 DHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNML--------FQQNKDG 410
Cdd:cd17639 250 GRLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLvdweeggySTDKPPP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 411 IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPII 490
Cdd:cd17639 330 RGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSN-PLV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 491 SNAMLVGD--KLKFLSMLLTlkcemNQmsgEPLDKlnfeainFCRGLGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEA 568
Cdd:cd17639 409 NNICVYADpdKSYPVAIVVP-----NE---KHLTK-------LAEKHGVINSEWEELCE--DKKLQKAVLKSLAETARAA 471
|
570 580 590
....*....|....*....|....*....|....*...
gi 1008909320 569 mnNAQRIE---KWVILEKDFSIYGGELGPMMKLKRHFV 603
Cdd:cd17639 472 --GLEKFEipqGVVLLDEEWTPENGLVTAAQKLKRKEI 507
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
7-615 |
1.15e-53 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 194.26 E-value: 1.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 7 FRESVNRFGTYPALA---SKNGK----KWEilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWfITAVGAILAG 79
Cdd:PLN02430 48 FSKSVEKYPDNKMLGwrrIVDGKvgpyMWK--TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQW-IVAMEACAAH 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 80 GL-CVGIYATNSAEVCQYVITHAKVNILLVEnDQQLQKILSIPQSSLEPLKAIIQYRLPMKKNNN--------LYSWDDF 150
Cdd:PLN02430 125 SLiCVPLYDTLGPGAVDYIVDHAEIDFVFVQ-DKKIKELLEPDCKSAKRLKAIVSFTSVTEEESDkasqigvkTYSWIDF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 151 MELGRSIPdtqlEQVIESQKANQCAVLiYTSGTTGIPKGVMLSHDNITWIAGAV---TKDFKLTDKHETV-VSYLPLSHI 226
Cdd:PLN02430 204 LHMGKENP----SETNPPKPLDICTIM-YTSGTSGDPKGVVLTHEAVATFVRGVdlfMEQFEDKMTHDDVyLSFLPLAHI 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 227 AAQMMDIWVPIKIGALTYF-AQADALKgtlvSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFvwarNIGFK 305
Cdd:PLN02430 279 LDRMIEEYFFRKGASVGYYhGDLNALR----DDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIF----NALYK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 306 VNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFF-LSLDIPIGELYGLSESSGPHTISNQ 384
Cdd:PLN02430 351 YKLAWMNRGYSHKKASPMADFLAFRKVKAKLG-GRLRLLISGGAPLSTEIEEFLrVTSCAFVVQGYGLTETLGPTTLGFP 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 385 NNYRLLSCGKILTGCKNMLFQQ---------NKDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGF 455
Cdd:PLN02430 430 DEMCMLGTVGAPAVYNELRLEEvpemgydplGEPPRGEICVRGKCLFSGYYKNPELTEEVMKD-GWFHTGDIGEILPNGV 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 456 LYVTGHIKEILITAGGENVppiPVETL--VKKKIPIISNAMLVGDKLKflSMLLTLKCemnqmsgepldkLNFEAINFCR 533
Cdd:PLN02430 509 LKIIDRKKNLIKLSQGEYV---ALEYLenVYGQNPIVEDIWVYGDSFK--SMLVAVVV------------PNEENTNKWA 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 534 GLGSQASTVTEIVKQqdPLVYKAIQQGINAVnqEAMNNAQRIE--KWVILE-KDFSIYGGELGPMMKLKRHFVAQKYKKQ 610
Cdd:PLN02430 572 KDNGFTGSFEELCSL--PELKEHILSELKST--AEKNKLRGFEyiKGVILEtKPFDVERDLVTATLKKRRNNLLKYYQVE 647
|
....*
gi 1008909320 611 IDHMY 615
Cdd:PLN02430 648 IDEMY 652
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
29-603 |
3.10e-52 |
|
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: 186.41 E-value: 3.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 29 EILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLV 108
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 109 ENDqqlqkilsipqssleplkaiiqyrlpmkkNNNLyswddfmelgrsipdtqleqviesqkanqcAVLIYTSGTTGIPK 188
Cdd:cd17640 84 END-----------------------------SDDL------------------------------ATIIYTSGTTGNPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 189 GVMLSHDNITWIAGAVTkDFKLTDKHETVVSYLPLSHIAAQmmdiwvpikigALTYFAqadALKG---------TLVSTL 259
Cdd:cd17640 105 GVMLTHANLLHQIRSLS-DIVPPQPGDRFLSILPIWHSYER-----------SAEYFI---FACGcsqaytsirTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 260 KEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIG-FKVNskkmlgkyntpvsyrmaktlvfskvktslgl 338
Cdd:cd17640 170 KRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFLSGGiFKFG------------------------------- 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 339 dhchsfISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGI------G 412
Cdd:cd17640 219 ------ISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVlppgekG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 413 EICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVE-TLVKKkiPIIS 491
Cdd:cd17640 293 IVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEeALMRS--PFIE 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 492 NAMLVGDKLKFLSMLLTlkcemnqmsgePldklNFEAINfcRGLGSQASTVTEIVKQ--QDPLVYKAIQQGINAV--NQE 567
Cdd:cd17640 371 QIMVVGQDQKRLGALIV-----------P----NFEELE--KWAKESGVKLANDRSQllASKKVLKLYKNEIKDEisNRP 433
|
570 580 590
....*....|....*....|....*....|....*.
gi 1008909320 568 AMNNAQRIEKWVILEKDFsIYGGELGPMMKLKRHFV 603
Cdd:cd17640 434 GFKSFEQIAPFALLEEPF-IENGEMTQTMKIKRNVV 468
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
5-615 |
5.48e-52 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 189.85 E-value: 5.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 5 EFFRESVNRFGTYPALASK---NGK--KWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAG 79
Cdd:PLN02614 49 DVFRMSVEKYPNNPMLGRReivDGKpgKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 80 GLCVGIYATNSAEVCQYVITHAKVNILLVEnDQQLQKILSIPQSSLEPLKAIIQYR--LPMKKNNN------LYSWDDFM 151
Cdd:PLN02614 129 LYCVPLYDTLGAGAVEFIISHSEVSIVFVE-EKKISELFKTCPNSTEYMKTVVSFGgvSREQKEEAetfglvIYAWDEFL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 152 ELGRSipdTQLEQVIEsQKANQCAVLiYTSGTTGIPKGVMLSHDNITWIAGAVTKDFK-----LTDKhETVVSYLPLSHI 226
Cdd:PLN02614 208 KLGEG---KQYDLPIK-KKSDICTIM-YTSGTTGDPKGVMISNESIVTLIAGVIRLLKsanaaLTVK-DVYLSYLPLAHI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 227 AAQMMDIWVpIKIGALTYFAQADAlkGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKv 306
Cdd:PLN02614 282 FDRVIEECF-IQHGAAIGFWRGDV--KLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFG- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 307 NSKKmlGKYNTPVSYRMAKtLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLD-IPIGELYGLSESSGPHTISNQN 385
Cdd:PLN02614 358 NMKK--GQSHVEASPLCDK-LVFNKVKQGLG-GNVRIILSGAAPLASHVESFLRVVAcCHVLQGYGLTESCAGTFVSLPD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 386 NYRLLscGKILTGCKNM------LFQQNKDGI-----GEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLG 454
Cdd:PLN02614 434 ELDML--GTVGPPVPNVdirlesVPEMEYDALastprGEICIRGKTLFSGYYKREDLTKEVLID-GWLHTGDVGEWQPNG 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 455 FLYVTGHIKEILITAGGENVPPIPVETlVKKKIPIISNAMLVGDklKFLSMLLTLKCEMNQM----SGEPLDKLNFEAIn 530
Cdd:PLN02614 511 SMKIIDRKKNIFKLSQGEYVAVENIEN-IYGEVQAVDSVWVYGN--SFESFLVAIANPNQQIlerwAAENGVSGDYNAL- 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 531 fCRGLGSQASTVTEIVKQQDPLVYKAIQQgINAVNQEAMNnaqriekwVILEKDFsiyggeLGPMMKLKRHFVAQKYKKQ 610
Cdd:PLN02614 587 -CQNEKAKEFILGELVKMAKEKKMKGFEI-IKAIHLDPVP--------FDMERDL------LTPTFKKKRPQLLKYYQSV 650
|
....*
gi 1008909320 611 IDHMY 615
Cdd:PLN02614 651 IDEMY 655
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
5-615 |
1.26e-50 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 185.82 E-value: 1.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 5 EFFRESVNRF------GTYPALASKNGKK-WeiLNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWfITAVGAIL 77
Cdd:PLN02861 47 QFFSDAVKKYpnnqmlGRRQVTDSKVGPYvW--LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEW-IIAMEACN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 78 AGGLC-VGIYATNSAEVCQYVITHAKVNILLVEnDQQLQKILSIPQSSLEPLKAIIQY---RLPMKKNN-----NLYSWD 148
Cdd:PLN02861 124 SQGITyVPLYDTLGANAVEFIINHAEVSIAFVQ-ESKISSILSCLPKCSSNLKTIVSFgdvSSEQKEEAeelgvSCFSWE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 149 DFMELGRSipDTQLEQvieSQKANQCAVLiYTSGTTGIPKGVMLSHDNItwIAGAVTKD--FKLTDK----HETVVSYLP 222
Cdd:PLN02861 203 EFSLMGSL--DCELPP---KQKTDICTIM-YTSGTTGEPKGVILTNRAI--IAEVLSTDhlLKVTDRvateEDSYFSYLP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 223 LSHIAAQMMDIWVpIKIGALTYFAQADALkgTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNi 302
Cdd:PLN02861 275 LAHVYDQVIETYC-ISKGASIGFWQGDIR--YLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYN- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 303 gFKV-NSKKMLGKYNTpvSYRMAKtLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLDIP-IGELYGLSESSGPHT 380
Cdd:PLN02861 351 -YKLgNLRKGLKQEEA--SPRLDR-LVFDKIKEGLG-GRVRLLLSGAAPLPRHVEEFLRVTSCSvLSQGYGLTESCGGCF 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 381 ISNQNNYRLL-SCGKILTGCKNMLFQQNKDGI--------GEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLD 451
Cdd:PLN02861 426 TSIANVFSMVgTVGVPMTTIEARLESVPEMGYdalsdvprGEICLRGNTLFSGYHKRQDLTEEVLID-GWFHTGDIGEWQ 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 452 GLGFLYVTGHIKEILITAGGENVppiPVETL--VKKKIPIISNAMLVGDklKFLSMLLTLKCEMNQmSGEPLDKLNFEAI 529
Cdd:PLN02861 505 PNGAMKIIDRKKNIFKLSQGEYV---AVENLenTYSRCPLIASIWVYGN--SFESFLVAVVVPDRQ-ALEDWAANNNKTG 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 530 NF---CrglgsqastvteivkqQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKD-FSIYGGELGPMMKLKRHFVAQ 605
Cdd:PLN02861 579 DFkslC----------------KNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNpFDIERDLITPTFKLKRPQLLK 642
|
650
....*....|
gi 1008909320 606 KYKKQIDHMY 615
Cdd:PLN02861 643 YYKDCIDQLY 652
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
31-482 |
1.28e-49 |
|
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: 179.72 E-value: 1.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 31 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEN 110
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 111 DQqLQKILSIpQSSLEPLKAIIQYRLPMKKNNNLYSWDDFmELGRSIPDtQLEQVIESqkANQCAVLIYTSGTTGIPKGV 190
Cdd:cd05911 91 DG-LEKVKEA-AKELGPKDKIIVLDDKPDGVLSIEDLLSP-TLGEEDED-LPPPLKDG--KDDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 191 MLSHDNIT-WIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKiGALTY----FAQADALKgtlvsTLKEVKPT 265
Cdd:cd05911 165 CLSHRNLIaNLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIimpkFDSELFLD-----LIEKYKIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 266 VFIGVPQIwekiheMVkknsaksmglkkkafvwarnigfkvnskkMLGKYNTPVSYRMAktlvfskvktSLgldhcHSFI 345
Cdd:cd05911 239 FLYLVPPI------AA-----------------------------ALAKSPLLDKYDLS----------SL-----RVIL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 346 SGTAPLNQETAEFFLSLDIP--IGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLF------QQNKDGIGEICLW 417
Cdd:cd05911 269 SGGAPLSKELQELLAKRFPNatIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVdddgkdSLGPNEPGEICVR 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008909320 418 GRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETL 482
Cdd:cd05911 349 GPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKE-LIKYKGFQVAPAELEAV 412
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
173-485 |
2.61e-47 |
|
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: 169.39 E-value: 2.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 173 QCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAaQMMDIWVPIKIGA----LTYFAQA 248
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTE-GDVFLSTLPLFHIG-GLFGLLGALLAGGtvvlLPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 249 DALKgtlvsTLKEVKPTVFIGVPQIWEKIhemvkknsaksmglkkkafvwARNIGFKvnskkmlgkyntpvsyrmakTLV 328
Cdd:cd04433 79 AALE-----LIEREKVTILLGVPTLLARL---------------------LKAPESA--------------------GYD 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 329 FSKVKTslgldhchsFISGTAPLNQETAEFFLSL-DIPIGELYGLSESSGPHTISN--QNNYRLLSCGKILTGCKNMLFQ 405
Cdd:cd04433 113 LSSLRA---------LVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPpdDDARKPGSVGRPVPGVEVRIVD 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 406 QNKD-----GIGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 480
Cdd:cd04433 184 PDGGelppgEIGELVVRGPSVMKGYWNNP-EATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVE 261
|
....*
gi 1008909320 481 TLVKK 485
Cdd:cd04433 262 AVLLG 266
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1-480 |
9.29e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 163.82 E-value: 9.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 1 MTIPEFFRESVNRFGTYPALASkNGKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWF-----ITAVGA 75
Cdd:PRK06187 6 LTIGRILRHGARKHPDKEAVYF-DGRRT---TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLeayfaVPKIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 76 ILAgglcvgiyATN---SAEVCQYVITHAKVNILLVEND--QQLQKILSipqsSLEPLKAIIQYRLPMKKNNNLYsWDDF 150
Cdd:PRK06187 82 VLH--------PINirlKPEEIAYILNDAEDRVVLVDSEfvPLLAAILP----QLPTVRTVIVEGDGPAAPLAPE-VGEY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 151 MELGRSIPDTQLEQVIEsqkANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAqm 230
Cdd:PRK06187 149 EELLAAASDTFDFPDID---ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRD-DVYLVIVPMFHVHA-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 231 mdiW----VPIKIGA-LTYFAQADAlkGTLVSTLKEVKPTVFIGVPQIWEkihemvkknsaksmglkkkafvwarnigfk 305
Cdd:PRK06187 223 ---WglpyLALMAGAkQVIPRRFDP--ENLLDLIETERVTFFFAVPTIWQ------------------------------ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 306 vnskkMLGKYntPVSYRMAktlvFSKVKTslgldhchsFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSG------- 377
Cdd:PRK06187 268 -----MLLKA--PRAYFVD----FSSLRL---------VIYGGAALPPALLREFKEkFGIDLVQGYGMTETSPvvsvlpp 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 378 PHTISNQNNYRlLSCGKILTGCK------NMLFQQNKDG-IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQL 450
Cdd:PRK06187 328 EDQLPGQWTKR-RSAGRPLPGVEarivddDGDELPPDGGeVGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGDVGYI 405
|
490 500 510
....*....|....*....|....*....|
gi 1008909320 451 DGLGFLYVTGHIKEILITaGGENVPPIPVE 480
Cdd:PRK06187 406 DEDGYLYITDRIKDVIIS-GGENIYPRELE 434
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-480 |
1.11e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 163.54 E-value: 1.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 1 MTIPEFFRESVNRFGTYPALASKNGKkweiLNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGG 80
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAYVFGDQR----LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 81 LCVGIYATNSAEVCQYVITHAKVNILLVEnDQQLQKILSIPQS--SLEpLKAIIQYRLPMKKNNNLYSWDDFMELGrsip 158
Cdd:PRK07656 81 VVVPLNTRYTADEAAYILARGDAKALFVL-GLFLGVDYSATTRlpALE-HVVICETEEDDPHTEKMKTFTDFLAAG---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 159 dTQLEQVIEsQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIK 238
Cdd:PRK07656 155 -DPAERAPE-VDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEG-DRYLAANPFFHVFGYKAGVNAPLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 239 IGA----LTYFAQADALKgtlvsTLKEVKPTVFIGVPQIwekihemvkknsaksmglkkkafvwarnigfkvnskkmlgk 314
Cdd:PRK07656 232 RGAtilpLPVFDPDEVFR-----LIETERITVLPGPPTM----------------------------------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 315 YNTPVSYRMAKTLVFSkvktSLGLdhchsFISGTAPLNQETAEFFLS-LDIP-IGELYGLSESSGPHTISNQNNYRLLSC 392
Cdd:PRK07656 266 YNSLLQHPDRSAEDLS----SLRL-----AVTGAASMPVALLERFESeLGVDiVLTGYGLSEASGVTTFNRLDDDRKTVA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 393 GKILTGCKNM-------LFQQNKDG-IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKE 464
Cdd:PRK07656 337 GTIGTAIAGVenkivneLGEEVPVGeVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKD 416
|
490
....*....|....*.
gi 1008909320 465 ILITaGGENVPPIPVE 480
Cdd:PRK07656 417 MFIV-GGFNVYPAEVE 431
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
2-616 |
1.79e-43 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 165.68 E-value: 1.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 2 TIPEFFRESVNRFGTYPAL-----------ASKNGKKWEILNFNQY--------YEACRKAAKSLIKLGLERFHGVGILG 62
Cdd:PLN02387 59 TLAALFEQSCKKYSDKRLLgtrklisrefeTSSDGRKFEKLHLGEYewitygqvFERVCNFASGLVALGHNKEERVAIFA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 63 FNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENdQQLQKILSIpQSSLEPLKAII---------Q 133
Cdd:PLN02387 139 DTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS-KQLKKLIDI-SSQLETVKRVIymddegvdsD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 134 YRLPMKKNNNLYSWDDFMELGRSIP-DTQLEqviesqKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTD 212
Cdd:PLN02387 217 SSLSGSSNWTVSSFSEVEKLGKENPvDPDLP------SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 213 KHETVVSYLPLSHI---AAQ--MMDIWVPIKIG-ALTYFAQADALK-GTL--VSTLkevKPTVFIGVPQIWEKIHEMVKK 283
Cdd:PLN02387 291 KNDVYLAYLPLAHIlelAAEsvMAAVGAAIGYGsPLTLTDTSNKIKkGTKgdASAL---KPTLMTAVPAILDRVRDGVRK 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 284 NSAKSMGLKKKAF--VWARNIGFKVNS-------KKMLgkYNtpvsyrmakTLVFSKVKTSLGlDHCHSFISGTAPLNQE 354
Cdd:PLN02387 368 KVDAKGGLAKKLFdiAYKRRLAAIEGSwfgawglEKLL--WD---------ALVFKKIRAVLG-GRIRFMLSGGAPLSGD 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 355 TAEFF-LSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGI---------GEICLWGRHIFMG 424
Cdd:PLN02387 436 TQRFInICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYlisdkpmprGEIVIGGPSVTLG 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 425 YLESETETTEA--IDDEG--WLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISNAMLVGDkl 500
Cdd:PLN02387 516 YFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVS-PYVDNIMVHAD-- 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 501 KFLSMLLTLKCEMNQMSGEPLDKLNFEAINFCRgLGSQASTVTEivkqqdplvykaIQQGINAVNQEAmnnaqRIEKWVI 580
Cdd:PLN02387 593 PFHSYCVALVVPSQQALEKWAKKAGIDYSNFAE-LCEKEEAVKE------------VQQSLSKAAKAA-----RLEKFEI 654
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1008909320 581 ------LEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMYH 616
Cdd:PLN02387 655 pakiklLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
3-480 |
5.44e-41 |
|
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: 155.03 E-value: 5.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 3 IPEFFRESVNRFGTYPALAskNGKKWeiLNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLC 82
Cdd:cd05936 1 LADLLEEAARRFPDKTALI--FMGRK--LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 83 VgiyatnsaevcqyvithaKVNILLVEndQQLQKILSIPQSsleplKAIIQYRlpmkknnnlyswdDFMELGRSIPDTQL 162
Cdd:cd05936 77 V------------------PLNPLYTP--RELEHILNDSGA-----KALIVAV-------------SFTDLLAAGAPLGE 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 163 EQVIesqKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFK-LTDKHETVVSYLPLSHIAAQMMDIWVPIKIGA 241
Cdd:cd05936 119 RVAL---TPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEdLLEGDDVVLAALPLFHVFGLTVALLLPLALGA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 242 ----LTYFAQADALKgtlvsTLKEVKPTVFIGVPQIWEKIhemvkknsaksMGLKKKAFVWarnigfkvnskkmlgkynt 317
Cdd:cd05936 196 tivlIPRFRPIGVLK-----EIRKHRVTIFPGVPTMYIAL-----------LNAPEFKKRD------------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 318 pvsyrmaktlvFSKVKTSlgldhchsfISGTAPLNQETAEFFLSL-DIPIGELYGLSESSgPHTISNQ--NNYRLLSCGK 394
Cdd:cd05936 241 -----------FSSLRLC---------ISGGAPLPVEVAERFEELtGVPIVEGYGLTETS-PVVAVNPldGPRKPGSIGI 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 395 ILTGCKNMLFqqNKDG-------IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILI 467
Cdd:cd05936 300 PLPGTEVKIV--DDDGeelppgeVGELWVRGPQVMKGYWNRPEETAEAFVD-GWLRTGDIGYMDEDGYFFIVDRKKDMII 376
|
490
....*....|...
gi 1008909320 468 tAGGENVPPIPVE 480
Cdd:cd05936 377 -VGGFNVYPREVE 388
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
31-482 |
6.06e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 146.66 E-value: 6.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 31 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVI--THAKVnilLV 108
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALreTECKA---IV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 109 ENDQQLQKILSIPQSSLEPlKAIIQY--RLPM---KKNNNLYSWDDFMELGRSIPDTQLEQVIESqkANQCAVLIYTSGT 183
Cdd:PTZ00216 199 CNGKNVPNLLRLMKSGGMP-NTTIIYldSLPAsvdTEGCRLVAWTDVVAKGHSAGSHHPLNIPEN--NDDLALIMYTSGT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 184 TGIPKGVMLSHDNITwiAGAVTKDFKLTD------KHETVVSYLPLSHIaaqmMDIWVP---IKIGALTYFAQADalkgT 254
Cdd:PTZ00216 276 TGDPKGVMHTHGSLT--AGILALEDRLNDligppeEDETYCSYLPLAHI----MEFGVTnifLARGALIGFGSPR----T 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 255 LVST-------LKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWArnigFKVNSKKMLGKYNTPvsYRMAKtl 327
Cdd:PTZ00216 346 LTDTfarphgdLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHA----YQSRLRALKEGKDTP--YWNEK-- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 328 VFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQN 407
Cdd:PTZ00216 418 VFSAPRAVLG-GRVRAMLSGGGPLSAATQEFVNVVFGMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTE 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 408 K-------DGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENvppIPVE 480
Cdd:PTZ00216 497 EykhtdtpEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEY---IALE 573
|
..
gi 1008909320 481 TL 482
Cdd:PTZ00216 574 AL 575
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1-480 |
1.77e-33 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 134.94 E-value: 1.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 1 MTIPEFFRESVNRFGTYPALASKN-GKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEW----FITA-VG 74
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRDqGLRW---TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWvltqFATAkIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 75 AILagglcVGI----------YATNSAEvCQYVIT---------HAKVNILLVENDQQLQKILsipQSSLEP-LKAIIqy 134
Cdd:PRK08315 93 AIL-----VTInpayrlseleYALNQSG-CKALIAadgfkdsdyVAMLYELAPELATCEPGQL---QSARLPeLRRVI-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 135 RLPMKKNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNIT----WIAGAVtkdfKL 210
Cdd:PRK08315 162 FLGDEKHPGMLNFDELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILnngyFIGEAM----KL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 211 TDKhETVVSYLPLSHIAAQMMDIWVPIKIGA-LTYFAQA-DALKgTLVSTLKEvKPTVFIGVPQ--IWEKIHEMVKKnsa 286
Cdd:PRK08315 238 TEE-DRLCIPVPLYHCFGMVLGNLACVTHGAtMVYPGEGfDPLA-TLAAVEEE-RCTALYGVPTmfIAELDHPDFAR--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 287 ksmglkkkafvwarnigFKVNSKK---MLGKyNTPVSyrmaktlVFSKVKTSLGLDhchsfisgtaplnqetaefflslD 363
Cdd:PRK08315 312 -----------------FDLSSLRtgiMAGS-PCPIE-------VMKRVIDKMHMS-----------------------E 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 364 IPIGelYGLSESSGPHTISNQNN---YRLLSCGKIL-----------TGCKNMLFQQnkdgiGEICLWGRHIFMGYLESE 429
Cdd:PRK08315 344 VTIA--YGMTETSPVSTQTRTDDpleKRVTTVGRALphlevkivdpeTGETVPRGEQ-----GELCTRGYSVMKGYWNDP 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1008909320 430 TETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 480
Cdd:PRK08315 417 EKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIR-GGENIYPREIE 466
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
175-480 |
2.00e-33 |
|
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: 132.73 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSyLPLSHIAAQMMDIWVPIKIGALTYFAQA-DAlkG 253
Cdd:cd17631 101 ALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVV-APLFHIGGLGVFTLPTLLRGGTVVILRKfDP--E 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 254 TLVSTLKEVKPTVFIGVPQIWEKihemvkknsaksmglkkkafvwarnigfkvnskkMLgkyNTPVsyrmAKTLVFSKVK 333
Cdd:cd17631 178 TVLDLIERHRVTSFFLVPTMIQA----------------------------------LL---QHPR----FATTDLSSLR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 334 TslgldhchsFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTI--SNQNNYRLLSCGKILTGCKNMLFQQNKD-- 409
Cdd:cd17631 217 A---------VIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFlsPEDHRRKLGSAGRPVFFVEVRIVDPDGRev 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1008909320 410 ---GIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 480
Cdd:cd17631 288 ppgEVGEIVVRGPHVMAGYWNRPEATAAAFRD-GWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVE 359
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
2-480 |
2.12e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 134.90 E-value: 2.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 2 TIPEFFRESVNRFGTYPALASKN-GKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGG 80
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVRHqALRY---TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 81 LCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKILSIPQSSLEPLK-----AIIQYRLPMKKN---------NNLYS 146
Cdd:PRK12583 96 ILVNINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELLPGLAegqpgALACERLPELRGvvslapappPGFLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 147 WDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHI 226
Cdd:PRK12583 176 WHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTE-HDRLCVPVPLYHC 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 227 AAQMMDIWVPIKIGA-LTYFAQA-DALkGTLvSTLKEVKPTVFIGVPQIWekIHEMvkknsaksmglkkkafvwarnigf 304
Cdd:PRK12583 255 FGMVLANLGCMTVGAcLVYPNEAfDPL-ATL-QAVEEERCTALYGVPTMF--IAEL------------------------ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 305 kvnSKKMLGKYNtpvsyrmaktlvFSKVKTSlgldhchsfISGTAPLNQET-----AEFFLSlDIPIGelYGLSESSGPH 379
Cdd:PRK12583 307 ---DHPQRGNFD------------LSSLRTG---------IMAGAPCPIEVmrrvmDEMHMA-EVQIA--YGMTETSPVS 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 380 TISNQNN---YRLLSCGKILTGCKNMLFQQN-----KDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLD 451
Cdd:PRK12583 360 LQTTAADdleRRVETVGRTQPHLEVKVVDPDgatvpRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMD 439
|
490 500
....*....|....*....|....*....
gi 1008909320 452 GLGFLYVTGHIKEILITaGGENVPPIPVE 480
Cdd:PRK12583 440 EQGYVRIVGRSKDMIIR-GGENIYPREIE 467
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
18-480 |
6.20e-29 |
|
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: 120.49 E-value: 6.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 18 PALASKNGKKWeiLNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYV 97
Cdd:cd05926 4 PALVVPGSTPA--LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 98 ITHAKVNILLVENDqqlqkilsipqSSLEPLKAIIQYRLPMKknnNLYsWDDFM--------ELGRSIPDTQLEQVIESQ 169
Cdd:cd05926 82 LADLGSKLVLTPKG-----------ELGPASRAASKLGLAIL---ELA-LDVGVlirapsaeSLSNLLADKKNAKSEGVP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 170 KANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVsYLPLSHIAAQMM----------DIWVPIKI 239
Cdd:cd05926 147 LPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLV-VMPLFHVHGLVAsllstlaaggSVVLPPRF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 240 GALTYFAQadalkgtlvstLKEVKPTVFIGVPQIwekiHEMVKKNSAKSmglkkkafvwarnigfkvnskkmlgKYNTPV 319
Cdd:cd05926 226 SASTFWPD-----------VRDYNATWYTAVPTI----HQILLNRPEPN-------------------------PESPPP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 320 SYRmaktlvfskvktslgldhchsFI-SGTAPLNQETAEFF-LSLDIPIGELYGLSESSGPHTiSNQ---NNYRLLSCGK 394
Cdd:cd05926 266 KLR---------------------FIrSCSASLPPAVLEALeATFGAPVLEAYGMTEAAHQMT-SNPlppGPRKPGSVGK 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 395 IlTGCKNMLFQQN----KDG-IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITA 469
Cdd:cd05926 324 P-VGVEVRILDEDgeilPPGvVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKEL-INR 401
|
490
....*....|.
gi 1008909320 470 GGENVPPIPVE 480
Cdd:cd05926 402 GGEKISPLEVD 412
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
2-483 |
8.14e-28 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 118.06 E-value: 8.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 2 TIPEFFRESVNRFGTYPALASkNGKKWEILNFNQYYEacRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGL 81
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHS-FGKTITYREADQLVE--QFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 82 CVGIYATNSAEVCQYVITHAKVNILLVEND-----QQ--------------LQKILSIPQSSLepLKAIIQY---RLPMK 139
Cdd:PRK08751 103 VVNVNPLYTPRELKHQLIDSGASVLVVIDNfgttvQQviadtpvkqvittgLGDMLGFPKAAL--VNFVVKYvkkLVPEY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 140 KNNNLYSWDDFMELGR--SIPDTQLEqviesqkANQCAVLIYTSGTTGIPKGVMLSHDNIT--------WIAGAvtkdFK 209
Cdd:PRK08751 181 RINGAIRFREALALGRkhSMPTLQIE-------PDDIAFLQYTGGTTGVAKGAMLTHRNLVanmqqahqWLAGT----GK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 210 LTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIhemvkknsaksm 289
Cdd:PRK08751 250 LEEGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGL------------ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 290 glkkkafvwarnigfkvnskkmlgkYNTPvsyrMAKTLVFSKVKTSLGldhchsfisGTAPLNQETAEFFLSLD-IPIGE 368
Cdd:PRK08751 318 -------------------------LNTP----GFDQIDFSSLKMTLG---------GGMAVQRSVAERWKQVTgLTLVE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 369 LYGLSESS-----GPHTISNQNNYRLL------SCGKILTGCKNMLFQqnkdgIGEICLWGRHIFMGYLESETETTEAID 437
Cdd:PRK08751 360 AYGLTETSpaaciNPLTLKEYNGSIGLpipstdACIKDDAGTVLAIGE-----IGELCIKGPQVMKGYWKRPEETAKVMD 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1008909320 438 DEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGeNVPPIPVETLV 483
Cdd:PRK08751 435 ADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGF-NVYPNEIEDVI 479
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
29-497 |
1.33e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 116.88 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 29 EILNFNQYYEACRKAAKSLI-KLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILL 107
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 108 VENDQQ-----LQKILSI-PQSSLEPLKAIIQYRLpmkknnnlyswDDFMELGRSIPdtqleqviesqkanqcAVLIYTS 181
Cdd:PRK06839 106 VEKTFQnmalsMQKVSYVqRVISITSLKEIEDRKI-----------DNFVEKNESAS----------------FIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 182 GTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIaaqmmdiwvpikiGALTYFAQADALKGTLV----- 256
Cdd:PRK06839 159 GTTGKPKGAVLTQENMFWNALNNTFAIDLT-MHDRSIVLLPLFHI-------------GGIGLFAFPTLFAGGVIivprk 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 257 -------STLKEVKPTVFIGVPQIWEKIHEMVKKnsaksmglkkkafvwarnigfkvnskkmlgkyntpvsyrmaktlvf 329
Cdd:PRK06839 225 feptkalSMIEKHKVTVVMGVPTIHQALINCSKF---------------------------------------------- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 330 skVKTSLglDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYR--LLSCGKILTGCKNMLFQQN 407
Cdd:PRK06839 259 --ETTNL--QSVRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARrkVGSIGKPVLFCDYELIDEN 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 408 KD-----GIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETL 482
Cdd:PRK06839 335 KNkvevgEVGELLIRGPNVMKEYWNRPDATEETIQD-GWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYPLEVEQV 412
|
490
....*....|....*
gi 1008909320 483 VkKKIPIISNAMLVG 497
Cdd:PRK06839 413 I-NKLSDVYEVAVVG 426
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
175-482 |
5.37e-26 |
|
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: 111.94 E-value: 5.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVV-SYLPLSHIAAqmmdiwvpikigaLTYFAQAD-ALK 252
Cdd:cd05904 161 AALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDVFlCVLPMFHIYG-------------LSSFALGLlRLG 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 253 GTLVStlkevkptvfigvpqiwekiheMVKKNSAKSMGLKKKafvwarnigFKVNSkkmlgkynTPVSYRMAKTLVFSKV 332
Cdd:cd05904 228 ATVVV----------------------MPRFDLEELLAAIER---------YKVTH--------LPVVPPIVLALVKSPI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 333 KTSLGLDHCHSFISGTAPLNQETAEFFLSL--DIPIGELYGLSESSGP-HTISN--QNNYRLLSCGKILTGCKNMLFQQN 407
Cdd:cd05904 269 VDKYDLSSLRQIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVvAMCFApeKDRAKYGSVGRLVPNVEAKIVDPE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 408 KDGI------GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVET 481
Cdd:cd05904 349 TGESlppnqtGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKE-LIKYKGFQVAPAELEA 427
|
.
gi 1008909320 482 L 482
Cdd:cd05904 428 L 428
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
152-497 |
6.67e-26 |
|
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: 110.84 E-value: 6.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 152 ELGRSIPDTQLEQVI---ESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIAA 228
Cdd:cd05941 66 PLNPSYPLAELEYVItdsEPSLVLDPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWT-EDDVLLHVLPLHHVHG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 229 QMMDIWVPIKIGA----LTYFaqaDAlkgTLVSTLKEVKP-TVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFvwarnig 303
Cdd:cd05941 145 LVNALLCPLFAGAsvefLPKF---DP---KEVAISRLMPSiTVFMGVPTIYTRLLQYYEAHFTDPQFARAAAA------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 304 fkvnsKKMlgkyntpvsyRMaktlvfskvktslgldhchsFISGTAPLNQETAEFFLSLD-IPIGELYGLSESSgpHTIS 382
Cdd:cd05941 212 -----ERL----------RL--------------------MVSGSAALPVPTLEEWEAITgHTLLERYGMTEIG--MALS 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 383 N--QNNYRLLSCGKILTGCKNMLFQQN------KDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLG 454
Cdd:cd05941 255 NplDGERRPGTVGMPLPGVQARIVDEEtgeplpRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDG 334
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1008909320 455 FLYVTGHIKEILITAGGENVPPIPVETLVkKKIPIISNAMLVG 497
Cdd:cd05941 335 YYWILGRSSVDIIKSGGYKVSALEIERVL-LAHPGVSECAVIG 376
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
33-480 |
8.35e-26 |
|
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: 110.46 E-value: 8.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 33 FNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVendq 112
Cdd:cd05934 6 YAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 113 qlqkilsipqssleplkaiiqyrlpmkknnnlyswDDFMelgrsipdtqleqviesqkanqcavLIYTSGTTGIPKGVML 192
Cdd:cd05934 82 -----------------------------------DPAS-------------------------ILYTSGTTGPPKGVVI 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 193 SHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGAltyfaqadalkgTLVsTLKEVKPTVFIGVpq 272
Cdd:cd05934 102 THANLTFAGYYSARRFGLGED-DVYLTVLPLFHINAQAVSVLAALSVGA------------TLV-LLPRFSASRFWSD-- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 273 iwekihemVKKNSAksmglkkkafVWARNIGfkvnskKMLGK-YNTPVSYRMAktlvfskvktslglDHCHSFISGTAPL 351
Cdd:cd05934 166 --------VRRYGA----------TVTNYLG------AMLSYlLAQPPSPDDR--------------AHRLRAAYGAPNP 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 352 NQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLF----QQNKDG-IGEICL-----WGrhI 421
Cdd:cd05934 208 PELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVdddgQELPAGePGELVIrglrgWG--F 285
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1008909320 422 FMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 480
Cdd:cd05934 286 FKGYYNMPEATAEAMRN-GWFHTGDLGYRDADGFFYFVDRKKD-MIRRRGENISSAEVE 342
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
2-480 |
3.14e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 109.64 E-value: 3.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 2 TIPEFFRESVNRFGTYPALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGL 81
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGD----RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 82 CVGI-YATNSAEVCqYVITHAKVNILLVEND--QQLQKILSIPQSSLEPLKAIIQYRLPMKknnnlySWDDFMELGRSIP 158
Cdd:PRK08316 88 HVPVnFMLTGEELA-YILDHSGARAFLVDPAlaPTAEAALALLPVDTLILSLVLGGREAPG------GWLDFADWAEAGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 159 DTQLEQVIESqkaNQCAVLIYTSGTTGIPKGVMLSHDNITW------IAGAVTKDfkltdkhETVVSYLPLSHiAAQMMD 232
Cdd:PRK08316 161 VAEPDVELAD---DDLAQILYTSGTESLPKGAMLTHRALIAeyvsciVAGDMSAD-------DIPLHALPLYH-CAQLDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 233 IWVP-IKIGALTYFAQADALkGTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksMGLkkkafvwARNIGFKVNSKKM 311
Cdd:PRK08316 230 FLGPyLYVGATNVILDAPDP-ELILRTIEAERITSFFAPPTVW--------------ISL-------LRHPDFDTRDLSS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 312 LGK--YNT-----PVSYRMAKTLvfskvkTSLGLDHChsfisgtaplnqetaefflsldipigelYGLSESSGPHTISNQ 384
Cdd:PRK08316 288 LRKgyYGAsimpvEVLKELRERL------PGLRFYNC----------------------------YGQTEIAPLATVLGP 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 385 NNY--RLLSCGkiltgcKNMLFQQNK----DG-------IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLD 451
Cdd:PRK08316 334 EEHlrRPGSAG------RPVLNVETRvvddDGndvapgeVGEIVHRSPQLMLGYWDDPEKTAEAFRG-GWFHSGDLGVMD 406
|
490 500
....*....|....*....|....*....
gi 1008909320 452 GLGFLYVTGHIKEILITaGGENVPPIPVE 480
Cdd:PRK08316 407 EEGYITVVDRKKDMIKT-GGENVASREVE 434
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
32-480 |
4.43e-25 |
|
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: 109.26 E-value: 4.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 32 NFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEND 111
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 112 qqLQKILSIPQSSLEPLKAIIQY----RLPMKKNNNLYSWDDFmeLGRSIPDTQLEQVIEsqkaNQCAVLIYTSGTTGIP 187
Cdd:cd12119 107 --FLPLLEAIAPRLPTVEHVVVMtddaAMPEPAGVGVLAYEEL--LAAESPEYDWPDFDE----NTAAAICYTSGTTGNP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 188 KGVMLSHDNITWIA-GAVTKDFKLTDKHETVVSYLPLSHIAAqmmdiW-VPIK---IGALTYFAQADALKGTLVSTLKEV 262
Cdd:cd12119 179 KGVVYSHRSLVLHAmAALLTDGLGLSESDVVLPVVPMFHVNA-----WgLPYAaamVGAKLVLPGPYLDPASLAELIERE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 263 KPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKkafvwarnigfkvnskkmlgkyntpvsyrmaktlvfskvktslgldhch 342
Cdd:cd12119 254 GVTFAAGVPTVWQGLLDHLEANGRDLSSLRR------------------------------------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 343 sFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTIS------------NQNNYRllscgkILTGCKNMLFQ---QN 407
Cdd:cd12119 285 -VVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSPLGTVArppsehsnlsedEQLALR------AKQGRPVPGVElriVD 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 408 KDG---------IGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIP 478
Cdd:cd12119 358 DDGrelpwdgkaVGELQVRGPWVTKSYYKND-EESEALTEDGWLRTGDVATIDEDGYLTITDRSKD-VIKSGGEWISSVE 435
|
..
gi 1008909320 479 VE 480
Cdd:cd12119 436 LE 437
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1-497 |
4.08e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 106.62 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 1 MTIPEFFRESVNRFGTYPALaskngkkwEILNFNQYY----EACRKAAKSLIKLGLERFHGVGILGFNSAEwFITAVGAI 76
Cdd:PRK05605 32 TTLVDLYDNAVARFGDRPAL--------DFFGATTTYaelgKQVRRAAAGLRALGVRPGDRVAIVLPNCPQ-HIVAFYAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 77 LAGGLCV-------------GIYATNSAEVcqyVITHAKVNILLVE--NDQQLQKILSIPQSSLEPLKAIIQYRLPMKK- 140
Cdd:PRK05605 103 LRLGAVVvehnplytaheleHPFEDHGARV---AIVWDKVAPTVERlrRTTPLETIVSVNMIAAMPLLQRLALRLPIPAl 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 141 ----------NNNLYSWDDFMElGRSIPDTQLEQVIESQKANQcAVLIYTSGTTGIPKGVMLSHDNI--------TWIAG 202
Cdd:PRK05605 180 rkaraaltgpAPGTVPWETLVD-AAIGGDGSDVSHPRPTPDDV-ALILYTSGTTGKPKGAQLTHRNLfanaaqgkAWVPG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 203 avtkdfkLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGA-LTYFAQADAlkGTLVSTLKEVKPTVFIGVPQIWEKIHEMV 281
Cdd:PRK05605 258 -------LGDGPERVLAALPMFHAYGLTLCLTLAVSIGGeLVLLPAPDI--DLILDAMKKHPPTWLPGVPPLYEKIAEAA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 282 KKnsaksmglkkkafvwaRNIGFKvnskkmlgkyntpvSYRMAktlvfskvktslgldhchsfISGTAPLNQETAEFFLS 361
Cdd:PRK05605 329 EE----------------RGVDLS--------------GVRNA--------------------FSGAMALPVSTVELWEK 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 362 LdipIG----ELYGLSESSgPHTISN--QNNYRLLSCG------KILTGCKNMLFQQNKDG-IGEICLWGRHIFMGYLES 428
Cdd:PRK05605 359 L---TGgllvEGYGLTETS-PIIVGNpmSDDRRPGYVGvpfpdtEVRIVDPEDPDETMPDGeEGELLVRGPQVFKGYWNR 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1008909320 429 ETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETlVKKKIPIISNAMLVG 497
Cdd:PRK05605 435 PEETAKSFLD-GWFRTGDVVVMEEDGFIRIVDRIKELIIT-GGFNVYPAEVEE-VLREHPGVEDAAVVG 500
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1-483 |
1.90e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 104.68 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 1 MTIPEFFRESVNRFGTYPALA-SKNGKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAG 79
Cdd:PLN02330 28 LTLPDFVLQDAELYADKVAFVeAVTGKAV---TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 80 GLCVGIYATN-SAEVCQYVitHAKVNILLVENDQQLQKILSIPqsslepLKAIIqyrLPMKKNNNLYSWDDFMELGRSIP 158
Cdd:PLN02330 105 GVFSGANPTAlESEIKKQA--EAAGAKLIVTNDTNYGKVKGLG------LPVIV---LGEEKIEGAVNWKELLEAADRAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 159 DTQLEQVIesQKANQCAvLIYTSGTTGIPKGVMLSHDNItwIAGAVTKDFKLTDK---HETVVSYLPLSHIAaqmmdiwv 235
Cdd:PLN02330 174 DTSDNEEI--LQTDLCA-LPFSSGTTGISKGVMLTHRNL--VANLCSSLFSVGPEmigQVVTLGLIPFFHIY-------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 236 pikigaltyfaqadALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVkknsaksmglkkkafvwARNIGFkvnskkmlgky 315
Cdd:PLN02330 241 --------------GITGICCATLRNKGKVVVMSRFELRTFLNALI-----------------TQEVSF----------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 316 nTPVSYRMAKTLVFSKVKTSLGLD--HCHSFISGTAPLNQETAEFFLSL--DIPIGELYGLSESS-------GP---HTI 381
Cdd:PLN02330 279 -APIVPPIILNLVKNPIVEEFDLSklKLQAIMTAAAPLAPELLTAFEAKfpGVQVQEAYGLTEHScitlthgDPekgHGI 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 382 SNQNnyrllSCGKILTGCKNMLFQQN------KDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGF 455
Cdd:PLN02330 358 AKKN-----SVGFILPNLEVKFIDPDtgrslpKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGD 432
|
490 500
....*....|....*....|....*...
gi 1008909320 456 LYVTGHIKEiLITAGGENVPPIPVETLV 483
Cdd:PLN02330 433 IFIVDRIKE-LIKYKGFQVAPAELEAIL 459
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
153-497 |
2.05e-23 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 104.44 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 153 LGRSIPDTQLEQVIESQK---------ANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPL 223
Cdd:PRK06087 159 LAPATSSLSLSQIIADYEplttaitthGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT-WQDVFMMPAPL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 224 SHIAAQMMDIWVPIKIGALTYFAQadalkgtlvstlkEVKPTVFIGVpqiwekihemvkknsaksmgLKKKAFVWarnig 303
Cdd:PRK06087 238 GHATGFLHGVTAPFLIGARSVLLD-------------IFTPDACLAL--------------------LEQQRCTC----- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 304 fkvnskkMLGKynTPVSYRMAKTLVFSKVK-TSLGLdhchsFISGTAPLNQETAEFFLSLDIPIGELYGLSESSgPHTIS 382
Cdd:PRK06087 280 -------MLGA--TPFIYDLLNLLEKQPADlSALRF-----FLCGGTTIPKKVARECQQRGIKLLSVYGSTESS-PHAVV 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 383 NQNN---YRLLSCGKILTGCKNMLFQQNKDGI-----GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLG 454
Cdd:PRK06087 345 NLDDplsRFMHTDGYAAAGVEIKVVDEARKTLppgceGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAG 424
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1008909320 455 FLYVTGHIKEILITaGGENVPPIPVETLVKKKiPIISNAMLVG 497
Cdd:PRK06087 425 YIKITGRKKDIIVR-GGENISSREVEDILLQH-PKIHDACVVA 465
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
175-497 |
2.53e-23 |
|
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: 102.81 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAqmmdiwVPIKIGALTYfaqadALKGT 254
Cdd:cd05912 80 ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTED-DNWLCALPLFHISG------LSILMRSVIY-----GMTVY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 255 LVSTLKEvkptvfigvpqiwEKIHEMVKKNSAKSMGLKKKAFVWarnigfkvnskkMLGKYNTPVSYRMAKTLVfskvkt 334
Cdd:cd05912 148 LVDKFDA-------------EQVLHLINSGKVTIISVVPTMLQR------------LLEILGEGYPNNLRCILL------ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 335 slgldhchsfisGTAPLNQETAEFFLSLDIPIGELYGLSE-SSGPHTISNQNNY-RLLSCGKILTGCKNMLFQ--QNKDG 410
Cdd:cd05912 197 ------------GGGPAPKPLLEQCKEKGIPVYQSYGMTEtCSQIVTLSPEDALnKIGSAGKPLFPVELKIEDdgQPPYE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 411 IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVkKKIPII 490
Cdd:cd05912 265 VGEILLKGPNVTKGYLNRPDATEESFEN-GWFKTGDIGYLDEEGFLYVLDRRSD-LIISGGENIYPAEIEEVL-LSHPAI 341
|
....*..
gi 1008909320 491 SNAMLVG 497
Cdd:cd05912 342 KEAGVVG 348
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
31-483 |
2.61e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 104.34 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 31 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILL--- 107
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcld 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 108 --------VENDQQLQKILSIPQSSLEPLKAIIQYRLPMKKNNNL---YSWDDFMELGRSIP---DTQLEQVIESQkaNQ 173
Cdd:PRK06710 130 lvfprvtnVQSATKIEHVIVTRIADFLPFPKNLLYPFVQKKQSNLvvkVSESETIHLWNSVEkevNTGVEVPCDPE--ND 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 174 CAVLIYTSGTTGIPKGVMLSHDN--------ITWIagavtkdFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYF 245
Cdd:PRK06710 208 LALLQYTGGTTGFPKGVMLTHKNlvsntlmgVQWL-------YNCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 246 AQADALKgTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksmglkkkafvwarnigfkvnskkmLGKYNTPvsyrMAK 325
Cdd:PRK06710 281 IPKFDMK-MVFEAIKKHKVTLFPGAPTIY-------------------------------------IALLNSP----LLK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 326 TLVFSKVKTSlgldhchsfISGTAPLNQETAEFFLSldIPIGEL---YGLSESSgPHTISN----------------QNN 386
Cdd:PRK06710 319 EYDISSIRAC---------ISGSAPLPVEVQEKFET--VTGGKLvegYGLTESS-PVTHSNflwekrvpgsigvpwpDTE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 387 YRLLS--CGKILTGCKnmlfqqnkdgIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKE 464
Cdd:PRK06710 387 AMIMSleTGEALPPGE----------IGEIVVKGPQIMKGYWNKPEETAAVLQD-GWLHTGDVGYMDEDGFFYVKDRKKD 455
|
490
....*....|....*....
gi 1008909320 465 iLITAGGENVPPIPVETLV 483
Cdd:PRK06710 456 -MIVASGFNVYPREVEEVL 473
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
33-497 |
3.96e-23 |
|
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: 103.38 E-value: 3.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 33 FNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGglcVGIYATNSAEVCQYVItHAkVNI----LLV 108
Cdd:cd17642 47 YAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIG---VGVAPTNDIYNERELD-HS-LNIskptIVF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 109 ENDQQLQKILSIpQSSLEPLKAIIQYrlpmkknNNLYSWDDFMEL----GRSIPDTQLEQVIESQKAN---QCAVLIYTS 181
Cdd:cd17642 122 CSKKGLQKVLNV-QKKLKIIKTIIIL-------DSKEDYKGYQCLytfiTQNLPPGFNEYDFKPPSFDrdeQVALIMNSS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 182 GTTGIPKGVMLSHDNI-TWIAGAVTKDFKLTDKHET-VVSYLPLSHiAAQMMDIWVPIKIGA----LTYFAQAdalkgTL 255
Cdd:cd17642 194 GSTGLPKGVQLTHKNIvARFSHARDPIFGNQIIPDTaILTVIPFHH-GFGMFTTLGYLICGFrvvlMYKFEEE-----LF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 256 VSTLKEVKPTVFIGVPQIWekihemvkknsaksmglkkkAFVwarnigfkvNSKKMLGKYNtpvsyrmaktlvfskvkts 335
Cdd:cd17642 268 LRSLQDYKVQSALLVPTLF--------------------AFF---------AKSTLVDKYD------------------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 336 lgLDHCHSFISGTAPLNQETAEFFLS-LDIP-IGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGI-- 411
Cdd:cd17642 300 --LSNLHEIASGGAPLSKEVGEAVAKrFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTlg 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 412 ----GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKi 487
Cdd:cd17642 378 pnerGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKS-LIKYKGYQVPPAELESILLQH- 455
|
490
....*....|
gi 1008909320 488 PIISNAMLVG 497
Cdd:cd17642 456 PKIFDAGVAG 465
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
35-497 |
1.30e-21 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 98.53 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 35 QYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVenDQQL 114
Cdd:cd12118 34 QTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFV--DREF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 115 QkilsipqssleplkaiiqyrlpmkknnnlysWDDFMELGRSIPDtqleqVIESQKANQCAVLIYTSGTTGIPKGVMLSH 194
Cdd:cd12118 112 E-------------------------------YEDLLAEGDPDFE-----WIPPADEWDPIALNYTSGTTGRPKGVVYHH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 195 DNITWIAGAVTKDFKLtdKHETVvsYL---PLSHiAAQMMDIWVPIKIGaltyfaqadalkGTLVsTLKEVKPtvfigvP 271
Cdd:cd12118 156 RGAYLNALANILEWEM--KQHPV--YLwtlPMFH-CNGWCFPWTVAAVG------------GTNV-CLRKVDA------K 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 272 QIWEKIHE----------MVKKNSAKSMGLKKKAFVWARNIgfkvnskkMLGKYNTPVSyrmaktlVFSKVkTSLGLDHC 341
Cdd:cd12118 212 AIYDLIEKhkvthfcgapTVLNMLANAPPSDARPLPHRVHV--------MTAGAPPPAA-------VLAKM-EELGFDVT 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 342 HSfisgtaplnqetaefflsldipigelYGLSESSGPHTI----------SNQNNYRLlscgKILTGCKNMLFQQ----- 406
Cdd:cd12118 276 HV--------------------------YGLTETYGPATVcawkpewdelPTEERARL----KARQGVRYVGLEEvdvld 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 407 -------NKDG--IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPI 477
Cdd:cd12118 326 petmkpvPRDGktIGEIVFRGNIVMKGYLKNPEATAEAFRG-GWFHSGDLAVIHPDGYIEIKDRSKDIIIS-GGENISSV 403
|
490 500
....*....|....*....|
gi 1008909320 478 PVETlVKKKIPIISNAMLVG 497
Cdd:cd12118 404 EVEG-VLYKHPAVLEAAVVA 422
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
175-480 |
1.88e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 96.40 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIA--GAVTKDFKLTDkheTVVSYLPLSHIAAQMMDIWVPIKIGALTYFA-----Q 247
Cdd:cd05944 5 AAYFHTGGTTGTPKLAQHTHSNEVYNAwmLALNSLFDPDD---VLLCGLPLFHVNGSVVTLLTPLASGAHVVLAgpagyR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 248 ADALKGTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksmglkkkAFVWARNIGFKVNSkkmlgkyntpvsYRMAktl 327
Cdd:cd05944 82 NPGLFDNFWKLVERYRITSLSTVPTVY--------------------AALLQVPVNADISS------------LRFA--- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 328 vfskvktslgldhchsfISGTAPLNQET-AEFFLSLDIPIGELYGLSESSGPHTISNQNN-YRLLSCG----------KI 395
Cdd:cd05944 127 -----------------MSGAAPLPVELrARFEDATGLPVVEGYGLTEATCLVAVNPPDGpKRPGSVGlrlpyarvriKV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 396 LTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVP 475
Cdd:cd05944 190 LDGVGRLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVAD-GWLNTGDLGRLDADGYLFITGRAKD-LIIRGGHNID 267
|
....*
gi 1008909320 476 PIPVE 480
Cdd:cd05944 268 PALIE 272
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
13-480 |
3.79e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 97.36 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 13 RFGTYPALASKNGkkweILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAE 92
Cdd:PRK06188 24 RYPDRPALVLGDT----RLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 93 VCQYVITHAKVNILLVENDQQLQKILSIpQSSLEPLKAIiqyrLPMKKNNNLyswDDFMELGRSIPDTQLEQVIESQKAn 172
Cdd:PRK06188 100 DHAYVLEDAGISTLIVDPAPFVERALAL-LARVPSLKHV----LTLGPVPDG---VDLLAAAAKFGPAPLVAAALPPDI- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 173 qcAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhetvVSYL---PLSHIAAQMMdiwVP--IKIGALTYFAQ 247
Cdd:PRK06188 171 --AGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPAD----PRFLmctPLSHAGGAFF---LPtlLRGGTVIVLAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 248 ADAlkGTLVSTLKEVKPTVFIGVP-QIWEKI-HEMVKKNSAKSMGLkkkafvwarnigfkvnskkmlgkyntpVSYrmak 325
Cdd:PRK06188 242 FDP--AEVLRAIEEQRITATFLVPtMIYALLdHPDLRTRDLSSLET---------------------------VYY---- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 326 tlvfskvktslgldhchsfisGTAPLN----QETAEFFLsldiPI-GELYGLSESsgPHTIS--------NQNNYRLLSC 392
Cdd:PRK06188 289 ---------------------GASPMSpvrlAEAIERFG----PIfAQYYGQTEA--PMVITylrkrdhdPDDPKRLTSC 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 393 GKILTGCKNMLFQQN-----KDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILI 467
Cdd:PRK06188 342 GRPTPGLRVALLDEDgrevaQGEVGEICVRGPLVMDGYWNRPEETAEAFRD-GWLHTGDVAREDEDGFYYIVDRKKDMIV 420
|
490
....*....|...
gi 1008909320 468 TaGGENVPPIPVE 480
Cdd:PRK06188 421 T-GGFNVFPREVE 432
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
177-497 |
6.40e-21 |
|
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: 94.10 E-value: 6.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 177 LIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT-DKHETVVSylPLSHIAAQMMDIWVPIKIGAlTYFAQA--DALKg 253
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTeDDRYLIIN--PFFHTFGYKAGIVACLLTGA-TVVPVAvfDVDA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 254 tLVSTLKEVKPTVFIGVPQIWEKI--HEMVKKnsaksmglkkkafvwarnigFKVNSKK--MLGKYNTPVSY--RMAKTL 327
Cdd:cd17638 81 -ILEAIERERITVLPGPPTLFQSLldHPGRKK--------------------FDLSSLRaaVTGAATVPVELvrRMRSEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 328 VFSKVKTSLGLDHChsfisGTAPLNQEtaefflsldipigelyglseSSGPHTISNqnnyrllSCGKILTGcknmlFQQN 407
Cdd:cd17638 140 GFETVLTAYGLTEA-----GVATMCRP--------------------GDDAETVAT-------TCGRACPG-----FEVR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 408 KDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILItAGGENVPPIPVETLVkKKI 487
Cdd:cd17638 183 IADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGAL-AEH 260
|
330
....*....|
gi 1008909320 488 PIISNAMLVG 497
Cdd:cd17638 261 PGVAQVAVIG 270
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
175-497 |
8.93e-21 |
|
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: 93.55 E-value: 8.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSyLPLSHIAAQMMdIWVPIKIGALTYFAQADALkgt 254
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLS-LPLYHVGGLAI-LVRSLLAGAELVLLERNQA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 255 LVSTLKEVKPTVFIGVP-QIWekiheMVKKNSAKSMGLKkkafvwarniGFKVnskkmlgkyntpvsyrmaktlVFSkvk 333
Cdd:cd17630 78 LAEDLAPPGVTHVSLVPtQLQ-----RLLDSGQGPAALK----------SLRA---------------------VLL--- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 334 tslgldhchsfisGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQnkdgiGE 413
Cdd:cd17630 119 -------------GGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED-----GE 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 414 ICLWGRHIFMGYLESETEttEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVkKKIPIISNA 493
Cdd:cd17630 181 IWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAAL-AAHPAVRDA 256
|
....
gi 1008909320 494 MLVG 497
Cdd:cd17630 257 FVVG 260
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
58-501 |
4.16e-19 |
|
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: 90.47 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 58 VGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEndQQLQKILSIPQSSLEPLKAIIQYRLP 137
Cdd:cd05909 34 VGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTS--KQFIEKLKLHHLFDVEYDARIVYLED 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 138 MKKNnnlYSWDD----FMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDK 213
Cdd:cd05909 112 LRAK---ISKADkckaFLAGKFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 214 hETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAqADALKG-TLVSTLKEVKPTVFIGVPQIWekihemvkknsaksMGLK 292
Cdd:cd05909 189 -DVVFGALPFFHSFGLTGCLWLPLLSGIKVVFH-PNPLDYkKIPELIYDKKATILLGTPTFL--------------RGYA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 293 KKAfvwarnigfkvnskkmlGKYNTPvSYRMAktlvfskvktslgldhchsfISGTAPLNQETAEFFLSL-DIPIGELYG 371
Cdd:cd05909 253 RAA-----------------HPEDFS-SLRLV--------------------VAGAEKLKDTLRQEFQEKfGIRILEGYG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 372 LSESSGPHTISNQNNYRLLSC-GKILTGCKNMLFQ---QNKDGIGE---ICLWGRHIFMGYLESETETTEAIDDeGWLHS 444
Cdd:cd05909 295 TTECSPVISVNTPQSPNKEGTvGRPLPGMEVKIVSvetHEEVPIGEgglLLVRGPNVMLGYLNEPELTSFAFGD-GWYDT 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1008909320 445 GDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKIPIISN--AMLVGDKLK 501
Cdd:cd05909 374 GDIGKIDGEGFLTITGRLSR-FAKIAGEMVSLEAIEDILSEILPEDNEvaVVSVPDGRK 431
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
179-497 |
1.00e-18 |
|
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: 88.10 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 179 YTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYlPLSHIAAQMMDIWVPIKIGALTYFAQA--DALkgTLV 256
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPV-PLFHCFGSVLGVLACLTHGATMVFPSPsfDPL--AVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 257 STLKEVKPTVFIGVPQIWEKIhemvkknsaksmglkkkafvwarnigfkVNSKKMLgKYNtpvsyrmaktlvFSKVKTSl 336
Cdd:cd05917 86 EAIEKEKCTALHGVPTMFIAE----------------------------LEHPDFD-KFD------------LSSLRTG- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 337 gldhchsfISGTAPLNQETAEFFLSL----DIPIGelYGLSESSGPHTISNQNN---YRLLSCGKIL----------TGC 399
Cdd:cd05917 124 --------IMAGAPCPPELMKRVIEVmnmkDVTIA--YGMTETSPVSTQTRTDDsieKRVNTVGRIMphteakivdpEGG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 400 KNMLFQQnkdgIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPV 479
Cdd:cd05917 194 IVPPVGV----PGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIR-GGENIYPREI 268
|
330
....*....|....*...
gi 1008909320 480 ETLVKKKiPIISNAMLVG 497
Cdd:cd05917 269 EEFLHTH-PKVSDVQVVG 285
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
9-499 |
1.13e-18 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 89.65 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 9 ESVNRFGTYPALAskNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLcvgIYAT 88
Cdd:PLN02246 31 ERLSEFSDRPCLI--DGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAV---TTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 89 N----SAEVC-QYVITHAKvniLLVENDQQLQKILSIPQSSLEPLKAIIQYRlpmkkNNNLYSWDDFMELGRSIPDTQLe 163
Cdd:PLN02246 106 NpfytPAEIAkQAKASGAK---LIITQSCYVDKLKGLAEDDGVTVVTIDDPP-----EGCLHFSELTQADENELPEVEI- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 164 qviesqKANQCAVLIYTSGTTGIPKGVMLSHDN-ITWIAGAVTKD-----FKLTDkheTVVSYLPLSHIaaqmmdiwvpi 237
Cdd:PLN02246 177 ------SPDDVVALPYSSGTTGLPKGVMLTHKGlVTSVAQQVDGEnpnlyFHSDD---VILCVLPMFHI----------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 238 kigaltYfaqadALKGTLVSTLKeVKPTVFIgvpqiwekiheMVKKNSAKSMGLKKKafvwarnigFKVNskkmLGKYNT 317
Cdd:PLN02246 237 ------Y-----SLNSVLLCGLR-VGAAILI-----------MPKFEIGALLELIQR---------HKVT----IAPFVP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 318 PVSYRMAKtlvfSKVKTSLGLDHCHSFISGTAPLNQETAEFFLSlDIP---IGELYGLSESsGPhtisnqnnyrLL---- 390
Cdd:PLN02246 281 PIVLAIAK----SPVVEKYDLSSIRMVLSGAAPLGKELEDAFRA-KLPnavLGQGYGMTEA-GP----------VLamcl 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 391 ------------SCG--------KIL---TGCKnmlFQQNKDGigEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDL 447
Cdd:PLN02246 345 afakepfpvksgSCGtvvrnaelKIVdpeTGAS---LPRNQPG--EICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDI 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1008909320 448 GQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKiPIISNAMLVGDK 499
Cdd:PLN02246 420 GYIDDDDELFIVDRLKEL-IKYKGFQVAPAELEALLISH-PSIADAAVVPMK 469
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
149-480 |
1.22e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 90.01 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 149 DFMELGRSIPDTQLEQViESQKANQCAVLIYTSGTTGIPKGVMLSHDNIT---WIAGAVTKDfkltDKHETVVSYLPLSH 225
Cdd:PRK07529 191 DFDAELARQPGDRLFSG-RPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVanaWLGALLLGL----GPGDTVFCGLPLFH 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 226 IAAQMMDIWVPIKIGALTYFAQADALKG-TLVSTLKEV----KPTVFIGVPqiwekihemvkknSAKSMGLKKKafVWAR 300
Cdd:PRK07529 266 VNALLVTGLAPLARGAHVVLATPQGYRGpGVIANFWKIveryRINFLSGVP-------------TVYAALLQVP--VDGH 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 301 NIgfkvnskkmlgkyntpvsyrmaktlvfSKVKTslgldhchsFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPH 379
Cdd:PRK07529 331 DI---------------------------SSLRY---------ALCGAAPLPVEVFRRFEAaTGVRIVEGYGLTEATCVS 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 380 TIsnqnNY-----RLLSCG--------KILTGCKNMLFQQN--KDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHS 444
Cdd:PRK07529 375 SV----NPpdgerRIGSVGlrlpyqrvRVVILDDAGRYLRDcaVDEVGVLCIAGPNVFSGYLEAAHNKGLWLED-GWLNT 449
|
330 340 350
....*....|....*....|....*....|....*.
gi 1008909320 445 GDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 480
Cdd:PRK07529 450 GDLGRIDADGYFWLTGRAKD-LIIRGGHNIDPAAIE 484
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
169-491 |
1.74e-18 |
|
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: 88.70 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 169 QKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSH----IAAQMmdiwVPIKIGALTY 244
Cdd:cd05908 103 ELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTK-DRILSWMPLTHdmglIAFHL----APLIAGMNQY 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 245 FAqadalkgtlvstlkevkPT-VFIGVPQIW-EKIHEmvkknsaksmglKKKAFVWARNIGFKVnskkMLGKYNTPVSYr 322
Cdd:cd05908 178 LM-----------------PTrLFIRRPILWlKKASE------------HKATIVSSPNFGYKY----FLKTLKPEKAN- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 323 maktlvfskvktSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIG-------ELYGLSESS--------GPHTI------ 381
Cdd:cd05908 224 ------------DWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGlkrnailPVYGLAEASvgaslpkaQSPFKtitlgr 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 382 --------------SNQNNYRLLSCGKILTGCK-NMLFQQNK---DG-IGEICLWGRHIFMGYLESETETTEAIDDEGWL 442
Cdd:cd05908 292 rhvthgepepevdkKDSECLTFVEVGKPIDETDiRICDEDNKilpDGyIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWL 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1008909320 443 HSGDLGQLDGlGFLYVTGHIKEILITaGGENVPPIPVETLVKKKIPIIS 491
Cdd:cd05908 372 KTGDLGFIRN-GRLVITGREKDIIFV-NGQNVYPHDIERIAEELEGVEL 418
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
3-483 |
2.71e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 88.67 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 3 IPEFFRESVNRFGTYPALaSKNGKKweiLNFNQYYEACRKAAKSLIKL-GLERFHGVGILGFNSAEWFITAVGAILAGGL 81
Cdd:PRK05677 26 IQAVLKQSCQRFADKPAF-SNLGKT---LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 82 CVG---IYATNSAEvCQYVITHAKVNILLVENDQQLQKILsiPQSSLE------------PLK-----AIIQYRLPMKKN 141
Cdd:PRK05677 102 VVNtnpLYTAREME-HQFNDSGAKALVCLANMAHLAEKVL--PKTGVKhvivtevadmlpPLKrllinAVVKHVKKMVPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 142 NNL---YSWDDFMELGRSIPDTQLeqvieSQKANQCAVLIYTSGTTGIPKGVMLSHDNItwIAGAV-TKDF---KLTDKH 214
Cdd:PRK05677 179 YHLpqaVKFNDALAKGAGQPVTEA-----NPQADDVAVLQYTGGTTGVAKGAMLTHRNL--VANMLqCRALmgsNLNEGC 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 215 ETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIwekihemvkknsaksmglkkk 294
Cdd:PRK05677 252 EILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTL--------------------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 295 aFV-WARNIGFKvnskkmlgkyntpvsyrmakTLVFSKVKTSLgldhchsfiSGTAPLNQETAEFFLSLD-IPIGELYGL 372
Cdd:PRK05677 311 -FVaLCNNEAFR--------------------KLDFSALKLTL---------SGGMALQLATAERWKEVTgCAICEGYGM 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 373 SESSGPHTISNQNNYRLLSCGKIL--TGCKNMlfqqNKDG-------IGEICLWGRHIFMGYLESETETTEAIDDEGWLH 443
Cdd:PRK05677 361 TETSPVVSVNPSQAIQVGTIGIPVpsTLCKVI----DDDGnelplgeVGELCVKGPQVMKGYWQRPEATDEILDSDGWLK 436
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1008909320 444 SGDLGQLDGLGFLYVTGHIKEILITAGGeNVPPIPVETLV 483
Cdd:PRK05677 437 TGDIALIQEDGYMRIVDRKKDMILVSGF-NVYPNELEDVL 475
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
35-497 |
1.17e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 86.39 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 35 QYYEACRKAAKSLIKLGLERFHGVGILGFNSA---EWF--ITAVGAILAgglcvgiyATNSaevcQYVITHAKVNILLVE 109
Cdd:PLN02860 37 EFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDlylEWLlaVACAGGIVA--------PLNY----RWSFEEAKSAMLLVR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 110 ndqqlQKILSIPQSsleplkaiIQYRLPMKKNNNLYS--WDDFME-LGRSI---------PDTQLEQVIESQKANQC--- 174
Cdd:PLN02860 105 -----PVMLVTDET--------CSSWYEELQNDRLPSlmWQVFLEsPSSSVfiflnsfltTEMLKQRALGTTELDYAwap 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 --AVLI-YTSGTTGIPKGVMLSHDNIT-------WIAGAVTKDFKLtdkHETvvsylPLSHIA------AQMMdiwvpik 238
Cdd:PLN02860 172 ddAVLIcFTSGTTGRPKGVTISHSALIvqslakiAIVGYGEDDVYL---HTA-----PLCHIGglssalAMLM------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 239 IGA----LTYFAQADALKgtlvsTLKEVKPTVFIGVPQIWEKIHEMvkknSAKSMGLKKKAFVwarnigfkvnsKKML-G 313
Cdd:PLN02860 237 VGAchvlLPKFDAKAALQ-----AIKQHNVTSMITVPAMMADLISL----TRKSMTWKVFPSV-----------RKILnG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 314 KYNTPVSYRMAKTLVF--SKVKTSLGL-DHCHSFIsgtaplnqetaefFLSLDIPIGELYGLSESSGPHTISNQNNYRLL 390
Cdd:PLN02860 297 GGSLSSRLLPDAKKLFpnAKLFSAYGMtEACSSLT-------------FMTLHDPTLESPKQTLQTVNQTKSSSVHQPQG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 391 SC-GKILTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITA 469
Cdd:PLN02860 364 VCvGKPAPHVELKIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDR-IKT 442
|
490 500
....*....|....*....|....*...
gi 1008909320 470 GGENVPPIPVETLVKKKiPIISNAMLVG 497
Cdd:PLN02860 443 GGENVYPEEVEAVLSQH-PGVASVVVVG 469
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
24-592 |
2.14e-17 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 85.56 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 24 NGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGI---YATNSAEVC--QYVI 98
Cdd:cd05921 19 GNGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVspaYSLMSQDLAklKHLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 99 THAKVNILLVENDQQLQKILSIPQSSLEPLkaIIQYRLPMKKNNNLyswddFMELGRSIPDTQLEQVIESQKANQCAVLI 178
Cdd:cd05921 99 ELLKPGLVFAQDAAPFARALAAIFPLGTPL--VVSRNAVAGRGAIS-----FAELAATPPTAAVDAAFAAVGPDTVAKFL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 179 YTSGTTGIPKGVMLSHDNITWIAGAVTKDF-KLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFaqaDALK----- 252
Cdd:cd05921 172 FTSGSTGLPKAVINTQRMLCANQAMLEQTYpFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGTLYI---DDGKpmpgg 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 253 -GTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAksmgLKKKAFvwarnigfkvnsKKMlgkyntpvsyrmaktlvfsk 331
Cdd:cd05921 249 fEETLRNLREISPTVYFNVPAGWEMLVAALEKDEA----LRRRFF------------KRL-------------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 332 vktslgldhcHSFISGTAPLNQETAEfflSLD----------IPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKN 401
Cdd:cd05921 293 ----------KLMFYAGAGLSQDVWD---RLQalavatvgerIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTEL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 402 MLFQQnkDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQL----DGLGFLYVTGHIKEILITAGGENVPPI 477
Cdd:cd05921 360 KLVPS--GGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLASGTWVSVG 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 478 PVET-LVKKKIPIISNAMLVGDKLKFLSMLLtlkcemnqmsgepldklnFEAINFCRGL-GSQASTVTEIVKQqdPLVYK 555
Cdd:cd05921 438 PLRArAVAACAPLVHDAVVAGEDRAEVGALV------------------FPDLLACRRLvGLQEASDAEVLRH--AKVRA 497
|
570 580 590
....*....|....*....|....*....|....*..
gi 1008909320 556 AIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGEL 592
Cdd:cd05921 498 AFRDRLAALNGEATGSSSRIARALLLDEPPSIDKGEI 534
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
176-497 |
2.68e-17 |
|
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: 83.47 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 176 VLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVpIKIGA----LTYFAQADAL 251
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTE-ADVYLNMLPLFHIAGLNLALAT-FHAGGanvvMEKFDPAEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 252 KgtlvsTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKsmglkkkafvwarnigfkvnskkmlgkyntpvsyrmaktlvFSK 331
Cdd:cd17637 82 E-----LIEEEKVTLMGSFPPILSNLLDAAEKSGVD-----------------------------------------LSS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 332 VKTSLGLDhchsfisgtAPlnqETAEFFLSL-DIPIGELYGLSESSGPHTISNQNNyRLLSCGKILTGCKNMLFQQNKDG 410
Cdd:cd17637 116 LRHVLGLD---------AP---ETIQRFEETtGATFWSLYGQTETSGLVTLSPYRE-RPGSAGRPGPLVRVRIVDDNDRP 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 411 I-----GEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHI--KEiLITAGGENVPPIPVETlV 483
Cdd:cd17637 183 VpagetGEIVVRGPLVFQGYWNLPELTAYTFRN-GWHHTGDLGRFDEDGYLWYAGRKpeKE-LIKPGGENVYPAEVEK-V 259
|
330
....*....|....
gi 1008909320 484 KKKIPIISNAMLVG 497
Cdd:cd17637 260 ILEHPAIAEVCVIG 273
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
173-497 |
2.76e-17 |
|
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: 84.74 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 173 QCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQA-DAL 251
Cdd:cd05903 94 AVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPG-DVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIwDPD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 252 KGtlVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKkaFVWArnigfkvnskkmlGKYNTPVSYRMAKTLVFSK 331
Cdd:cd05903 173 KA--LALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRT--FVCG-------------GATVPRSLARRAAELLGAK 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 332 VKTSLGLDHCHSFISGTAPLNQETAEF-----FLSLDIPIGELYGLSESSGPhtisnqnnyrllscgkiltgcknmlfqq 406
Cdd:cd05903 236 VCSAYGSTECPGAVTSITPAPEDRRLYtdgrpLPGVEIKVVDDTGATLAPGV---------------------------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 407 nkdgIGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVkKK 486
Cdd:cd05903 288 ----EGELLSRGPSVFLGYLDRP-DLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIR-GGENIPVLEVEDLL-LG 360
|
330
....*....|.
gi 1008909320 487 IPIISNAMLVG 497
Cdd:cd05903 361 HPGVIEAAVVA 371
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
25-497 |
3.40e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 84.63 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 25 GKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFItavgAILA----GGLCVGIYATNSAEVCQYVITH 100
Cdd:PRK03640 25 EKKV---TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMIL----VIHAlqqlGAVAVLLNTRLSREELLWQLDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 101 AKVNILLVenDQQLQKILSIPQSSLeplkaiiqyrlpmkknnnlysWDDFMELGRSIPDTQleqviESQKANQCAVLIYT 180
Cdd:PRK03640 98 AEVKCLIT--DDDFEAKLIPGISVK---------------------FAELMNGPKEEAEIQ-----EEFDLDEVATIMYT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 181 SGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHI---AAQMMDIWVPIKIGALTYFaqaDAlkgtlvs 257
Cdd:PRK03640 150 SGTTGKPKGVIQTYGNHWWSAVGSALNLGLTE-DDCWLAAVPIFHIsglSILMRSVIYGMRVVLVEKF---DA------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 258 tlkevkptvfigvpqiwEKIHEMVKKNSAKSMGlkkkafvwarnigfkvnskkmlgkyntpVSYRMAKTLVfskvkTSLG 337
Cdd:PRK03640 219 -----------------EKINKLLQTGGVTIIS----------------------------VVSTMLQRLL-----ERLG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 338 LDHCHS----FISGTAPLNQETAEFFLSLDIPIGELYGLSESSG------PHTISNqnnyRLLSCGKILTGC-----KNM 402
Cdd:PRK03640 249 EGTYPSsfrcMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETASqivtlsPEDALT----KLGSAGKPLFPCelkieKDG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 403 LFQQNKDgIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETl 482
Cdd:PRK03640 325 VVVPPFE-EGEIVVKGPNVTKGYLNREDATRETFQD-GWFKTGDIGYLDEEGFLYVLDRRSD-LIISGGENIYPAEIEE- 400
|
490
....*....|....*
gi 1008909320 483 VKKKIPIISNAMLVG 497
Cdd:PRK03640 401 VLLSHPGVAEAGVVG 415
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
175-476 |
7.13e-17 |
|
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: 83.83 E-value: 7.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQadalkgt 254
Cdd:cd05931 152 AYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDP-GDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMS------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 255 lvstlkevkPTVFIGVPQIWekiHEMVKKNSAKSMGlkkkafvwARNIGF-----KVNSKKM----LGKYNT------PV 319
Cdd:cd05931 224 ---------PAAFLRRPLRW---LRLISRYRATISA--------APNFAYdlcvrRVRDEDLegldLSSWRValngaePV 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 320 SyrmAKTL-VFSKVKTSLGLD-HCHS----------FISGTAPLNQETAEFFLSLdipigELYGLSESSGPHTisnQNNY 387
Cdd:cd05931 284 R---PATLrRFAEAFAPFGFRpEAFRpsyglaeatlFVSGGPPGTGPVVLRVDRD-----ALAGRAVAVAADD---PAAR 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 388 RLLSCGKILTGcknMLF--------QQNKDG-IGEICLWGRHIFMGYL--ESETETT----EAIDDEGWLHSGDLGQLDG 452
Cdd:cd05931 353 ELVSCGRPLPD---QEVrivdpetgRELPDGeVGEIWVRGPSVASGYWgrPEATAETfgalAATDEGGWLRTGDLGFLHD 429
|
330 340
....*....|....*....|....
gi 1008909320 453 lGFLYVTGHIKEILITAgGENVPP 476
Cdd:cd05931 430 -GELYITGRLKDLIIVR-GRNHYP 451
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
175-483 |
1.07e-16 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 83.56 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNI-------TWIAGAVtkdfkLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGAltyfaq 247
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRNMlanleqaKAAYGPL-----LHPGKELVVTALPLYHIFALTVNCLLFIELGG------ 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 248 adalKGTLVSTLKEvkptvfigvpqiwekIHEMVKKnsaksmgLKKKAFVWARNigfkVNSkkmlgKYNTPVSYRMAKTL 327
Cdd:PRK08974 278 ----QNLLITNPRD---------------IPGFVKE-------LKKYPFTAITG----VNT-----LFNALLNNEEFQEL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 328 VFSKVKTSLGldhchsfisGTAPLNQETAEFFLSL-DIPIGELYGLSESS-----GPHTISNQNNyrllSCG-------- 393
Cdd:PRK08974 323 DFSSLKLSVG---------GGMAVQQAVAERWVKLtGQYLLEGYGLTECSplvsvNPYDLDYYSG----SIGlpvpstei 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 394 KILTGCKNMLFQqnkDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGEN 473
Cdd:PRK08974 390 KLVDDDGNEVPP---GEPGELWVKGPQVMLGYWQRPEATDEVIKD-GWLATGDIAVMDEEGFLRIVDRKKDM-ILVSGFN 464
|
330
....*....|
gi 1008909320 474 VPPIPVETLV 483
Cdd:PRK08974 465 VYPNEIEDVV 474
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
29-483 |
1.19e-16 |
|
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: 83.10 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 29 EILNFNQYYEACRKAAKSLIKLGLERFHGVgILGFNSAEWFITAV-GAILAGGLCV-----GIYATNSAEvcqyvITHAK 102
Cdd:cd05906 38 EFQSYQDLLEDARRLAAGLRQLGLRPGDSV-ILQFDDNEDFIPAFwACVLAGFVPApltvpPTYDEPNAR-----LRKLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 103 vNILlvendQQLQK--ILSIPqSSLEPLKAIIQYRlpmkknnnlySWDDFMELGRSI-PDTQLEQVIESQKANQCAVLIY 179
Cdd:cd05906 112 -HIW-----QLLGSpvVLTDA-ELVAEFAGLETLS----------GLPGIRVLSIEElLDTAADHDLPQSRPDDLALLML 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 180 TSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALkgtlvstL 259
Cdd:cd05906 175 TSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQ-DVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPTEEI-------L 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 260 KEvkPTVFIgvpqiwekihEMVKKNSAksmglkkkAFVWARNigFkvnskkMLGKYNTPVSYRMAKTLVFSKVKtslgld 339
Cdd:cd05906 247 AD--PLRWL----------DLIDRYRV--------TITWAPN--F------AFALLNDLLEEIEDGTWDLSSLR------ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 340 hchSFISGTAPLNQETAEFFLSLDIPIG-------ELYGLSE-------SSGPHTISNQNNYRLLSCGKILTGCKNMLFQ 405
Cdd:cd05906 293 ---YLVNAGEAVVAKTIRRLLRLLEPYGlppdairPAFGMTEtcsgviySRSFPTYDHSQALEFVSLGRPIPGVSMRIVD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 406 QNKDG-----IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGlGFLYVTGHIKEILITaGGENVPPIPVE 480
Cdd:cd05906 370 DEGQLlpegeVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDN-GNLTITGRTKDTIIV-NGVNYYSHEIE 447
|
...
gi 1008909320 481 TLV 483
Cdd:cd05906 448 AAV 450
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
175-470 |
1.41e-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.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 82.49 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLSHIAAqMMDIWVPIKIGALTYFAQADALKGT 254
Cdd:cd05922 120 ALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI-TADDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVLDDA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 255 LVSTLKEVKPTVFIGVPQIWEKIhemvkknsaKSMGLKKKAFVWARnigfkvnskkmlgkYNTPVSYRMAKTLVfskvkt 334
Cdd:cd05922 198 FWEDLREHGATGLAGVPSTYAML---------TRLGFDPAKLPSLR--------------YLTQAGGRLPQETI------ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 335 slgldhchsfisgtaplnQETAEFFLSLDIPIgeLYGLSESSG------PHTISNqnnyRLLSCGKILTGCKnmLFQQNK 408
Cdd:cd05922 249 ------------------ARLRELLPGAQVYV--MYGQTEATRrmtylpPERILE----KPGSIGLAIPGGE--FEILDD 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1008909320 409 DG-------IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAG 470
Cdd:cd05922 303 DGtptppgePGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFG 371
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
175-447 |
2.11e-15 |
|
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: 79.42 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNIT--WIAGAVTKDfkLTDKHETVVSYLPLSHIAAQMmdiwvpIKIGALT-----YFAQ 247
Cdd:cd17632 226 ALLIYTSGSTGTPKGAMYTERLVAtfWLKVSSIQD--IRPPASITLNFMPMSHIAGRI------SLYGTLArggtaYFAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 248 ADALKgTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKYNTPVsyrmaktl 327
Cdd:cd17632 298 ASDMS-TLFDDLALVRPTELFLVPRVCDMLFQRYQAELDRRSVAGADAETLAERVKAELRERVLGGRLLAAV-------- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 328 vfskvktslgldhchsfiSGTAPLNQETAEFFLS-LDIPIGELYGLSEsSGPHTISNQ------NNYRLLSC---GKILT 397
Cdd:cd17632 369 ------------------CGSAPLSAEMKAFMESlLDLDLHDGYGSTE-AGAVILDGVivrppvLDYKLVDVpelGYFRT 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1008909320 398 gcknmlfqQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDL 447
Cdd:cd17632 430 --------DRPHPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDV 471
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
31-497 |
2.27e-15 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 79.06 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 31 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILlVEN 110
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL-VTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 111 DQQLQKILSIPQSSLEPLKAII----QYRLPMKKNNNLYSWDDFMELGRSIPdtqLEQVIESQkanqCAVLIYTSGTTGI 186
Cdd:TIGR03098 105 SERLDLLHPALPGCHDLRTLIIvgdpAHASEGHPGEEPASWPKLLALGDADP---PHPVIDSD----MAAILYTSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 187 PKGVMLSHDNItwIAGA--VTKDFKLTDKhETVVSYLPLSHIAA--QMMDIWVpikIGA----LTYFAQADALKgtlvsT 258
Cdd:TIGR03098 178 PKGVVLSHRNL--VAGAqsVATYLENRPD-DRLLAVLPLSFDYGfnQLTTAFY---VGAtvvlHDYLLPRDVLK-----A 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 259 LKEVKPTVFIGVPQIWEKIHEMVKKNSAksmglkkkafvwARNIGFKVNSKKmlgkyntpvsyRMAKTLVfSKVKTSLGL 338
Cdd:TIGR03098 247 LEKHGITGLAAVPPLWAQLAQLDWPESA------------APSLRYLTNSGG-----------AMPRATL-SRLRSFLPN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 339 dhchsfisgtaplnqetAEFFLsldipigeLYGLSESSGPHTISNQN-NYRLLSCGKILTGCKNMLFqqNKDG------- 410
Cdd:TIGR03098 303 -----------------ARLFL--------MYGLTEAFRSTYLPPEEvDRRPDSIGKAIPNAEVLVL--REDGsecapge 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 411 IGEICLWGRHIFMGYLESETETTEAI------DDEGWLH-----SGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPV 479
Cdd:TIGR03098 356 EGELVHRGALVAMGYWNDPEKTAERFrplppfPGELHLPelavwSGDTVRRDEEGFLYFVGR-RDEMIKTSGYRVSPTEV 434
|
490
....*....|....*...
gi 1008909320 480 ETlVKKKIPIISNAMLVG 497
Cdd:TIGR03098 435 EE-VAYATGLVAEAVAFG 451
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
175-480 |
2.36e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 79.27 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGAltyfaqaDALKGT 254
Cdd:PRK07768 155 ALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFHDMGMVGFLTVPMYFGA-------ELVKVT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 255 lvstlkevkPTVFIGVPQIWekihemvkknsAKSMGLKKKAFVWARNIGFKVNSKKmLGKYNTPVSYRMaktlvfSKVKT 334
Cdd:PRK07768 228 ---------PMDFLRDPLLW-----------AELISKYRGTMTAAPNFAYALLARR-LRRQAKPGAFDL------SSLRF 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 335 SLgldhchsfiSGTAPLNQETAEFFLSLDIPIG-------ELYGLSESSGPHTIS------------------------- 382
Cdd:PRK07768 281 AL---------NGAEPIDPADVEDLLDAGARFGlrpeailPAYGMAEATLAVSFSpcgaglvvdevdadllaalrravpa 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 383 -NQNNYRLLSCGKILTGCKNMLFQQNKD-----GIGEICLWGRHIFMGYLESETeTTEAIDDEGWLHSGDLGQLDGLGFL 456
Cdd:PRK07768 352 tKGNTRRLATLGPPLPGLEVRVVDEDGQvlpprGVGVIELRGESVTPGYLTMDG-FIPAQDADGWLDTGDLGYLTEEGEV 430
|
330 340
....*....|....*....|....
gi 1008909320 457 YVTGHIKEILITaGGENVPPIPVE 480
Cdd:PRK07768 431 VVCGRVKDVIIM-AGRNIYPTDIE 453
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
175-483 |
6.52e-15 |
|
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: 76.53 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKgT 254
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK-S 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 255 LVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLkkkafvwaRNIGFkvnskkmlgkyntpvsyrmaktlvfskvkt 334
Cdd:cd17635 83 LFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSL--------RLIGY------------------------------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 335 slgldhchsfiSGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLL-SCGKILTGCK-----NMLFQQNK 408
Cdd:cd17635 125 -----------GGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIEInAVGRPYPGVDvylaaTDGIAGPS 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008909320 409 DGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLV 483
Cdd:cd17635 194 ASFGTIWIKSPANMLGYWNNPERTAEVLID-GWVNTGDLGERREDGFLFITGRSSES-INCGGVKIAPDEVERIA 266
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
18-497 |
1.37e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 76.46 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 18 PALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYV 97
Cdd:PRK06145 19 AALVYRD----QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 98 ITHAKVNILLVenDQQLQKIlsipqSSLEPLKAIIqyrlpmkknnNLYSWDDFMELGRS-IPDTQLEQVIESQKANqcav 176
Cdd:PRK06145 95 LGDAGAKLLLV--DEEFDAI-----VALETPKIVI----------DAAAQADSRRLAQGgLEIPPQAAVAPTDLVR---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 177 LIYTSGTTGIPKGVMLSHDNITW------IAGAVTKDFKLTdkhetVVSylPLSHIAA-QMMDIWVPIKIGALTYFAQAD 249
Cdd:PRK06145 154 LMYTSGTTDRPKGVMHSYGNLHWksidhvIALGLTASERLL-----VVG--PLYHVGAfDLPGIAVLWVGGTLRIHREFD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 250 AlkGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSaksmgLKKKAFVWArnIGfkvnskkmlGKYNTPVSYRMAKTLVF 329
Cdd:PRK06145 227 P--EAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDR-----FDLDSLAWC--IG---------GGEKTPESRIRDFTRVF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 330 SKVKtslgldhchsFISGtaplnqetaefflsldipigelYGLSESSGPHTISNQNNY--RLLSCGK--------ILTGC 399
Cdd:PRK06145 289 TRAR----------YIDA----------------------YGLTETCSGDTLMEAGREieKIGSTGRalahveirIADGA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 400 KNMLFQQNKdgiGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPV 479
Cdd:PRK06145 337 GRWLPPNMK---GEICMRGPKVTKGYWKDPEKTAEAFYG-DWFRSGDVGYLDEEGFLYLTDRKKDMIIS-GGENIASSEV 411
|
490
....*....|....*...
gi 1008909320 480 ETLVkKKIPIISNAMLVG 497
Cdd:PRK06145 412 ERVI-YELPEVAEAAVIG 428
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
175-480 |
2.21e-14 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 76.08 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVsYLPLSH----IAAQMMDIwvpIKIGALTYFAQADA 250
Cdd:PRK05852 179 AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVA-VMPLYHghglIAALLATL---ASGGAVLLPARGRF 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 251 LKGTLVSTLKEVKPTVFIGVPqiweKIHEMvkknsaksmglkkkafvwarnigfkvnskkMLGKYNTPVSYRMAKTLVFS 330
Cdd:PRK05852 255 SAHTFWDDIKAVGATWYTAVP----TIHQI------------------------------LLERAATEPSGRKPAALRFI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 331 KvktslgldhchsfiSGTAPLNQETAEF----FLSldiPIGELYGLSE---------------------SSGPHTISNQN 385
Cdd:PRK05852 301 R--------------SCSAPLTAETAQAlqteFAA---PVVCAFGMTEathqvtttqiegigqtenpvvSTGLVGRSTGA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 386 NYRLL-SCGKILTgcknmlfqqnKDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKE 464
Cdd:PRK05852 364 QIRIVgSDGLPLP----------AGAVGEVWLRGTTVVRGYLGDPTITAANFTD-GWLRTGDLGSLSAAGDLSIRGRIKE 432
|
330
....*....|....*.
gi 1008909320 465 iLITAGGENVPPIPVE 480
Cdd:PRK05852 433 -LINRGGEKISPERVE 447
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
35-495 |
4.63e-14 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 75.06 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 35 QYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEND--- 111
Cdd:PLN03102 44 QTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSfep 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 112 --QQLQKILSIPQSSLEPLKAII-QYRLPMKKNNNLYSWDDFMELGRSIPdTQLEQVIESQKANQCAVLIYTSGTTGIPK 188
Cdd:PLN03102 124 laREVLHLLSSEDSNLNLPVIFIhEIDFPKRPSSEELDYECLIQRGEPTP-SLVARMFRIQDEHDPISLNYTSGTTADPK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 189 GVMLSHDnitwiaGAvtkdfkltdkhetvvsYL-PLSHIAAQMMDIWvPIKIGALTYF-------AQADALKGTLVSTLK 260
Cdd:PLN03102 203 GVVISHR------GA----------------YLsTLSAIIGWEMGTC-PVYLWTLPMFhcngwtfTWGTAARGGTSVCMR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 261 EVKptvfigVPQIWEKIhEMvkkNSAKSMGLKKKAFvwarNIGFKVNSkkmlgkynTPVSYRMAKTLVfskvktslgldh 340
Cdd:PLN03102 260 HVT------APEIYKNI-EM---HNVTHMCCVPTVF----NILLKGNS--------LDLSPRSGPVHV------------ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 341 chsfISGTAPLNQETAEFFLSLDIPIGELYGLSESSGP------------------HTISNQNNYRLLSCGKILTGCKNM 402
Cdd:PLN03102 306 ----LTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPvlfcewqdewnrlpenqqMELKARQGVSILGLADVDVKNKET 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 403 LFQQNKDG--IGEICLWGRHIFMGYLESETETTEAIDdEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 480
Cdd:PLN03102 382 QESVPRDGktMGEIVIKGSSIMKGYLKNPKATSEAFK-HGWLNTGDVGVIHPDGHVEIKDRSKDIIIS-GGENISSVEVE 459
|
490
....*....|....*
gi 1008909320 481 TLVKKKIPIISNAML 495
Cdd:PLN03102 460 NVLYKYPKVLETAVV 474
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
31-497 |
4.68e-14 |
|
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: 74.44 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 31 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVen 110
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 111 dqqlqkilsipQSSLEPLkaiiqyrlpmkknnnlyswddfmelgrsipdtqleqviesqkanqcAVLIYTSGTTGIPKGV 190
Cdd:cd05935 80 -----------GSELDDL----------------------------------------------ALIPYTSGTTGLPKGC 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 191 MLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGAlTYFAQADALKGTLVSTLKEVKPTVfigv 270
Cdd:cd05935 103 MHTHFSAAANALQSAVWTGLTPS-DVILACLPLFHVTGFVGSLNTAVYVGG-TYVLMARWDRETALELIEKYKVTF---- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 271 pqiWEKIHEMVKKNSAkSMGLKKKAFvwarnigfkvNSKKMLGKYNTPVSYRMAKtlvfsKVKTSLGLDHChsfisgtap 350
Cdd:cd05935 177 ---WTNIPTMLVDLLA-TPEFKTRDL----------SSLKVLTGGGAPMPPAVAE-----KLLKLTGLRFV--------- 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 351 lnqetaefflsldipigELYGLSESSgPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGI-------GEICLWGRHIFM 423
Cdd:cd05935 229 -----------------EGYGLTETM-SQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRelppnevGEIVVRGPQIFK 290
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1008909320 424 GYLESETETTEA-IDDEG--WLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKiPIISNAMLVG 497
Cdd:cd05935 291 GYWNRPEETEESfIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKR-MINVSGFKVWPAEVEAKLYKH-PAI*EVCVIS 365
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
175-497 |
7.16e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 74.46 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNitwiAGAVTKDFKLTDKHETVVSYL---PLSHIaaqmmdiwvpikIGALTYFAQADAL 251
Cdd:PRK09088 138 SLILFTSGTSGQPKGVMLSERN----LQQTAHNFGVLGRVDAHSSFLcdaPMFHI------------IGLITSVRPVLAV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 252 KGT-LVSTLKEVKPTV------------FIGVPQIWEKIHemvkknsaksmglkkkafvwaRNIGFKVNSkkmlgkyntp 318
Cdd:PRK09088 202 GGSiLVSNGFEPKRTLgrlgdpalgithYFCVPQMAQAFR---------------------AQPGFDAAA---------- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 319 vsyrmaktlvfskvktslgLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSE-------SSGPHTISNqnnyRLLS 391
Cdd:PRK09088 251 -------------------LRHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEagtvfgmSVDCDVIRA----KAGA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 392 CGKILTGCKNMLFQQNKDGI-----GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIL 466
Cdd:PRK09088 308 AGIPTPTVQTRVVDDQGNDCpagvpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF 387
|
330 340 350
....*....|....*....|....*....|.
gi 1008909320 467 ITaGGENVPPIPVETLVKKKiPIISNAMLVG 497
Cdd:PRK09088 388 IS-GGENVYPAEIEAVLADH-PGIRECAVVG 416
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
370-497 |
7.92e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 74.31 E-value: 7.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 370 YGLSESSG-----P---HTISNQNNYRLLSCGKILTGcknMLFQ-QNKDG-------IGEICLWGRHIFMGYLESETETT 433
Cdd:PRK07470 312 FGLGEVTGnitvlPpalHDAEDGPDARIGTCGFERTG---MEVQiQDDEGrelppgeTGEICVIGPAVFAGYYNNPEANA 388
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1008909320 434 EAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVEtlvkKKI---PIISNAMLVG 497
Cdd:PRK07470 389 KAFRD-GWFRTGDLGHLDARGFLYITGRASDMYIS-GGSNVYPREIE----EKLlthPAVSEVAVLG 449
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
156-462 |
1.11e-13 |
|
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: 73.44 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 156 SIPDTQLEQVIESQKA-------NQCAVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVtKDFKLTDkHETVVSYLPLSHIA 227
Cdd:cd05945 74 SSPAERIREILDAAKPalliadgDDNAYIIFTSGSTGRPKGVQISHDNLvSFTNWML-SDFPLGP-GDVFLNQAPFSFDL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 228 AqMMDIWVPIKIGALTYFAQADALK--GTLVSTLKEVKPTVFIGVPQIWEkihemvkknsaksMGLKKKAFvwarnigfk 305
Cdd:cd05945 152 S-VMDLYPALASGATLVPVPRDATAdpKQLFRFLAEHGITVWVSTPSFAA-------------MCLLSPTF--------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 306 vNSKKMlgkyntpvsyrmaKTLVfskvktslgldhcHSFISGTaPLNQETAEFFLSL--DIPIGELYGLSESSGP---HT 380
Cdd:cd05945 209 -TPESL-------------PSLR-------------HFLFCGE-VLPHKTARALQQRfpDARIYNTYGPTEATVAvtyIE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 381 ISNQ--NNYRLLSCGKILTGCKNMLFqqNKDG-------IGEICLWGRHIFMGYLESETETTEA---IDDEGWLHSGDLG 448
Cdd:cd05945 261 VTPEvlDGYDRLPIGYAKPGAKLVIL--DEDGrpvppgeKGELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLV 338
|
330
....*....|....
gi 1008909320 449 QLDGLGFLYVTGHI 462
Cdd:cd05945 339 RLEADGLLFYRGRL 352
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
157-497 |
1.15e-13 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 73.26 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 157 IPDTQLEQVIESQKAnqCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSylplshiAAQMM----- 231
Cdd:cd05919 78 ARDCEARLVVTSADD--IAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFS-------SAKMFfgygl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 232 --DIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWekihemvkKNSAKSMGLKKKAFVWARnigfkvnsk 309
Cdd:cd05919 149 gnSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFY--------ANLLDSCAGSPDALRSLR--------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 310 kmlgkyntpvsyrmaktlvfskvktslgldHChsfISGTAPLNQETAEFFLS-LDIPIGELYGLSESSgpHT-ISNQ-NN 386
Cdd:cd05919 212 ------------------------------LC---VSAGEALPRGLGERWMEhFGGPILDGIGATEVG--HIfLSNRpGA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 387 YRLLSCGKILTGCKNMLFqqNKDG-------IGEICLWGRHIFMGYLESeTETTEAIDDEGWLHSGDLGQLDGLGFLYVT 459
Cdd:cd05919 257 WRLGSTGRPVPGYEIRLV--DEEGhtippgeEGDLLVRGPSAAVGYWNN-PEKSRATFNGGWYRTGDKFCRDADGWYTHA 333
|
330 340 350
....*....|....*....|....*....|....*...
gi 1008909320 460 GHIKEILITaGGENVPPIPVETLVkKKIPIISNAMLVG 497
Cdd:cd05919 334 GRADDMLKV-GGQWVSPVEVESLI-IQHPAVAEAAVVA 369
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
179-497 |
6.14e-13 |
|
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: 70.13 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 179 YTSGTTGIPKGVMLSHDniTWIAGAVT--KDFKLtDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGtlV 256
Cdd:cd17633 7 FTSGTTGLPKAYYRSER--SWIESFVCneDLFNI-SGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSW--I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 257 STLKEVKPTVFIGVPQiwekiheMVKknsaksmglkkkafvwarnigfkvnskkMLGKYNTPVSyrmaktlvfsKVKtsl 336
Cdd:cd17633 82 RKINQYNATVIYLVPT-------MLQ----------------------------ALARTLEPES----------KIK--- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 337 gldhchSFISGTAPLNQETAEFF--LSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGIGEI 414
Cdd:cd17633 114 ------SIFSSGQKLFESTKKKLknIFPKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIGKI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 415 CLWGRHIFMGYLESEtetteAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVkKKIPIISNAM 494
Cdd:cd17633 188 FVKSEMVFSGYVRGG-----FSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIII-GGINIFPTEIESVL-KAIPGIEEAI 260
|
...
gi 1008909320 495 LVG 497
Cdd:cd17633 261 VVG 263
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
175-497 |
7.10e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 71.39 E-value: 7.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFK---------LTDKHETVVSYLPLSHIAAQMMDIWVPIKIGaltyf 245
Cdd:PRK12492 210 AVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSqlgpdgqplMKEGQEVMIAPLPLYHIYAFTANCMCMMVSG----- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 246 aqadalkgtlvstlkevKPTVFIGVPQiweKIHEMVKKnsaksmgLKKKAFvwarnigfkvnsKKMLGkYNTPVSYRMA- 324
Cdd:PRK12492 285 -----------------NHNVLITNPR---DIPGFIKE-------LGKWRF------------SALLG-LNTLFVALMDh 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 325 ---KTLVFSKVKTSlgldhchsfISGTAPLNQETAEFFLSLD-IPIGELYGLSESSgphTISNQNNY----RLLSCGKIL 396
Cdd:PRK12492 325 pgfKDLDFSALKLT---------NSGGTALVKATAERWEQLTgCTIVEGYGLTETS---PVASTNPYgelaRLGTVGIPV 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 397 TGCKNMLFqqNKDGI-------GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITA 469
Cdd:PRK12492 393 PGTALKVI--DDDGNelplgerGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVS 470
|
330 340
....*....|....*....|....*...
gi 1008909320 470 GGeNVPPIPVETLVKKKiPIISNAMLVG 497
Cdd:PRK12492 471 GF-NVYPNEIEDVVMAH-PKVANCAAIG 496
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
42-497 |
1.06e-12 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 70.87 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 42 KAAKSLIKLGLERFHGVGILGFNSAE----WFITA-VGAILagglcVGIYATNSAEVCQYVITHAKVNiLLVENDQQLQK 116
Cdd:PRK08008 49 RTANLFYSLGIRKGDKVALHLDNCPEfifcWFGLAkIGAIM-----VPINARLLREESAWILQNSQAS-LLVTSAQFYPM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 117 ILSIPQSSLEPLKAIIQYRLPMKKNNNLYswdDFMELGRSIPDTQLEQVIESqkANQCAVLIYTSGTTGIPKGVMLSHDN 196
Cdd:PRK08008 123 YRQIQQEDATPLRHICLTRVALPADDGVS---SFTQLKAQQPATLCYAPPLS--TDDTAEILFTSGTTSRPKGVVITHYN 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 197 I-------TWiAGAVTKDfkltDKHETVvsyLPLSHIAAQMMDIWVPIKIGAltyfaqadalkgTLVstlkevkptvfig 269
Cdd:PRK08008 198 LrfagyysAW-QCALRDD----DVYLTV---MPAFHIDCQCTAAMAAFSAGA------------TFV------------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 270 vpqiwekiheMVKKNSAKsmglkkkAFvWarnigfkvnskKMLGKYNTPVSYRMA---KTLVFSKVkTSLGLDHCHSFIS 346
Cdd:PRK08008 245 ----------LLEKYSAR-------AF-W-----------GQVCKYRATITECIPmmiRTLMVQPP-SANDRQHCLREVM 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 347 GTAPL-NQETAEFFLSLDIPIGELYGLSES-SGPHTISNQNNYRLLSCGKILTGCKNMLfqQNKDG-------IGEICLW 417
Cdd:PRK08008 295 FYLNLsDQEKDAFEERFGVRLLTSYGMTETiVGIIGDRPGDKRRWPSIGRPGFCYEAEI--RDDHNrplpageIGEICIK 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 418 G---RHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETLVKKKiPIISNAM 494
Cdd:PRK08008 373 GvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDR-RCNMIKRGGENVSCVELENIIATH-PKIQDIV 450
|
...
gi 1008909320 495 LVG 497
Cdd:PRK08008 451 VVG 453
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
166-612 |
1.37e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 70.90 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 166 IESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTK-DFKLTDKHETVVSYLPLSHI-------AAQMMDIWVPI 237
Cdd:PTZ00342 298 IQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKhSIFKKYNPKTHLSYLPISHIyerviayLSFMLGGTINI 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 238 KIGALTYFAqadalkgtlvSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKK---KAFVWARNIGFKVNSKKMLGK 314
Cdd:PTZ00342 378 WSKDINYFS----------KDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRflvKKILSLRKSNNNGGFSKFLEG 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 315 YnTPVSYRMAktlvfSKVKTSLGLdhchsFISGTAPLNQETA-EFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCG 393
Cdd:PTZ00342 448 I-THISSKIK-----DKVNPNLEV-----ILNGGGKLSPKIAeELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIG 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 394 KILtgCKNMLFQ-------QNKDGI--GEICLWGRHIFMGY-LESETeTTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIK 463
Cdd:PTZ00342 517 GPI--SPNTKYKvrtwetyKATDTLpkGELLIKSDSIFSGYfLEKEQ-TKNAFTEDGYFKTGDIVQINKNGSLTFLDRSK 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 464 EILITAGGENvppIPVETL--VKKKIPIISNAMLVGDK-----LKFLSM--LLTLKC----EMNQMSG----EPLDKLNF 526
Cdd:PTZ00342 594 GLVKLSQGEY---IETDMLnnLYSQISFINFCVVYGDDsmdgpLAIISVdkYLLFKClkddNMLESTGinekNYLEKLTD 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 527 EAINfcrglgsqASTVTEIVKQQDPLVYKaiQQGINAVNqeAMNNAQRIEK-WvilekDFSIYggeLGPMMKLKRHFVAQ 605
Cdd:PTZ00342 671 ETIN--------NNIYVDYVKGKMLEVYK--KTNLNRYN--IINDIYLTSKvW-----DTNNY---LTPTFKVKRFYVFK 730
|
....*..
gi 1008909320 606 KYKKQID 612
Cdd:PTZ00342 731 DYAFFID 737
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
171-497 |
3.44e-12 |
|
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: 68.52 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 171 ANQCAVLIYTSGTTGIPKGVMLSHdnitwiagavtkdfkltdkhetvvSYlPLSHIAAqmMDIWVPIKIGALtYFAQADA 250
Cdd:cd05972 80 AEDPALIYFTSGTTGLPKGVLHTH------------------------SY-PLGHIPT--AAYWLGLRPDDI-HWNIADP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 251 --LKGTLvSTLKEVkptVFIGVPQIwekIHEMVKKNSAKSMGLKKKafvwarnigFKVNSKkmlgkYNTPVSYRM-AKTL 327
Cdd:cd05972 132 gwAKGAW-SSFFGP---WLLGATVF---VYEGPRFDAERILELLER---------YGVTSF-----CGPPTAYRMlIKQD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 328 VFSKVKTSLgldhcHSFISGTAPLNQETAEFFLS-LDIPIGELYGLSEssgphTISNQNNYRLL-----SCGKILTGCKN 401
Cdd:cd05972 191 LSSYKFSHL-----RLVVSAGEPLNPEVIEWWRAaTGLPIRDGYGQTE-----TGLTVGNFPDMpvkpgSMGRPTPGYDV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 402 MLFQQNKDGI-----GEICL-WGRH-IFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENV 474
Cdd:cd05972 261 AIIDDDGRELppgeeGDIAIkLPPPgLFLGYVGDPEKTEASIRG-DYYLTGDRAYRDEDGYFWFVGRADDI-IKSSGYRI 338
|
330 340
....*....|....*....|....
gi 1008909320 475 PPIPVE-TLVKKkiPIISNAMLVG 497
Cdd:cd05972 339 GPFEVEsALLEH--PAVAEAAVVG 360
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
175-497 |
3.54e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 69.04 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAA-----QMMDIWVPIKIGALTYFaqaD 249
Cdd:PRK07786 177 ALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGigsmlPGLLLGAPTVIYPLGAF---D 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 250 AlkGTLVSTLKEVKPTVFIGVPQIWEKIhemVKKNSAKSMGLKKKAFVWarnigfkvnskkmlgkyntpvsyrmaktlvf 329
Cdd:PRK07786 254 P--GQLLDVLEAEKVTGIFLVPAQWQAV---CAEQQARPRDLALRVLSW------------------------------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 330 skvktslgldhchsfisGTAP----LNQETAEFFLslDIPIGELYGLSESSgPHT--ISNQNNYRLL-SCGKILTGCKNM 402
Cdd:PRK07786 298 -----------------GAAPasdtLLRQMAATFP--EAQILAAFGQTEMS-PVTcmLLGEDAIRKLgSVGKVIPTVAAR 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 403 LFQQNKDG-----IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPI 477
Cdd:PRK07786 358 VVDENMNDvpvgeVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIIS-GGENIYCA 435
|
330 340
....*....|....*....|
gi 1008909320 478 PVETLVKKKiPIISNAMLVG 497
Cdd:PRK07786 436 EVENVLASH-PDIVEVAVIG 454
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
150-483 |
6.07e-12 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 68.36 E-value: 6.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 150 FMELGRSIPDTqLEQVieSQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPL------ 223
Cdd:PRK07514 137 LLEAAAAAPDD-FETV--PRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPD-DVLIHALPIfhthgl 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 224 ---SHIA----AQMmdIWVPiKIGA---LTYFAQAdalkgtlvstlkevkpTVFIGVPQIWEKI--HEMVKKNSAKSMGL 291
Cdd:PRK07514 213 fvaTNVAllagASM--IFLP-KFDPdavLALMPRA----------------TVMMGVPTFYTRLlqEPRLTREAAAHMRL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 292 kkkafvwarnigfkvnskkmlgkyntpvsyrmaktlvfskvktslgldhchsFISGTAPLNQET-AEFFLSLDIPIGELY 370
Cdd:PRK07514 274 ----------------------------------------------------FISGSAPLLAEThREFQERTGHAILERY 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 371 GLSEssgphTISNQNN-Y------------------RLLSC--GKILTgcknmlfqqnKDGIGEICLWGRHIFMGYLESE 429
Cdd:PRK07514 302 GMTE-----TNMNTSNpYdgerragtvgfplpgvslRVTDPetGAELP----------PGEIGMIEVKGPNVFKGYWRMP 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1008909320 430 TETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLV 483
Cdd:PRK07514 367 EKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIIS-GGYNVYPKEVEGEI 419
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
31-274 |
9.02e-12 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 67.78 E-value: 9.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 31 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEn 110
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVS- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 111 dQQLQKILSIPQSSLEPLKAIiqyrlpMKKNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGV 190
Cdd:cd05959 109 -GELAPVLAAALTKSEHTLVV------LIVSGGAGPEAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 191 MLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGV 270
Cdd:cd05959 182 VHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPTPAAVFKRIRRYRPTVFFGV 261
|
....
gi 1008909320 271 PQIW 274
Cdd:cd05959 262 PTLY 265
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
175-471 |
9.94e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 67.32 E-value: 9.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIG---------ALTYF 245
Cdd:PRK07787 131 ALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTAD-DVLVHGLPLFHVHGLVLGVLGPLRIGnrfvhtgrpTPEAY 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 246 AQADALKGTLvstlkevkptvFIGVPQIWEKIHEmvKKNSAKSMglkkkafvwarnigfkvnskkmlgkyntpvsyRMAK 325
Cdd:PRK07787 210 AQALSEGGTL-----------YFGVPTVWSRIAA--DPEAARAL--------------------------------RGAR 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 326 TLVfskvktslgldhchsfiSGTAPLNQETAEFFLSLD-IPIGELYGLSES--------SGPHtisnqnnyRLLSCGKIL 396
Cdd:PRK07787 245 LLV-----------------SGSAALPVPVFDRLAALTgHRPVERYGMTETlitlstraDGER--------RPGWVGLPL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 397 TGCKNMLFQQN-----KDG--IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITA 469
Cdd:PRK07787 300 AGVETRLVDEDggpvpHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRESTDLIKS 379
|
..
gi 1008909320 470 GG 471
Cdd:PRK07787 380 GG 381
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
166-488 |
1.24e-11 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 68.03 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 166 IESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLSHiaaqmmdiwvpikigaltyf 245
Cdd:PRK08633 776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNL-RNDDVILSSLPFFH-------------------- 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 246 aqADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMgLKKKAF--VWARNIgfKVNsKKMLGkyntpvSYRM 323
Cdd:PRK08633 835 --SFGLTVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATIL-LGTPTFlrLYLRNK--KLH-PLMFA------SLRL 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 324 AktlvfskvktslgldhchsfISGTAPLNQETAEFF-LSLDIPIGELYGLSESSGPHTISNQNnyRLLSCGKILTGCKN- 401
Cdd:PRK08633 903 V--------------------VAGAEKLKPEVADAFeEKFGIRILEGYGATETSPVASVNLPD--VLAADFKRQTGSKEg 960
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 402 ----------------MLFQQNKDGI-GEICLWGRHIFMGYLESETETTEAI---DDEGWLHSGDLGQLDGLGFLYVTGH 461
Cdd:PRK08633 961 svgmplpgvavrivdpETFEELPPGEdGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDR 1040
|
330 340 350
....*....|....*....|....*....|
gi 1008909320 462 IK---EIlitaGGENVPPIPVETLVKKKIP 488
Cdd:PRK08633 1041 YSrfaKI----GGEMVPLGAVEEELAKALG 1066
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
158-289 |
2.80e-11 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 66.01 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 158 PDTQLEQVIESQKA-------NQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIAAqM 230
Cdd:cd05930 72 PAERLAYILEDSGAklvltdpDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLT-PGDRVLQFTSFSFDVS-V 149
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1008909320 231 MDIWVPIKIGALTYFAQADALK--GTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSM 289
Cdd:cd05930 150 WEIFGALLAGATLVVLPEEVRKdpEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL 210
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
175-497 |
4.00e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 65.83 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGA-LTYFAQADALkg 253
Cdd:PRK06178 212 AALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGAtLVLLARWDAV-- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 254 TLVSTLKEVKPTVFIG-VPQIWEKI-HEMVKKNSAKSmgLKKK---AFVWARNIGFKVNSKKMLGKYNTPVSYRMAKTlv 328
Cdd:PRK06178 290 AFMAAVERYRVTRTVMlVDNAVELMdHPRFAEYDLSS--LRQVrvvSFVKKLNPDYRQRWRALTGSVLAEAAWGMTET-- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 329 fskvktslgldH-CHSFISG--TAPLNQETAEFFLSLDIPIGELYGLSESSGphtisnqnnyRLLSCGkiltgcknmlfq 405
Cdd:PRK06178 366 -----------HtCDTFTAGfqDDDFDLLSQPVFVGLPVPGTEFKICDFETG----------ELLPLG------------ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 406 qnkdGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITAgGENVPPIPVETLVKK 485
Cdd:PRK06178 413 ----AEGEIVVRTPSLLKGYWNKPEATAEALRD-GWLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GMSVFPSEVEALLGQ 486
|
330
....*....|..
gi 1008909320 486 KiPIISNAMLVG 497
Cdd:PRK06178 487 H-PAVLGSAVVG 497
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
175-483 |
5.42e-11 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 65.43 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNI--------TWIAGAVTKdfKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALtyfa 246
Cdd:PRK07059 207 AFLQYTGGTTGVSKGATLLHRNIvanvlqmeAWLQPAFEK--KPRPDQLNFVCALPLYHIFALTVCGLLGMRTGGR---- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 247 qadalkgtlvstlkevkpTVFIGVPQiweKIHEMVKKnsaksmgLKKKAFvwarNIGFKVNSkkmlgKYNTPVSYRMAKT 326
Cdd:PRK07059 281 ------------------NILIPNPR---DIPGFIKE-------LKKYQV----HIFPAVNT-----LYNALLNNPDFDK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 327 LVFSKVKTSLGldhchsfisGTAPLNQETAEFFLSLD-IPIGELYGLSESSgPHTISNQNNyrllscGKILTGCKNM--- 402
Cdd:PRK07059 324 LDFSKLIVANG---------GGMAVQRPVAERWLEMTgCPITEGYGLSETS-PVATCNPVD------ATEFSGTIGLplp 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 403 ---LFQQNKDG-------IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGE 472
Cdd:PRK07059 388 steVSIRDDDGndlplgePGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKD-MILVSGF 466
|
330
....*....|.
gi 1008909320 473 NVPPIPVETLV 483
Cdd:PRK07059 467 NVYPNEIEEVV 477
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
150-499 |
7.03e-11 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 64.86 E-value: 7.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 150 FMELGRSIPDTQLEQVIESQKAnqcAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTK----DFKLTDKHETVVSYLPLSH 225
Cdd:PLN02574 179 FYELIKEDFDFVPKPVIKQDDV---AAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfeasQYEYPGSDNVYLAALPMFH 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 226 IAAQMMDIWVPIKIG-ALTYFAQADAlkGTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksMGLKKKAfvwarnigf 304
Cdd:PLN02574 256 IYGLSLFVVGLLSLGsTIVVMRRFDA--SDMVKVIDRFKVTHFPVVPPIL--------------MALTKKA--------- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 305 kvnskkmlgkynTPVSYRMAKTLVfskvktslgldhchSFISGTAPLNQETAEFFLS----LDIPIGelYGLSESS--GP 378
Cdd:PLN02574 311 ------------KGVCGEVLKSLK--------------QVSCGAAPLSGKFIQDFVQtlphVDFIQG--YGMTESTavGT 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 379 HTISNQNNYRLLSCG--------KIL---TGCknMLFQQNKdgiGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDL 447
Cdd:PLN02574 363 RGFNTEKLSKYSSVGllapnmqaKVVdwsTGC--LLPPGNC---GELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDI 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1008909320 448 GQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKIPIISNAML-VGDK 499
Cdd:PLN02574 438 AYFDEDGYLYIVDRLKEI-IKYKGFQIAPADLEAVLISHPEIIDAAVTaVPDK 489
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
31-483 |
7.67e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 64.95 E-value: 7.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 31 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSaEWFITAVGAilAGGLCVGIYATNS-------AEVCQyvitHAKV 103
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNH-RGFVLALYA--AGKVGARIILLNTgfsgpqlAEVAA----REGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 104 NILLVenDQQLQKILSIPQSSLEPLKAIIQYRlpmkknnnlyswDDFMELGRSIPDtqLEQVIESQKAN-------QCAV 176
Cdd:PRK07788 148 KALVY--DDEFTDLLSALPPDLGRLRAWGGNP------------DDDEPSGSTDET--LDDLIAGSSTAplpkppkPGGI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 177 LIYTSGTTGIPKGVMLSHDNI-TWIAGAVTK-DFKltdKHETVVsylplshIAAQMMDIWvpikigALTYFAQADALKGT 254
Cdd:PRK07788 212 VILTSGTTGTPKGAPRPEPSPlAPLAGLLSRvPFR---AGETTL-------LPAPMFHAT------GWAHLTLAMALGST 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 255 LV--------STLKEV---KPTVFIGVPQIwekIHEMVKKnsaksmglkkkafvwarnigfkvnSKKMLGKYNTPvSYRM 323
Cdd:PRK07788 276 VVlrrrfdpeATLEDIakhKATALVVVPVM---LSRILDL------------------------GPEVLAKYDTS-SLKI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 324 AktlvfskvktslgldhchsFISG---TAPLNQETAEFFlsldipiGE----LYGLSESSGPhTISNQNNYRL--LSCGK 394
Cdd:PRK07788 328 I-------------------FVSGsalSPELATRALEAF-------GPvlynLYGSTEVAFA-TIATPEDLAEapGTVGR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 395 ILTGCKNMLFQQNKDGI-----GEICLWGRHIFMGYleSETETTEAIDdeGWLHSGDLGQLDGLGFLYVTGHIKEiLITA 469
Cdd:PRK07788 381 PPKGVTVKILDENGNEVprgvvGRIFVGNGFPFEGY--TDGRDKQIID--GLLSSGDVGYFDEDGLLFVDGRDDD-MIVS 455
|
490
....*....|....
gi 1008909320 470 GGENVPPIPVETLV 483
Cdd:PRK07788 456 GGENVFPAEVEDLL 469
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
5-271 |
9.44e-11 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 64.27 E-value: 9.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 5 EFFRESVNRFGTYPALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVG 84
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFED----QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 85 IYATNSAEVCQYVITHAKVNILLVendqqlqkilsipQSSLEPLKAIIQYRLPMKKNNnlyswddfmelGRSIPDTQLEQ 164
Cdd:cd17655 77 IDPDYPEERIQYILEDSGADILLT-------------QSHLQPPIAFIGLIDLLDEDT-----------IYHEESENLEP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 165 VIesqKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLShIAAQMMDIWVPIKIGA-LT 243
Cdd:cd17655 133 VS---KSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQ-GEHLRVALFASIS-FDASVTEIFASLLSGNtLY 207
|
250 260
....*....|....*....|....*....
gi 1008909320 244 YFAQADALKG-TLVSTLKEVKPTVFIGVP 271
Cdd:cd17655 208 IVRKETVLDGqALTQYIRQNRITIIDLTP 236
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
149-539 |
1.28e-10 |
|
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: 63.68 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 149 DFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNIT--WIAGAVTKDFKLTDKHETVVSylPlSHI 226
Cdd:cd05969 66 DRLENSEAKVLITTEELYERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIfyYFTGKYVLDLHPDDIYWCTAD--P-GWV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 227 AAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVfigvpqiwekihemvkknsaksmglkkkafvWarnigfkv 306
Cdd:cd05969 143 TGTVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTV-------------------------------W-------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 307 nskkmlgkYNTPVSYRMAKTLVFSKVKtSLGLDHCHSFISGTAPLNQETAEFFLS-LDIPIGELYGLSESsGPHTISNQ- 384
Cdd:cd05969 184 --------YTAPTAIRMLMKEGDELAR-KYDLSSLRFIHSVGEPLNPEAIRWGMEvFGVPIHDTWWQTET-GSIMIANYp 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 385 -NNYRLLSCGKILTGCKNMLFQQNKDGI-----GEICL---WGRhIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGF 455
Cdd:cd05969 254 cMPIKPGSMGKPLPGVKAAVVDENGNELppgtkGILALkpgWPS-MFRGIWNDEERYKNSFID-GWYLTGDLAYRDEDGY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 456 LYVTGHIKEILITAgGENVPPIPVETLVKKKiPIISNAMLVG--DKLK--FLSMLLTLKcemnqmSG-EPLDKLNFEAIN 530
Cdd:cd05969 332 FWFVGRADDIIKTS-GHRVGPFEVESALMEH-PAVAEAGVIGkpDPLRgeIIKAFISLK------EGfEPSDELKEEIIN 403
|
410
....*....|
gi 1008909320 531 FCR-GLGSQA 539
Cdd:cd05969 404 FVRqKLGAHV 413
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
58-275 |
1.45e-10 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 63.44 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 58 VGILGFNSAeWFITAVGAIL-AGGLCVGIYATNSAEVCQYVITHAKVNILLVenDQQLQkilsiPQSSLEPLKAIIqyrl 136
Cdd:TIGR01733 28 VAVLLERSA-ELVVAILAVLkAGAAYVPLDPAYPAERLAFILEDAGARLLLT--DSALA-----SRLAGLVLPVIL---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 137 pmkknnnlyswDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVTKDFKLTDkhE 215
Cdd:TIGR01733 96 -----------LDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLvNLLAWLARRYGLDPD--D 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1008909320 216 TVVSYLPLSHIAAqMMDIWVPIKIGALTYFAQADALKGTLVST---LKEVKPTVFIGVPQIWE 275
Cdd:TIGR01733 163 RVLQFASLSFDAS-VEEIFGALLAGATLVVPPEDEERDDAALLaalIAEHPVTVLNLTPSLLA 224
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
175-490 |
3.46e-10 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 62.84 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSH----DNITWIAGAVtkdfKLTDKHETVVSYLPLSHIAAQMMdIWVPikigaltyfaqadA 250
Cdd:PRK12476 196 SHLQYTSGSTRPPVGVEITHravgTNLVQMILSI----DLLDRNTHGVSWLPLYHDMGLSM-IGFP-------------A 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 251 LKG---TLVStlkevkPTVFIGVPQIWekIHEMVKKNSAKSM--GLKKKAFVWARNIGFKVN------SKKMLGKYNTPV 319
Cdd:PRK12476 258 VYGghsTLMS------PTAFVRRPQRW--IKALSEGSRTGRVvtAAPNFAYEWAAQRGLPAEgddidlSNVVLIIGSEPV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 320 SyrMAKTLVFSK-----------VKTSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSgPHTISNqnnyr 388
Cdd:PRK12476 330 S--IDAVTTFNKafapyglprtaFKPSYGIAEATLFVATIAPDAEPSVVYLDREQLGAGRAVRVAADA-PNAVAH----- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 389 lLSCGKIL-----------TGCknmlfqQNKDG-IGEICLWGRHIFMGYLE--SETETT----------------EAIDD 438
Cdd:PRK12476 402 -VSCGQVArsqwavivdpdTGA------ELPDGeVGEIWLHGDNIGRGYWGrpEETERTfgaklqsrlaegshadGAADD 474
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1008909320 439 EGWLHSGDLG-QLDGLgfLYVTGHIKEiLITAGGENVPPIPVETLVKKKIPII 490
Cdd:PRK12476 475 GTWLRTGDLGvYLDGE--LYITGRIAD-LIVIDGRNHYPQDIEATVAEASPMV 524
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
175-592 |
3.53e-10 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 62.97 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFK-LTDKHETVVSYLPLSHIaaqmmdiwvpikIGALTYFAQADALKG 253
Cdd:PRK08180 212 AKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPfLAEEPPVLVDWLPWNHT------------FGGNHNLGIVLYNGG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 254 TL---------------VSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAksmglkkkafvwarnigfkvnskkmlgkyntp 318
Cdd:PRK08180 280 TLyiddgkptpggfdetLRNLREISPTVYFNVPKGWEMLVPALERDAA-------------------------------- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 319 vsyrMAKTLvFSKVKtslgldhchSFISGTAPLNQETAEfflSLD----------IPIGELYGLSESSGPHTISNQNNYR 388
Cdd:PRK08180 328 ----LRRRF-FSRLK---------LLFYAGAALSQDVWD---RLDrvaeatcgerIRMMTGLGMTETAPSATFTTGPLSR 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 389 LLSCGKILTGCKNMLFQQnkDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQL-D----GLGFLYvTGHIK 463
Cdd:PRK08180 391 AGNIGLPAPGCEVKLVPV--GGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvDpadpERGLMF-DGRIA 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 464 EILITAGGE--NVPPIPVEtLVKKKIPIISNAMLVGDKLKFLSMLLtlkcemnqmsgepldklnFEAINFCRGLGSQAST 541
Cdd:PRK08180 468 EDFKLSSGTwvSVGPLRAR-AVSAGAPLVQDVVITGHDRDEIGLLV------------------FPNLDACRRLAGLLAD 528
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1008909320 542 VTEIVKQQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGEL 592
Cdd:PRK08180 529 ASLAEVLAHPAVRAAFRERLARLNAQATGSSTRVARALLLDEPPSLDAGEI 579
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
33-550 |
3.60e-10 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 62.83 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 33 FNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDq 112
Cdd:cd05915 27 YAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPN- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 113 qlqkILSIPQSSLEPLKAIIQYRLPMKKNNNlysWDDFMELGRsiPDTQleqviESQKANQC--AVLIYTSGTTGIPKGV 190
Cdd:cd05915 106 ----LLPLVEAIRGELKTVQHFVVMDEKAPE---GYLAYEEAL--GEEA-----DPVRVPERaaCGMAYTTGTTGLPKGV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 191 MLSHDNITWIAGAVTKDFKLTDKHETV-VSYLPLSHIAAQMMdIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIG 269
Cdd:cd05915 172 VYSHRALVLHSLAASLVDGTALSEKDVvLPVVPMFHVNAWCL-PYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 270 VPQIWEKIhemvkKNSAKSMglkKKAFVWARNIgfkvnskkMLGKYNTPVSYRMAKTLVFSKVKTSLGLDHCHSFisGTA 349
Cdd:cd05915 251 VPTVWLAL-----ADYLEST---GHRLKTLRRL--------VVGGSAAPRSLIARFERMGVEVRQGYGLTETSPV--VVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 350 PLNQETAEfflslDIPIGELYGLSESSGPHTISNQNNyrllscgkiLTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESE 429
Cdd:cd05915 313 NFVKSHLE-----SLSEEEKLTLKAKTGLPIPLVRLR---------VADEEGRPVPKDGKALGEVQLKGPWITGGYYGNE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 430 TETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKiPIISNAMLVG--DKLKFLSMLL 507
Cdd:cd05915 379 EATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDL-IKSGGEWISSVDLENALMGH-PKVKEAAVVAipHPKWQERPLA 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1008909320 508 TLKCEMNQMSGEpldklnfEAINFC-RGLGSQASTVTEIVKQQD 550
Cdd:cd05915 457 VVVPRGEKPTPE-------ELNEHLlKAGFAKWQLPDAYVFAEE 493
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
32-497 |
5.42e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 62.08 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 32 NFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVenD 111
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT--D 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 112 QQLQKILSIPQSSLEPLKAIIQY----RLPMKKNNNLYSWDDFMELGRSipDTQLEQVIESQKANQCavliYTSGTTGIP 187
Cdd:PRK06018 119 LTFVPILEKIADKLPSVERYVVLtdaaHMPQTTLKNAVAYEEWIAEADG--DFAWKTFDENTAAGMC----YTSGTTGDP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 188 KGVMLSH-DNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPiKIGALTYFAQADALKGTLVSTLKEVKPTV 266
Cdd:PRK06018 193 KGVLYSHrSNVLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAP-SMGTKLVMPGAKLDGASVYELLDTEKVTF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 267 FIGVPQIWEKIHEMVKKNSAKSMGLKKKAfvwarnIGFKVNSKKMLG---KYNTPV--SYRMAKTlvfSKVKTSLGLDHC 341
Cdd:PRK06018 272 TAGVPTVWLMLLQYMEKEGLKLPHLKMVV------CGGSAMPRSMIKafeDMGVEVrhAWGMTEM---SPLGTLAALKPP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 342 HSFISGTAPLN----QETAEFFLSLDipigelyglsessgphtISNQNNYRLLSCGKILtgcknmlfqqnkdgiGEICLW 417
Cdd:PRK06018 343 FSKLPGDARLDvlqkQGYPPFGVEMK-----------------ITDDAGKELPWDGKTF---------------GRLKVR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 418 GRHIFMGYLESETETteaIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKiPIISNAMLVG 497
Cdd:PRK06018 391 GPAVAAAYYRVDGEI---LDDDGFFDTGDVATIDAYGYMRITDRSKDV-IKSGGEWISSIDLENLAVGH-PKVAEAAVIG 465
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
411-497 |
7.13e-10 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 61.61 E-value: 7.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 411 IGEICLWGRHIFMGYLESETETteAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVKKKiPII 490
Cdd:PRK13295 392 IGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVIIR-GGENIPVVEIEALLYRH-PAI 467
|
....*..
gi 1008909320 491 SNAMLVG 497
Cdd:PRK13295 468 AQVAIVA 474
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
35-483 |
1.19e-09 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 61.01 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 35 QYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGL--CVGIYAtnSAEVCQYVITHAKVNILLVEN-- 110
Cdd:PLN02479 50 QTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVvnCVNIRL--NAPTIAFLLEHSKSEVVMVDQef 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 111 ----DQQLQKILSIPQSSLEPLKAII-----------QYRLpmkkNNNLYSWDDFMELGRsiPDTQLEQvieSQKANQCA 175
Cdd:PLN02479 128 ftlaEEALKILAEKKKSSFKPPLLIVigdptcdpkslQYAL----GKGAIEYEKFLETGD--PEFAWKP---PADEWQSI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 176 VLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAqmmdiWVpikigaltYFAQADALKGTL 255
Cdd:PLN02479 199 ALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEG-AVYLWTLPMFHCNG-----WC--------FTWTLAALCGTN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 256 VStLKEVKPTvfigvpqiweKIHEMVKKNSAKSMGlkkKAFVWARNIgfkvnskkmlgkYNTPVSyrmaktlvfskvKTS 335
Cdd:PLN02479 265 IC-LRQVTAK----------AIYSAIANYGVTHFC---AAPVVLNTI------------VNAPKS------------ETI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 336 LGLDH-CHSFISGTAPlnqeTAEFFLSLDIP---IGELYGLSESSGPHTISN----------QNNYRLLSCGKI----LT 397
Cdd:PLN02479 307 LPLPRvVHVMTAGAAP----PPSVLFAMSEKgfrVTHTYGLSETYGPSTVCAwkpewdslppEEQARLNARQGVryigLE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 398 GCKNMLFQQNK----DG--IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGG 471
Cdd:PLN02479 383 GLDVVDTKTMKpvpaDGktMGEIVMRGNMVMKGYLKNPKANEEAFAN-GWFHSGDLGVKHPDGYIEIKDRSKDIIIS-GG 460
|
490
....*....|..
gi 1008909320 472 ENVPPIPVETLV 483
Cdd:PLN02479 461 ENISSLEVENVV 472
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
5-241 |
4.53e-09 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 59.14 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 5 EFFRESVNRFGTYPALASKNGKkweiLNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEwFITAVGAIL-AGGLCV 83
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRS----LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPE-LVVALLAVLkAGAAYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 84 GIYATNSAEVCQYVITHAKVNILLVENdqqlqkilSIPQSSLEPLKAIIQYRLPMKKnnnlyswddfmelgrsiPDTQLE 163
Cdd:cd12117 76 PLDPELPAERLAFMLADAGAKVLLTDR--------SLAGRAGGLEVAVVIDEALDAG-----------------PAGNPA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1008909320 164 QVIEsqkANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVtkDFKLTDKHETVVSYLPLSHIAAqMMDIWVPIKIGA 241
Cdd:cd12117 131 VPVS---PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNT--NYVTLGPDDRVLQTSPLAFDAS-TFEIWGALLNGA 202
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
409-480 |
4.62e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 59.19 E-value: 4.62e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1008909320 409 DG--IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 480
Cdd:PRK08162 384 DGetIGEIMFRGNIVMKGYLKNPKATEEAFAG-GWFHTGDLAVLHPDGYIKIKDRSKDIIIS-GGENISSIEVE 455
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
159-470 |
8.05e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 58.42 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 159 DTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFkLTDKHE------TVVSYLPLSHIAAQMMD 232
Cdd:PRK05850 147 DSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDY-FGDTGGvpppdtTVVSWLPFYHDMGLVLG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 233 IWVPIKIGALTYfaqadalkgtLVStlkevkPTVFIGVPQIWekIHeMVKKNSAksmglkkkAFVWARNIGFKVNSKK-- 310
Cdd:PRK05850 226 VCAPILGGCPAV----------LTS------PVAFLQRPARW--MQ-LLASNPH--------AFSAAPNFAFELAVRKts 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 311 ---MLGkyntpvsyrmaktlvfskvktsLGLDHCHSFISGTAPLNQET--------AEFFLSlDIPIGELYGLSE----- 374
Cdd:PRK05850 279 dddMAG----------------------LDLGGVLGIISGSERVHPATlkrfadrfAPFNLR-ETAIRPSYGLAEatvyv 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 375 -----SSGPHTIS---------------NQNNYRLLSCG-------KILTGCKNMlfqQNKDG-IGEICLWGRHIFMGYL 426
Cdd:PRK05850 336 atrepGQPPESVRfdyeklsaghakrceTGGGTPLVSYGsprsptvRIVDPDTCI---ECPAGtVGEIWVHGDNVAAGYW 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1008909320 427 E--SETETT--EAIDD------EG-WLHSGDLGQLDGlGFLYVTGHIKEILITAG 470
Cdd:PRK05850 413 QkpEETERTfgATLVDpspgtpEGpWLRTGDLGFISE-GELFIVGRIKDLLIVDG 466
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
49-497 |
1.88e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 57.28 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 49 KLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITH--AKVNILLVE---------NDQQLQKI 117
Cdd:PRK08314 55 ECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDsgARVAIVGSElapkvapavGNLRLRHV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 118 LS------IPQSSLEPLKAIIQYR--LPMKKNNNLYSWDDFMELGRSIPDTQLeqviesqKANQCAVLIYTSGTTGIPKG 189
Cdd:PRK08314 135 IVaqysdyLPAEPEIAVPAWLRAEppLQALAPGGVVAWKEALAAGLAPPPHTA-------GPDDLAVLPYTSGTTGVPKG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 190 VMLSHDNItwIAGAVTKDFKLTDKHETVV-SYLPLSHIAAQMMDIWVPIKIGA-LTYFAQAD-ALKGTLVSTLkevKPTV 266
Cdd:PRK08314 208 CMHTHRTV--MANAVGSVLWSNSTPESVVlAVLPLFHVTGMVHSMNAPIYAGAtVVLMPRWDrEAAARLIERY---RVTH 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 267 figvpqiWEKIHEMVkknsaksmglkkkafvwarnIGFKVNSKkmLGKYNtpvsyrmaktlvFSKVKTSLGldhchsfis 346
Cdd:PRK08314 283 -------WTNIPTMV--------------------VDFLASPG--LAERD------------LSSLRYIGG--------- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 347 GTAPLNQETAEFFLSL-DIPIGELYGLSESSGPhTISNQNNYRLLSCGKILTgcknmlfqQNKDG--------------- 410
Cdd:PRK08314 313 GGAAMPEAVAERLKELtGLDYVEGYGLTETMAQ-THSNPPDRPKLQCLGIPT--------FGVDArvidpetleelppge 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 411 IGEICLWGRHIFMGYLESETETTEA---IDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKi 487
Cdd:PRK08314 384 VGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKR-MINASGFKVWPAEVENLLYKH- 461
|
490
....*....|
gi 1008909320 488 PIISNAMLVG 497
Cdd:PRK08314 462 PAIQEACVIA 471
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
30-483 |
3.89e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 56.36 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 30 ILNFNQYYEACRKAAKSLIKLGLERfhgVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVE 109
Cdd:PRK06334 45 KLSYNQVRKAVIALATKVSKYPDQH---IGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 110 ndQQLQKILSIPQSSLEPLKAIIQYRLPMKKNnnlYSWDDFMELG--RSIPDTQLEQV--IESQKANQCAVLIYTSGTTG 185
Cdd:PRK06334 122 --KQLMQHLAQTHGEDAEYPFSLIYMEEVRKE---LSFWEKCRIGiyMSIPFEWLMRWfgVSDKDPEDVAVILFTSGTEK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 186 IPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPT 265
Cdd:PRK06334 197 LPKGVPLTHANLLANQRACLKFFSPKED-DVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNPLYPKKIVEMIDEAKVT 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 266 VFIGVPQIWEKIHEMVKKNSAKSMGLKkkaFVWARNIGFKvnskkmlgkyntpvsyrmaktlvfskvktslgldhcHSfi 345
Cdd:PRK06334 276 FLGSTPVFFDYILKTAKKQESCLPSLR---FVVIGGDAFK------------------------------------DS-- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 346 sgtapLNQETAEFFLSLDIPIGelYGLSESSGPHTISNQNNYRLLSC-GKILTGCKNMLFQQ------NKDGIGEICLWG 418
Cdd:PRK06334 315 -----LYQEALKTFPHIQLRQG--YGTTECSPVITINTVNSPKHESCvGMPIRGMDVLIVSEetkvpvSSGETGLVLTRG 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1008909320 419 RHIFMGYL-ESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLV 483
Cdd:PRK06334 388 TSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSR-FVKIGAEMVSLEALESIL 452
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
29-198 |
4.01e-08 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 55.94 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 29 EILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEwFITAVGAIL-AGGLCVGIYATNSAEVCQYVITHAKVNILL 107
Cdd:cd17656 12 QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAE-MIVGILGILkAGGAFVPIDPEYPEERRIYIMLDSGVRVVL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 108 VENDQQlqkilsipqSSLEPLKAIIqyrlpmkknnnLYSWDDfmelgrsIPDTQLEQVIESQKANQCAVLIYTSGTTGIP 187
Cdd:cd17656 91 TQRHLK---------SKLSFNKSTI-----------LLEDPS-------ISQEDTSNIDYINNSDDLLYIIYTSGTTGKP 143
|
170
....*....|.
gi 1008909320 188 KGVMLSHDNIT 198
Cdd:cd17656 144 KGVQLEHKNMV 154
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
29-470 |
4.98e-08 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 55.89 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 29 EILNFNQYYEACRKAAKSLIKLGLERfhG--VGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNIL 106
Cdd:COG0365 38 RTLTYAELRREVNRFANALRALGVKK--GdrVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 107 LVENDQ-------QLQKILSIPQSSLEPLKAIIQYRLPMKKNN--NLYSWDDFMELGRSIPDTqleqviESQKANQCAVL 177
Cdd:COG0365 116 ITADGGlrggkviDLKEKVDEALEELPSLEHVIVVGRTGADVPmeGDLDWDELLAAASAEFEP------EPTDADDPLFI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 178 IYTSGTTGIPKGVMLSHdniTWIAGAVTKDFKLT-DKHE-------------TVVSYL---PLSHIAAQ-MMDiwvpiki 239
Cdd:COG0365 190 LYTSGTTGKPKGVVHTH---GGYLVHAATTAKYVlDLKPgdvfwctadigwaTGHSYIvygPLLNGATVvLYE------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 240 GALTYfaqADAlkGTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksMGLKKKAFVWARnigfkvnskkmlgKYNtpv 319
Cdd:COG0365 260 GRPDF---PDP--GRLWELIEKYGVTVFFTAPTAI--------------RALMKAGDEPLK-------------KYD--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 320 syrmaktlvFSKVKtslgldHChsfisGTA--PLNQETAEFFLS-LDIPIGELYGLSESSGpHTISnqnNYRLL-----S 391
Cdd:COG0365 305 ---------LSSLR------LL-----GSAgePLNPEVWEWWYEaVGVPIVDGWGQTETGG-IFIS---NLPGLpvkpgS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 392 CGKILTGCKNMLFqqNKDG-------IGEICL---W-GrhIFMGYLESETETTEAI--DDEGWLHSGDLGQLDGLGFLYV 458
Cdd:COG0365 361 MGKPVPGYDVAVV--DEDGnpvppgeEGELVIkgpWpG--MFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWI 436
|
490
....*....|..
gi 1008909320 459 TGHIKEILITAG 470
Cdd:COG0365 437 LGRSDDVINVSG 448
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
40-497 |
7.01e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 55.52 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 40 CRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYAT-NSAEVcQYVITHAKVNILLVE---NDQQLQ 115
Cdd:PRK06164 45 VDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRyRSHEV-AHILGRGRARWLVVWpgfKGIDFA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 116 KILS-IPQSSLEPLKAIIQYRLPMKKNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSH 194
Cdd:PRK06164 124 AILAaVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 195 DNITWIAGAVTKDFKLTDKHETVVSyLPLShiaaqmmdiwvpikiGALTYFAQADALKGtlvstlkevkptvfiGVPQIW 274
Cdd:PRK06164 204 ATLLRHARAIARAYGYDPGAVLLAA-LPFC---------------GVFGFSTLLGALAG---------------GAPLVC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 275 EKIHEMVKknSAKSMGLKKKAFVWARNIGFKvnskKMLGKYNTPVSYRMAKTLVFSkvktslgldhchSFISGTAplnqE 354
Cdd:PRK06164 253 EPVFDAAR--TARALRRHRVTHTFGNDEMLR----RILDTAGERADFPSARLFGFA------------SFAPALG----E 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 355 TAEFFLSLDIPIGELYGLSE-----SSGPHTISNQnnYRLLSCGKILTGCKNMLFQQNKDG-------IGEICLWGRHIF 422
Cdd:PRK06164 311 LAALARARGVPLTGLYGSSEvqalvALQPATDPVS--VRIEGGGRPASPEARVRARDPQDGallpdgeSGEIEIRAPSLM 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1008909320 423 MGYLESETETTEAIDDEGWLHSGDLGQLDGLG-FLYVT--GHIkeilITAGGENVPPIPVETLVkKKIPIISNAMLVG 497
Cdd:PRK06164 389 RGYLDNPDATARALTDDGYFRTGDLGYTRGDGqFVYQTrmGDS----LRLGGFLVNPAEIEHAL-EALPGVAAAQVVG 461
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
175-483 |
7.19e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 55.74 E-value: 7.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVTK-DFKLTDKhetVVSYLPLSHiaaqmmdiwvpiKIGaLTyfaqadalK 252
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLlANRAQVAARiDFSPEDK---VFNALPVFH------------SFG-LT--------G 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 253 GTLVSTLKEVkPTVFIGVPQIWEKIHEMVkknsaksmglkkkafvwarnigFKVNSKKMLG---------KYNTPVSYRM 323
Cdd:PRK06814 852 GLVLPLLSGV-KVFLYPSPLHYRIIPELI----------------------YDTNATILFGtdtflngyaRYAHPYDFRS 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 324 AKtLVFskvktslgldhchsfiSGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNM 402
Cdd:PRK06814 909 LR-YVF----------------AGAEKVKEETRQTWMEkFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYR 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 403 LfqQNKDGI---GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIK---EIlitaGGENVPP 476
Cdd:PRK06814 972 L--EPVPGIdegGRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKrfaKI----AGEMISL 1045
|
....*..
gi 1008909320 477 IPVETLV 483
Cdd:PRK06814 1046 AAVEELA 1052
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
41-480 |
7.37e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 55.48 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 41 RKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEndqqlqkilsi 120
Cdd:PRK07008 50 KQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD----------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 121 pqSSLEPLKAIIQYRLPMKKNNNLYSWDDFMELGrSIPDTQLEQVIESQKA---------NQCAVLIYTSGTTGIPKGVM 191
Cdd:PRK07008 119 --LTFLPLVDALAPQCPNVKGWVAMTDAAHLPAG-STPLLCYETLVGAQDGdydwprfdeNQASSLCYTSGTTGNPKGAL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 192 LSHDNITWIA-GAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIkIGALTYFAqADALKGTLVSTLKEVKPTVF-IG 269
Cdd:PRK07008 196 YSHRSTVLHAyGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLP-GPDLDGKSLYELIEAERVTFsAG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 270 VPQIWEKIHEMVKKNSAKSMGLKkkafvwarnigfkvnsKKMLGKYNTPVSyrMAKTLvfskvKTSLGLDHCHSF-ISGT 348
Cdd:PRK07008 274 VPTVWLGLLNHMREAGLRFSTLR----------------RTVIGGSACPPA--MIRTF-----EDEYGVEVIHAWgMTEM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 349 APLNQETAEFFLSLDIPIGELYGLSESSGpHTIsnqnnyrllsCG---KILTGCKNMLfqqNKDGI--GEICLWGRHIFM 423
Cdd:PRK07008 331 SPLGTLCKLKWKHSQLPLDEQRKLLEKQG-RVI----------YGvdmKIVGDDGREL---PWDGKafGDLQVRGPWVID 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1008909320 424 GYLESETETTeaidDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVE 480
Cdd:PRK07008 397 RYFRGDASPL----VDGWFPTGDVATIDADGFMQITDRSKDV-IKSGGEWISSIDIE 448
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
366-497 |
8.51e-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: 8.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 366 IGELYGLSESSGPHTISNQNnyrLL----SCGKILTGCKNMLfqqNKDG-------IGEICLWGRHIFMgYLESETETTE 434
Cdd:cd05929 272 IWEYYGGTEGQGLTIINGEE---WLthpgSVGRAVLGKVHIL---DEDGnevppgeIGEVYFANGPGFE-YTNDPEKTAA 344
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1008909320 435 AIDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETLVKKKiPIISNAMLVG 497
Cdd:cd05929 345 ARNEGGWSTLGDVGYLDEDGYLYLTDR-RSDMIISGGVNIYPQEIENALIAH-PKVLDAAVVG 405
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
2-592 |
1.15e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 54.67 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 2 TIPEFFRESVNRFGTYPALASKNG--KKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAG 79
Cdd:PRK12582 50 SIPHLLAKWAAEAPDRPWLAQREPghGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 80 GLCVGI---YATNSAEVCQ--YVITHAKVNILLVENDQQLQKILSIPQssLEPLKAIIQYRLPmkknnnlyswDD----- 149
Cdd:PRK12582 130 VPAAPVspaYSLMSHDHAKlkHLFDLVKPRVVFAQSGAPFARALAALD--LLDVTVVHVTGPG----------EGiasia 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 150 FMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSH----DNITWIAGavTKDFKLTDKHETVVSYLPLSH 225
Cdd:PRK12582 198 FADLAATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQrmmcANIAMQEQ--LRPREPDPPPPVSLDWMPWNH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 226 IAAQMMdIWVPIKIGALTYFAQAD----ALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAksmgLKKKAFvwaRN 301
Cdd:PRK12582 276 TMGGNA-NFNGLLWGGGTLYIDDGkplpGMFEETIRNLREISPTVYGNVPAGYAMLAEAMEKDDA----LRRSFF---KN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 302 IGfkvnskkmlgkyntpvsyRMAktlvfskvktslgldhchsfiSGTAPLNQETAEFFLSL-------DIPIGELYGLSE 374
Cdd:PRK12582 348 LR------------------LMA---------------------YGGATLSDDLYERMQALavrttghRIPFYTGYGATE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 375 SSGPHTISNQNNYRLLSCGKILTGCKNMLFQqnkdgIG---EICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQ-L 450
Cdd:PRK12582 389 TAPTTTGTHWDTERVGLIGLPLPGVELKLAP-----VGdkyEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARfV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 451 D------GLGFlyvTGHIKEILITAGGENVPPIPVET-LVKKKIPIISNAMLVGDKLKFLSMLLtlkcemnqmsgepldk 523
Cdd:PRK12582 464 DpddpekGLIF---DGRVAEDFKLSTGTWVSVGTLRPdAVAACSPVIHDAVVAGQDRAFIGLLA---------------- 524
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1008909320 524 lnFEAINFCRGLGSQASTVTEIVKqQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGEL 592
Cdd:PRK12582 525 --WPNPAACRQLAGDPDAAPEDVV-KHPAVLAILREGLSAHNAEAGGSSSRIARALLMTEPPSIDAGEI 590
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2-275 |
1.38e-07 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 54.86 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 2 TIPEFFRESVNRFGTYPALASKNGKkweiLNfnqYYEACRKA---AKSLIKLGLERFHGVGILGFNSAEwFITAVGAIL- 77
Cdd:COG1020 477 TLHELFEAQAARTPDAVAVVFGDQS----LT---YAELNARAnrlAHHLRALGVGPGDLVGVCLERSLE-MVVALLAVLk 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 78 AGGLCVGIYATNSAEVCQYVITHAKVNILLVenDQQLQKILsiPQSSLEPLkaiiqyrlpmkknnnlySWDDfmELGRSI 157
Cdd:COG1020 549 AGAAYVPLDPAYPAERLAYMLEDAGARLVLT--QSALAARL--PELGVPVL-----------------ALDA--LALAAE 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 158 PDTQLEQVIESQkanQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAqMMDIWVPI 237
Cdd:COG1020 606 PATNPPVPVTPD---DLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGP-GDRVLQFASLSFDAS-VWEIFGAL 680
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1008909320 238 KIGALTYFAQADALKGT--LVSTLKEVKPTVFIGVPQIWE 275
Cdd:COG1020 681 LSGATLVLAPPEARRDPaaLAELLARHRVTVLNLTPSLLR 720
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
175-475 |
1.42e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 54.35 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLSHIAAQMMdIWVPIKIGAltYFaqadalkgT 254
Cdd:PRK07769 183 AYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEG-QEGDRGVSWLPFFHDMGLIT-VLLPALLGH--YI--------T 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 255 LVStlkevkPTVFIGVPQIWekIHEMVKKNsaksmGLKKKAFVWARNIGFKVNSKKMLGKYNTPvsyrmaktlvfskvkt 334
Cdd:PRK07769 251 FMS------PAAFVRRPGRW--IRELARKP-----GGTGGTFSAAPNFAFEHAAARGLPKDGEP---------------- 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 335 SLGLDHCHSFISGTAPLNQETAEFFLSLDIPIG-------ELYGLSE-----SSGPHTISNQ---------NNYRLL--- 390
Cdd:PRK07769 302 PLDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGlpptaikPSYGMAEatlfvSTTPMDEEPTviyvdrdelNAGRFVevp 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 391 ----------SCGKIL-----------TGcknmlfQQNKDG-IGEICLWGRHIFMGYLESETETTE-------------- 434
Cdd:PRK07769 382 adapnavaqvSAGKVGvsewavivdpeTA------SELPDGqIGEIWLHGNNIGTGYWGKPEETAAtfqnilksrlsesh 455
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1008909320 435 ---AIDDEGWLHSGDLGQ-LDglGFLYVTGHIKEILITAGGENVP 475
Cdd:PRK07769 456 aegAPDDALWVRTGDYGVyFD--GELYITGRVKDLVIIDGRNHYP 498
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1-480 |
1.85e-07 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 53.99 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 1 MTIPEFFRESVNRFGTYPaLASKNGKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGG 80
Cdd:PRK06155 21 RTLPAMLARQAERYPDRP-LLVFGGTRW---TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 81 LCVGIYATNSAEVCQYVITHAKVNILLVENDqqlqkilsipqsSLEPLKAIIQYRLPMKK-----NNNLYSWDDFMELGR 155
Cdd:PRK06155 97 IAVPINTALRGPQLEHILRNSGARLLVVEAA------------LLAALEAADPGDLPLPAvwlldAPASVSVPAGWSTAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 156 SIPDTQLEQVIESQKANQCAVLiYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMdiwv 235
Cdd:PRK06155 165 LPPLDAPAPAAAVQPGDTAAIL-YTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGAD-DVLYTTLPLFHTNALNA---- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 236 pikigaltyFAQADALKGTLVSTlkevkptvfigvpqiwekihemvKKNSAKSMglkkkafvWARnigfkvnskkmLGKY 315
Cdd:PRK06155 239 ---------FFQALLAGATYVLE-----------------------PRFSASGF--------WPA-----------VRRH 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 316 NTPVSY---RMAKTLVFSKVKTSlglDHCHSFISGTAP--LNQETAEFFLSLDIPIGELYGLSESSGP--HTISNQnnyR 388
Cdd:PRK06155 268 GATVTYllgAMVSILLSQPARES---DRAHRVRVALGPgvPAALHAAFRERFGVDLLDGYGSTETNFViaVTHGSQ---R 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 389 LLSCGKILTGCKNMLFQQNKDGI-----GEICLWGR--HIFM-GYLESETETTEAIDDEgWLHSGDLGQLDGLGFLYVTG 460
Cdd:PRK06155 342 PGSMGRLAPGFEARVVDEHDQELpdgepGELLLRADepFAFAtGYFGMPEKTVEAWRNL-WFHTGDRVVRDADGWFRFVD 420
|
490 500
....*....|....*....|
gi 1008909320 461 HIKEIlITAGGENVPPIPVE 480
Cdd:PRK06155 421 RIKDA-IRRRGENISSFEVE 439
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
173-497 |
2.26e-07 |
|
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: 53.67 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 173 QCAVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVTKDFKLTDKHETVVSYLPLSHIaaqmmdiwvpikIGALTYFAQADAL 251
Cdd:cd05923 151 QPAFVFYTSGTTGLPKGAVIPQRAAeSRVLFMSTQAGLRHGRHNVVLGLMPLYHV------------IGFFAVLVAALAL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 252 KGTLVsTLKEVKPtvfigvpqiwekihemvkknsaksmglkKKAFVWarnigfkVNSKKMLGKYNTPVSYrmaKTLVFSK 331
Cdd:cd05923 219 DGTYV-VVEEFDP----------------------------ADALKL-------IEQERVTSLFATPTHL---DALAAAA 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 332 VKTSLGLDHCHSFISGTAPLNQ---ETAEFFLSldIPIGELYGLSESSgpHTISNQN-------------NYRLLSCGki 395
Cdd:cd05923 260 EFAGLKLSSLRHVTFAGATMPDavlERVNQHLP--GEKVNIYGTTEAM--NSLYMRDartgtemrpgffsEVRIVRIG-- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 396 ltGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVP 475
Cdd:cd05923 334 --GSPDEALANGEEGELIVAAAADAAFTGYLNQPEATAKKLQD-GWYRTGDVGYVDPSGDVRILGRVDDMIIS-GGENIH 409
|
330 340
....*....|....*....|..
gi 1008909320 476 PIPVETLVKKKiPIISNAMLVG 497
Cdd:cd05923 410 PSEIERVLSRH-PGVTEVVVIG 430
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
170-490 |
2.41e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 170 KANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKL-TDKHETVVSYLPLSHiaaqmmDIWVpikIGALtyfaqa 248
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIdLNPDDVIVSWLPLYH------DMGL---IGGL------ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 249 dalkgtlvstlkeVKPtVFIGVPQIwekihemvkknsaksmgLKKKAFVWARnigfKVNSKKMLGKYNTPVS------YR 322
Cdd:PRK05691 229 -------------LQP-IFSGVPCV-----------------LMSPAYFLER----PLRWLEAISEYGGTISggpdfaYR 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 323 MAKTLVFSKVKTSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIG-------ELYGLSESS----------GPHTIS--- 382
Cdd:PRK05691 274 LCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGfdpdsffASYGLAEATlfvsggrrgqGIPALElda 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 383 ---NQNNYR------LLSCGK------ILTGCKNMLFQQNKDGIGEICLWGRHIFMGYL---ESETETTEAIDDEGWLHS 444
Cdd:PRK05691 354 ealARNRAEpgtgsvLMSCGRsqpghaVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWrnpEASAKTFVEHDGRTWLRT 433
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1008909320 445 GDLGQLDGlGFLYVTGHIKEILITAgGENVPPIPVETLVKKKIPII 490
Cdd:PRK05691 434 GDLGFLRD-GELFVTGRLKDMLIVR-GHNLYPQDIEKTVEREVEVV 477
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
96-472 |
2.66e-07 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 53.63 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 96 YVITHAKVNILLVenDQQLQKILSIPQSSLEPLKAII--------QYRLPMKKNNNLYSWDDFMElGRSI----PDtqle 163
Cdd:PRK05620 105 HIINHAEDEVIVA--DPRLAEQLGEILKECPCVRAVVfigpsdadSAAAHMPEGIKVYSYEALLD-GRSTvydwPE---- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 164 qviesQKANQCAVLIYTSGTTGIPKGVMLSHDNItWIAGA---VTKDFKLTDKhETVVSYLPLSHIAAqmmdiW-VPIKI 239
Cdd:PRK05620 178 -----LDETTAAAICYSTGTTGAPKGVVYSHRSL-YLQSLslrTTDSLAVTHG-ESFLCCVPIYHVLS-----WgVPLAA 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 240 ---GALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLkKKAFV------------WARNIGF 304
Cdd:PRK05620 246 fmsGTPLVFPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSL-QEIYVggsavppilikaWEERYGV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 305 KVNSkkmlgkyntpvSYRMAKTLVFSKVKtslgldHCHSFISGTAPLNqetaefflsldipigelYGLSESSGPHTIsnq 384
Cdd:PRK05620 325 DVVH-----------VWGMTETSPVGTVA------RPPSGVSGEARWA-----------------YRVSQGRFPASL--- 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 385 nNYRLLSCGKILTGcknmlfqqNKDGIGEICLWGRHIFMGYLESETETT---------EAIDDE-------GWLHSGDLG 448
Cdd:PRK05620 368 -EYRIVNDGQVMES--------TDRNEGEIQVRGNWVTASYYHSPTEEGggaastfrgEDVEDAndrftadGWLRTGDVG 438
|
410 420
....*....|....*....|....
gi 1008909320 449 QLDGLGFLYVTGHIKEIlITAGGE 472
Cdd:PRK05620 439 SVTRDGFLTIHDRARDV-IRSGGE 461
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
410-483 |
3.40e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 53.09 E-value: 3.40e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1008909320 410 GIGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGlGFLYVTGHIKEiLITAGGENVPPIPVETLV 483
Cdd:PRK09192 410 VVGHICVRGPSLMSGYFRDE-ESQDVLAADGWLDTGDLGYLLD-GYLYITGRAKD-LIIINGRNIWPQDIEWIA 480
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-497 |
3.79e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 52.38 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 177 LIYTSGTTGIPKGVMLSHDNI-------TWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDiwvpikiGALTYFAQAD 249
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIfrmlmggADFGTGEFTPSEDAH-KAAAAAAGTVMFPAPPLMH-------GTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 250 ALKGTLVstlkeVKPTVFIGVPQIWEKIHEMvkknsaksmglkkkafvwarnigfKVNSKKMLGKyntpvsyRMAKTLV- 328
Cdd:cd05924 80 LLGGQTV-----VLPDDRFDPEEVWRTIEKH------------------------KVTSMTIVGD-------AMARPLId 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 329 -FSKVKTsLGLDHCHSFISGTAPLNQETAEFFLSL--DIPIGELYGLSESSGPHTISNQNN------YRLLSCGKILTGC 399
Cdd:cd05924 124 aLRDAGP-YDLSSLFAISSGGALLSPEVKQGLLELvpNITLVDAFGSSETGFTGSGHSAGSgpetgpFTRANPDTVVLDD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 400 KNMLFQQNKDGIGEICLWGrHIFMGYLESETETTEA---IDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPP 476
Cdd:cd05924 203 DGRVVPPGSGGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGR-GSVCINTGGEKVFP 280
|
330 340
....*....|....*....|.
gi 1008909320 477 IPVETLVKKKiPIISNAMLVG 497
Cdd:cd05924 281 EEVEEALKSH-PAVYDVLVVG 300
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
160-481 |
3.90e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 52.85 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 160 TQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHiaaqmmDIwvpiki 239
Cdd:PRK05851 140 TNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSWLPLYH------DM------ 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 240 gALTyFAQADALKGTlvsTLKEVKPTVFIGVPQIWekihemvkknsAKSMGLKKKAFVWARNIGFKvnskkMLGKYNTPV 319
Cdd:PRK05851 208 -GLA-FLLTAALAGA---PLWLAPTTAFSASPFRW-----------LSWLSDSRATLTAAPNFAYN-----LIGKYARRV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 320 SYRMAKTLVFSkvktslgldhchsfISGTAPLNQETAEFFLSLDIPIG-------ELYGLSESSGPHTIS---------- 382
Cdd:PRK05851 267 SDVDLGALRVA--------------LNGGEPVDCDGFERFATAMAPFGfdagaaaPSYGLAESTCAVTVPvpgiglrvde 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 383 -----NQNNYRLLSCGKILTG------CKNMLFQQNKDGIGEICLWGRHIFMGYLESETetteaIDDEGWLHSGDLGQLd 451
Cdd:PRK05851 333 vttddGSGARRHAVLGNPIPGmevrisPGDGAAGVAGREIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTGDLGYL- 406
|
330 340 350
....*....|....*....|....*....|
gi 1008909320 452 GLGFLYVTGHIKEiLITAGGENVPPIPVET 481
Cdd:PRK05851 407 VDGGLVVCGRAKE-LITVAGRNIFPTEIER 435
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
408-497 |
5.28e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 52.47 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 408 KDGIGEICLWGRHIFMGYLeSETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETlVKKKI 487
Cdd:PRK07638 330 KGEIGTVYVKSPQFFMGYI-IGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILF-GGINIFPEEIES-VLHEH 406
|
90
....*....|
gi 1008909320 488 PIISNAMLVG 497
Cdd:PRK07638 407 PAVDEIVVIG 416
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-241 |
7.79e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 52.65 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 7 FRESVNRFGTYPALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWfITAVGAIL-AGGLCVGI 85
Cdd:PRK12316 517 FEEQVERTPEAPALAFGE----ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEM-VVALLAILkAGGAYVPL 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 86 YATNSAEVCQYVITHAKVNILLveNDQQLQKILSIPQSSLEPLKAIIQYRLPMKKNNNlyswddfmelgrsiPDTQLEqv 165
Cdd:PRK12316 592 DPEYPAERLAYMLEDSGVQLLL--SQSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEEN--------------PGTELN-- 653
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1008909320 166 iesqkANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLShIAAQMMDIWVPIKIGA 241
Cdd:PRK12316 654 -----PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGL-GVGDTVLQKTPFS-FDVSVWEFFWPLMSGA 722
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
362-483 |
1.43e-06 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 51.15 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 362 LDIPIGELYGLSESSG------PHTISNQNNyrllSCGKILTGCKNMLFQQNkdgIGEICLWGRHIFMGYLEsetettEA 435
Cdd:PRK07445 253 LQLRLAPTYGMTETASqiatlkPDDFLAGNN----SSGQVLPHAQITIPANQ---TGNITIQAQSLALGYYP------QI 319
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1008909320 436 IDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLV 483
Cdd:PRK07445 320 LDSQGIFETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAI 366
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
171-497 |
2.06e-06 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 50.51 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 171 ANQCAVLIYTSGTTGIPKGVMlsHdnitwiagavtkdfkltdKHETVVSYLPLSHIAAQMMDiwvpiKIGALtYFAQAD- 249
Cdd:cd05971 87 SDDPALIIYTSGTTGPPKGAL--H------------------AHRVLLGHLPGVQFPFNLFP-----RDGDL-YWTPADw 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 250 ALKGTLVSTLKevkPTVFIGVPQIwekIHEMVKKNSAKSMglkkkafvwarnigfkvnskKMLGKYN------TPVSYRM 323
Cdd:cd05971 141 AWIGGLLDVLL---PSLYFGVPVL---AHRMTKFDPKAAL--------------------DLMSRYGvttaflPPTALKM 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 324 AKtlvFSKVKTSLGLDHCHSFISGTAPLNQE-TAEFFLSLDIPIGELYGLSESSgpHTISNQNNY---RLLSCGKILTGC 399
Cdd:cd05971 195 MR---QQGEQLKHAQVKLRAIATGGESLGEElLGWAREQFGVEVNEFYGQTECN--LVIGNCSALfpiKPGSMGKPIPGH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 400 KNMLFQQN-----KDGIGEICLW--GRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGE 472
Cdd:cd05971 270 RVAIVDDNgtplpPGEVGEIAVElpDPVAFLGYWNNP-SATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDV-ITSSGY 347
|
330 340
....*....|....*....|....*
gi 1008909320 473 NVPPIPVETLVKKKiPIISNAMLVG 497
Cdd:cd05971 348 RIGPAEIEECLLKH-PAVLMAAVVG 371
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
39-196 |
2.20e-06 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 50.35 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 39 ACRKAAKsLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKIL 118
Cdd:cd12114 22 ARRVAGA-LKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDGPDAQLDVA 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1008909320 119 sIPQSSLEPLKAIIQyrlpmkknnnlyswddfmelgrsiPDTQLEQVIESQkanQCAVLIYTSGTTGIPKGVMLSHDN 196
Cdd:cd12114 101 -VFDVLILDLDALAA------------------------PAPPPPVDVAPD---DLAYVIFTSGSTGTPKGVMISHRA 150
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
404-480 |
2.30e-06 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 50.53 E-value: 2.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1008909320 404 FQQNKDG-IGEICLWGRHIFMGYLESETETTEaiddEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 480
Cdd:PRK13382 383 FREVPTGeVGTIFVRNDTQFDGYTSGSTKDFH----DGFMASGDVGYLDENGRLFVVGRDDE-MIVSGGENVYPIEVE 455
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
164-212 |
3.00e-06 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 50.23 E-value: 3.00e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1008909320 164 QVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTD 212
Cdd:cd05918 98 KVVLTSSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTS 146
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
411-497 |
3.49e-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: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 411 IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVkKKIPII 490
Cdd:cd05920 335 EGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKD-QINRGGEKIAAEEVENLL-LRHPAV 412
|
....*..
gi 1008909320 491 SNAMLVG 497
Cdd:cd05920 413 HDAAVVA 419
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
411-497 |
3.64e-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: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 411 IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKiPII 490
Cdd:COG1021 380 VGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKD-QINRGGEKIAAEEVENLLLAH-PAV 457
|
....*..
gi 1008909320 491 SNAMLVG 497
Cdd:COG1021 458 HDAAVVA 464
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
152-497 |
4.06e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 49.77 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 152 ELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQM- 230
Cdd:cd05910 65 NLKQCLQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALg 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 231 MDIWVPikigALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEmvkknsaksmglkkkafvWARNIGFKVNSKK 310
Cdd:cd05910 145 LTSVIP----DMDPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVAR------------------YCAQHGITLPSLR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 311 MLGKYNTPVsyRMAKTLVFSK-------VKTSLGLDHC--------HSFISGTAPLNQETAEFFLSLDIPIGELYGLSES 375
Cdd:cd05910 203 RVLSAGAPV--PIALAARLRKmlsdeaeILTPYGATEAlpvssigsRELLATTTAATSGGAGTCVGRPIPGVRVRIIEID 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 376 SGPhtISNQNNYRLLSCGkiltgcknmlfqqnkdGIGEICLWGRHIFMGYLESETETTEA-IDDEG---WLHSGDLGQLD 451
Cdd:cd05910 281 DEP--IAEWDDTLELPRG----------------EIGEITVTGPTVTPTYVNRPVATALAkIDDNSegfWHRMGDLGYLD 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1008909320 452 GLGFLYVTGHIKEILITAGGeNVPPIPVETlVKKKIPIISNAMLVG 497
Cdd:cd05910 343 DEGRLWFCGRKAHRVITTGG-TLYTEPVER-VFNTHPGVRRSALVG 386
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
175-211 |
4.11e-06 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 49.56 E-value: 4.11e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT 211
Cdd:cd17652 96 AYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVG 132
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
128-241 |
5.17e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 49.21 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 128 LKAIIQYRLPMKKNNNLYSW--------DDFMELGRSIPDTQLEQVIESQKANQC----AVLIYTSGTTGIPKGVMLSHD 195
Cdd:cd05938 88 LQEAVEEVLPALRADGVSVWylshtsntEGVISLLDKVDAASDEPVPASLRAHVTikspALYIYTSGTTGLPKAARISHL 167
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1008909320 196 NItWIAGAVTKDFKLTdKHETVVSYLPLSHIAAQMMDIWVPIKIGA 241
Cdd:cd05938 168 RV-LQCSGFLSLCGVT-ADDVIYITLPLYHSSGFLLGIGGCIELGA 211
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
38-236 |
5.19e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 49.29 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 38 EACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEV---------CQYVITHAKVNILLv 108
Cdd:PRK07867 37 GSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAAlardiahadCQLVLTESAHAELL- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 109 enDQQLQKILSIPQSSLEPLKAIIQYRlpmkknnnlyswDDFMELGRSIPDTQLeqviesqkanqcaVLIYTSGTTGIPK 188
Cdd:PRK07867 116 --DGLDPGVRVINVDSPAWADELAAHR------------DAEPPFRVADPDDLF-------------MLIFTSGTSGDPK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1008909320 189 GVMLSHDNITWIAGAVTKDFKLTdkhETVVSYL--PLSHIAAQMMDiWVP 236
Cdd:PRK07867 169 AVRCTHRKVASAGVMLAQRFGLG---PDDVCYVsmPLFHSNAVMAG-WAV 214
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
170-198 |
7.56e-06 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 48.84 E-value: 7.56e-06
10 20
....*....|....*....|....*....
gi 1008909320 170 KANQCAVLIYTSGTTGIPKGVMLSHDNIT 198
Cdd:cd17653 103 SPDDLAYIIFTSGSTGIPKGVMVPHRGVL 131
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
18-211 |
8.30e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 49.39 E-value: 8.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 18 PALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYV 97
Cdd:PRK12467 529 PALVFGE----QVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYM 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 98 ITHAKVNILLveNDQQLQKILSIPqssleplkaiiqyrlpmkknnnlyswDDFMELGRSIPDTQLEQVIE-----SQKAN 172
Cdd:PRK12467 605 LDDSGVRLLL--TQSHLLAQLPVP--------------------------AGLRSLCLDEPADLLCGYSGhnpevALDPD 656
|
170 180 190
....*....|....*....|....*....|....*....
gi 1008909320 173 QCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT 211
Cdd:PRK12467 657 NLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLA 695
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
178-233 |
9.98e-06 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 48.58 E-value: 9.98e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1008909320 178 IYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIAAQMMDI 233
Cdd:cd05939 110 IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMR-PEDVVYDCLPLYHSAGGIMGV 164
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
171-212 |
1.04e-05 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 48.46 E-value: 1.04e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1008909320 171 ANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTD 212
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNE 133
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
31-263 |
1.54e-05 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 47.85 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 31 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEn 110
Cdd:cd17650 13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLTQ- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 111 dqqlqkilsipqssleplkaiiqyrlpmkknnnlyswddfmelgrsiPDtqleqviesqkanQCAVLIYTSGTTGIPKGV 190
Cdd:cd17650 92 -----------------------------------------------PE-------------DLAYVIYTSGTTGKPKGV 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1008909320 191 MLSHDNITWIAGAVTKDFKLTDKhetvvsylplSHIAAQMMDIWVPIKIGAltyFAQADALKGTLVSTLKEVK 263
Cdd:cd17650 112 MVEHRNVAHAAHAWRREYELDSF----------PVRLLQMASFSFDVFAGD---FARSLLNGGTLVICPDEVK 171
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
2-228 |
1.75e-05 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 47.95 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 2 TIPEFFRESVNRFGTYPALASkNGKKWEILNFNQYyeaCRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGl 81
Cdd:PRK08279 38 SLGDVFEEAAARHPDRPALLF-EDQSISYAELNAR---ANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGA- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 82 CVGIYATN-SAEVCQYVITHAKVNILLVENDQqLQKILSIPQsslEPLKAIIQYRLPMKKNNNLYSWDDFMELGRSIPDT 160
Cdd:PRK08279 113 VVALLNTQqRGAVLAHSLNLVDAKHLIVGEEL-VEAFEEARA---DLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTT 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1008909320 161 QLEqVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNIT----WIAGavtkdfkLTDKHETVVSY--LPLSHIAA 228
Cdd:PRK08279 189 NPA-SRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLkamgGFGG-------LLRLTPDDVLYccLPLYHNTG 254
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
58-274 |
2.03e-05 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 47.29 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 58 VGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDqqlqkilsipqsSLEPLKAIIqyrlp 137
Cdd:cd12116 40 VAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDDA------------LPDRLPAGL----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 138 mkknnnlyswdDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT--DKHE 215
Cdd:cd12116 103 -----------PVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGpgDRLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1008909320 216 TVVSYlpLSHIAAqmMDIWVPIKIGALTYFAQADALK--GTLVSTLKEVKPTVFIGVPQIW 274
Cdd:cd12116 172 AVTTY--AFDISL--LELLLPLLAGARVVIAPRETQRdpEALARLIEAHSITVMQATPATW 228
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
38-237 |
2.04e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 47.33 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 38 EACRKAAkSLIKL--GLERFHgVGILGFNSAEwFITAV-GAILAGGLCVGIYATN-----SAEV----CQYVITHAK--- 102
Cdd:PRK13388 35 EAAARAA-ALIALadPDRPLH-VGVLLGNTPE-MLFWLaAAALGGYVLVGLNTTRrgaalAADIrradCQLLVTDAEhrp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 103 ---------VNILLVENDQQLQKILsiPQSSLEPLKAIIqyrlpmkknnnlyswddfmelgrsiPDTQLeqviesqkanq 173
Cdd:PRK13388 112 lldgldlpgVRVLDVDTPAYAELVA--AAGALTPHREVD-------------------------AMDPF----------- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1008909320 174 caVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdkhETVVSYL--PLSHIAAqMMDIWVPI 237
Cdd:PRK13388 154 --MLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLT---RDDVCYVsmPLFHSNA-VMAGWAPA 213
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
168-488 |
2.19e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 47.40 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 168 SQKANQCAVLIYTSGTTGIPKGVMLSHDN-------ITWIAgavtkDFKLTDKhetVVSYLPLSHIAAQMMDIWVPIKIG 240
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSllanveqIKTIA-----DFTPNDR---FMSALPLFHSFGLTVGLFTPLLTG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 241 AltyfaqadalkgtlvstlkevkpTVFIgvpqiwekihemvkknsaksmglkkkafvwarnigfkvnskkmlgkYNTPVS 320
Cdd:PRK08043 433 A-----------------------EVFL----------------------------------------------YPSPLH 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 321 YRMAKTLVFSK-----VKTSLGLDHCHSF------------ISGTAPLNQETAEFFL-SLDIPIGELYGLSESSGPHTIS 382
Cdd:PRK08043 444 YRIVPELVYDRnctvlFGTSTFLGNYARFanpydfarlryvVAGAEKLQESTKQLWQdKFGLRILEGYGVTECAPVVSIN 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 383 NQNNYRLLSCGKILTGCKNMLFqqNKDGI---GEICLWGRHIFMGYLESE---------TETTEAIDDEGWLHSGDLGQL 450
Cdd:PRK08043 524 VPMAAKPGTVGRILPGMDARLL--SVPGIeqgGRLQLKGPNIMNGYLRVEkpgvlevptAENARGEMERGWYDTGDIVRF 601
|
330 340 350
....*....|....*....|....*....|....*...
gi 1008909320 451 DGLGFLYVTGHIKEILITAgGENVPPIPVETLVKKKIP 488
Cdd:PRK08043 602 DEQGFVQIQGRAKRFAKIA-GEMVSLEMVEQLALGVSP 638
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
7-194 |
2.37e-05 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 47.34 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 7 FRESVNRFGTYPALASkNGKKWEilnfnqYYEACRKA---AKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCV 83
Cdd:cd17651 1 FERQAARTPDAPALVA-EGRRLT------YAELDRRAnrlAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 84 GIYATNSAEVCQYVITHAKVNILLVENDqqlqkilsiPQSSLEPLKAIIqyrlpmkknnnlysWDDFMELGRSIPDTqlE 163
Cdd:cd17651 74 PLDPAYPAERLAFMLADAGPVLVLTHPA---------LAGELAVELVAV--------------TLLDQPGAAAGADA--E 128
|
170 180 190
....*....|....*....|....*....|.
gi 1008909320 164 QVIESQKANQcAVLIYTSGTTGIPKGVMLSH 194
Cdd:cd17651 129 PDPALDADDL-AYVIYTSGSTGRPKGVVMPH 158
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
159-197 |
3.72e-05 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 46.62 E-value: 3.72e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1008909320 159 DTQLEQVIESQKanQCAVLIYTSGTTGIPKGVMLSHDNI 197
Cdd:cd17648 83 DTGARVVITNST--DLAYAIYTSGTTGKPKGVLVEHGSV 119
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
178-210 |
3.85e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 46.43 E-value: 3.85e-05
10 20 30
....*....|....*....|....*....|...
gi 1008909320 178 IYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKL 210
Cdd:PRK04813 149 IFTSGTTGKPKGVQISHDNLVSFTNWMLEDFAL 181
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
29-482 |
5.32e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 46.22 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 29 EILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEwFITAVGAILAGGL---CVGIYATnsAEVCQYVITHAKVNI 105
Cdd:PRK13391 23 EVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLR-YLEVCWAAERSGLyytCVNSHLT--PAEAAYIVDDSGARA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 106 LLVENDQqlqkiLSIPQSSLEPLKAIiQYRLPMKKNNNLYSWDDFMELGRSIPDTqleqVIESQKANQcaVLIYTSGTTG 185
Cdd:PRK13391 100 LITSAAK-----LDVARALLKQCPGV-RHRLVLDGDGELEGFVGYAEAVAGLPAT----PIADESLGT--DMLYSSGTTG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 186 IPKGVM--LSHDNI---TWIAGAVTKDFKLTDkhETVvsYL---PLSHIAAQMmdiWVPIKIgaltyfaqadALKGTLVs 257
Cdd:PRK13391 168 RPKGIKrpLPEQPPdtpLPLTAFLQRLWGFRS--DMV--YLspaPLYHSAPQR---AVMLVI----------RLGGTVI- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 258 TLKEVKPTVFIGVPQIWEKIHEMVkknsAKSMglkkkaFVwarnigfkvnskKMLgkyNTPVSYRMAKTLvfSKVKTSlg 337
Cdd:PRK13391 230 VMEHFDAEQYLALIEEYGVTHTQL----VPTM------FS------------RML---KLPEEVRDKYDL--SSLEVA-- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 338 ldhchsfISGTAPLNQETAEFFLSLDIP-IGELYGLSESSGPHTI-SNQNNYRLLSCGKILTGCKNMLFQQNKD----GI 411
Cdd:PRK13391 281 -------IHAAAPCPPQVKEQMIDWWGPiIHEYYAATEGLGFTACdSEEWLAHPGTVGRAMFGDLHILDDDGAElppgEP 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1008909320 412 GEICLWGRHIFMgYLESETETTEAID-DEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETL 482
Cdd:PRK13391 354 GTIWFEGGRPFE-YLNDPAKTAEARHpDGTWSTVGDIGYVDEDGYLYLTDR-AAFMIISGGVNIYPQEAENL 423
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
391-495 |
6.06e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 46.14 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 391 SCGKILTGCKNMLFQQNKDGIGEIcLWGRHIFMGYLESETETT---EAIDDeGWLHSGDLGQLDGLGFLYVTGHiKEILI 467
Cdd:PRK13383 346 TVGKPVAGCPVRILDRNNRPVGPR-VTGRIFVGGELAGTRYTDgggKAVVD-GMTSTGDMGYLDNAGRLFIVGR-EDDMI 422
|
90 100
....*....|....*....|....*...
gi 1008909320 468 TAGGENVPPIPVETLVKKKIPIISNAML 495
Cdd:PRK13383 423 ISGGENVYPRAVENALAAHPAVADNAVI 450
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
159-211 |
8.41e-05 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 45.50 E-value: 8.41e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1008909320 159 DTQLeQVIESQKANqCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT 211
Cdd:cd17644 95 DAQI-SVLLTQPEN-LAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGIT 145
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
42-190 |
8.56e-05 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 45.46 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 42 KAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEND--QQLQKIL- 118
Cdd:PRK12406 23 RAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADllHGLASALp 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1008909320 119 -SIPQSSLEPLKAIIQ-YRLP---MKKNNNLYSWDDFMELGRSIPDTQLEQViesqkanqcAVLIYTSGTTGIPKGV 190
Cdd:PRK12406 103 aGVTVLSVPTPPEIAAaYRISpalLTPPAGAIDWEGWLAQQEPYDGPPVPQP---------QSMIYTSGTTGHPKGV 170
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
19-212 |
8.58e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 45.66 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 19 ALASKNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAE-VCQYV 97
Cdd:PRK04319 62 ALRYLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEaVRDRL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 98 -ITHAKVnilLVENDQQLQKIlsiPQSSLEPLKAIIQYRLPMKKNNNLYSWDDFMELGrsipDTQLEqvIESQKANQCAV 176
Cdd:PRK04319 142 eDSEAKV---LITTPALLERK---PADDLPSLKHVLLVGEDVEEGPGTLDFNALMEQA----SDEFD--IEWTDREDGAI 209
|
170 180 190
....*....|....*....|....*....|....*...
gi 1008909320 177 LIYTSGTTGIPKGVMLSHDNIT--WIAGAVTKDFKLTD 212
Cdd:PRK04319 210 LHYTSGSTGKPKGVLHVHNAMLqhYQTGKYVLDLHEDD 247
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
168-211 |
1.08e-04 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 45.05 E-value: 1.08e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1008909320 168 SQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT 211
Cdd:cd17649 90 THHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLT 133
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
44-230 |
1.11e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 45.26 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 44 AKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGI-YATNSAEVcQYVITHAKVNILLVEnDQQLQKILSIPq 122
Cdd:PRK07798 42 AHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnYRYVEDEL-RYLLDDSDAVALVYE-REFAPRVAEVL- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 123 SSLEPLKAIIQYrlpmkknnnlyswDDFMELGRSIPDTQLEQVIESQKANQCAV--------LIYTSGTTGIPKGVMLSH 194
Cdd:PRK07798 119 PRLPKLRTLVVV-------------EDGSGNDLLPGAVDYEDALAAGSPERDFGerspddlyLLYTGGTTGMPKGVMWRQ 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1008909320 195 DNItWIAGAVTKDF----KLTDKHETVVSYL-----------PLSHIAAQM 230
Cdd:PRK07798 186 EDI-FRVLLGGRDFatgePIEDEEELAKRAAagpgmrrfpapPLMHGAGQW 235
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
158-197 |
1.13e-04 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 44.96 E-value: 1.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1008909320 158 PDTQLEQVIESQKAnqcAVLIYTSGTTGIPKGVMLSHDNI 197
Cdd:cd17646 127 PATPPLVPPRPDNL---AYVIYTSGSTGRPKGVMVTHAGI 163
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
175-230 |
1.30e-04 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 44.65 E-value: 1.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNItWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQM 230
Cdd:cd05940 84 ALYIYTSGTTGLPKAAIISHRRA-WRGGAFFAGSGGALPSDVLYTCLPLYHSTALI 138
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
171-207 |
1.90e-04 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 44.23 E-value: 1.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1008909320 171 ANQCAVLIYTSGTTGIPKGVMLSHDN----ITWIAGAVTKD 207
Cdd:cd12115 104 PDDLAYVIYTSGSTGRPKGVAIEHRNaaafLQWAAAAFSAE 144
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
5-259 |
2.43e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.56 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 5 EFFRESVNRFGTYPALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVG 84
Cdd:PRK12316 3061 RLFEEQVERTPDAVALAFGE----QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVP 3136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 85 IYATNSAEVCQYVITHAKVNILLVendqqlQKILSIPQSsleplkaiiqyrlpmKKNNNLYSWDDFMELGRSIPDTQLEq 164
Cdd:PRK12316 3137 LDPEYPEERLAYMLEDSGAQLLLS------QSHLRLPLA---------------QGVQVLDLDRGDENYAEANPAIRTM- 3194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 165 viesqkANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIAAQMMDIWVPIKIGALTY 244
Cdd:PRK12316 3195 ------PENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLG-VGDRVLQFTTFSFDVFVEELFWPLMSGARVVL 3267
|
250
....*....|....*
gi 1008909320 245 FAQADALKGTLVSTL 259
Cdd:PRK12316 3268 AGPEDWRDPALLVEL 3282
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
36-194 |
3.47e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.18 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 36 YYEACRKA---AKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDq 112
Cdd:PRK12316 2031 YAELDSRAnrlAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRH- 2109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 113 qLQKILSIPQSSLeplkaiiqyRLPMKKNNNLYSWDDFMELGRSIPDTqleqviesqkanqCAVLIYTSGTTGIPKGVML 192
Cdd:PRK12316 2110 -LLERLPLPAGVA---------RLPLDRDAEWADYPDTAPAVQLAGEN-------------LAYVIYTSGSTGLPKGVAV 2166
|
..
gi 1008909320 193 SH 194
Cdd:PRK12316 2167 SH 2168
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
175-208 |
5.46e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 43.23 E-value: 5.46e-04
10 20 30
....*....|....*....|....*....|....
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDF 208
Cdd:PRK05691 2336 AYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERF 2369
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
177-249 |
6.29e-04 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 42.50 E-value: 6.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008909320 177 LIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHEtvvsYLPLSHIAAQMM--DIWVPIKIGALTYFAQAD 249
Cdd:cd17647 114 LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDK----FTMLSGIAHDPIqrDMFTPLFLGAQLLVPTQD 184
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
36-242 |
9.42e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 42.46 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 36 YYEACRKA---AKSLIKLGL--ERFhgVGILGFNSAEwFITAVGAIL-AGGLCVGIYATNSAEVCQYVITHAKVNILLVE 109
Cdd:PRK12467 3123 YAELNRRAnrlAHRLIAIGVgpDVL--VGVAVERSVE-MIVALLAVLkAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQ 3199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 110 ndqqlqkilsipQSSLEplkaiiqyRLPMKKNNNLYSWDDFMELGrsIPDTQLEQVIESQkanQCAVLIYTSGTTGIPKG 189
Cdd:PRK12467 3200 ------------AHLLE--------QLPAPAGDTALTLDRLDLNG--YSENNPSTRVMGE---NLAYVIYTSGSTGKPKG 3254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1008909320 190 VMLSHDNIT----WIAGAvtkdfKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGAL 242
Cdd:PRK12467 3255 VGVRHGALAnhlcWIAEA-----YELDANDRVLLFMSFSFDGAQERFLWTLICGGCL 3306
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
423-480 |
1.53e-03 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 41.53 E-value: 1.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1008909320 423 MGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 480
Cdd:PRK05857 386 LGYWNNPERTAEVLID-GWVNTGDLLERREDGFFYIKGRSSEMIIC-GGVNIAPDEVD 441
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
175-197 |
1.70e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 41.57 E-value: 1.70e-03
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
175-228 |
1.92e-03 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 40.88 E-value: 1.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1008909320 175 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAA 228
Cdd:cd05937 90 AILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNG-DRTYTCMPLYHGTA 142
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
36-197 |
2.09e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 41.30 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 36 YYEACRKA---AKSLIKLGLERFHGVGILGFNSAEwFITAVGAIL-AGGLCVGIYATNSAEVCQYVITHAKVNILLVend 111
Cdd:PRK12467 1602 YGELNRRAnrlAHRLIALGVGPEVLVGIAVERSLE-MVVGLLAILkAGGAYVPLDPEYPRERLAYMIEDSGIELLLT--- 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 112 qqlqkilsipQSSLEPlkaiiqyRLPMKKNNNLYSWDDFMELGRSIPDTQLEQVIESQkanQCAVLIYTSGTTGIPKGVM 191
Cdd:PRK12467 1678 ----------QSHLQA-------RLPLPDGLRSLVLDQEDDWLEGYSDSNPAVNLAPQ---NLAYVIYTSGSTGRPKGAG 1737
|
....*.
gi 1008909320 192 LSHDNI 197
Cdd:PRK12467 1738 NRHGAL 1743
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
177-266 |
2.28e-03 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 41.20 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008909320 177 LIYTSGTTGIPKGVMLSHDNIT----WIAgavtKDFKLTDKHEtvvsYLPLSHIAAQMM--DIWVPIKIGALTYFAQADA 250
Cdd:TIGR03443 420 LSFTSGSEGIPKGVLGRHFSLAyyfpWMA----KRFGLSENDK----FTMLSGIAHDPIqrDMFTPLFLGAQLLVPTADD 491
|
90
....*....|....*...
gi 1008909320 251 L--KGTLVSTLKEVKPTV 266
Cdd:TIGR03443 492 IgtPGRLAEWMAKYGATV 509
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
171-197 |
2.86e-03 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 40.62 E-value: 2.86e-03
10 20
....*....|....*....|....*..
gi 1008909320 171 ANQCAVLIYTSGTTGIPKGVMLSHDNI 197
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNL 129
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
409-480 |
4.28e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 40.05 E-value: 4.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1008909320 409 DGIGEIC-LWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILiTAGGENVPPIPVE 480
Cdd:PRK07867 350 EAIGELVnTAGPGGFEGYYNDPEADAERMRG-GVYWSGDLAYRDADGYAYFAGRLGDWM-RVDGENLGTAPIE 420
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
412-480 |
5.64e-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: 5.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1008909320 412 GEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVE 480
Cdd:cd17636 190 GEIVARGPTVMAGYWNRPEVNARRTRG-GWHHTNDLGRREPDGSLSFVGP-KTRMIKSGAENIYPAEVE 256
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
425-482 |
6.30e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 39.50 E-value: 6.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1008909320 425 YLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETL 482
Cdd:PRK08276 354 YHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDR-KSDMIISGGVNIYPQEIENL 410
|
|
| |
