NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|574584557|ref|NP_001276107|]
View 

long-chain-fatty-acid--CoA ligase ACSBG2 isoform a [Homo sapiens]

Protein Classification

bubblegum family long-chain-fatty-acid--CoA ligase( domain architecture ID 10149260)

bubblegum family long-chain-fatty-acid--CoA ligase catalyzes the conversion of fatty acids such as long-chain and very long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
73-665 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: 1108.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  73 KNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAK 152
Cdd:cd05933    1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 153 VNILLVENDQQLQKILSIpQSSLEPLKAIIQYRLPMK-KNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTS 231
Cdd:cd05933   81 ANILVVENQKQLQKILQI-QDKLPHLKAIIQYKEPLKeKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 232 GTTGIPKGVMLSHDNITWIAGAVTKDFKL---TDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVST 308
Cdd:cd05933  160 GTTGMPKGVMLSHDNITWTAKAASQHMDLrpaTVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKGTLVKT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 309 LKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGL 388
Cdd:cd05933  240 LREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLFYRLAKKLVFKKVRKALGL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 389 DHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGIGEICLWG 468
Cdd:cd05933  320 DRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGIGEICFWG 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 469 RHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKIPIISNAMLVGD 548
Cdd:cd05933  400 RHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPIISNAMLIGD 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 549 KLKFLSMLLTLKCEMNQMSGEPLDKLNFEAINFCRGLGSQASTVTEIVKQQDPLVYKAIQQGINAVNQEAMNNAQRIEKW 628
Cdd:cd05933  480 KRKFLSMLLTLKCEVNPETGEPLDELTEEAIEFCRKLGSQATRVSEIAGGKDPKVYEAIEEGIKRVNKKAISNAQKIQKW 559
                        570       580       590
                 ....*....|....*....|....*....|....*..
gi 574584557 629 VILEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 665
Cdd:cd05933  560 VILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
 
Name Accession Description Interval E-value
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
73-665 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: 1108.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  73 KNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAK 152
Cdd:cd05933    1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 153 VNILLVENDQQLQKILSIpQSSLEPLKAIIQYRLPMK-KNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTS 231
Cdd:cd05933   81 ANILVVENQKQLQKILQI-QDKLPHLKAIIQYKEPLKeKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 232 GTTGIPKGVMLSHDNITWIAGAVTKDFKL---TDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVST 308
Cdd:cd05933  160 GTTGMPKGVMLSHDNITWTAKAASQHMDLrpaTVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKGTLVKT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 309 LKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGL 388
Cdd:cd05933  240 LREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLFYRLAKKLVFKKVRKALGL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 389 DHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGIGEICLWG 468
Cdd:cd05933  320 DRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGIGEICFWG 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 469 RHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKIPIISNAMLVGD 548
Cdd:cd05933  400 RHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPIISNAMLIGD 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 549 KLKFLSMLLTLKCEMNQMSGEPLDKLNFEAINFCRGLGSQASTVTEIVKQQDPLVYKAIQQGINAVNQEAMNNAQRIEKW 628
Cdd:cd05933  480 KRKFLSMLLTLKCEVNPETGEPLDELTEEAIEFCRKLGSQATRVSEIAGGKDPKVYEAIEEGIKRVNKKAISNAQKIQKW 559
                        570       580       590
                 ....*....|....*....|....*....|....*..
gi 574584557 629 VILEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 665
Cdd:cd05933  560 VILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
48-665 0e+00

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 549.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  48 ETPMTIPEFFRESVNRFGTYPALASKNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAIL 127
Cdd:COG1022    8 PPADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 128 AGGLCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKILSIpQSSLEPLKAIIQY-RLPMKKNNNLYSWDDFMELGRS 206
Cdd:COG1022   88 AGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV-RDELPSLRHIVVLdPRGLRDDPRLLSLDELLALGRE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 207 I-PDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWV 285
Cdd:COG1022  167 VaDPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGP-GDRTLSFLPLAHVFERTVSYYA 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 286 pIKIGALTYFAQADAlkgTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKY 365
Cdd:COG1022  246 -LAAGATVAFAESPD---TLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARLAGKS 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 366 NTP---VSYRMAKTLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSC 442
Cdd:COG1022  322 PSLllrLKHALADKLVFSKLREALG-GRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRIGTV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 443 GKILTGCKNMLfqqnkDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGE 522
Cdd:COG1022  401 GPPLPGVEVKI-----AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGK 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 523 NVPPIPVETLVkKKIPIISNAMLVGDKLKFLSMLLTlkcemnqmsgepldkLNFEAI-NFCRGLGSQASTVTEIVkqQDP 601
Cdd:COG1022  476 NVAPQPIENAL-KASPLIEQAVVVGDGRPFLAALIV---------------PDFEALgEWAEENGLPYTSYAELA--QDP 537
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574584557 602 LVYKAIQQGINAVNQEaMNNAQRIEKWVILEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 665
Cdd:COG1022  538 EVRALIQEEVDRANAG-LSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALY 600
AMP-binding pfam00501
AMP-binding enzyme;
57-519 1.57e-77

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 253.39  E-value: 1.57e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557   57 FRESVNRFGTYPALaskNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIY 136
Cdd:pfam00501   1 LERQAARTPDKTAL---EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  137 ATNSAEVCQYVITHAKVNILLVENDQQLQKILSIPQSSLEPLKAIIQYRLPMKKNNNLYSWDDfmelgrsiPDTQLEQVI 216
Cdd:pfam00501  78 PRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAK--------PADVPPPPP 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  217 ESQKANQCAVLIYTSGTTGIPKGVMLSHDNI----TWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGA- 291
Cdd:pfam00501 150 PPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLvanvLSIKRVRPRGFGLGP-DDRVLSTLPLFHDFGLSLGLLGPLLAGAt 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  292 LTYFAQADALKGT-LVSTLKEVKPTVFIGVPQIWEKIhemvkknsaksmglkkkafvwarnigfkvnskkmlgkyntpVS 370
Cdd:pfam00501 229 VVLPPGFPALDPAaLLELIERYKVTVLYGVPTLLNML-----------------------------------------LE 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  371 YRMAKTLVFSKVKTslgldhchsFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNYRLL---SCGKIL 446
Cdd:pfam00501 268 AGAPKRALLSSLRL---------VLSGGAPLPPELARRFRElFGGALVNGYGLTETTGVVTTPLPLDEDLRslgSVGRPL 338
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574584557  447 TGCK------NMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITA 519
Cdd:pfam00501 339 PGTEvkivddETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
PLN02736 PLN02736
long-chain acyl-CoA synthetase
28-665 3.88e-59

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 210.34  E-value: 3.88e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  28 WTTCRDGEVLLRLSKHGPGHETPMTIPEFFRESVNRFGTYPALASK---NGK----KWeiLNFNQYYEAcRKAAKS-LIK 99
Cdd:PLN02736  21 WNVYRSARSPLKLVSRFPDHPEIGTLHDNFVYAVETFRDYKYLGTRirvDGTvgeyKW--MTYGEAGTA-RTAIGSgLVQ 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 100 LGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVeNDQQLQKILSIpQSSLEPLK 179
Cdd:PLN02736  98 HGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSC-LSEIPSVR 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 180 AIIQY--------RLPMKKNNNLYSWDDFMELGRSIPdtqleQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDN-ITWI 250
Cdd:PLN02736 176 LIVVVggadeplpSLPSGTGVEIVTYSKLLAQGRSSP-----QPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNlIANV 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 251 AGA-VTKDFKLTDKHetvVSYLPLSHI---AAQMMDIWVPIKIGaltyFAQADALKgtLVSTLKEVKPTVFIGVPQIWEK 326
Cdd:PLN02736 251 AGSsLSTKFYPSDVH---ISYLPLAHIyerVNQIVMLHYGVAVG----FYQGDNLK--LMDDLAALRPTIFCSVPRLYNR 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 327 IHEMVKKNSAKSMGLKKKAFvwarNIGFkvNSKK---MLGKYNTPvsyrMAKTLVFSKVKTSLGlDHCHSFISGTAPLNQ 403
Cdd:PLN02736 322 IYDGITNAVKESGGLKERLF----NAAY--NAKKqalENGKNPSP----MWDRLVFNKIKAKLG-GRVRFMSSGASPLSP 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 404 ETAEFflsLDIPIG----ELYGLSESSGPHTISNQNNYrllSCGKI----------LTGCKNMLFqQNKDGI---GEICL 466
Cdd:PLN02736 391 DVMEF---LRICFGgrvlEGYGMTETSCVISGMDEGDN---LSGHVgspnpacevkLVDVPEMNY-TSEDQPyprGEICV 463
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 467 WGRHIFMGYLESETETTEAIDDEGWLHSGDLGQ-LDGlGFLYVTGHIKEILITAGGENVPPIPVETlVKKKIPIISNAML 545
Cdd:PLN02736 464 RGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLwLPG-GRLKIIDRKKNIFKLAQGEYIAPEKIEN-VYAKCKFVAQCFV 541
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 546 VGDKLKflSMLLTLkcemnqMSGEPLDKLNFEAINfcrglGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEAMNNAQRI 625
Cdd:PLN02736 542 YGDSLN--SSLVAV------VVVDPEVLKAWAASE-----GIKYEDLKQLCN--DPRVRAAVLADMDAVGREAQLRGFEF 606
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|.
gi 574584557 626 EKWVILEKD-FSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 665
Cdd:PLN02736 607 AKAVTLVPEpFTVENGLLTPTFKVKRPQAKAYFAKAISDMY 647
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
81-547 2.63e-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: 2.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557   81 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILlVEN 160
Cdd:TIGR03098  26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL-VTS 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  161 DQQLQKILSIPQSSLEPLKAII----QYRLPMKKNNNLYSWDDFMELGRSIPdtqLEQVIESQkanqCAVLIYTSGTTGI 236
Cdd:TIGR03098 105 SERLDLLHPALPGCHDLRTLIIvgdpAHASEGHPGEEPASWPKLLALGDADP---PHPVIDSD----MAAILYTSGSTGR 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  237 PKGVMLSHDNItwIAGA--VTKDFKLTDKhETVVSYLPLSHIAA--QMMDIWVpikIGA----LTYFAQADALKgtlvsT 308
Cdd:TIGR03098 178 PKGVVLSHRNL--VAGAqsVATYLENRPD-DRLLAVLPLSFDYGfnQLTTAFY---VGAtvvlHDYLLPRDVLK-----A 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  309 LKEVKPTVFIGVPQIWEKIHEMVKKNSAksmglkkkafvwARNIGFKVNSKKmlgkyntpvsyRMAKTLVfSKVKTSLGL 388
Cdd:TIGR03098 247 LEKHGITGLAAVPPLWAQLAQLDWPESA------------APSLRYLTNSGG-----------AMPRATL-SRLRSFLPN 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  389 dhchsfisgtaplnqetAEFFLsldipigeLYGLSESSGPHTISNQN-NYRLLSCGKILTGCKNMLFqqNKDG------- 460
Cdd:TIGR03098 303 -----------------ARLFL--------MYGLTEAFRSTYLPPEEvDRRPDSIGKAIPNAEVLVL--REDGsecapge 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  461 IGEICLWGRHIFMGYLESETETTEAI------DDEGWLH-----SGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPV 529
Cdd:TIGR03098 356 EGELVHRGALVAMGYWNDPEKTAERFrplppfPGELHLPelavwSGDTVRRDEEGFLYFVGR-RDEMIKTSGYRVSPTEV 434
                         490
                  ....*....|....*...
gi 574584557  530 ETlVKKKIPIISNAMLVG 547
Cdd:TIGR03098 435 EE-VAYATGLVAEAVAFG 451
 
Name Accession Description Interval E-value
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
73-665 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: 1108.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  73 KNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAK 152
Cdd:cd05933    1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 153 VNILLVENDQQLQKILSIpQSSLEPLKAIIQYRLPMK-KNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTS 231
Cdd:cd05933   81 ANILVVENQKQLQKILQI-QDKLPHLKAIIQYKEPLKeKEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYTS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 232 GTTGIPKGVMLSHDNITWIAGAVTKDFKL---TDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVST 308
Cdd:cd05933  160 GTTGMPKGVMLSHDNITWTAKAASQHMDLrpaTVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKGTLVKT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 309 LKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGL 388
Cdd:cd05933  240 LREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLFYRLAKKLVFKKVRKALGL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 389 DHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGIGEICLWG 468
Cdd:cd05933  320 DRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGIGEICFWG 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 469 RHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKIPIISNAMLVGD 548
Cdd:cd05933  400 RHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPIISNAMLIGD 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 549 KLKFLSMLLTLKCEMNQMSGEPLDKLNFEAINFCRGLGSQASTVTEIVKQQDPLVYKAIQQGINAVNQEAMNNAQRIEKW 628
Cdd:cd05933  480 KRKFLSMLLTLKCEVNPETGEPLDELTEEAIEFCRKLGSQATRVSEIAGGKDPKVYEAIEEGIKRVNKKAISNAQKIQKW 559
                        570       580       590
                 ....*....|....*....|....*....|....*..
gi 574584557 629 VILEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 665
Cdd:cd05933  560 VILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
48-665 0e+00

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 549.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  48 ETPMTIPEFFRESVNRFGTYPALASKNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAIL 127
Cdd:COG1022    8 PPADTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 128 AGGLCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKILSIpQSSLEPLKAIIQY-RLPMKKNNNLYSWDDFMELGRS 206
Cdd:COG1022   88 AGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV-RDELPSLRHIVVLdPRGLRDDPRLLSLDELLALGRE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 207 I-PDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWV 285
Cdd:COG1022  167 VaDPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGP-GDRTLSFLPLAHVFERTVSYYA 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 286 pIKIGALTYFAQADAlkgTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKY 365
Cdd:COG1022  246 -LAAGATVAFAESPD---TLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARLAGKS 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 366 NTP---VSYRMAKTLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSC 442
Cdd:COG1022  322 PSLllrLKHALADKLVFSKLREALG-GRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRIGTV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 443 GKILTGCKNMLfqqnkDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGE 522
Cdd:COG1022  401 GPPLPGVEVKI-----AEDGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGK 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 523 NVPPIPVETLVkKKIPIISNAMLVGDKLKFLSMLLTlkcemnqmsgepldkLNFEAI-NFCRGLGSQASTVTEIVkqQDP 601
Cdd:COG1022  476 NVAPQPIENAL-KASPLIEQAVVVGDGRPFLAALIV---------------PDFEALgEWAEENGLPYTSYAELA--QDP 537
                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574584557 602 LVYKAIQQGINAVNQEaMNNAQRIEKWVILEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 665
Cdd:COG1022  538 EVRALIQEEVDRANAG-LSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALY 600
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
78-653 1.30e-139

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: 1.30e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  78 WEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILL 157
Cdd:cd05907    3 WQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 158 VENdqqlqkilsipqssleplkaiiqyrlpmkknnnlyswddfmelgrsiPDtqleqviesqkanQCAVLIYTSGTTGIP 237
Cdd:cd05907   83 VED-----------------------------------------------PD-------------DLATIIYTSGTTGRP 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 238 KGVMLSHDNITWIAGAVTkDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADAlkgTLVSTLKEVKPTVF 317
Cdd:cd05907  103 KGVMLSHRNILSNALALA-ERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAE---TLLDDLSEVRPTVF 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 318 IGVPQIWEKIHEMVKKnsAKSMGLKKKAFVWArnigfkvnskkMLGKyntpvsyrmaktlvfskvktslgldhCHSFISG 397
Cdd:cd05907  179 LAVPRVWEKVYAAIKV--KAVPGLKRKLFDLA-----------VGGR--------------------------LRFAASG 219
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 398 TAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKnmlFQQNKDGigEICLWGRHIFMGYLE 477
Cdd:cd05907  220 GAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVE---VRIADDG--EILVRGPNVMLGYYK 294
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 478 SETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISNAMLVGDKLKFLSMLL 557
Cdd:cd05907  295 NPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKAS-PLISQAVVIGDGRPFLVALI 373
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 558 TLKCEMNQMSGEPldklnfeainfcrgLGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEaMNNAQRIEKWVILEKDFSI 637
Cdd:cd05907  374 VPDPEALEAWAEE--------------HGIAYTDVAELAA--NPAVRAEIEAAVEAANAR-LSRYEQIKKFLLLPEPFTI 436
                        570
                 ....*....|....*.
gi 574584557 638 YGGELGPMMKLKRHFV 653
Cdd:cd05907  437 ENGELTPTLKLKRPVI 452
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
77-665 1.12e-86

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: 281.80  E-value: 1.12e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  77 KWEILNFNQYYEACRKAAKSLIKLGLERFHG--VGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVN 154
Cdd:cd05927    2 PYEWISYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEIS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 155 ILLVENDQqlqkilsipqssleplkaiiqyrlpmkknnNLYSWDDFMELGRSIPdtqlEQVIESqKANQCAVLIYTSGTT 234
Cdd:cd05927   82 IVFCDAGV------------------------------KVYSLEEFEKLGKKNK----VPPPPP-KPEDLATICYTSGTT 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 235 GIPKGVMLSHDNI-TWIAGA--VTKDFKLTDKHETVVSYLPLSHIAAQMMdIWVPIKIGALTYFAQADALKgtLVSTLKE 311
Cdd:cd05927  127 GNPKGVMLTHGNIvSNVAGVfkILEILNKINPTDVYISYLPLAHIFERVV-EALFLYHGAKIGFYSGDIRL--LLDDIKA 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 312 VKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNigFKVNSKKMLGKYNTPVSYRmaktLVFSKVKTSLGLdHC 391
Cdd:cd05927  204 LKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALN--YKLAELRSGVVRASPFWDK----LVFNKIKQALGG-NV 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 392 HSFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNML--------FQQNKDGIG 462
Cdd:cd05927  277 RLMLTGSAPLSPEVLEFLRVaLGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLvdvpemnyDAKDPNPRG 356
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 463 EICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISN 542
Cdd:cd05927  357 EVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARS-PFVAQ 435
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 543 AMLVGDKLKflSMLLTLKCemnqmsgepldkLNFEAI-NFCRGLGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEamNN 621
Cdd:cd05927  436 IFVYGDSLK--SFLVAIVV------------PDPDVLkEWAASKGGGTGSFEELCK--NPEVKKAILEDLVRLGKE--NG 497
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*..
gi 574584557 622 AQRIE--KWVILEKD-FSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 665
Cdd:cd05927  498 LKGFEqvKAIHLEPEpFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
AMP-binding pfam00501
AMP-binding enzyme;
57-519 1.57e-77

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 253.39  E-value: 1.57e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557   57 FRESVNRFGTYPALaskNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIY 136
Cdd:pfam00501   1 LERQAARTPDKTAL---EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  137 ATNSAEVCQYVITHAKVNILLVENDQQLQKILSIPQSSLEPLKAIIQYRLPMKKNNNLYSWDDfmelgrsiPDTQLEQVI 216
Cdd:pfam00501  78 PRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAK--------PADVPPPPP 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  217 ESQKANQCAVLIYTSGTTGIPKGVMLSHDNI----TWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGA- 291
Cdd:pfam00501 150 PPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLvanvLSIKRVRPRGFGLGP-DDRVLSTLPLFHDFGLSLGLLGPLLAGAt 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  292 LTYFAQADALKGT-LVSTLKEVKPTVFIGVPQIWEKIhemvkknsaksmglkkkafvwarnigfkvnskkmlgkyntpVS 370
Cdd:pfam00501 229 VVLPPGFPALDPAaLLELIERYKVTVLYGVPTLLNML-----------------------------------------LE 267
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  371 YRMAKTLVFSKVKTslgldhchsFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNYRLL---SCGKIL 446
Cdd:pfam00501 268 AGAPKRALLSSLRL---------VLSGGAPLPPELARRFRElFGGALVNGYGLTETTGVVTTPLPLDEDLRslgSVGRPL 338
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574584557  447 TGCK------NMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITA 519
Cdd:pfam00501 339 PGTEvkivddETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
78-657 6.59e-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: 6.59e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  78 WEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILL 157
Cdd:cd17641    9 WQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 158 VENDQQLQKILSIpQSSLEPLKAIIqYRLP--MKKNNN--LYSWDDFMELGRSI----PDtQLEQVIESQKANQCAVLIY 229
Cdd:cd17641   89 AEDEEQVDKLLEI-ADRIPSVRYVI-YCDPrgMRKYDDprLISFEDVVALGRALdrrdPG-LYEREVAAGKGEDVAVLCT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 230 TSGTTGIPKGVMLSHDN-ITWIAGAVTKDFKLTDkhETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADAlkgTLVST 308
Cdd:cd17641  166 TSGTTGKPKLAMLSHGNfLGHCAAYLAADPLGPG--DEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPEEPE---TMMED 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 309 LKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGK---YNTPVSYRMAKTLVFSKVKTS 385
Cdd:cd17641  241 LREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLRALDRGKRGRpvsLWLRLASWLADALLFRPLRDR 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 386 LGLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCknmlfQQNKDGIGEIC 465
Cdd:cd17641  321 LGFSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGT-----EVRIDEVGEIL 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 466 LWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISNAML 545
Cdd:cd17641  396 VRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLKFS-PYIAEAVV 474
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 546 VGDKLKFLSMLLTLKcemnqmsgepldklnFEAI-NFCRGLGSQASTVTEIVKQqdPLVYKAIQQGINAVNQEaMNNAQR 624
Cdd:cd17641  475 LGAGRPYLTAFICID---------------YAIVgKWAEQRGIAFTTYTDLASR--PEVYELIRKEVEKVNAS-LPEAQR 536
                        570       580       590
                 ....*....|....*....|....*....|...
gi 574584557 625 IEKWVILEKDFSIYGGELGPMMKLKRHFVAQKY 657
Cdd:cd17641  537 IRRFLLLYKELDADDGELTRTRKVRRGVIAEKY 569
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
75-657 1.93e-69

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: 1.93e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  75 GKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVN 154
Cdd:cd05932    1 GGQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 155 ILLV----ENDQQLQKILSIPQSSLEPlkaiiqyrlPMKKNNNLYSWDDFMELGrsipdtQLEQVIESQKANQCAVLIYT 230
Cdd:cd05932   81 ALFVgkldDWKAMAPGVPEGLISISLP---------PPSAANCQYQWDDLIAQH------PPLEERPTRFPEQLATLIYT 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 231 SGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQA-DalkgTLVSTL 309
Cdd:cd05932  146 SGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEE-NDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESlD----TFVEDV 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 310 KEVKPTVFIGVPQIWEKIHEmvkknsaksmglkkkafvwarNIGFKVNSKKMlgkyNTPVSYRMAKTLVFSKVKTSLGLD 389
Cdd:cd05932  221 QRARPTLFFSVPRLWTKFQQ---------------------GVQDKIPQQKL----NLLLKIPVVNSLVKRKVLKGLGLD 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 390 HCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQnkdgiGEICLWGR 469
Cdd:cd05932  276 QCRLAGCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISED-----GEILVRSP 350
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 470 HIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVEtlvkKKI---PIISNAMLV 546
Cdd:cd05932  351 ALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIE----NKLaehDRVEMVCVI 426
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 547 GDKLKFLSMLLtlkcemnQMSGEPldklNFEAINFCRGlGSQASTvteivkqqdplvyKAIQQGINAvnqeAMNNAQRIE 626
Cdd:cd05932  427 GSGLPAPLALV-------VLSEEA----RLRADAFARA-ELEASL-------------RAHLARVNS----TLDSHEQLA 477
                        570       580       590
                 ....*....|....*....|....*....|.
gi 574584557 627 KWVILEKDFSIYGGELGPMMKLKRHFVAQKY 657
Cdd:cd05932  478 GIVVVKDPWSIDNGILTPTLKIKRNVLEKAY 508
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
85-583 8.68e-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: 215.77  E-value: 8.68e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  85 QYYEACRKAAKSLIKL---GLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEND 161
Cdd:cd05914    9 TYKDLADNIAKFALLLkinGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSDE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 162 QQLqkilsipqssleplkaiiqyrlpmkknnnlyswddfmelgrsipdtqleqviesqkanqcAVLIYTSGTTGIPKGVM 241
Cdd:cd05914   89 DDV------------------------------------------------------------ALINYTSGTTGNSKGVM 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 242 LSHDNITWIAGAVtKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAqaDALKGTLVSTLKEVKPTVFIGVP 321
Cdd:cd05914  109 LTYRNIVSNVDGV-KEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFL--DKIPSAKIIALAFAQVTPTLGVP 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 322 QIW--EKIHEMVKKNsaksmglkkkafvwarnigfKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGlDHCHSFISGTA 399
Cdd:cd05914  186 VPLviEKIFKMDIIP--------------------KLTLKKFKFKLAKKINNRKIRKLAFKKVHEAFG-GNIKEFVIGGA 244
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 400 PLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQN-KDGIGEICLWGRHIFMGYLES 478
Cdd:cd05914  245 KINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPDpATGEGEIIVRGPNVMKGYYKN 324
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 479 ETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVET-LVKKKIPIISNAMLVGDKLKFLSML- 556
Cdd:cd05914  325 PEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAkINNMPFVLESLVVVQEKKLVALAYId 404
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 574584557 557 ---LTLKCEMNQ-----MSGEPLDKLNFEAINFCR 583
Cdd:cd05914  405 pdfLDVKALKQRniidaIKWEVRDKVNQKVPNYKK 439
PLN02736 PLN02736
long-chain acyl-CoA synthetase
28-665 3.88e-59

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 210.34  E-value: 3.88e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  28 WTTCRDGEVLLRLSKHGPGHETPMTIPEFFRESVNRFGTYPALASK---NGK----KWeiLNFNQYYEAcRKAAKS-LIK 99
Cdd:PLN02736  21 WNVYRSARSPLKLVSRFPDHPEIGTLHDNFVYAVETFRDYKYLGTRirvDGTvgeyKW--MTYGEAGTA-RTAIGSgLVQ 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 100 LGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVeNDQQLQKILSIpQSSLEPLK 179
Cdd:PLN02736  98 HGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSC-LSEIPSVR 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 180 AIIQY--------RLPMKKNNNLYSWDDFMELGRSIPdtqleQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDN-ITWI 250
Cdd:PLN02736 176 LIVVVggadeplpSLPSGTGVEIVTYSKLLAQGRSSP-----QPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNlIANV 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 251 AGA-VTKDFKLTDKHetvVSYLPLSHI---AAQMMDIWVPIKIGaltyFAQADALKgtLVSTLKEVKPTVFIGVPQIWEK 326
Cdd:PLN02736 251 AGSsLSTKFYPSDVH---ISYLPLAHIyerVNQIVMLHYGVAVG----FYQGDNLK--LMDDLAALRPTIFCSVPRLYNR 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 327 IHEMVKKNSAKSMGLKKKAFvwarNIGFkvNSKK---MLGKYNTPvsyrMAKTLVFSKVKTSLGlDHCHSFISGTAPLNQ 403
Cdd:PLN02736 322 IYDGITNAVKESGGLKERLF----NAAY--NAKKqalENGKNPSP----MWDRLVFNKIKAKLG-GRVRFMSSGASPLSP 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 404 ETAEFflsLDIPIG----ELYGLSESSGPHTISNQNNYrllSCGKI----------LTGCKNMLFqQNKDGI---GEICL 466
Cdd:PLN02736 391 DVMEF---LRICFGgrvlEGYGMTETSCVISGMDEGDN---LSGHVgspnpacevkLVDVPEMNY-TSEDQPyprGEICV 463
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 467 WGRHIFMGYLESETETTEAIDDEGWLHSGDLGQ-LDGlGFLYVTGHIKEILITAGGENVPPIPVETlVKKKIPIISNAML 545
Cdd:PLN02736 464 RGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLwLPG-GRLKIIDRKKNIFKLAQGEYIAPEKIEN-VYAKCKFVAQCFV 541
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 546 VGDKLKflSMLLTLkcemnqMSGEPLDKLNFEAINfcrglGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEAMNNAQRI 625
Cdd:PLN02736 542 YGDSLN--SSLVAV------VVVDPEVLKAWAASE-----GIKYEDLKQLCN--DPRVRAAVLADMDAVGREAQLRGFEF 606
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|.
gi 574584557 626 EKWVILEKD-FSIYGGELGPMMKLKRHFVAQKYKKQIDHMY 665
Cdd:PLN02736 607 AKAVTLVPEpFTVENGLLTPTFKVKRPQAKAYFAKAISDMY 647
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
53-547 1.23e-57

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: 1.23e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  53 IPEFFRESVNRFGTYPALASKngkkWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLC 132
Cdd:COG0318    1 LADLLRRAAARHPDRPALVFG----GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 133 VGIYATNSAEVCQYVITHAKVNILLvendqqlqkilsipqssleplkaiiqyrlpmkknnnlyswddfmelgrsipdtql 212
Cdd:COG0318   77 VPLNPRLTAEELAYILEDSGARALV------------------------------------------------------- 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 213 eqviesqkanqCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGA- 291
Cdd:COG0318  102 -----------TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTP-GDVVLVALPLFHVFGLTVGLLAPLLAGAt 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 292 ---LTYFAQADALKgtlvsTLKEVKPTVFIGVPQIWekihemvkknsaksmglkkkafvwarnigfkvnskkmlgkyntp 368
Cdd:COG0318  170 lvlLPRFDPERVLE-----LIERERVTVLFGVPTML-------------------------------------------- 200
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 369 vsYRMAKTLVFSKVKTSlgldHCHSFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNY--RLLSCGKI 445
Cdd:COG0318  201 --ARLLRHPEFARYDLS----SLRLVVSGGAPLPPELLERFEErFGVRIVEGYGLTETSPVVTVNPEDPGerRPGSVGRP 274
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 446 LTGCKNMLFqqNKDG-------IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILIT 518
Cdd:COG0318  275 LPGVEVRIV--DEDGrelppgeVGEIVVRGPNVMKGYWNDPEATAEAFRD-GWLRTGDLGRLDEDGYLYIVGRKKDMIIS 351
                        490       500
                 ....*....|....*....|....*....
gi 574584557 519 aGGENVPPIPVETLVkKKIPIISNAMLVG 547
Cdd:COG0318  352 -GGENVYPAEVEEVL-AAHPGVAEAAVVG 378
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
81-653 2.41e-54

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: 2.41e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  81 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYvithakvnillven 160
Cdd:cd17639    6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIH-------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 161 dqqlqkilsipqssleplkaiiqyrlpmkknnnlyswddfmelgrSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGV 240
Cdd:cd17639   72 ---------------------------------------------SLNETECSAIFTDGKPDDLACIMYTSGSTGNPKGV 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 241 MLSHDNITW-IAGAVTKDFKLTDKHETVVSYLPLSHI---AAQMmdiwVPIKIGALTYFAQADAL--------KGTLVst 308
Cdd:cd17639  107 MLTHGNLVAgIAGLGDRVPELLGPDDRYLAYLPLAHIfelAAEN----VCLYRGGTIGYGSPRTLtdkskrgcKGDLT-- 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 309 lkEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFvwarNIGFKVNSKKMLGKYNTPVsyrmAKTLVFSKVKTSLGl 388
Cdd:cd17639  181 --EFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLF----WTAYQSKLKALKEGPGTPL----LDELVFKKVRAALG- 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 389 DHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNML--------FQQNKDG 460
Cdd:cd17639  250 GRLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLvdweeggySTDKPPP 329
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 461 IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPII 540
Cdd:cd17639  330 RGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSN-PLV 408
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 541 SNAMLVGD--KLKFLSMLLTlkcemNQmsgEPLDKlnfeainFCRGLGSQASTVTEIVKqqDPLVYKAIQQGINAVNQEA 618
Cdd:cd17639  409 NNICVYADpdKSYPVAIVVP-----NE---KHLTK-------LAEKHGVINSEWEELCE--DKKLQKAVLKSLAETARAA 471
                        570       580       590
                 ....*....|....*....|....*....|....*...
gi 574584557 619 mnNAQRIE---KWVILEKDFSIYGGELGPMMKLKRHFV 653
Cdd:cd17639  472 --GLEKFEipqGVVLLDEEWTPENGLVTAAQKLKRKEI 507
PLN02430 PLN02430
long-chain-fatty-acid-CoA ligase
40-665 3.89e-54

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178049 [Multi-domain]  Cd Length: 660  Bit Score: 196.57  E-value: 3.89e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  40 LSKHG-PGHETPMTIP-EFFRESVNRFGTYPALA---SKNGK----KWEilNFNQYYEACRKAAKSLIKLGLERFHGVGI 110
Cdd:PLN02430  29 LSKKGfPPIDSDITTAwDIFSKSVEKYPDNKMLGwrrIVDGKvgpyMWK--TYKEVYEEVLQIGSALRASGAEPGSRVGI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 111 LGFNSAEWfITAVGAILAGGL-CVGIYATNSAEVCQYVITHAKVNILLVEnDQQLQKILSIPQSSLEPLKAIIQYRLPMK 189
Cdd:PLN02430 107 YGSNCPQW-IVAMEACAAHSLiCVPLYDTLGPGAVDYIVDHAEIDFVFVQ-DKKIKELLEPDCKSAKRLKAIVSFTSVTE 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 190 KNNN--------LYSWDDFMELGRSIPdtqlEQVIESQKANQCAVLiYTSGTTGIPKGVMLSHDNITWIAGAV---TKDF 258
Cdd:PLN02430 185 EESDkasqigvkTYSWIDFLHMGKENP----SETNPPKPLDICTIM-YTSGTSGDPKGVVLTHEAVATFVRGVdlfMEQF 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 259 KLTDKHETV-VSYLPLSHIAAQMMDIWVPIKIGALTYF-AQADALKgtlvSTLKEVKPTVFIGVPQIWEKIHEMVKKNSA 336
Cdd:PLN02430 260 EDKMTHDDVyLSFLPLAHILDRMIEEYFFRKGASVGYYhGDLNALR----DDLMELKPTLLAGVPRVFERIHEGIQKALQ 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 337 KSMGLKKKAFvwarNIGFKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFF-LSLDIP 415
Cdd:PLN02430 336 ELNPRRRLIF----NALYKYKLAWMNRGYSHKKASPMADFLAFRKVKAKLG-GRLRLLISGGAPLSTEIEEFLrVTSCAF 410
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 416 IGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQ---------NKDGIGEICLWGRHIFMGYLESETETTEAI 486
Cdd:PLN02430 411 VVQGYGLTETLGPTTLGFPDEMCMLGTVGAPAVYNELRLEEvpemgydplGEPPRGEICVRGKCLFSGYYKNPELTEEVM 490
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 487 DDeGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVppiPVETL--VKKKIPIISNAMLVGDKLKflSMLLTLKCemn 564
Cdd:PLN02430 491 KD-GWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYV---ALEYLenVYGQNPIVEDIWVYGDSFK--SMLVAVVV--- 561
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 565 qmsgepldkLNFEAINFCRGLGSQASTVTEIVKQqdPLVYKAIQQGINAVnqEAMNNAQRIE--KWVILE-KDFSIYGGE 641
Cdd:PLN02430 562 ---------PNEENTNKWAKDNGFTGSFEELCSL--PELKEHILSELKST--AEKNKLRGFEyiKGVILEtKPFDVERDL 628
                        650       660
                 ....*....|....*....|....
gi 574584557 642 LGPMMKLKRHFVAQKYKKQIDHMY 665
Cdd:PLN02430 629 VTATLKKRRNNLLKYYQVEIDEMY 652
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
79-653 5.23e-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: 5.23e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  79 EILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLV 158
Cdd:cd17640    4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 159 ENDqqlqkilsipqssleplkaiiqyrlpmkkNNNLyswddfmelgrsipdtqleqviesqkanqcAVLIYTSGTTGIPK 238
Cdd:cd17640   84 END-----------------------------SDDL------------------------------ATIIYTSGTTGNPK 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 239 GVMLSHDNITWIAGAVTkDFKLTDKHETVVSYLPLSHIAAQmmdiwvpikigALTYFAqadALKG---------TLVSTL 309
Cdd:cd17640  105 GVMLTHANLLHQIRSLS-DIVPPQPGDRFLSILPIWHSYER-----------SAEYFI---FACGcsqaytsirTLKDDL 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 310 KEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIG-FKVNskkmlgkyntpvsyrmaktlvfskvktslgl 388
Cdd:cd17640  170 KRVKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFFLSGGiFKFG------------------------------- 218
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 389 dhchsfISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGI------G 462
Cdd:cd17640  219 ------ISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVlppgekG 292
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 463 EICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVE-TLVKKkiPIIS 541
Cdd:cd17640  293 IVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEeALMRS--PFIE 370
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 542 NAMLVGDKLKFLSMLLTlkcemnqmsgePldklNFEAINfcRGLGSQASTVTEIVKQ--QDPLVYKAIQQGINAV--NQE 617
Cdd:cd17640  371 QIMVVGQDQKRLGALIV-----------P----NFEELE--KWAKESGVKLANDRSQllASKKVLKLYKNEIKDEisNRP 433
                        570       580       590
                 ....*....|....*....|....*....|....*.
gi 574584557 618 AMNNAQRIEKWVILEKDFsIYGGELGPMMKLKRHFV 653
Cdd:cd17640  434 GFKSFEQIAPFALLEEPF-IENGEMTQTMKIKRNVV 468
PLN02614 PLN02614
long-chain acyl-CoA synthetase
55-665 1.21e-51

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 189.85  E-value: 1.21e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  55 EFFRESVNRFGTYPALASK---NGK--KWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAG 129
Cdd:PLN02614  49 DVFRMSVEKYPNNPMLGRReivDGKpgKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHG 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 130 GLCVGIYATNSAEVCQYVITHAKVNILLVEnDQQLQKILSIPQSSLEPLKAIIQYR--LPMKKNNN------LYSWDDFM 201
Cdd:PLN02614 129 LYCVPLYDTLGAGAVEFIISHSEVSIVFVE-EKKISELFKTCPNSTEYMKTVVSFGgvSREQKEEAetfglvIYAWDEFL 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 202 ELGRSipdTQLEQVIEsQKANQCAVLiYTSGTTGIPKGVMLSHDNITWIAGAVTKDFK-----LTDKhETVVSYLPLSHI 276
Cdd:PLN02614 208 KLGEG---KQYDLPIK-KKSDICTIM-YTSGTTGDPKGVMISNESIVTLIAGVIRLLKsanaaLTVK-DVYLSYLPLAHI 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 277 AAQMMDIWVpIKIGALTYFAQADAlkGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKv 356
Cdd:PLN02614 282 FDRVIEECF-IQHGAAIGFWRGDV--KLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFG- 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 357 NSKKmlGKYNTPVSYRMAKtLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLD-IPIGELYGLSESSGPHTISNQN 435
Cdd:PLN02614 358 NMKK--GQSHVEASPLCDK-LVFNKVKQGLG-GNVRIILSGAAPLASHVESFLRVVAcCHVLQGYGLTESCAGTFVSLPD 433
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 436 NYRLLscGKILTGCKNM------LFQQNKDGI-----GEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLG 504
Cdd:PLN02614 434 ELDML--GTVGPPVPNVdirlesVPEMEYDALastprGEICIRGKTLFSGYYKREDLTKEVLID-GWLHTGDVGEWQPNG 510
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 505 FLYVTGHIKEILITAGGENVPPIPVETlVKKKIPIISNAMLVGDklKFLSMLLTLKCEMNQM----SGEPLDKLNFEAIn 580
Cdd:PLN02614 511 SMKIIDRKKNIFKLSQGEYVAVENIEN-IYGEVQAVDSVWVYGN--SFESFLVAIANPNQQIlerwAAENGVSGDYNAL- 586
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 581 fCRGLGSQASTVTEIVKQQDPLVYKAIQQgINAVNQEAMNnaqriekwVILEKDFsiyggeLGPMMKLKRHFVAQKYKKQ 660
Cdd:PLN02614 587 -CQNEKAKEFILGELVKMAKEKKMKGFEI-IKAIHLDPVP--------FDMERDL------LTPTFKKKRPQLLKYYQSV 650

                 ....*
gi 574584557 661 IDHMY 665
Cdd:PLN02614 651 IDEMY 655
PLN02861 PLN02861
long-chain-fatty-acid-CoA ligase
55-665 2.74e-50

long-chain-fatty-acid-CoA ligase


Pssm-ID: 178452 [Multi-domain]  Cd Length: 660  Bit Score: 185.82  E-value: 2.74e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  55 EFFRESVNRF------GTYPALASKNGKK-WeiLNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWfITAVGAIL 127
Cdd:PLN02861  47 QFFSDAVKKYpnnqmlGRRQVTDSKVGPYvW--LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEW-IIAMEACN 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 128 AGGLC-VGIYATNSAEVCQYVITHAKVNILLVEnDQQLQKILSIPQSSLEPLKAIIQY---RLPMKKNN-----NLYSWD 198
Cdd:PLN02861 124 SQGITyVPLYDTLGANAVEFIINHAEVSIAFVQ-ESKISSILSCLPKCSSNLKTIVSFgdvSSEQKEEAeelgvSCFSWE 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 199 DFMELGRSipDTQLEQvieSQKANQCAVLiYTSGTTGIPKGVMLSHDNItwIAGAVTKD--FKLTDK----HETVVSYLP 272
Cdd:PLN02861 203 EFSLMGSL--DCELPP---KQKTDICTIM-YTSGTTGEPKGVILTNRAI--IAEVLSTDhlLKVTDRvateEDSYFSYLP 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 273 LSHIAAQMMDIWVpIKIGALTYFAQADALkgTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNi 352
Cdd:PLN02861 275 LAHVYDQVIETYC-ISKGASIGFWQGDIR--YLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYN- 350
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 353 gFKV-NSKKMLGKYNTpvSYRMAKtLVFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLDIP-IGELYGLSESSGPHT 430
Cdd:PLN02861 351 -YKLgNLRKGLKQEEA--SPRLDR-LVFDKIKEGLG-GRVRLLLSGAAPLPRHVEEFLRVTSCSvLSQGYGLTESCGGCF 425
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 431 ISNQNNYRLL-SCGKILTGCKNMLFQQNKDGI--------GEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLD 501
Cdd:PLN02861 426 TSIANVFSMVgTVGVPMTTIEARLESVPEMGYdalsdvprGEICLRGNTLFSGYHKRQDLTEEVLID-GWFHTGDIGEWQ 504
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 502 GLGFLYVTGHIKEILITAGGENVppiPVETL--VKKKIPIISNAMLVGDklKFLSMLLTLKCEMNQmSGEPLDKLNFEAI 579
Cdd:PLN02861 505 PNGAMKIIDRKKNIFKLSQGEYV---AVENLenTYSRCPLIASIWVYGN--SFESFLVAVVVPDRQ-ALEDWAANNNKTG 578
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 580 NF---CrglgsqastvteivkqQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKD-FSIYGGELGPMMKLKRHFVAQ 655
Cdd:PLN02861 579 DFkslC----------------KNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNpFDIERDLITPTFKLKRPQLLK 642
                        650
                 ....*....|
gi 574584557 656 KYKKQIDHMY 665
Cdd:PLN02861 643 YYKDCIDQLY 652
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
81-532 2.30e-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: 2.30e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  81 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEN 160
Cdd:cd05911   11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 161 DQqLQKILSIpQSSLEPLKAIIQYRLPMKKNNNLYSWDDFmELGRSIPDtQLEQVIESqkANQCAVLIYTSGTTGIPKGV 240
Cdd:cd05911   91 DG-LEKVKEA-AKELGPKDKIIVLDDKPDGVLSIEDLLSP-TLGEEDED-LPPPLKDG--KDDTAAILYSSGTTGLPKGV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 241 MLSHDNIT-WIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKiGALTY----FAQADALKgtlvsTLKEVKPT 315
Cdd:cd05911  165 CLSHRNLIaNLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIimpkFDSELFLD-----LIEKYKIT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 316 VFIGVPQIwekiheMVkknsaksmglkkkafvwarnigfkvnskkMLGKYNTPVSYRMAktlvfskvktSLgldhcHSFI 395
Cdd:cd05911  239 FLYLVPPI------AA-----------------------------ALAKSPLLDKYDLS----------SL-----RVIL 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 396 SGTAPLNQETAEFFLSLDIP--IGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLF------QQNKDGIGEICLW 467
Cdd:cd05911  269 SGGAPLSKELQELLAKRFPNatIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVdddgkdSLGPNEPGEICVR 348
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 574584557 468 GRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETL 532
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 ...
223-535 4.91e-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: 4.91e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 223 QCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAaQMMDIWVPIKIGA----LTYFAQA 298
Cdd:cd04433    1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTE-GDVFLSTLPLFHIG-GLFGLLGALLAGGtvvlLPKFDPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 299 DALKgtlvsTLKEVKPTVFIGVPQIWEKIhemvkknsaksmglkkkafvwARNIGFKvnskkmlgkyntpvsyrmakTLV 378
Cdd:cd04433   79 AALE-----LIEREKVTILLGVPTLLARL---------------------LKAPESA--------------------GYD 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 379 FSKVKTslgldhchsFISGTAPLNQETAEFFLSL-DIPIGELYGLSESSGPHTISN--QNNYRLLSCGKILTGCKNMLFQ 455
Cdd:cd04433  113 LSSLRA---------LVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPpdDDARKPGSVGRPVPGVEVRIVD 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 456 QNKD-----GIGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:cd04433  184 PDGGelppgEIGELVVRGPSVMKGYWNNP-EATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVE 261

                 ....*
gi 574584557 531 TLVKK 535
Cdd:cd04433  262 AVLLG 266
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
50-530 2.94e-44

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 166.13  E-value: 2.94e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  50 PMTIPEFFRESVNRFGTYPALASkNGKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWF-----ITAVG 124
Cdd:PRK06187   5 PLTIGRILRHGARKHPDKEAVYF-DGRRT---TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLeayfaVPKIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 125 AILAgglcvgiyATN---SAEVCQYVITHAKVNILLVEND--QQLQKILSipqsSLEPLKAIIQYRLPMKKNNNLYsWDD 199
Cdd:PRK06187  81 AVLH--------PINirlKPEEIAYILNDAEDRVVLVDSEfvPLLAAILP----QLPTVRTVIVEGDGPAAPLAPE-VGE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 200 FMELGRSIPDTQLEQVIEsqkANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAq 279
Cdd:PRK06187 148 YEELLAAASDTFDFPDID---ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRD-DVYLVIVPMFHVHA- 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 280 mmdiW----VPIKIGA-LTYFAQADAlkGTLVSTLKEVKPTVFIGVPQIWEkihemvkknsaksmglkkkafvwarnigf 354
Cdd:PRK06187 223 ----WglpyLALMAGAkQVIPRRFDP--ENLLDLIETERVTFFFAVPTIWQ----------------------------- 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 355 kvnskkMLGKYntPVSYRMAktlvFSKVKTslgldhchsFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSG------ 427
Cdd:PRK06187 268 ------MLLKA--PRAYFVD----FSSLRL---------VIYGGAALPPALLREFKEkFGIDLVQGYGMTETSPvvsvlp 326
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 428 -PHTISNQNNYRlLSCGKILTGCK------NMLFQQNKDG-IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQ 499
Cdd:PRK06187 327 pEDQLPGQWTKR-RSAGRPLPGVEarivddDGDELPPDGGeVGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGDVGY 404
                        490       500       510
                 ....*....|....*....|....*....|.
gi 574584557 500 LDGLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:PRK06187 405 IDEDGYLYITDRIKDVIIS-GGENIYPRELE 434
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
50-530 8.82e-44

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 164.69  E-value: 8.82e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  50 PMTIPEFFRESVNRFGTYPALASKNGKkweiLNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAG 129
Cdd:PRK07656   4 WMTLPELLARAARRFGDKEAYVFGDQR----LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 130 GLCVGIYATNSAEVCQYVITHAKVNILLVEnDQQLQKILSIPQS--SLEpLKAIIQYRLPMKKNNNLYSWDDFMELGrsi 207
Cdd:PRK07656  80 AVVVPLNTRYTADEAAYILARGDAKALFVL-GLFLGVDYSATTRlpALE-HVVICETEEDDPHTEKMKTFTDFLAAG--- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 208 pdTQLEQVIEsQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPI 287
Cdd:PRK07656 155 --DPAERAPE-VDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEG-DRYLAANPFFHVFGYKAGVNAPL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 288 KIGA----LTYFAQADALKgtlvsTLKEVKPTVFIGVPQIwekihemvkknsaksmglkkkafvwarnigfkvnskkmlg 363
Cdd:PRK07656 231 MRGAtilpLPVFDPDEVFR-----LIETERITVLPGPPTM---------------------------------------- 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 364 kYNTPVSYRMAKTLVFSkvktSLGLdhchsFISGTAPLNQETAEFFLS-LDIP-IGELYGLSESSGPHTISNQNNYRLLS 441
Cdd:PRK07656 266 -YNSLLQHPDRSAEDLS----SLRL-----AVTGAASMPVALLERFESeLGVDiVLTGYGLSEASGVTTFNRLDDDRKTV 335
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 442 CGKILTGCKNM-------LFQQNKDG-IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIK 513
Cdd:PRK07656 336 AGTIGTAIAGVenkivneLGEEVPVGeVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKK 415
                        490
                 ....*....|....*..
gi 574584557 514 EILITaGGENVPPIPVE 530
Cdd:PRK07656 416 DMFIV-GGFNVYPAEVE 431
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
48-666 2.18e-43

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 166.45  E-value: 2.18e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  48 ETP----MTIPEFFRESVNRFGTYPAL-----------ASKNGKKWEILNFNQY--------YEACRKAAKSLIKLGLER 104
Cdd:PLN02387  51 ETPwegaTTLAALFEQSCKKYSDKRLLgtrklisrefeTSSDGRKFEKLHLGEYewitygqvFERVCNFASGLVALGHNK 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 105 FHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENdQQLQKILSIpQSSLEPLKAII-- 182
Cdd:PLN02387 131 EERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS-KQLKKLIDI-SSQLETVKRVIym 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 183 -------QYRLPMKKNNNLYSWDDFMELGRSIP-DTQLEqviesqKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAV 254
Cdd:PLN02387 209 ddegvdsDSSLSGSSNWTVSSFSEVEKLGKENPvDPDLP------SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGV 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 255 TKDFKLTDKHETVVSYLPLSHI---AAQ--MMDIWVPIKIG-ALTYFAQADALK-GTL--VSTLkevKPTVFIGVPQIWE 325
Cdd:PLN02387 283 MTVVPKLGKNDVYLAYLPLAHIlelAAEsvMAAVGAAIGYGsPLTLTDTSNKIKkGTKgdASAL---KPTLMTAVPAILD 359
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 326 KIHEMVKKNSAKSMGLKKKAF--VWARNIGFKVNS-------KKMLgkYNtpvsyrmakTLVFSKVKTSLGlDHCHSFIS 396
Cdd:PLN02387 360 RVRDGVRKKVDAKGGLAKKLFdiAYKRRLAAIEGSwfgawglEKLL--WD---------ALVFKKIRAVLG-GRIRFMLS 427
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 397 GTAPLNQETAEFF-LSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGI---------GEICL 466
Cdd:PLN02387 428 GGAPLSGDTQRFInICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYlisdkpmprGEIVI 507
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 467 WGRHIFMGYLESETETTEA--IDDEG--WLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKiPIISN 542
Cdd:PLN02387 508 GGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVS-PYVDN 586
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 543 AMLVGDklKFLSMLLTLKCEMNQMSGEPLDKLNFEAINFCRgLGSQASTVTEivkqqdplvykaIQQGINAVNQEAmnna 622
Cdd:PLN02387 587 IMVHAD--PFHSYCVALVVPSQQALEKWAKKAGIDYSNFAE-LCEKEEAVKE------------VQQSLSKAAKAA---- 647
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|
gi 574584557 623 qRIEKWVI------LEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMYH 666
Cdd:PLN02387 648 -RLEKFEIpakiklLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
53-530 9.16e-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: 9.16e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  53 IPEFFRESVNRFGTYPALAskNGKKWeiLNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLC 132
Cdd:cd05936    1 LADLLEEAARRFPDKTALI--FMGRK--LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 133 VgiyatnsaevcqyvithaKVNILLVEndQQLQKILSIPQSsleplKAIIQYRlpmkknnnlyswdDFMELGRSIPDTQL 212
Cdd:cd05936   77 V------------------PLNPLYTP--RELEHILNDSGA-----KALIVAV-------------SFTDLLAAGAPLGE 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 213 EQVIesqKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFK-LTDKHETVVSYLPLSHIAAQMMDIWVPIKIGA 291
Cdd:cd05936  119 RVAL---TPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEdLLEGDDVVLAALPLFHVFGLTVALLLPLALGA 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 292 ----LTYFAQADALKgtlvsTLKEVKPTVFIGVPQIWEKIhemvkknsaksMGLKKKAFVWarnigfkvnskkmlgkynt 367
Cdd:cd05936  196 tivlIPRFRPIGVLK-----EIRKHRVTIFPGVPTMYIAL-----------LNAPEFKKRD------------------- 240
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 368 pvsyrmaktlvFSKVKTSlgldhchsfISGTAPLNQETAEFFLSL-DIPIGELYGLSESSgPHTISNQ--NNYRLLSCGK 444
Cdd:cd05936  241 -----------FSSLRLC---------ISGGAPLPVEVAERFEELtGVPIVEGYGLTETS-PVVAVNPldGPRKPGSIGI 299
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 445 ILTGCKNMLFqqNKDG-------IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILI 517
Cdd:cd05936  300 PLPGTEVKIV--DDDGeelppgeVGELWVRGPQVMKGYWNRPEETAEAFVD-GWLRTGDIGYMDEDGYFFIVDRKKDMII 376
                        490
                 ....*....|...
gi 574584557 518 tAGGENVPPIPVE 530
Cdd:cd05936  377 -VGGFNVYPREVE 388
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
46-532 3.97e-37

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 147.82  E-value: 3.97e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  46 GHETPMTIpEFFRESVNRfgTYPALaskngkkWE-ILNFnqyyeacrkaAKSLIKLGLERFHGVGILGFNSAEWFITAVG 124
Cdd:PTZ00216 106 GKERTMEV-THFNETRYI--TYAEL-------WErIVNF----------GRGLAELGLTKGSNVAIYEETRWEWLASIYG 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 125 AILAGGLCVGIYATNSAEVCQYVI--THAKVnilLVENDQQLQKILSIPQSSLEPlKAIIQY--RLPM---KKNNNLYSW 197
Cdd:PTZ00216 166 IWSQSMVAATVYANLGEDALAYALreTECKA---IVCNGKNVPNLLRLMKSGGMP-NTTIIYldSLPAsvdTEGCRLVAW 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 198 DDFMELGRSIPDTQLEQVIESqkANQCAVLIYTSGTTGIPKGVMLSHDNITwiAGAVTKDFKLTD------KHETVVSYL 271
Cdd:PTZ00216 242 TDVVAKGHSAGSHHPLNIPEN--NDDLALIMYTSGTTGDPKGVMHTHGSLT--AGILALEDRLNDligppeEDETYCSYL 317
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 272 PLSHIaaqmMDIWVP---IKIGALTYFAQADalkgTLVST-------LKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGL 341
Cdd:PTZ00216 318 PLAHI----MEFGVTnifLARGALIGFGSPR----TLTDTfarphgdLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSL 389
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 342 KKKAFVWArnigFKVNSKKMLGKYNTPvsYRMAKtlVFSKVKTSLGlDHCHSFISGTAPLNQETAEFFLSLDIPIGELYG 421
Cdd:PTZ00216 390 KRRVFDHA----YQSRLRALKEGKDTP--YWNEK--VFSAPRAVLG-GRVRAMLSGGGPLSAATQEFVNVVFGMVIQGWG 460
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 422 LSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNK-------DGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHS 494
Cdd:PTZ00216 461 LTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEEykhtdtpEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHT 540
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 574584557 495 GDLGQLDGLGFLYVTGHIKEILITAGGENvppIPVETL 532
Cdd:PTZ00216 541 GDVGSIAANGTLRIIGRVKALAKNCLGEY---IALEAL 575
PRK08315 PRK08315
AMP-binding domain protein; Validated
51-530 2.56e-33

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 134.94  E-value: 2.56e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  51 MTIPEFFRESVNRFGTYPALASKN-GKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEW----FITA-VG 124
Cdd:PRK08315  16 QTIGQLLDRTAARYPDREALVYRDqGLRW---TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWvltqFATAkIG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 125 AILagglcVGI----------YATNSAEvCQYVIT---------HAKVNILLVENDQQLQKILsipQSSLEP-LKAIIqy 184
Cdd:PRK08315  93 AIL-----VTInpayrlseleYALNQSG-CKALIAadgfkdsdyVAMLYELAPELATCEPGQL---QSARLPeLRRVI-- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 185 RLPMKKNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNIT----WIAGAVtkdfKL 260
Cdd:PRK08315 162 FLGDEKHPGMLNFDELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILnngyFIGEAM----KL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 261 TDKhETVVSYLPLSHIAAQMMDIWVPIKIGA-LTYFAQA-DALKgTLVSTLKEvKPTVFIGVPQ--IWEKIHEMVKKnsa 336
Cdd:PRK08315 238 TEE-DRLCIPVPLYHCFGMVLGNLACVTHGAtMVYPGEGfDPLA-TLAAVEEE-RCTALYGVPTmfIAELDHPDFAR--- 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 337 ksmglkkkafvwarnigFKVNSKK---MLGKyNTPVSyrmaktlVFSKVKTSLGLDhchsfisgtaplnqetaefflslD 413
Cdd:PRK08315 312 -----------------FDLSSLRtgiMAGS-PCPIE-------VMKRVIDKMHMS-----------------------E 343
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 414 IPIGelYGLSESSGPHTISNQNN---YRLLSCGKIL-----------TGCKNMLFQQnkdgiGEICLWGRHIFMGYLESE 479
Cdd:PRK08315 344 VTIA--YGMTETSPVSTQTRTDDpleKRVTTVGRALphlevkivdpeTGETVPRGEQ-----GELCTRGYSVMKGYWNDP 416
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 574584557 480 TETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:PRK08315 417 EKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIR-GGENIYPREIE 466
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
225-530 2.79e-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: 2.79e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSyLPLSHIAAQMMDIWVPIKIGALTYFAQA-DAlkG 303
Cdd:cd17631  101 ALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVV-APLFHIGGLGVFTLPTLLRGGTVVILRKfDP--E 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 304 TLVSTLKEVKPTVFIGVPQIWEKihemvkknsaksmglkkkafvwarnigfkvnskkMLgkyNTPVsyrmAKTLVFSKVK 383
Cdd:cd17631  178 TVLDLIERHRVTSFFLVPTMIQA----------------------------------LL---QHPR----FATTDLSSLR 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 384 TslgldhchsFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTI--SNQNNYRLLSCGKILTGCKNMLFQQNKD-- 459
Cdd:cd17631  217 A---------VIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFlsPEDHRRKLGSAGRPVFFVEVRIVDPDGRev 287
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574584557 460 ---GIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:cd17631  288 ppgEVGEIVVRGPHVMAGYWNRPEATAAAFRD-GWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVE 359
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
52-530 3.05e-33

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 134.90  E-value: 3.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  52 TIPEFFRESVNRFGTYPALASKN-GKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGG 130
Cdd:PRK12583  19 TIGDAFDATVARFPDREALVVRHqALRY---TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 131 LCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKILSIPQSSLEPLK-----AIIQYRLPMKKN---------NNLYS 196
Cdd:PRK12583  96 ILVNINPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELLPGLAegqpgALACERLPELRGvvslapappPGFLA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 197 WDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHI 276
Cdd:PRK12583 176 WHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTE-HDRLCVPVPLYHC 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 277 AAQMMDIWVPIKIGA-LTYFAQA-DALkGTLvSTLKEVKPTVFIGVPQIWekIHEMvkknsaksmglkkkafvwarnigf 354
Cdd:PRK12583 255 FGMVLANLGCMTVGAcLVYPNEAfDPL-ATL-QAVEEERCTALYGVPTMF--IAEL------------------------ 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 355 kvnSKKMLGKYNtpvsyrmaktlvFSKVKTSlgldhchsfISGTAPLNQET-----AEFFLSlDIPIGelYGLSESSGPH 429
Cdd:PRK12583 307 ---DHPQRGNFD------------LSSLRTG---------IMAGAPCPIEVmrrvmDEMHMA-EVQIA--YGMTETSPVS 359
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 430 TISNQNN---YRLLSCGKILTGCKNMLFQQN-----KDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLD 501
Cdd:PRK12583 360 LQTTAADdleRRVETVGRTQPHLEVKVVDPDgatvpRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMD 439
                        490       500
                 ....*....|....*....|....*....
gi 574584557 502 GLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:PRK12583 440 EQGYVRIVGRSKDMIIR-GGENIYPREIE 467
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
68-530 8.02e-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: 8.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  68 PALASKNGKKWeiLNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYV 147
Cdd:cd05926    4 PALVVPGSTPA--LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 148 ITHAKVNILLVENDqqlqkilsipqSSLEPLKAIIQYRLPMKknnNLYsWDDFM--------ELGRSIPDTQLEQVIESQ 219
Cdd:cd05926   82 LADLGSKLVLTPKG-----------ELGPASRAASKLGLAIL---ELA-LDVGVlirapsaeSLSNLLADKKNAKSEGVP 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 220 KANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVsYLPLSHIAAQMM----------DIWVPIKI 289
Cdd:cd05926  147 LPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLV-VMPLFHVHGLVAsllstlaaggSVVLPPRF 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 290 GALTYFAQadalkgtlvstLKEVKPTVFIGVPQIwekiHEMVKKNSAKSmglkkkafvwarnigfkvnskkmlgKYNTPV 369
Cdd:cd05926  226 SASTFWPD-----------VRDYNATWYTAVPTI----HQILLNRPEPN-------------------------PESPPP 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 370 SYRmaktlvfskvktslgldhchsFI-SGTAPLNQETAEFF-LSLDIPIGELYGLSESSGPHTiSNQ---NNYRLLSCGK 444
Cdd:cd05926  266 KLR---------------------FIrSCSASLPPAVLEALeATFGAPVLEAYGMTEAAHQMT-SNPlppGPRKPGSVGK 323
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 445 IlTGCKNMLFQQN----KDG-IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITA 519
Cdd:cd05926  324 P-VGVEVRILDEDgeilPPGvVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKEL-INR 401
                        490
                 ....*....|.
gi 574584557 520 GGENVPPIPVE 530
Cdd:cd05926  402 GGEKISPLEVD 412
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
52-533 1.88e-27

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 117.29  E-value: 1.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  52 TIPEFFRESVNRFGTYPALASkNGKKWEILNFNQYYEacRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGL 131
Cdd:PRK08751  26 TVAEVFATSVAKFADRPAYHS-FGKTITYREADQLVE--QFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLT 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 132 CVGIYATNSAEVCQYVITHAKVNILLVEND-----QQ--------------LQKILSIPQSSLepLKAIIQY---RLPMK 189
Cdd:PRK08751 103 VVNVNPLYTPRELKHQLIDSGASVLVVIDNfgttvQQviadtpvkqvittgLGDMLGFPKAAL--VNFVVKYvkkLVPEY 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 190 KNNNLYSWDDFMELGR--SIPDTQLEqviesqkANQCAVLIYTSGTTGIPKGVMLSHDNIT--------WIAGAvtkdFK 259
Cdd:PRK08751 181 RINGAIRFREALALGRkhSMPTLQIE-------PDDIAFLQYTGGTTGVAKGAMLTHRNLVanmqqahqWLAGT----GK 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 260 LTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIhemvkknsaksm 339
Cdd:PRK08751 250 LEEGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGL------------ 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 340 glkkkafvwarnigfkvnskkmlgkYNTPvsyrMAKTLVFSKVKTSLGldhchsfisGTAPLNQETAEFFLSLD-IPIGE 418
Cdd:PRK08751 318 -------------------------LNTP----GFDQIDFSSLKMTLG---------GGMAVQRSVAERWKQVTgLTLVE 359
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 419 LYGLSESS-----GPHTISNQNNYRLL------SCGKILTGCKNMLFQqnkdgIGEICLWGRHIFMGYLESETETTEAID 487
Cdd:PRK08751 360 AYGLTETSpaaciNPLTLKEYNGSIGLpipstdACIKDDAGTVLAIGE-----IGELCIKGPQVMKGYWKRPEETAKVMD 434
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 574584557 488 DEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGeNVPPIPVETLV 533
Cdd:PRK08751 435 ADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGF-NVYPNEIEDVI 479
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
79-547 2.07e-27

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 116.50  E-value: 2.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  79 EILNFNQYYEACRKAAKSLI-KLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILL 157
Cdd:PRK06839  26 EEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 158 VENDQQ-----LQKILSI-PQSSLEPLKAIIQYRLpmkknnnlyswDDFMELGRSIPdtqleqviesqkanqcAVLIYTS 231
Cdd:PRK06839 106 VEKTFQnmalsMQKVSYVqRVISITSLKEIEDRKI-----------DNFVEKNESAS----------------FIICYTS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 232 GTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIaaqmmdiwvpikiGALTYFAQADALKGTLV----- 306
Cdd:PRK06839 159 GTTGKPKGAVLTQENMFWNALNNTFAIDLT-MHDRSIVLLPLFHI-------------GGIGLFAFPTLFAGGVIivprk 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 307 -------STLKEVKPTVFIGVPQIWEKIHEMVKKnsaksmglkkkafvwarnigfkvnskkmlgkyntpvsyrmaktlvf 379
Cdd:PRK06839 225 feptkalSMIEKHKVTVVMGVPTIHQALINCSKF---------------------------------------------- 258
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 380 skVKTSLglDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYR--LLSCGKILTGCKNMLFQQN 457
Cdd:PRK06839 259 --ETTNL--QSVRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARrkVGSIGKPVLFCDYELIDEN 334
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 458 KD-----GIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETL 532
Cdd:PRK06839 335 KNkvevgEVGELLIRGPNVMKEYWNRPDATEETIQD-GWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYPLEVEQV 412
                        490
                 ....*....|....*
gi 574584557 533 VkKKIPIISNAMLVG 547
Cdd:PRK06839 413 I-NKLSDVYEVAVVG 426
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
225-532 6.66e-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: 6.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVV-SYLPLSHIAAqmmdiwvpikigaLTYFAQAD-ALK 302
Cdd:cd05904  161 AALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDVFlCVLPMFHIYG-------------LSSFALGLlRLG 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 303 GTLVStlkevkptvfigvpqiwekiheMVKKNSAKSMGLKKKafvwarnigFKVNSkkmlgkynTPVSYRMAKTLVFSKV 382
Cdd:cd05904  228 ATVVV----------------------MPRFDLEELLAAIER---------YKVTH--------LPVVPPIVLALVKSPI 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 383 KTSLGLDHCHSFISGTAPLNQETAEFFLSL--DIPIGELYGLSESSGP-HTISN--QNNYRLLSCGKILTGCKNMLFQQN 457
Cdd:cd05904  269 VDKYDLSSLRQIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVvAMCFApeKDRAKYGSVGRLVPNVEAKIVDPE 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 458 KDGI------GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVET 531
Cdd:cd05904  349 TGESlppnqtGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKE-LIKYKGFQVAPAELEA 427

                 .
gi 574584557 532 L 532
Cdd:cd05904  428 L 428
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
202-547 8.13e-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: 8.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 202 ELGRSIPDTQLEQVI---ESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIAA 278
Cdd:cd05941   66 PLNPSYPLAELEYVItdsEPSLVLDPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWT-EDDVLLHVLPLHHVHG 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 279 QMMDIWVPIKIGA----LTYFaqaDAlkgTLVSTLKEVKP-TVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFvwarnig 353
Cdd:cd05941  145 LVNALLCPLFAGAsvefLPKF---DP---KEVAISRLMPSiTVFMGVPTIYTRLLQYYEAHFTDPQFARAAAA------- 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 354 fkvnsKKMlgkyntpvsyRMaktlvfskvktslgldhchsFISGTAPLNQETAEFFLSLD-IPIGELYGLSESSgpHTIS 432
Cdd:cd05941  212 -----ERL----------RL--------------------MVSGSAALPVPTLEEWEAITgHTLLERYGMTEIG--MALS 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 433 N--QNNYRLLSCGKILTGCKNMLFQQN------KDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLG 504
Cdd:cd05941  255 NplDGERRPGTVGMPLPGVQARIVDEEtgeplpRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDG 334
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 574584557 505 FLYVTGHIKEILITAGGENVPPIPVETLVkKKIPIISNAMLVG 547
Cdd:cd05941  335 YYWILGRSSVDIIKSGGYKVSALEIERVL-LAHPGVSECAVIG 376
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
83-530 1.01e-25

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 110.46  E-value: 1.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  83 FNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVendq 162
Cdd:cd05934    6 YAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV---- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 163 qlqkilsipqssleplkaiiqyrlpmkknnnlyswDDFMelgrsipdtqleqviesqkanqcavLIYTSGTTGIPKGVML 242
Cdd:cd05934   82 -----------------------------------DPAS-------------------------ILYTSGTTGPPKGVVI 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 243 SHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGAltyfaqadalkgTLVsTLKEVKPTVFIGVpq 322
Cdd:cd05934  102 THANLTFAGYYSARRFGLGED-DVYLTVLPLFHINAQAVSVLAALSVGA------------TLV-LLPRFSASRFWSD-- 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 323 iwekihemVKKNSAksmglkkkafVWARNIGfkvnskKMLGK-YNTPVSYRMAktlvfskvktslglDHCHSFISGTAPL 401
Cdd:cd05934  166 --------VRRYGA----------TVTNYLG------AMLSYlLAQPPSPDDR--------------AHRLRAAYGAPNP 207
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 402 NQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLF----QQNKDG-IGEICL-----WGrhI 471
Cdd:cd05934  208 PELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVdddgQELPAGePGELVIrglrgWG--F 285
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 574584557 472 FMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 530
Cdd:cd05934  286 FKGYYNMPEATAEAMRN-GWFHTGDLGYRDADGFFYFVDRKKD-MIRRRGENISSAEVE 342
PRK08316 PRK08316
acyl-CoA synthetase; Validated
52-530 3.88e-25

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 109.64  E-value: 3.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  52 TIPEFFRESVNRFGTYPALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGL 131
Cdd:PRK08316  12 TIGDILRRSARRYPDKTALVFGD----RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 132 CVGI-YATNSAEVCqYVITHAKVNILLVEND--QQLQKILSIPQSSLEPLKAIIQYRLPMKknnnlySWDDFMELGRSIP 208
Cdd:PRK08316  88 HVPVnFMLTGEELA-YILDHSGARAFLVDPAlaPTAEAALALLPVDTLILSLVLGGREAPG------GWLDFADWAEAGS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 209 DTQLEQVIESqkaNQCAVLIYTSGTTGIPKGVMLSHDNITW------IAGAVTKDfkltdkhETVVSYLPLSHiAAQMMD 282
Cdd:PRK08316 161 VAEPDVELAD---DDLAQILYTSGTESLPKGAMLTHRALIAeyvsciVAGDMSAD-------DIPLHALPLYH-CAQLDV 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 283 IWVP-IKIGALTYFAQADALkGTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksMGLkkkafvwARNIGFKVNSKKM 361
Cdd:PRK08316 230 FLGPyLYVGATNVILDAPDP-ELILRTIEAERITSFFAPPTVW--------------ISL-------LRHPDFDTRDLSS 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 362 LGK--YNT-----PVSYRMAKTLvfskvkTSLGLDHChsfisgtaplnqetaefflsldipigelYGLSESSGPHTISNQ 434
Cdd:PRK08316 288 LRKgyYGAsimpvEVLKELRERL------PGLRFYNC----------------------------YGQTEIAPLATVLGP 333
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 435 NNY--RLLSCGkiltgcKNMLFQQNK----DG-------IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLD 501
Cdd:PRK08316 334 EEHlrRPGSAG------RPVLNVETRvvddDGndvapgeVGEIVHRSPQLMLGYWDDPEKTAEAFRG-GWFHSGDLGVMD 406
                        490       500
                 ....*....|....*....|....*....
gi 574584557 502 GLGFLYVTGHIKEILITaGGENVPPIPVE 530
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 ...
82-530 5.46e-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: 5.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  82 NFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEND 161
Cdd:cd12119   27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 162 qqLQKILSIPQSSLEPLKAIIQY----RLPMKKNNNLYSWDDFmeLGRSIPDTQLEQVIEsqkaNQCAVLIYTSGTTGIP 237
Cdd:cd12119  107 --FLPLLEAIAPRLPTVEHVVVMtddaAMPEPAGVGVLAYEEL--LAAESPEYDWPDFDE----NTAAAICYTSGTTGNP 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 238 KGVMLSHDNITWIA-GAVTKDFKLTDKHETVVSYLPLSHIAAqmmdiW-VPIK---IGALTYFAQADALKGTLVSTLKEV 312
Cdd:cd12119  179 KGVVYSHRSLVLHAmAALLTDGLGLSESDVVLPVVPMFHVNA-----WgLPYAaamVGAKLVLPGPYLDPASLAELIERE 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 313 KPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKkafvwarnigfkvnskkmlgkyntpvsyrmaktlvfskvktslgldhch 392
Cdd:cd12119  254 GVTFAAGVPTVWQGLLDHLEANGRDLSSLRR------------------------------------------------- 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 393 sFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTIS------------NQNNYRllscgkILTGCKNMLFQ---QN 457
Cdd:cd12119  285 -VVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSPLGTVArppsehsnlsedEQLALR------AKQGRPVPGVElriVD 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 458 KDG---------IGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIP 528
Cdd:cd12119  358 DDGrelpwdgkaVGELQVRGPWVTKSYYKND-EESEALTEDGWLRTGDVATIDEDGYLTITDRSKD-VIKSGGEWISSVE 435

                 ..
gi 574584557 529 VE 530
Cdd:cd12119  436 LE 437
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
42-547 3.39e-24

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 106.84  E-value: 3.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  42 KHGPGHETPM---TIPEFFRESVNRFGTYP-ALASKNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAE 117
Cdd:cd17642    2 IVGPGPFYPLedgTAGEQLHKAMKRYASVPgTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 118 WFITAVGAILAGglcVGIYATNSAEVCQYVItHAkVNI----LLVENDQQLQKILSIpQSSLEPLKAIIQYrlpmkknNN 193
Cdd:cd17642   82 FFLPVIAGLFIG---VGVAPTNDIYNERELD-HS-LNIskptIVFCSKKGLQKVLNV-QKKLKIIKTIIIL-------DS 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 194 LYSWDDFMEL----GRSIPDTQLEQVIESQKAN---QCAVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVTKDFKLTDKHE 265
Cdd:cd17642  149 KEDYKGYQCLytfiTQNLPPGFNEYDFKPPSFDrdeQVALIMNSSGSTGLPKGVQLTHKNIvARFSHARDPIFGNQIIPD 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 266 T-VVSYLPLSHiAAQMMDIWVPIKIGA----LTYFAQAdalkgTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksmg 340
Cdd:cd17642  229 TaILTVIPFHH-GFGMFTTLGYLICGFrvvlMYKFEEE-----LFLRSLQDYKVQSALLVPTLF---------------- 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 341 lkkkAFVwarnigfkvNSKKMLGKYNtpvsyrmaktlvfskvktslgLDHCHSFISGTAPLNQETAEFFLS-LDIP-IGE 418
Cdd:cd17642  287 ----AFF---------AKSTLVDKYD---------------------LSNLHEIASGGAPLSKEVGEAVAKrFKLPgIRQ 332
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 419 LYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGI------GEICLWGRHIFMGYLESETETTEAIDDEGWL 492
Cdd:cd17642  333 GYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTlgpnerGELCVKGPMIMKGYVNNPEATKALIDKDGWL 412
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 574584557 493 HSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:cd17642  413 HSGDIAYYDEDGHFFIVDRLKS-LIKYKGYQVPPAELESILLQH-PKIFDAGVAG 465
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
51-547 5.06e-24

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 106.62  E-value: 5.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  51 MTIPEFFRESVNRFGTYPALaskngkkwEILNFNQYY----EACRKAAKSLIKLGLERFHGVGILGFNSAEwFITAVGAI 126
Cdd:PRK05605  32 TTLVDLYDNAVARFGDRPAL--------DFFGATTTYaelgKQVRRAAAGLRALGVRPGDRVAIVLPNCPQ-HIVAFYAV 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 127 LAGGLCV-------------GIYATNSAEVcqyVITHAKVNILLVE--NDQQLQKILSIPQSSLEPLKAIIQYRLPMKK- 190
Cdd:PRK05605 103 LRLGAVVvehnplytaheleHPFEDHGARV---AIVWDKVAPTVERlrRTTPLETIVSVNMIAAMPLLQRLALRLPIPAl 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 191 ----------NNNLYSWDDFMElGRSIPDTQLEQVIESQKANQcAVLIYTSGTTGIPKGVMLSHDNI--------TWIAG 252
Cdd:PRK05605 180 rkaraaltgpAPGTVPWETLVD-AAIGGDGSDVSHPRPTPDDV-ALILYTSGTTGKPKGAQLTHRNLfanaaqgkAWVPG 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 253 avtkdfkLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGA-LTYFAQADAlkGTLVSTLKEVKPTVFIGVPQIWEKIHEMV 331
Cdd:PRK05605 258 -------LGDGPERVLAALPMFHAYGLTLCLTLAVSIGGeLVLLPAPDI--DLILDAMKKHPPTWLPGVPPLYEKIAEAA 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 332 KKnsaksmglkkkafvwaRNIGFKvnskkmlgkyntpvSYRMAktlvfskvktslgldhchsfISGTAPLNQETAEFFLS 411
Cdd:PRK05605 329 EE----------------RGVDLS--------------GVRNA--------------------FSGAMALPVSTVELWEK 358
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 412 LdipIG----ELYGLSESSgPHTISN--QNNYRLLSCG------KILTGCKNMLFQQNKDG-IGEICLWGRHIFMGYLES 478
Cdd:PRK05605 359 L---TGgllvEGYGLTETS-PIIVGNpmSDDRRPGYVGvpfpdtEVRIVDPEDPDETMPDGeEGELLVRGPQVFKGYWNR 434
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574584557 479 ETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETlVKKKIPIISNAMLVG 547
Cdd:PRK05605 435 PEETAKSFLD-GWFRTGDVVVMEEDGFIRIVDRIKELIIT-GGFNVYPAEVEE-VLREHPGVEDAAVVG 500
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
51-533 2.32e-23

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 104.68  E-value: 2.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  51 MTIPEFFRESVNRFGTYPALA-SKNGKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAG 129
Cdd:PLN02330  28 LTLPDFVLQDAELYADKVAFVeAVTGKAV---TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 130 GLCVGIYATN-SAEVCQYVitHAKVNILLVENDQQLQKILSIPqsslepLKAIIqyrLPMKKNNNLYSWDDFMELGRSIP 208
Cdd:PLN02330 105 GVFSGANPTAlESEIKKQA--EAAGAKLIVTNDTNYGKVKGLG------LPVIV---LGEEKIEGAVNWKELLEAADRAG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 209 DTQLEQVIesQKANQCAvLIYTSGTTGIPKGVMLSHDNItwIAGAVTKDFKLTDK---HETVVSYLPLSHIAaqmmdiwv 285
Cdd:PLN02330 174 DTSDNEEI--LQTDLCA-LPFSSGTTGISKGVMLTHRNL--VANLCSSLFSVGPEmigQVVTLGLIPFFHIY-------- 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 286 pikigaltyfaqadALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVkknsaksmglkkkafvwARNIGFkvnskkmlgky 365
Cdd:PLN02330 241 --------------GITGICCATLRNKGKVVVMSRFELRTFLNALI-----------------TQEVSF----------- 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 366 nTPVSYRMAKTLVFSKVKTSLGLD--HCHSFISGTAPLNQETAEFFLSL--DIPIGELYGLSESS-------GP---HTI 431
Cdd:PLN02330 279 -APIVPPIILNLVKNPIVEEFDLSklKLQAIMTAAAPLAPELLTAFEAKfpGVQVQEAYGLTEHScitlthgDPekgHGI 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 432 SNQNnyrllSCGKILTGCKNMLFQQN------KDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGF 505
Cdd:PLN02330 358 AKKN-----SVGFILPNLEVKFIDPDtgrslpKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGD 432
                        490       500
                 ....*....|....*....|....*...
gi 574584557 506 LYVTGHIKEiLITAGGENVPPIPVETLV 533
Cdd:PLN02330 433 IFIVDRIKE-LIKYKGFQVAPAELEAIL 459
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
203-547 2.50e-23

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 104.44  E-value: 2.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 203 LGRSIPDTQLEQVIESQK---------ANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPL 273
Cdd:PRK06087 159 LAPATSSLSLSQIIADYEplttaitthGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT-WQDVFMMPAPL 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 274 SHIAAQMMDIWVPIKIGALTYFAQadalkgtlvstlkEVKPTVFIGVpqiwekihemvkknsaksmgLKKKAFVWarnig 353
Cdd:PRK06087 238 GHATGFLHGVTAPFLIGARSVLLD-------------IFTPDACLAL--------------------LEQQRCTC----- 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 354 fkvnskkMLGKynTPVSYRMAKTLVFSKVK-TSLGLdhchsFISGTAPLNQETAEFFLSLDIPIGELYGLSESSgPHTIS 432
Cdd:PRK06087 280 -------MLGA--TPFIYDLLNLLEKQPADlSALRF-----FLCGGTTIPKKVARECQQRGIKLLSVYGSTESS-PHAVV 344
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 433 NQNN---YRLLSCGKILTGCKNMLFQQNKDGI-----GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLG 504
Cdd:PRK06087 345 NLDDplsRFMHTDGYAAAGVEIKVVDEARKTLppgceGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAG 424
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 574584557 505 FLYVTGHIKEILITaGGENVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:PRK06087 425 YIKITGRKKDIIVR-GGENISSREVEDILLQH-PKIHDACVVA 465
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
225-547 2.57e-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: 2.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAqmmdiwVPIKIGALTYfaqadALKGT 304
Cdd:cd05912   80 ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTED-DNWLCALPLFHISG------LSILMRSVIY-----GMTVY 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 305 LVSTLKEvkptvfigvpqiwEKIHEMVKKNSAKSMGLKKKAFVWarnigfkvnskkMLGKYNTPVSYRMAKTLVfskvkt 384
Cdd:cd05912  148 LVDKFDA-------------EQVLHLINSGKVTIISVVPTMLQR------------LLEILGEGYPNNLRCILL------ 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 385 slgldhchsfisGTAPLNQETAEFFLSLDIPIGELYGLSE-SSGPHTISNQNNY-RLLSCGKILTGCKNMLFQ--QNKDG 460
Cdd:cd05912  197 ------------GGGPAPKPLLEQCKEKGIPVYQSYGMTEtCSQIVTLSPEDALnKIGSAGKPLFPVELKIEDdgQPPYE 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 461 IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVkKKIPII 540
Cdd:cd05912  265 VGEILLKGPNVTKGYLNRPDATEESFEN-GWFKTGDIGYLDEEGFLYVLDRRSD-LIISGGENIYPAEIEEVL-LSHPAI 341

                 ....*..
gi 574584557 541 SNAMLVG 547
Cdd:cd05912  342 KEAGVVG 348
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
81-533 7.26e-23

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 103.19  E-value: 7.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  81 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILL--- 157
Cdd:PRK06710  50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcld 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 158 --------VENDQQLQKILSIPQSSLEPLKAIIQYRLPMKKNNNL---YSWDDFMELGRSIP---DTQLEQVIESQkaNQ 223
Cdd:PRK06710 130 lvfprvtnVQSATKIEHVIVTRIADFLPFPKNLLYPFVQKKQSNLvvkVSESETIHLWNSVEkevNTGVEVPCDPE--ND 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 224 CAVLIYTSGTTGIPKGVMLSHDN--------ITWIagavtkdFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYF 295
Cdd:PRK06710 208 LALLQYTGGTTGFPKGVMLTHKNlvsntlmgVQWL-------YNCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVL 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 296 AQADALKgTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksmglkkkafvwarnigfkvnskkmLGKYNTPvsyrMAK 375
Cdd:PRK06710 281 IPKFDMK-MVFEAIKKHKVTLFPGAPTIY-------------------------------------IALLNSP----LLK 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 376 TLVFSKVKTSlgldhchsfISGTAPLNQETAEFFLSldIPIGEL---YGLSESSgPHTISN----------------QNN 436
Cdd:PRK06710 319 EYDISSIRAC---------ISGSAPLPVEVQEKFET--VTGGKLvegYGLTESS-PVTHSNflwekrvpgsigvpwpDTE 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 437 YRLLS--CGKILTGCKnmlfqqnkdgIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKE 514
Cdd:PRK06710 387 AMIMSleTGEALPPGE----------IGEIVVKGPQIMKGYWNKPEETAAVLQD-GWLHTGDVGYMDEDGFFYVKDRKKD 455
                        490
                 ....*....|....*....
gi 574584557 515 iLITAGGENVPPIPVETLV 533
Cdd:PRK06710 456 -MIVASGFNVYPREVEEVL 473
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
49-547 8.45e-22

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: 99.30  E-value: 8.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  49 TPMTIPEFFRESVNRFGTYPALAskNGKKWeiLNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILA 128
Cdd:cd12118    2 VPLTPLSFLERAAAVYPDRTSIV--YGDRR--YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 129 GGLCVGIYATNSAEVCQYVITHAKVNILLVenDQQLQkilsipqssleplkaiiqyrlpmkknnnlysWDDFMELGRSIP 208
Cdd:cd12118   78 GAVLNALNTRLDAEEIAFILRHSEAKVLFV--DREFE-------------------------------YEDLLAEGDPDF 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 209 DtqleqVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtdKHETVvsYL---PLSHiAAQMMDIWV 285
Cdd:cd12118  125 E-----WIPPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEM--KQHPV--YLwtlPMFH-CNGWCFPWT 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 286 PIKIGaltyfaqadalkGTLVsTLKEVKPtvfigvPQIWEKIHE----------MVKKNSAKSMGLKKKAFVWARNIgfk 355
Cdd:cd12118  195 VAAVG------------GTNV-CLRKVDA------KAIYDLIEKhkvthfcgapTVLNMLANAPPSDARPLPHRVHV--- 252
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 356 vnskkMLGKYNTPVSyrmaktlVFSKVkTSLGLDHCHSfisgtaplnqetaefflsldipigelYGLSESSGPHTI---- 431
Cdd:cd12118  253 -----MTAGAPPPAA-------VLAKM-EELGFDVTHV--------------------------YGLTETYGPATVcawk 293
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 432 ------SNQNNYRLlscgKILTGCKNMLFQQ------------NKDG--IGEICLWGRHIFMGYLESETETTEAIDDeGW 491
Cdd:cd12118  294 pewdelPTEERARL----KARQGVRYVGLEEvdvldpetmkpvPRDGktIGEIVFRGNIVMKGYLKNPEATAEAFRG-GW 368
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 574584557 492 LHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETlVKKKIPIISNAMLVG 547
Cdd:cd12118  369 FHSGDLAVIHPDGYIEIKDRSKDIIIS-GGENISSVEVEG-VLYKHPAVLEAAVVA 422
PRK06188 PRK06188
acyl-CoA synthetase; Validated
43-530 1.14e-21

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 98.90  E-value: 1.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  43 HGPGHETPMTIpeffrESVNRFGTYPALASKNGkkweILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITA 122
Cdd:PRK06188   9 HSGATYGHLLV-----SALKRYPDRPALVLGDT----RLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 123 VGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKILSIpQSSLEPLKAIiqyrLPMKKNNNLyswDDFME 202
Cdd:PRK06188  80 GAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPAPFVERALAL-LARVPSLKHV----LTLGPVPDG---VDLLA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 203 LGRSIPDTQLEQVIESQKAnqcAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhetvVSYL---PLSHIAAQ 279
Cdd:PRK06188 152 AAAKFGPAPLVAAALPPDI---AGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPAD----PRFLmctPLSHAGGA 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 280 MMdiwVP--IKIGALTYFAQADAlkGTLVSTLKEVKPTVFIGVP-QIWEKI-HEMVKKNSAKSMGLkkkafvwarnigfk 355
Cdd:PRK06188 225 FF---LPtlLRGGTVIVLAKFDP--AEVLRAIEEQRITATFLVPtMIYALLdHPDLRTRDLSSLET-------------- 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 356 vnskkmlgkyntpVSYrmaktlvfskvktslgldhchsfisGTAPLN----QETAEFFLsldiPI-GELYGLSESsgPHT 430
Cdd:PRK06188 286 -------------VYY-------------------------GASPMSpvrlAEAIERFG----PIfAQYYGQTEA--PMV 321
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 431 IS--------NQNNYRLLSCGKILTGCKNMLFQQN-----KDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDL 497
Cdd:PRK06188 322 ITylrkrdhdPDDPKRLTSCGRPTPGLRVALLDEDgrevaQGEVGEICVRGPLVMDGYWNRPEETAEAFRD-GWLHTGDV 400
                        490       500       510
                 ....*....|....*....|....*....|...
gi 574584557 498 GQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:PRK06188 401 AREDEDGFYYIVDRKKDMIVT-GGFNVFPREVE 432
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
225-530 2.16e-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: 2.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIA--GAVTKDFKLTDkheTVVSYLPLSHIAAQMMDIWVPIKIGALTYFA-----Q 297
Cdd:cd05944    5 AAYFHTGGTTGTPKLAQHTHSNEVYNAwmLALNSLFDPDD---VLLCGLPLFHVNGSVVTLLTPLASGAHVVLAgpagyR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 298 ADALKGTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksmglkkkAFVWARNIGFKVNSkkmlgkyntpvsYRMAktl 377
Cdd:cd05944   82 NPGLFDNFWKLVERYRITSLSTVPTVY--------------------AALLQVPVNADISS------------LRFA--- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 378 vfskvktslgldhchsfISGTAPLNQET-AEFFLSLDIPIGELYGLSESSGPHTISNQNN-YRLLSCG----------KI 445
Cdd:cd05944  127 -----------------MSGAAPLPVELrARFEDATGLPVVEGYGLTEATCLVAVNPPDGpKRPGSVGlrlpyarvriKV 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 446 LTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVP 525
Cdd:cd05944  190 LDGVGRLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVAD-GWLNTGDLGRLDADGYLFITGRAKD-LIIRGGHNID 267

                 ....*
gi 574584557 526 PIPVE 530
Cdd:cd05944  268 PALIE 272
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
227-547 7.28e-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: 7.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 227 LIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT-DKHETVVSylPLSHIAAQMMDIWVPIKIGAlTYFAQA--DALKg 303
Cdd:cd17638    5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTeDDRYLIIN--PFFHTFGYKAGIVACLLTGA-TVVPVAvfDVDA- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 304 tLVSTLKEVKPTVFIGVPQIWEKI--HEMVKKnsaksmglkkkafvwarnigFKVNSKK--MLGKYNTPVSY--RMAKTL 377
Cdd:cd17638   81 -ILEAIERERITVLPGPPTLFQSLldHPGRKK--------------------FDLSSLRaaVTGAATVPVELvrRMRSEL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 378 VFSKVKTSLGLDHChsfisGTAPLNQEtaefflsldipigelyglseSSGPHTISNqnnyrllSCGKILTGcknmlFQQN 457
Cdd:cd17638  140 GFETVLTAYGLTEA-----GVATMCRP--------------------GDDAETVAT-------TCGRACPG-----FEVR 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 458 KDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILItAGGENVPPIPVETLVkKKI 537
Cdd:cd17638  183 IADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGAL-AEH 260
                        330
                 ....*....|
gi 574584557 538 PIISNAMLVG 547
Cdd:cd17638  261 PGVAQVAVIG 270
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
225-547 1.02e-20

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: 1.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSyLPLSHIAAQMMdIWVPIKIGALTYFAQADALkgt 304
Cdd:cd17630    3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLS-LPLYHVGGLAI-LVRSLLAGAELVLLERNQA--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 305 LVSTLKEVKPTVFIGVP-QIWekiheMVKKNSAKSMGLKkkafvwarniGFKVnskkmlgkyntpvsyrmaktlVFSkvk 383
Cdd:cd17630   78 LAEDLAPPGVTHVSLVPtQLQ-----RLLDSGQGPAALK----------SLRA---------------------VLL--- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 384 tslgldhchsfisGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQnkdgiGE 463
Cdd:cd17630  119 -------------GGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED-----GE 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 464 ICLWGRHIFMGYLESETEttEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVkKKIPIISNA 543
Cdd:cd17630  181 IWVGGASLAMGYLRGQLV--PEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAAL-AAHPAVRDA 256

                 ....
gi 574584557 544 MLVG 547
Cdd:cd17630  257 FVVG 260
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
108-551 5.06e-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: 5.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 108 VGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEndQQLQKILSIPQSSLEPLKAIIQYRLP 187
Cdd:cd05909   34 VGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTS--KQFIEKLKLHHLFDVEYDARIVYLED 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 188 MKKNnnlYSWDD----FMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDK 263
Cdd:cd05909  112 LRAK---ISKADkckaFLAGKFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPE 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 264 hETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAqADALKG-TLVSTLKEVKPTVFIGVPQIWekihemvkknsaksMGLK 342
Cdd:cd05909  189 -DVVFGALPFFHSFGLTGCLWLPLLSGIKVVFH-PNPLDYkKIPELIYDKKATILLGTPTFL--------------RGYA 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 343 KKAfvwarnigfkvnskkmlGKYNTPvSYRMAktlvfskvktslgldhchsfISGTAPLNQETAEFFLSL-DIPIGELYG 421
Cdd:cd05909  253 RAA-----------------HPEDFS-SLRLV--------------------VAGAEKLKDTLRQEFQEKfGIRILEGYG 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 422 LSESSGPHTISNQNNYRLLSC-GKILTGCKNMLFQ---QNKDGIGE---ICLWGRHIFMGYLESETETTEAIDDeGWLHS 494
Cdd:cd05909  295 TTECSPVISVNTPQSPNKEGTvGRPLPGMEVKIVSvetHEEVPIGEgglLLVRGPNVMLGYLNEPELTSFAFGD-GWYDT 373
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 574584557 495 GDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKIPIISN--AMLVGDKLK 551
Cdd:cd05909  374 GDIGKIDGEGFLTITGRLSR-FAKIAGEMVSLEAIEDILSEILPEDNEvaVVSVPDGRK 431
PLN02246 PLN02246
4-coumarate--CoA ligase
59-549 1.33e-18

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 89.65  E-value: 1.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  59 ESVNRFGTYPALAskNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLcvgIYAT 138
Cdd:PLN02246  31 ERLSEFSDRPCLI--DGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAV---TTTA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 139 N----SAEVC-QYVITHAKvniLLVENDQQLQKILSIPQSSLEPLKAIIQYRlpmkkNNNLYSWDDFMELGRSIPDTQLe 213
Cdd:PLN02246 106 NpfytPAEIAkQAKASGAK---LIITQSCYVDKLKGLAEDDGVTVVTIDDPP-----EGCLHFSELTQADENELPEVEI- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 214 qviesqKANQCAVLIYTSGTTGIPKGVMLSHDN-ITWIAGAVTKD-----FKLTDkheTVVSYLPLSHIaaqmmdiwvpi 287
Cdd:PLN02246 177 ------SPDDVVALPYSSGTTGLPKGVMLTHKGlVTSVAQQVDGEnpnlyFHSDD---VILCVLPMFHI----------- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 288 kigaltYfaqadALKGTLVSTLKeVKPTVFIgvpqiwekiheMVKKNSAKSMGLKKKafvwarnigFKVNskkmLGKYNT 367
Cdd:PLN02246 237 ------Y-----SLNSVLLCGLR-VGAAILI-----------MPKFEIGALLELIQR---------HKVT----IAPFVP 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 368 PVSYRMAKtlvfSKVKTSLGLDHCHSFISGTAPLNQETAEFFLSlDIP---IGELYGLSESsGPhtisnqnnyrLL---- 440
Cdd:PLN02246 281 PIVLAIAK----SPVVEKYDLSSIRMVLSGAAPLGKELEDAFRA-KLPnavLGQGYGMTEA-GP----------VLamcl 344
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 441 ------------SCG--------KIL---TGCKnmlFQQNKDGigEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDL 497
Cdd:PLN02246 345 afakepfpvksgSCGtvvrnaelKIVdpeTGAS---LPRNQPG--EICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDI 419
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 574584557 498 GQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKiPIISNAMLVGDK 549
Cdd:PLN02246 420 GYIDDDDELFIVDRLKEL-IKYKGFQVAPAELEALLISH-PSIADAAVVPMK 469
PRK07529 PRK07529
AMP-binding domain protein; Validated
199-530 1.46e-18

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 90.01  E-value: 1.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 199 DFMELGRSIPDTQLEQViESQKANQCAVLIYTSGTTGIPKGVMLSHDNIT---WIAGAVTKDfkltDKHETVVSYLPLSH 275
Cdd:PRK07529 191 DFDAELARQPGDRLFSG-RPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVanaWLGALLLGL----GPGDTVFCGLPLFH 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 276 IAAQMMDIWVPIKIGALTYFAQADALKG-TLVSTLKEV----KPTVFIGVPqiwekihemvkknSAKSMGLKKKafVWAR 350
Cdd:PRK07529 266 VNALLVTGLAPLARGAHVVLATPQGYRGpGVIANFWKIveryRINFLSGVP-------------TVYAALLQVP--VDGH 330
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 351 NIgfkvnskkmlgkyntpvsyrmaktlvfSKVKTslgldhchsFISGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPH 429
Cdd:PRK07529 331 DI---------------------------SSLRY---------ALCGAAPLPVEVFRRFEAaTGVRIVEGYGLTEATCVS 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 430 TIsnqnNY-----RLLSCG--------KILTGCKNMLFQQN--KDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHS 494
Cdd:PRK07529 375 SV----NPpdgerRIGSVGlrlpyqrvRVVILDDAGRYLRDcaVDEVGVLCIAGPNVFSGYLEAAHNKGLWLED-GWLNT 449
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 574584557 495 GDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 530
Cdd:PRK07529 450 GDLGRIDADGYFWLTGRAKD-LIIRGGHNIDPAAIE 484
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
219-541 1.61e-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: 89.08  E-value: 1.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 219 QKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSH----IAAQMmdiwVPIKIGALTY 294
Cdd:cd05908  103 ELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTK-DRILSWMPLTHdmglIAFHL----APLIAGMNQY 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 295 FAqadalkgtlvstlkevkPT-VFIGVPQIW-EKIHEmvkknsaksmglKKKAFVWARNIGFKVnskkMLGKYNTPVSYr 372
Cdd:cd05908  178 LM-----------------PTrLFIRRPILWlKKASE------------HKATIVSSPNFGYKY----FLKTLKPEKAN- 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 373 maktlvfskvktSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIG-------ELYGLSESS--------GPHTI------ 431
Cdd:cd05908  224 ------------DWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGlkrnailPVYGLAEASvgaslpkaQSPFKtitlgr 291
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 432 --------------SNQNNYRLLSCGKILTGCK-NMLFQQNK---DG-IGEICLWGRHIFMGYLESETETTEAIDDEGWL 492
Cdd:cd05908  292 rhvthgepepevdkKDSECLTFVEVGKPIDETDiRICDEDNKilpDGyIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWL 371
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 574584557 493 HSGDLGQLDGlGFLYVTGHIKEILITaGGENVPPIPVETLVKKKIPIIS 541
Cdd:cd05908  372 KTGDLGFIRN-GRLVITGREKDIIFV-NGQNVYPHDIERIAEELEGVEL 418
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
229-547 1.86e-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: 87.33  E-value: 1.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 229 YTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYlPLSHIAAQMMDIWVPIKIGALTYFAQA--DALkgTLV 306
Cdd:cd05917    9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPV-PLFHCFGSVLGVLACLTHGATMVFPSPsfDPL--AVL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 307 STLKEVKPTVFIGVPQIWEKIhemvkknsaksmglkkkafvwarnigfkVNSKKMLgKYNtpvsyrmaktlvFSKVKTSl 386
Cdd:cd05917   86 EAIEKEKCTALHGVPTMFIAE----------------------------LEHPDFD-KFD------------LSSLRTG- 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 387 gldhchsfISGTAPLNQETAEFFLSL----DIPIGelYGLSESSGPHTISNQNN---YRLLSCGKIL----------TGC 449
Cdd:cd05917  124 --------IMAGAPCPPELMKRVIEVmnmkDVTIA--YGMTETSPVSTQTRTDDsieKRVNTVGRIMphteakivdpEGG 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 450 KNMLFQQnkdgIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPV 529
Cdd:cd05917  194 IVPPVGV----PGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIR-GGENIYPREI 268
                        330
                 ....*....|....*...
gi 574584557 530 ETLVKKKiPIISNAMLVG 547
Cdd:cd05917  269 EEFLHTH-PKVSDVQVVG 285
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
53-533 3.79e-18

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 88.28  E-value: 3.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  53 IPEFFRESVNRFGTYPALaSKNGKKweiLNFNQYYEACRKAAKSLIKL-GLERFHGVGILGFNSAEWFITAVGAILAGGL 131
Cdd:PRK05677  26 IQAVLKQSCQRFADKPAF-SNLGKT---LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLI 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 132 CVG---IYATNSAEvCQYVITHAKVNILLVENDQQLQKILsiPQSSLE------------PLK-----AIIQYRLPMKKN 191
Cdd:PRK05677 102 VVNtnpLYTAREME-HQFNDSGAKALVCLANMAHLAEKVL--PKTGVKhvivtevadmlpPLKrllinAVVKHVKKMVPA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 192 NNL---YSWDDFMELGRSIPDTQLeqvieSQKANQCAVLIYTSGTTGIPKGVMLSHDNItwIAGAV-TKDF---KLTDKH 264
Cdd:PRK05677 179 YHLpqaVKFNDALAKGAGQPVTEA-----NPQADDVAVLQYTGGTTGVAKGAMLTHRNL--VANMLqCRALmgsNLNEGC 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 265 ETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIwekihemvkknsaksmglkkk 344
Cdd:PRK05677 252 EILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTL--------------------- 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 345 aFV-WARNIGFKvnskkmlgkyntpvsyrmakTLVFSKVKTSLgldhchsfiSGTAPLNQETAEFFLSLD-IPIGELYGL 422
Cdd:PRK05677 311 -FVaLCNNEAFR--------------------KLDFSALKLTL---------SGGMALQLATAERWKEVTgCAICEGYGM 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 423 SESSGPHTISNQNNYRLLSCGKIL--TGCKNMlfqqNKDG-------IGEICLWGRHIFMGYLESETETTEAIDDEGWLH 493
Cdd:PRK05677 361 TETSPVVSVNPSQAIQVGTIGIPVpsTLCKVI----DDDGnelplgeVGELCVKGPQVMKGYWQRPEATDEILDSDGWLK 436
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 574584557 494 SGDLGQLDGLGFLYVTGHIKEILITAGGeNVPPIPVETLV 533
Cdd:PRK05677 437 TGDIALIQEDGYMRIVDRKKDMILVSGF-NVYPNELEDVL 475
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
85-547 1.37e-17

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 86.39  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  85 QYYEACRKAAKSLIKLGLERFHGVGILGFNSA---EWF--ITAVGAILAgglcvgiyATNSaevcQYVITHAKVNILLVE 159
Cdd:PLN02860  37 EFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDlylEWLlaVACAGGIVA--------PLNY----RWSFEEAKSAMLLVR 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 160 ndqqlQKILSIPQSsleplkaiIQYRLPMKKNNNLYS--WDDFME-LGRSI---------PDTQLEQVIESQKANQC--- 224
Cdd:PLN02860 105 -----PVMLVTDET--------CSSWYEELQNDRLPSlmWQVFLEsPSSSVfiflnsfltTEMLKQRALGTTELDYAwap 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 --AVLI-YTSGTTGIPKGVMLSHDNIT-------WIAGAVTKDFKLtdkHETvvsylPLSHIA------AQMMdiwvpik 288
Cdd:PLN02860 172 ddAVLIcFTSGTTGRPKGVTISHSALIvqslakiAIVGYGEDDVYL---HTA-----PLCHIGglssalAMLM------- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 289 IGA----LTYFAQADALKgtlvsTLKEVKPTVFIGVPQIWEKIHEMvkknSAKSMGLKKKAFVwarnigfkvnsKKML-G 363
Cdd:PLN02860 237 VGAchvlLPKFDAKAALQ-----AIKQHNVTSMITVPAMMADLISL----TRKSMTWKVFPSV-----------RKILnG 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 364 KYNTPVSYRMAKTLVF--SKVKTSLGL-DHCHSFIsgtaplnqetaefFLSLDIPIGELYGLSESSGPHTISNQNNYRLL 440
Cdd:PLN02860 297 GGSLSSRLLPDAKKLFpnAKLFSAYGMtEACSSLT-------------FMTLHDPTLESPKQTLQTVNQTKSSSVHQPQG 363
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 441 SC-GKILTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITA 519
Cdd:PLN02860 364 VCvGKPAPHVELKIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDR-IKT 442
                        490       500
                 ....*....|....*....|....*...
gi 574584557 520 GGENVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:PLN02860 443 GGENVYPEEVEAVLSQH-PGVASVVVVG 469
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
74-642 2.52e-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: 2.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  74 NGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGI---YATNSAEVC--QYVI 148
Cdd:cd05921   19 GNGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVspaYSLMSQDLAklKHLF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 149 THAKVNILLVENDQQLQKILSIPQSSLEPLkaIIQYRLPMKKNNNLyswddFMELGRSIPDTQLEQVIESQKANQCAVLI 228
Cdd:cd05921   99 ELLKPGLVFAQDAAPFARALAAIFPLGTPL--VVSRNAVAGRGAIS-----FAELAATPPTAAVDAAFAAVGPDTVAKFL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 229 YTSGTTGIPKGVMLSHDNITWIAGAVTKDF-KLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFaqaDALK----- 302
Cdd:cd05921  172 FTSGSTGLPKAVINTQRMLCANQAMLEQTYpFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGTLYI---DDGKpmpgg 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 303 -GTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAksmgLKKKAFvwarnigfkvnsKKMlgkyntpvsyrmaktlvfsk 381
Cdd:cd05921  249 fEETLRNLREISPTVYFNVPAGWEMLVAALEKDEA----LRRRFF------------KRL-------------------- 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 382 vktslgldhcHSFISGTAPLNQETAEfflSLD----------IPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKN 451
Cdd:cd05921  293 ----------KLMFYAGAGLSQDVWD---RLQalavatvgerIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTEL 359
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 452 MLFQQnkDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQL----DGLGFLYVTGHIKEILITAGGENVPPI 527
Cdd:cd05921  360 KLVPS--GGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLadpdDPAKGLVFDGRVAEDFKLASGTWVSVG 437
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 528 PVET-LVKKKIPIISNAMLVGDKLKFLSMLLtlkcemnqmsgepldklnFEAINFCRGL-GSQASTVTEIVKQqdPLVYK 605
Cdd:cd05921  438 PLRArAVAACAPLVHDAVVAGEDRAEVGALV------------------FPDLLACRRLvGLQEASDAEVLRH--AKVRA 497
                        570       580       590
                 ....*....|....*....|....*....|....*..
gi 574584557 606 AIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGEL 642
Cdd:cd05921  498 AFRDRLAALNGEATGSSSRIARALLLDEPPSIDKGEI 534
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
226-547 3.03e-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: 3.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 226 VLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVpIKIGA----LTYFAQADAL 301
Cdd:cd17637    4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTE-ADVYLNMLPLFHIAGLNLALAT-FHAGGanvvMEKFDPAEAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 302 KgtlvsTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKsmglkkkafvwarnigfkvnskkmlgkyntpvsyrmaktlvFSK 381
Cdd:cd17637   82 E-----LIEEEKVTLMGSFPPILSNLLDAAEKSGVD-----------------------------------------LSS 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 382 VKTSLGLDhchsfisgtAPlnqETAEFFLSL-DIPIGELYGLSESSGPHTISNQNNyRLLSCGKILTGCKNMLFQQNKDG 460
Cdd:cd17637  116 LRHVLGLD---------AP---ETIQRFEETtGATFWSLYGQTETSGLVTLSPYRE-RPGSAGRPGPLVRVRIVDDNDRP 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 461 I-----GEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHI--KEiLITAGGENVPPIPVETlV 533
Cdd:cd17637  183 VpagetGEIVVRGPLVFQGYWNLPELTAYTFRN-GWHHTGDLGRFDEDGYLWYAGRKpeKE-LIKPGGENVYPAEVEK-V 259
                        330
                 ....*....|....
gi 574584557 534 KKKIPIISNAMLVG 547
Cdd:cd17637  260 ILEHPAIAEVCVIG 273
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
223-547 3.19e-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: 3.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 223 QCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQA-DAL 301
Cdd:cd05903   94 AVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPG-DVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIwDPD 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 302 KGtlVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKkaFVWArnigfkvnskkmlGKYNTPVSYRMAKTLVFSK 381
Cdd:cd05903  173 KA--LALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRT--FVCG-------------GATVPRSLARRAAELLGAK 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 382 VKTSLGLDHCHSFISGTAPLNQETAEF-----FLSLDIPIGELYGLSESSGPhtisnqnnyrllscgkiltgcknmlfqq 456
Cdd:cd05903  236 VCSAYGSTECPGAVTSITPAPEDRRLYtdgrpLPGVEIKVVDDTGATLAPGV---------------------------- 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 457 nkdgIGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVkKK 536
Cdd:cd05903  288 ----EGELLSRGPSVFLGYLDRP-DLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIR-GGENIPVLEVEDLL-LG 360
                        330
                 ....*....|.
gi 574584557 537 IPIISNAMLVG 547
Cdd:cd05903  361 HPGVIEAAVVA 371
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
75-547 3.65e-17

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 84.63  E-value: 3.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  75 GKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFItavgAILA----GGLCVGIYATNSAEVCQYVITH 150
Cdd:PRK03640  25 EKKV---TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMIL----VIHAlqqlGAVAVLLNTRLSREELLWQLDD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 151 AKVNILLVenDQQLQKILSIPQSSLeplkaiiqyrlpmkknnnlysWDDFMELGRSIPDTQleqviESQKANQCAVLIYT 230
Cdd:PRK03640  98 AEVKCLIT--DDDFEAKLIPGISVK---------------------FAELMNGPKEEAEIQ-----EEFDLDEVATIMYT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 231 SGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHI---AAQMMDIWVPIKIGALTYFaqaDAlkgtlvs 307
Cdd:PRK03640 150 SGTTGKPKGVIQTYGNHWWSAVGSALNLGLTE-DDCWLAAVPIFHIsglSILMRSVIYGMRVVLVEKF---DA------- 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 308 tlkevkptvfigvpqiwEKIHEMVKKNSAKSMGlkkkafvwarnigfkvnskkmlgkyntpVSYRMAKTLVfskvkTSLG 387
Cdd:PRK03640 219 -----------------EKINKLLQTGGVTIIS----------------------------VVSTMLQRLL-----ERLG 248
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 388 LDHCHS----FISGTAPLNQETAEFFLSLDIPIGELYGLSESSG------PHTISNqnnyRLLSCGKILTGC-----KNM 452
Cdd:PRK03640 249 EGTYPSsfrcMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETASqivtlsPEDALT----KLGSAGKPLFPCelkieKDG 324
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 453 LFQQNKDgIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETl 532
Cdd:PRK03640 325 VVVPPFE-EGEIVVKGPNVTKGYLNREDATRETFQD-GWFKTGDIGYLDEEGFLYVLDRRSD-LIISGGENIYPAEIEE- 400
                        490
                 ....*....|....*
gi 574584557 533 VKKKIPIISNAMLVG 547
Cdd:PRK03640 401 VLLSHPGVAEAGVVG 415
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
225-526 8.35e-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: 8.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQadalkgt 304
Cdd:cd05931  152 AYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDP-GDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMS------- 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 305 lvstlkevkPTVFIGVPQIWekiHEMVKKNSAKSMGlkkkafvwARNIGF-----KVNSKKM----LGKYNT------PV 369
Cdd:cd05931  224 ---------PAAFLRRPLRW---LRLISRYRATISA--------APNFAYdlcvrRVRDEDLegldLSSWRValngaePV 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 370 SyrmAKTL-VFSKVKTSLGLD-HCHS----------FISGTAPLNQETAEFFLSLdipigELYGLSESSGPHTisnQNNY 437
Cdd:cd05931  284 R---PATLrRFAEAFAPFGFRpEAFRpsyglaeatlFVSGGPPGTGPVVLRVDRD-----ALAGRAVAVAADD---PAAR 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 438 RLLSCGKILTGcknMLF--------QQNKDG-IGEICLWGRHIFMGYL--ESETETT----EAIDDEGWLHSGDLGQLDG 502
Cdd:cd05931  353 ELVSCGRPLPD---QEVrivdpetgRELPDGeVGEIWVRGPSVASGYWgrPEATAETfgalAATDEGGWLRTGDLGFLHD 429
                        330       340
                 ....*....|....*....|....
gi 574584557 503 lGFLYVTGHIKEILITAgGENVPP 526
Cdd:cd05931  430 -GELYITGRLKDLIIVR-GRNHYP 451
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
225-533 1.26e-16

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 83.56  E-value: 1.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNI-------TWIAGAVtkdfkLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGAltyfaq 297
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRNMlanleqaKAAYGPL-----LHPGKELVVTALPLYHIFALTVNCLLFIELGG------ 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 298 adalKGTLVSTLKEvkptvfigvpqiwekIHEMVKKnsaksmgLKKKAFVWARNigfkVNSkkmlgKYNTPVSYRMAKTL 377
Cdd:PRK08974 278 ----QNLLITNPRD---------------IPGFVKE-------LKKYPFTAITG----VNT-----LFNALLNNEEFQEL 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 378 VFSKVKTSLGldhchsfisGTAPLNQETAEFFLSL-DIPIGELYGLSESS-----GPHTISNQNNyrllSCG-------- 443
Cdd:PRK08974 323 DFSSLKLSVG---------GGMAVQQAVAERWVKLtGQYLLEGYGLTECSplvsvNPYDLDYYSG----SIGlpvpstei 389
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 444 KILTGCKNMLFQqnkDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGEN 523
Cdd:PRK08974 390 KLVDDDGNEVPP---GEPGELWVKGPQVMLGYWQRPEATDEVIKD-GWLATGDIAVMDEEGFLRIVDRKKDM-ILVSGFN 464
                        330
                 ....*....|
gi 574584557 524 VPPIPVETLV 533
Cdd:PRK08974 465 VYPNEIEDVV 474
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
79-533 1.39e-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: 1.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  79 EILNFNQYYEACRKAAKSLIKLGLERFHGVgILGFNSAEWFITAV-GAILAGGLCV-----GIYATNSAEvcqyvITHAK 152
Cdd:cd05906   38 EFQSYQDLLEDARRLAAGLRQLGLRPGDSV-ILQFDDNEDFIPAFwACVLAGFVPApltvpPTYDEPNAR-----LRKLR 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 153 vNILlvendQQLQK--ILSIPqSSLEPLKAIIQYRlpmkknnnlySWDDFMELGRSI-PDTQLEQVIESQKANQCAVLIY 229
Cdd:cd05906  112 -HIW-----QLLGSpvVLTDA-ELVAEFAGLETLS----------GLPGIRVLSIEElLDTAADHDLPQSRPDDLALLML 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 230 TSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALkgtlvstL 309
Cdd:cd05906  175 TSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQ-DVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPTEEI-------L 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 310 KEvkPTVFIgvpqiwekihEMVKKNSAksmglkkkAFVWARNigFkvnskkMLGKYNTPVSYRMAKTLVFSKVKtslgld 389
Cdd:cd05906  247 AD--PLRWL----------DLIDRYRV--------TITWAPN--F------AFALLNDLLEEIEDGTWDLSSLR------ 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 390 hchSFISGTAPLNQETAEFFLSLDIPIG-------ELYGLSE-------SSGPHTISNQNNYRLLSCGKILTGCKNMLFQ 455
Cdd:cd05906  293 ---YLVNAGEAVVAKTIRRLLRLLEPYGlppdairPAFGMTEtcsgviySRSFPTYDHSQALEFVSLGRPIPGVSMRIVD 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 456 QNKDG-----IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGlGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:cd05906  370 DEGQLlpegeVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDN-GNLTITGRTKDTIIV-NGVNYYSHEIE 447

                 ...
gi 574584557 531 TLV 533
Cdd:cd05906  448 AAV 450
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
225-520 1.63e-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: 1.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLSHIAAqMMDIWVPIKIGALTYFAQADALKGT 304
Cdd:cd05922  120 ALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI-TADDRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVLDDA 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 305 LVSTLKEVKPTVFIGVPQIWEKIhemvkknsaKSMGLKKKAFVWARnigfkvnskkmlgkYNTPVSYRMAKTLVfskvkt 384
Cdd:cd05922  198 FWEDLREHGATGLAGVPSTYAML---------TRLGFDPAKLPSLR--------------YLTQAGGRLPQETI------ 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 385 slgldhchsfisgtaplnQETAEFFLSLDIPIgeLYGLSESSG------PHTISNqnnyRLLSCGKILTGCKnmLFQQNK 458
Cdd:cd05922  249 ------------------ARLRELLPGAQVYV--MYGQTEATRrmtylpPERILE----KPGSIGLAIPGGE--FEILDD 302
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574584557 459 DG-------IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAG 520
Cdd:cd05922  303 DGtptppgePGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFG 371
AFD_CAR-like cd17632
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ...
225-497 2.46e-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: 2.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNIT--WIAGAVTKDfkLTDKHETVVSYLPLSHIAAQMmdiwvpIKIGALT-----YFAQ 297
Cdd:cd17632  226 ALLIYTSGSTGTPKGAMYTERLVAtfWLKVSSIQD--IRPPASITLNFMPMSHIAGRI------SLYGTLArggtaYFAA 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 298 ADALKgTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKYNTPVsyrmaktl 377
Cdd:cd17632  298 ASDMS-TLFDDLALVRPTELFLVPRVCDMLFQRYQAELDRRSVAGADAETLAERVKAELRERVLGGRLLAAV-------- 368
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 378 vfskvktslgldhchsfiSGTAPLNQETAEFFLS-LDIPIGELYGLSEsSGPHTISNQ------NNYRLLSC---GKILT 447
Cdd:cd17632  369 ------------------CGSAPLSAEMKAFMESlLDLDLHDGYGSTE-AGAVILDGVivrppvLDYKLVDVpelGYFRT 429
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 574584557 448 gcknmlfqQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDL 497
Cdd:cd17632  430 --------DRPHPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDV 471
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
81-547 2.63e-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: 2.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557   81 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILlVEN 160
Cdd:TIGR03098  26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL-VTS 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  161 DQQLQKILSIPQSSLEPLKAII----QYRLPMKKNNNLYSWDDFMELGRSIPdtqLEQVIESQkanqCAVLIYTSGTTGI 236
Cdd:TIGR03098 105 SERLDLLHPALPGCHDLRTLIIvgdpAHASEGHPGEEPASWPKLLALGDADP---PHPVIDSD----MAAILYTSGSTGR 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  237 PKGVMLSHDNItwIAGA--VTKDFKLTDKhETVVSYLPLSHIAA--QMMDIWVpikIGA----LTYFAQADALKgtlvsT 308
Cdd:TIGR03098 178 PKGVVLSHRNL--VAGAqsVATYLENRPD-DRLLAVLPLSFDYGfnQLTTAFY---VGAtvvlHDYLLPRDVLK-----A 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  309 LKEVKPTVFIGVPQIWEKIHEMVKKNSAksmglkkkafvwARNIGFKVNSKKmlgkyntpvsyRMAKTLVfSKVKTSLGL 388
Cdd:TIGR03098 247 LEKHGITGLAAVPPLWAQLAQLDWPESA------------APSLRYLTNSGG-----------AMPRATL-SRLRSFLPN 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  389 dhchsfisgtaplnqetAEFFLsldipigeLYGLSESSGPHTISNQN-NYRLLSCGKILTGCKNMLFqqNKDG------- 460
Cdd:TIGR03098 303 -----------------ARLFL--------MYGLTEAFRSTYLPPEEvDRRPDSIGKAIPNAEVLVL--REDGsecapge 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  461 IGEICLWGRHIFMGYLESETETTEAI------DDEGWLH-----SGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPV 529
Cdd:TIGR03098 356 EGELVHRGALVAMGYWNDPEKTAERFrplppfPGELHLPelavwSGDTVRRDEEGFLYFVGR-RDEMIKTSGYRVSPTEV 434
                         490
                  ....*....|....*...
gi 574584557  530 ETlVKKKIPIISNAMLVG 547
Cdd:TIGR03098 435 EE-VAYATGLVAEAVAFG 451
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
225-530 2.74e-15

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 79.27  E-value: 2.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGAltyfaqaDALKGT 304
Cdd:PRK07768 155 ALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFHDMGMVGFLTVPMYFGA-------ELVKVT 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 305 lvstlkevkPTVFIGVPQIWekihemvkknsAKSMGLKKKAFVWARNIGFKVNSKKmLGKYNTPVSYRMaktlvfSKVKT 384
Cdd:PRK07768 228 ---------PMDFLRDPLLW-----------AELISKYRGTMTAAPNFAYALLARR-LRRQAKPGAFDL------SSLRF 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 385 SLgldhchsfiSGTAPLNQETAEFFLSLDIPIG-------ELYGLSESSGPHTIS------------------------- 432
Cdd:PRK07768 281 AL---------NGAEPIDPADVEDLLDAGARFGlrpeailPAYGMAEATLAVSFSpcgaglvvdevdadllaalrravpa 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 433 -NQNNYRLLSCGKILTGCKNMLFQQNKD-----GIGEICLWGRHIFMGYLESETeTTEAIDDEGWLHSGDLGQLDGLGFL 506
Cdd:PRK07768 352 tKGNTRRLATLGPPLPGLEVRVVDEDGQvlpprGVGVIELRGESVTPGYLTMDG-FIPAQDADGWLDTGDLGYLTEEGEV 430
                        330       340
                 ....*....|....*....|....
gi 574584557 507 YVTGHIKEILITaGGENVPPIPVE 530
Cdd:PRK07768 431 VVCGRVKDVIIM-AGRNIYPTDIE 453
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
225-533 7.36e-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: 7.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKgT 304
Cdd:cd17635    4 LAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK-S 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 305 LVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLkkkafvwaRNIGFkvnskkmlgkyntpvsyrmaktlvfskvkt 384
Cdd:cd17635   83 LFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSL--------RLIGY------------------------------ 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 385 slgldhchsfiSGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLL-SCGKILTGCK-----NMLFQQNK 458
Cdd:cd17635  125 -----------GGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIEInAVGRPYPGVDvylaaTDGIAGPS 193
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 574584557 459 DGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLV 533
Cdd:cd17635  194 ASFGTIWIKSPANMLGYWNNPERTAEVLID-GWVNTGDLGERREDGFLFITGRSSES-INCGGVKIAPDEVERIA 266
PRK06145 PRK06145
acyl-CoA synthetase; Validated
68-547 1.58e-14

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 76.46  E-value: 1.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  68 PALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYV 147
Cdd:PRK06145  19 AALVYRD----QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYI 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 148 ITHAKVNILLVenDQQLQKIlsipqSSLEPLKAIIqyrlpmkknnNLYSWDDFMELGRS-IPDTQLEQVIESQKANqcav 226
Cdd:PRK06145  95 LGDAGAKLLLV--DEEFDAI-----VALETPKIVI----------DAAAQADSRRLAQGgLEIPPQAAVAPTDLVR---- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 227 LIYTSGTTGIPKGVMLSHDNITW------IAGAVTKDFKLTdkhetVVSylPLSHIAA-QMMDIWVPIKIGALTYFAQAD 299
Cdd:PRK06145 154 LMYTSGTTDRPKGVMHSYGNLHWksidhvIALGLTASERLL-----VVG--PLYHVGAfDLPGIAVLWVGGTLRIHREFD 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 300 AlkGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSaksmgLKKKAFVWArnIGfkvnskkmlGKYNTPVSYRMAKTLVF 379
Cdd:PRK06145 227 P--EAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDR-----FDLDSLAWC--IG---------GGEKTPESRIRDFTRVF 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 380 SKVKtslgldhchsFISGtaplnqetaefflsldipigelYGLSESSGPHTISNQNNY--RLLSCGK--------ILTGC 449
Cdd:PRK06145 289 TRAR----------YIDA----------------------YGLTETCSGDTLMEAGREieKIGSTGRalahveirIADGA 336
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 450 KNMLFQQNKdgiGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPV 529
Cdd:PRK06145 337 GRWLPPNMK---GEICMRGPKVTKGYWKDPEKTAEAFYG-DWFRSGDVGYLDEEGFLYLTDRKKDMIIS-GGENIASSEV 411
                        490
                 ....*....|....*...
gi 574584557 530 ETLVkKKIPIISNAMLVG 547
Cdd:PRK06145 412 ERVI-YELPEVAEAAVIG 428
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
225-530 2.55e-14

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 76.08  E-value: 2.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVsYLPLSH----IAAQMMDIwvpIKIGALTYFAQADA 300
Cdd:PRK05852 179 AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVA-VMPLYHghglIAALLATL---ASGGAVLLPARGRF 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 301 LKGTLVSTLKEVKPTVFIGVPqiweKIHEMvkknsaksmglkkkafvwarnigfkvnskkMLGKYNTPVSYRMAKTLVFS 380
Cdd:PRK05852 255 SAHTFWDDIKAVGATWYTAVP----TIHQI------------------------------LLERAATEPSGRKPAALRFI 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 381 KvktslgldhchsfiSGTAPLNQETAEF----FLSldiPIGELYGLSE---------------------SSGPHTISNQN 435
Cdd:PRK05852 301 R--------------SCSAPLTAETAQAlqteFAA---PVVCAFGMTEathqvtttqiegigqtenpvvSTGLVGRSTGA 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 436 NYRLL-SCGKILTgcknmlfqqnKDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKE 514
Cdd:PRK05852 364 QIRIVgSDGLPLP----------AGAVGEVWLRGTTVVRGYLGDPTITAANFTD-GWLRTGDLGSLSAAGDLSIRGRIKE 432
                        330
                 ....*....|....*.
gi 574584557 515 iLITAGGENVPPIPVE 530
Cdd:PRK05852 433 -LINRGGEKISPERVE 447
PLN03102 PLN03102
acyl-activating enzyme; Provisional
85-545 5.35e-14

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 75.06  E-value: 5.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  85 QYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEND--- 161
Cdd:PLN03102  44 QTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSfep 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 162 --QQLQKILSIPQSSLEPLKAII-QYRLPMKKNNNLYSWDDFMELGRSIPdTQLEQVIESQKANQCAVLIYTSGTTGIPK 238
Cdd:PLN03102 124 laREVLHLLSSEDSNLNLPVIFIhEIDFPKRPSSEELDYECLIQRGEPTP-SLVARMFRIQDEHDPISLNYTSGTTADPK 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 239 GVMLSHDnitwiaGAvtkdfkltdkhetvvsYL-PLSHIAAQMMDIWvPIKIGALTYF-------AQADALKGTLVSTLK 310
Cdd:PLN03102 203 GVVISHR------GA----------------YLsTLSAIIGWEMGTC-PVYLWTLPMFhcngwtfTWGTAARGGTSVCMR 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 311 EVKptvfigVPQIWEKIhEMvkkNSAKSMGLKKKAFvwarNIGFKVNSkkmlgkynTPVSYRMAKTLVfskvktslgldh 390
Cdd:PLN03102 260 HVT------APEIYKNI-EM---HNVTHMCCVPTVF----NILLKGNS--------LDLSPRSGPVHV------------ 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 391 chsfISGTAPLNQETAEFFLSLDIPIGELYGLSESSGP------------------HTISNQNNYRLLSCGKILTGCKNM 452
Cdd:PLN03102 306 ----LTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPvlfcewqdewnrlpenqqMELKARQGVSILGLADVDVKNKET 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 453 LFQQNKDG--IGEICLWGRHIFMGYLESETETTEAIDdEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:PLN03102 382 QESVPRDGktMGEIVIKGSSIMKGYLKNPKATSEAFK-HGWLNTGDVGVIHPDGHVEIKDRSKDIIIS-GGENISSVEVE 459
                        490
                 ....*....|....*
gi 574584557 531 TLVKKKIPIISNAML 545
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 ...
81-547 5.35e-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: 5.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  81 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVen 160
Cdd:cd05935    2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 161 dqqlqkilsipQSSLEPLkaiiqyrlpmkknnnlyswddfmelgrsipdtqleqviesqkanqcAVLIYTSGTTGIPKGV 240
Cdd:cd05935   80 -----------GSELDDL----------------------------------------------ALIPYTSGTTGLPKGC 102
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 241 MLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGAlTYFAQADALKGTLVSTLKEVKPTVfigv 320
Cdd:cd05935  103 MHTHFSAAANALQSAVWTGLTPS-DVILACLPLFHVTGFVGSLNTAVYVGG-TYVLMARWDRETALELIEKYKVTF---- 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 321 pqiWEKIHEMVKKNSAkSMGLKKKAFvwarnigfkvNSKKMLGKYNTPVSYRMAKtlvfsKVKTSLGLDHChsfisgtap 400
Cdd:cd05935  177 ---WTNIPTMLVDLLA-TPEFKTRDL----------SSLKVLTGGGAPMPPAVAE-----KLLKLTGLRFV--------- 228
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 401 lnqetaefflsldipigELYGLSESSgPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGI-------GEICLWGRHIFM 473
Cdd:cd05935  229 -----------------EGYGLTETM-SQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRelppnevGEIVVRGPQIFK 290
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 574584557 474 GYLESETETTEA-IDDEG--WLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:cd05935  291 GYWNRPEETEESfIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKR-MINVSGFKVWPAEVEAKLYKH-PAI*EVCVIS 365
PRK09088 PRK09088
acyl-CoA synthetase; Validated
225-547 8.22e-14

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 74.46  E-value: 8.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNitwiAGAVTKDFKLTDKHETVVSYL---PLSHIaaqmmdiwvpikIGALTYFAQADAL 301
Cdd:PRK09088 138 SLILFTSGTSGQPKGVMLSERN----LQQTAHNFGVLGRVDAHSSFLcdaPMFHI------------IGLITSVRPVLAV 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 302 KGT-LVSTLKEVKPTV------------FIGVPQIWEKIHemvkknsaksmglkkkafvwaRNIGFKVNSkkmlgkyntp 368
Cdd:PRK09088 202 GGSiLVSNGFEPKRTLgrlgdpalgithYFCVPQMAQAFR---------------------AQPGFDAAA---------- 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 369 vsyrmaktlvfskvktslgLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSE-------SSGPHTISNqnnyRLLS 441
Cdd:PRK09088 251 -------------------LRHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEagtvfgmSVDCDVIRA----KAGA 307
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 442 CGKILTGCKNMLFQQNKDGI-----GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIL 516
Cdd:PRK09088 308 AGIPTPTVQTRVVDDQGNDCpagvpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF 387
                        330       340       350
                 ....*....|....*....|....*....|.
gi 574584557 517 ITaGGENVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:PRK09088 388 IS-GGENVYPAEIEAVLADH-PGIRECAVVG 416
PRK07470 PRK07470
acyl-CoA synthetase; Validated
420-547 9.12e-14

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 74.31  E-value: 9.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 420 YGLSESSG-----P---HTISNQNNYRLLSCGKILTGcknMLFQ-QNKDG-------IGEICLWGRHIFMGYLESETETT 483
Cdd:PRK07470 312 FGLGEVTGnitvlPpalHDAEDGPDARIGTCGFERTG---MEVQiQDDEGrelppgeTGEICVIGPAVFAGYYNNPEANA 388
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 574584557 484 EAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVEtlvkKKI---PIISNAMLVG 547
Cdd:PRK07470 389 KAFRD-GWFRTGDLGHLDARGFLYITGRASDMYIS-GGSNVYPREIE----EKLlthPAVSEVAVLG 449
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
206-512 1.27e-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: 1.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 206 SIPDTQLEQVIESQKA-------NQCAVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVtKDFKLTDkHETVVSYLPLSHIA 277
Cdd:cd05945   74 SSPAERIREILDAAKPalliadgDDNAYIIFTSGSTGRPKGVQISHDNLvSFTNWML-SDFPLGP-GDVFLNQAPFSFDL 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 278 AqMMDIWVPIKIGALTYFAQADALK--GTLVSTLKEVKPTVFIGVPQIWEkihemvkknsaksMGLKKKAFvwarnigfk 355
Cdd:cd05945  152 S-VMDLYPALASGATLVPVPRDATAdpKQLFRFLAEHGITVWVSTPSFAA-------------MCLLSPTF--------- 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 356 vNSKKMlgkyntpvsyrmaKTLVfskvktslgldhcHSFISGTaPLNQETAEFFLSL--DIPIGELYGLSESSGP---HT 430
Cdd:cd05945  209 -TPESL-------------PSLR-------------HFLFCGE-VLPHKTARALQQRfpDARIYNTYGPTEATVAvtyIE 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 431 ISNQ--NNYRLLSCGKILTGCKNMLFqqNKDG-------IGEICLWGRHIFMGYLESETETTEA---IDDEGWLHSGDLG 498
Cdd:cd05945  261 VTPEvlDGYDRLPIGYAKPGAKLVIL--DEDGrpvppgeKGELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLV 338
                        330
                 ....*....|....
gi 574584557 499 QLDGLGFLYVTGHI 512
Cdd:cd05945  339 RLEADGLLFYRGRL 352
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
207-547 1.32e-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: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 207 IPDTQLEQVIESQKAnqCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSylplshiAAQMM----- 281
Cdd:cd05919   78 ARDCEARLVVTSADD--IAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFS-------SAKMFfgygl 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 282 --DIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWekihemvkKNSAKSMGLKKKAFVWARnigfkvnsk 359
Cdd:cd05919  149 gnSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFY--------ANLLDSCAGSPDALRSLR--------- 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 360 kmlgkyntpvsyrmaktlvfskvktslgldHChsfISGTAPLNQETAEFFLS-LDIPIGELYGLSESSgpHT-ISNQ-NN 436
Cdd:cd05919  212 ------------------------------LC---VSAGEALPRGLGERWMEhFGGPILDGIGATEVG--HIfLSNRpGA 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 437 YRLLSCGKILTGCKNMLFqqNKDG-------IGEICLWGRHIFMGYLESeTETTEAIDDEGWLHSGDLGQLDGLGFLYVT 509
Cdd:cd05919  257 WRLGSTGRPVPGYEIRLV--DEEGhtippgeEGDLLVRGPSAAVGYWNN-PEKSRATFNGGWYRTGDKFCRDADGWYTHA 333
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 574584557 510 GHIKEILITaGGENVPPIPVETLVkKKIPIISNAMLVG 547
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, ...
229-547 3.91e-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: 70.90  E-value: 3.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 229 YTSGTTGIPKGVMLSHDniTWIAGAVT--KDFKLtDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGtlV 306
Cdd:cd17633    7 FTSGTTGLPKAYYRSER--SWIESFVCneDLFNI-SGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSW--I 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 307 STLKEVKPTVFIGVPQiwekiheMVKknsaksmglkkkafvwarnigfkvnskkMLGKYNTPVSyrmaktlvfsKVKtsl 386
Cdd:cd17633   82 RKINQYNATVIYLVPT-------MLQ----------------------------ALARTLEPES----------KIK--- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 387 gldhchSFISGTAPLNQETAEFF--LSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGIGEI 464
Cdd:cd17633  114 ------SIFSSGQKLFESTKKKLknIFPKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIGKI 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 465 CLWGRHIFMGYLESEtetteAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVkKKIPIISNAM 544
Cdd:cd17633  188 FVKSEMVFSGYVRGG-----FSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIII-GGINIFPTEIESVL-KAIPGIEEAI 260

                 ...
gi 574584557 545 LVG 547
Cdd:cd17633  261 VVG 263
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
216-662 6.57e-13

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 72.06  E-value: 6.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 216 IESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTK-DFKLTDKHETVVSYLPLSHI-------AAQMMDIWVPI 287
Cdd:PTZ00342 298 IQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKhSIFKKYNPKTHLSYLPISHIyerviayLSFMLGGTINI 377
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 288 KIGALTYFAqadalkgtlvSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKK---KAFVWARNIGFKVNSKKMLGK 364
Cdd:PTZ00342 378 WSKDINYFS----------KDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRflvKKILSLRKSNNNGGFSKFLEG 447
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 365 YnTPVSYRMAktlvfSKVKTSLGLdhchsFISGTAPLNQETA-EFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCG 443
Cdd:PTZ00342 448 I-THISSKIK-----DKVNPNLEV-----ILNGGGKLSPKIAeELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIG 516
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 444 KILtgCKNMLFQ-------QNKDGI--GEICLWGRHIFMGY-LESETeTTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIK 513
Cdd:PTZ00342 517 GPI--SPNTKYKvrtwetyKATDTLpkGELLIKSDSIFSGYfLEKEQ-TKNAFTEDGYFKTGDIVQINKNGSLTFLDRSK 593
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 514 EILITAGGENvppIPVETL--VKKKIPIISNAMLVGDK-----LKFLSM--LLTLKC----EMNQMSG----EPLDKLNF 576
Cdd:PTZ00342 594 GLVKLSQGEY---IETDMLnnLYSQISFINFCVVYGDDsmdgpLAIISVdkYLLFKClkddNMLESTGinekNYLEKLTD 670
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 577 EAINfcrglgsqASTVTEIVKQQDPLVYKaiQQGINAVNqeAMNNAQRIEK-WvilekDFSIYggeLGPMMKLKRHFVAQ 655
Cdd:PTZ00342 671 ETIN--------NNIYVDYVKGKMLEVYK--KTNLNRYN--IINDIYLTSKvW-----DTNNY---LTPTFKVKRFYVFK 730

                 ....*..
gi 574584557 656 KYKKQID 662
Cdd:PTZ00342 731 DYAFFID 737
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
225-547 8.16e-13

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 71.39  E-value: 8.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFK---------LTDKHETVVSYLPLSHIAAQMMDIWVPIKIGaltyf 295
Cdd:PRK12492 210 AVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSqlgpdgqplMKEGQEVMIAPLPLYHIYAFTANCMCMMVSG----- 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 296 aqadalkgtlvstlkevKPTVFIGVPQiweKIHEMVKKnsaksmgLKKKAFvwarnigfkvnsKKMLGkYNTPVSYRMA- 374
Cdd:PRK12492 285 -----------------NHNVLITNPR---DIPGFIKE-------LGKWRF------------SALLG-LNTLFVALMDh 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 375 ---KTLVFSKVKTSlgldhchsfISGTAPLNQETAEFFLSLD-IPIGELYGLSESSgphTISNQNNY----RLLSCGKIL 446
Cdd:PRK12492 325 pgfKDLDFSALKLT---------NSGGTALVKATAERWEQLTgCTIVEGYGLTETS---PVASTNPYgelaRLGTVGIPV 392
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 447 TGCKNMLFqqNKDGI-------GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITA 519
Cdd:PRK12492 393 PGTALKVI--DDDGNelplgerGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVS 470
                        330       340
                 ....*....|....*....|....*...
gi 574584557 520 GGeNVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:PRK12492 471 GF-NVYPNEIEDVVMAH-PKVANCAAIG 496
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
92-547 1.21e-12

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 70.87  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  92 KAAKSLIKLGLERFHGVGILGFNSAE----WFITA-VGAILagglcVGIYATNSAEVCQYVITHAKVNiLLVENDQQLQK 166
Cdd:PRK08008  49 RTANLFYSLGIRKGDKVALHLDNCPEfifcWFGLAkIGAIM-----VPINARLLREESAWILQNSQAS-LLVTSAQFYPM 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 167 ILSIPQSSLEPLKAIIQYRLPMKKNNNLYswdDFMELGRSIPDTQLEQVIESqkANQCAVLIYTSGTTGIPKGVMLSHDN 246
Cdd:PRK08008 123 YRQIQQEDATPLRHICLTRVALPADDGVS---SFTQLKAQQPATLCYAPPLS--TDDTAEILFTSGTTSRPKGVVITHYN 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 247 I-------TWiAGAVTKDfkltDKHETVvsyLPLSHIAAQMMDIWVPIKIGAltyfaqadalkgTLVstlkevkptvfig 319
Cdd:PRK08008 198 LrfagyysAW-QCALRDD----DVYLTV---MPAFHIDCQCTAAMAAFSAGA------------TFV------------- 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 320 vpqiwekiheMVKKNSAKsmglkkkAFvWarnigfkvnskKMLGKYNTPVSYRMA---KTLVFSKVkTSLGLDHCHSFIS 396
Cdd:PRK08008 245 ----------LLEKYSAR-------AF-W-----------GQVCKYRATITECIPmmiRTLMVQPP-SANDRQHCLREVM 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 397 GTAPL-NQETAEFFLSLDIPIGELYGLSES-SGPHTISNQNNYRLLSCGKILTGCKNMLfqQNKDG-------IGEICLW 467
Cdd:PRK08008 295 FYLNLsDQEKDAFEERFGVRLLTSYGMTETiVGIIGDRPGDKRRWPSIGRPGFCYEAEI--RDDHNrplpageIGEICIK 372
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 468 G---RHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETLVKKKiPIISNAM 544
Cdd:PRK08008 373 GvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDR-RCNMIKRGGENVSCVELENIIATH-PKIQDIV 450

                 ...
gi 574584557 545 LVG 547
Cdd:PRK08008 451 VVG 453
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
221-547 3.91e-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: 3.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 221 ANQCAVLIYTSGTTGIPKGVMLSHdnitwiagavtkdfkltdkhetvvSYlPLSHIAAqmMDIWVPIKIGALtYFAQADA 300
Cdd:cd05972   80 AEDPALIYFTSGTTGLPKGVLHTH------------------------SY-PLGHIPT--AAYWLGLRPDDI-HWNIADP 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 301 --LKGTLvSTLKEVkptVFIGVPQIwekIHEMVKKNSAKSMGLKKKafvwarnigFKVNSKkmlgkYNTPVSYRM-AKTL 377
Cdd:cd05972  132 gwAKGAW-SSFFGP---WLLGATVF---VYEGPRFDAERILELLER---------YGVTSF-----CGPPTAYRMlIKQD 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 378 VFSKVKTSLgldhcHSFISGTAPLNQETAEFFLS-LDIPIGELYGLSEssgphTISNQNNYRLL-----SCGKILTGCKN 451
Cdd:cd05972  191 LSSYKFSHL-----RLVVSAGEPLNPEVIEWWRAaTGLPIRDGYGQTE-----TGLTVGNFPDMpvkpgSMGRPTPGYDV 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 452 MLFQQNKDGI-----GEICL-WGRH-IFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENV 524
Cdd:cd05972  261 AIIDDDGRELppgeeGDIAIkLPPPgLFLGYVGDPEKTEASIRG-DYYLTGDRAYRDEDGYFWFVGRADDI-IKSSGYRI 338
                        330       340
                 ....*....|....*....|....
gi 574584557 525 PPIPVE-TLVKKkiPIISNAMLVG 547
Cdd:cd05972  339 GPFEVEsALLEH--PAVAEAAVVG 360
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
225-547 4.05e-12

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 69.04  E-value: 4.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAA-----QMMDIWVPIKIGALTYFaqaD 299
Cdd:PRK07786 177 ALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGigsmlPGLLLGAPTVIYPLGAF---D 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 300 AlkGTLVSTLKEVKPTVFIGVPQIWEKIhemVKKNSAKSMGLKKKAFVWarnigfkvnskkmlgkyntpvsyrmaktlvf 379
Cdd:PRK07786 254 P--GQLLDVLEAEKVTGIFLVPAQWQAV---CAEQQARPRDLALRVLSW------------------------------- 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 380 skvktslgldhchsfisGTAP----LNQETAEFFLslDIPIGELYGLSESSgPHT--ISNQNNYRLL-SCGKILTGCKNM 452
Cdd:PRK07786 298 -----------------GAAPasdtLLRQMAATFP--EAQILAAFGQTEMS-PVTcmLLGEDAIRKLgSVGKVIPTVAAR 357
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 453 LFQQNKDG-----IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPI 527
Cdd:PRK07786 358 VVDENMNDvpvgeVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIIS-GGENIYCA 435
                        330       340
                 ....*....|....*....|
gi 574584557 528 PVETLVKKKiPIISNAMLVG 547
Cdd:PRK07786 436 EVENVLASH-PDIVEVAVIG 454
PRK07514 PRK07514
malonyl-CoA synthase; Validated
200-533 6.92e-12

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 68.36  E-value: 6.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 200 FMELGRSIPDTqLEQVieSQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPL------ 273
Cdd:PRK07514 137 LLEAAAAAPDD-FETV--PRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPD-DVLIHALPIfhthgl 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 274 ---SHIA----AQMmdIWVPiKIGA---LTYFAQAdalkgtlvstlkevkpTVFIGVPQIWEKI--HEMVKKNSAKSMGL 341
Cdd:PRK07514 213 fvaTNVAllagASM--IFLP-KFDPdavLALMPRA----------------TVMMGVPTFYTRLlqEPRLTREAAAHMRL 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 342 kkkafvwarnigfkvnskkmlgkyntpvsyrmaktlvfskvktslgldhchsFISGTAPLNQET-AEFFLSLDIPIGELY 420
Cdd:PRK07514 274 ----------------------------------------------------FISGSAPLLAEThREFQERTGHAILERY 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 421 GLSEssgphTISNQNN-Y------------------RLLSC--GKILTgcknmlfqqnKDGIGEICLWGRHIFMGYLESE 479
Cdd:PRK07514 302 GMTE-----TNMNTSNpYdgerragtvgfplpgvslRVTDPetGAELP----------PGEIGMIEVKGPNVFKGYWRMP 366
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 574584557 480 TETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLV 533
Cdd:PRK07514 367 EKTAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIIS-GGYNVYPKEVEGEI 419
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
216-538 7.36e-12

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 68.80  E-value: 7.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  216 IESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLSHiaaqmmdiwvpikigaltyf 295
Cdd:PRK08633  776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNL-RNDDVILSSLPFFH-------------------- 834
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  296 aqADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMgLKKKAF--VWARNIgfKVNsKKMLGkyntpvSYRM 373
Cdd:PRK08633  835 --SFGLTVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATIL-LGTPTFlrLYLRNK--KLH-PLMFA------SLRL 902
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  374 AktlvfskvktslgldhchsfISGTAPLNQETAEFF-LSLDIPIGELYGLSESSGPHTISNQNnyRLLSCGKILTGCKN- 451
Cdd:PRK08633  903 V--------------------VAGAEKLKPEVADAFeEKFGIRILEGYGATETSPVASVNLPD--VLAADFKRQTGSKEg 960
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  452 ----------------MLFQQNKDGI-GEICLWGRHIFMGYLESETETTEAI---DDEGWLHSGDLGQLDGLGFLYVTGH 511
Cdd:PRK08633  961 svgmplpgvavrivdpETFEELPPGEdGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDR 1040
                         330       340       350
                  ....*....|....*....|....*....|
gi 574584557  512 IK---EIlitaGGENVPPIPVETLVKKKIP 538
Cdd:PRK08633 1041 YSrfaKI----GGEMVPLGAVEEELAKALG 1066
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
81-324 1.03e-11

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 67.78  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  81 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEn 160
Cdd:cd05959   30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVS- 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 161 dQQLQKILSIPQSSLEPLKAIiqyrlpMKKNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGV 240
Cdd:cd05959  109 -GELAPVLAAALTKSEHTLVV------LIVSGGAGPEAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGV 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 241 MLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGV 320
Cdd:cd05959  182 VHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPTPAAVFKRIRRYRPTVFFGV 261

                 ....
gi 574584557 321 PQIW 324
Cdd:cd05959  262 PTLY 265
PRK07787 PRK07787
acyl-CoA synthetase; Validated
225-521 1.13e-11

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 67.32  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIG---------ALTYF 295
Cdd:PRK07787 131 ALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTAD-DVLVHGLPLFHVHGLVLGVLGPLRIGnrfvhtgrpTPEAY 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 296 AQADALKGTLvstlkevkptvFIGVPQIWEKIHEmvKKNSAKSMglkkkafvwarnigfkvnskkmlgkyntpvsyRMAK 375
Cdd:PRK07787 210 AQALSEGGTL-----------YFGVPTVWSRIAA--DPEAARAL--------------------------------RGAR 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 376 TLVfskvktslgldhchsfiSGTAPLNQETAEFFLSLD-IPIGELYGLSES--------SGPHtisnqnnyRLLSCGKIL 446
Cdd:PRK07787 245 LLV-----------------SGSAALPVPVFDRLAALTgHRPVERYGMTETlitlstraDGER--------RPGWVGLPL 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 447 TGCKNMLFQQN-----KDG--IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITA 519
Cdd:PRK07787 300 AGVETRLVDEDggpvpHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRESTDLIKS 379

                 ..
gi 574584557 520 GG 521
Cdd:PRK07787 380 GG 381
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
208-339 3.18e-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: 3.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 208 PDTQLEQVIESQKA-------NQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIAAqM 280
Cdd:cd05930   72 PAERLAYILEDSGAklvltdpDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLT-PGDRVLQFTSFSFDVS-V 149
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 574584557 281 MDIWVPIKIGALTYFAQADALK--GTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSM 339
Cdd:cd05930  150 WEIFGALLAGATLVVLPEEVRKdpEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSL 210
PRK06178 PRK06178
acyl-CoA synthetase; Validated
225-547 4.56e-11

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 65.83  E-value: 4.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGA-LTYFAQADALkg 303
Cdd:PRK06178 212 AALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGAtLVLLARWDAV-- 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 304 TLVSTLKEVKPTVFIG-VPQIWEKI-HEMVKKNSAKSmgLKKK---AFVWARNIGFKVNSKKMLGKYNTPVSYRMAKTlv 378
Cdd:PRK06178 290 AFMAAVERYRVTRTVMlVDNAVELMdHPRFAEYDLSS--LRQVrvvSFVKKLNPDYRQRWRALTGSVLAEAAWGMTET-- 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 379 fskvktslgldH-CHSFISG--TAPLNQETAEFFLSLDIPIGELYGLSESSGphtisnqnnyRLLSCGkiltgcknmlfq 455
Cdd:PRK06178 366 -----------HtCDTFTAGfqDDDFDLLSQPVFVGLPVPGTEFKICDFETG----------ELLPLG------------ 412
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 456 qnkdGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITAgGENVPPIPVETLVKK 535
Cdd:PRK06178 413 ----AEGEIVVRTPSLLKGYWNKPEATAEALRD-GWLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GMSVFPSEVEALLGQ 486
                        330
                 ....*....|..
gi 574584557 536 KiPIISNAMLVG 547
Cdd:PRK06178 487 H-PAVLGSAVVG 497
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
225-533 6.17e-11

Long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 65.43  E-value: 6.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNI--------TWIAGAVTKdfKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALtyfa 296
Cdd:PRK07059 207 AFLQYTGGTTGVSKGATLLHRNIvanvlqmeAWLQPAFEK--KPRPDQLNFVCALPLYHIFALTVCGLLGMRTGGR---- 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 297 qadalkgtlvstlkevkpTVFIGVPQiweKIHEMVKKnsaksmgLKKKAFvwarNIGFKVNSkkmlgKYNTPVSYRMAKT 376
Cdd:PRK07059 281 ------------------NILIPNPR---DIPGFIKE-------LKKYQV----HIFPAVNT-----LYNALLNNPDFDK 323
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 377 LVFSKVKTSLGldhchsfisGTAPLNQETAEFFLSLD-IPIGELYGLSESSgPHTISNQNNyrllscGKILTGCKNM--- 452
Cdd:PRK07059 324 LDFSKLIVANG---------GGMAVQRPVAERWLEMTgCPITEGYGLSETS-PVATCNPVD------ATEFSGTIGLplp 387
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 453 ---LFQQNKDG-------IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGE 522
Cdd:PRK07059 388 steVSIRDDDGndlplgePGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKD-MILVSGF 466
                        330
                 ....*....|.
gi 574584557 523 NVPPIPVETLV 533
Cdd:PRK07059 467 NVYPNEIEEVV 477
PLN02574 PLN02574
4-coumarate--CoA ligase-like
200-549 8.00e-11

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 64.86  E-value: 8.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 200 FMELGRSIPDTQLEQVIESQKAnqcAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTK----DFKLTDKHETVVSYLPLSH 275
Cdd:PLN02574 179 FYELIKEDFDFVPKPVIKQDDV---AAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfeasQYEYPGSDNVYLAALPMFH 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 276 IAAQMMDIWVPIKIG-ALTYFAQADAlkGTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksMGLKKKAfvwarnigf 354
Cdd:PLN02574 256 IYGLSLFVVGLLSLGsTIVVMRRFDA--SDMVKVIDRFKVTHFPVVPPIL--------------MALTKKA--------- 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 355 kvnskkmlgkynTPVSYRMAKTLVfskvktslgldhchSFISGTAPLNQETAEFFLS----LDIPIGelYGLSESS--GP 428
Cdd:PLN02574 311 ------------KGVCGEVLKSLK--------------QVSCGAAPLSGKFIQDFVQtlphVDFIQG--YGMTESTavGT 362
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 429 HTISNQNNYRLLSCG--------KIL---TGCknMLFQQNKdgiGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDL 497
Cdd:PLN02574 363 RGFNTEKLSKYSSVGllapnmqaKVVdwsTGC--LLPPGNC---GELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDI 437
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 574584557 498 GQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKIPIISNAML-VGDK 549
Cdd:PLN02574 438 AYFDEDGYLYIVDRLKEI-IKYKGFQIAPADLEAVLISHPEIIDAAVTaVPDK 489
PRK07788 PRK07788
acyl-CoA synthetase; Validated
81-533 8.72e-11

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 64.95  E-value: 8.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  81 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSaEWFITAVGAilAGGLCVGIYATNS-------AEVCQyvitHAKV 153
Cdd:PRK07788  75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNH-RGFVLALYA--AGKVGARIILLNTgfsgpqlAEVAA----REGV 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 154 NILLVenDQQLQKILSIPQSSLEPLKAIIQYRlpmkknnnlyswDDFMELGRSIPDtqLEQVIESQKAN-------QCAV 226
Cdd:PRK07788 148 KALVY--DDEFTDLLSALPPDLGRLRAWGGNP------------DDDEPSGSTDET--LDDLIAGSSTAplpkppkPGGI 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 227 LIYTSGTTGIPKGVMLSHDNI-TWIAGAVTK-DFKltdKHETVVsylplshIAAQMMDIWvpikigALTYFAQADALKGT 304
Cdd:PRK07788 212 VILTSGTTGTPKGAPRPEPSPlAPLAGLLSRvPFR---AGETTL-------LPAPMFHAT------GWAHLTLAMALGST 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 305 LV--------STLKEV---KPTVFIGVPQIwekIHEMVKKnsaksmglkkkafvwarnigfkvnSKKMLGKYNTPvSYRM 373
Cdd:PRK07788 276 VVlrrrfdpeATLEDIakhKATALVVVPVM---LSRILDL------------------------GPEVLAKYDTS-SLKI 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 374 AktlvfskvktslgldhchsFISG---TAPLNQETAEFFlsldipiGE----LYGLSESSGPhTISNQNNYRL--LSCGK 444
Cdd:PRK07788 328 I-------------------FVSGsalSPELATRALEAF-------GPvlynLYGSTEVAFA-TIATPEDLAEapGTVGR 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 445 ILTGCKNMLFQQNKDGI-----GEICLWGRHIFMGYleSETETTEAIDdeGWLHSGDLGQLDGLGFLYVTGHIKEiLITA 519
Cdd:PRK07788 381 PPKGVTVKILDENGNEVprgvvGRIFVGNGFPFEGY--TDGRDKQIID--GLLSSGDVGYFDEDGLLFVDGRDDD-MIVS 455
                        490
                 ....*....|....
gi 574584557 520 GGENVPPIPVETLV 533
Cdd:PRK07788 456 GGENVFPAEVEDLL 469
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
55-321 1.07e-10

bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341310 [Multi-domain]  Cd Length: 490  Bit Score: 64.27  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  55 EFFRESVNRFGTYPALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVG 134
Cdd:cd17655    1 ELFEEQAEKTPDHTAVVFED----QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 135 IYATNSAEVCQYVITHAKVNILLVendqqlqkilsipQSSLEPLKAIIQYRLPMKKNNnlyswddfmelGRSIPDTQLEQ 214
Cdd:cd17655   77 IDPDYPEERIQYILEDSGADILLT-------------QSHLQPPIAFIGLIDLLDEDT-----------IYHEESENLEP 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 215 VIesqKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLShIAAQMMDIWVPIKIGA-LT 293
Cdd:cd17655  133 VS---KSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQ-GEHLRVALFASIS-FDASVTEIFASLLSGNtLY 207
                        250       260
                 ....*....|....*....|....*....
gi 574584557 294 YFAQADALKG-TLVSTLKEVKPTVFIGVP 321
Cdd:cd17655  208 IVRKETVLDGqALTQYIRQNRITIIDLTP 236
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
33-642 1.22e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 64.68  E-value: 1.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  33 DGEVLLRlSKHGPGhETPMTIPEFFRESVNRFGTYPALASKNG--KKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGI 110
Cdd:PRK12582  33 DGSIVIK-SRHPLG-PYPRSIPHLLAKWAAEAPDRPWLAQREPghGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMI 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 111 LGFNSAEWFITAVGAILAGGLCVGI---YATNSAEVCQ--YVITHAKVNILLVENDQQLQKILSIPQssLEPLKAIIQYR 185
Cdd:PRK12582 111 LSGNSIEHALMTLAAMQAGVPAAPVspaYSLMSHDHAKlkHLFDLVKPRVVFAQSGAPFARALAALD--LLDVTVVHVTG 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 186 LPmkknnnlyswDD-----FMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSH----DNITWIAGavTK 256
Cdd:PRK12582 189 PG----------EGiasiaFADLAATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQrmmcANIAMQEQ--LR 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 257 DFKLTDKHETVVSYLPLSHIAAQMMdIWVPIKIGALTYFAQAD----ALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVK 332
Cdd:PRK12582 257 PREPDPPPPVSLDWMPWNHTMGGNA-NFNGLLWGGGTLYIDDGkplpGMFEETIRNLREISPTVYGNVPAGYAMLAEAME 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 333 KNSAksmgLKKKAFvwaRNIGfkvnskkmlgkyntpvsyRMAktlvfskvktslgldhchsfiSGTAPLNQETAEFFLSL 412
Cdd:PRK12582 336 KDDA----LRRSFF---KNLR------------------LMA---------------------YGGATLSDDLYERMQAL 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 413 -------DIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQqnkdgIG---EICLWGRHIFMGYLESETET 482
Cdd:PRK12582 370 avrttghRIPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLAP-----VGdkyEVRVKGPNVTPGYHKDPELT 444
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 483 TEAIDDEGWLHSGDLGQ-LD------GLGFlyvTGHIKEILITAGGENVPPIPVET-LVKKKIPIISNAMLVGDKLKFLS 554
Cdd:PRK12582 445 AAAFDEEGFYRLGDAARfVDpddpekGLIF---DGRVAEDFKLSTGTWVSVGTLRPdAVAACSPVIHDAVVAGQDRAFIG 521
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 555 MLLtlkcemnqmsgepldklnFEAINFCRGLGSQASTVTEIVKqQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKD 634
Cdd:PRK12582 522 LLA------------------WPNPAACRQLAGDPDAAPEDVV-KHPAVLAILREGLSAHNAEAGGSSSRIARALLMTEP 582

                 ....*...
gi 574584557 635 FSIYGGEL 642
Cdd:PRK12582 583 PSIDAGEI 590
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
199-589 1.45e-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: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 199 DFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNIT--WIAGAVTKDFKLTDKHETVVSylPlSHI 276
Cdd:cd05969   66 DRLENSEAKVLITTEELYERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIfyYFTGKYVLDLHPDDIYWCTAD--P-GWV 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 277 AAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVfigvpqiwekihemvkknsaksmglkkkafvWarnigfkv 356
Cdd:cd05969  143 TGTVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTV-------------------------------W-------- 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 357 nskkmlgkYNTPVSYRMAKTLVFSKVKtSLGLDHCHSFISGTAPLNQETAEFFLS-LDIPIGELYGLSESsGPHTISNQ- 434
Cdd:cd05969  184 --------YTAPTAIRMLMKEGDELAR-KYDLSSLRFIHSVGEPLNPEAIRWGMEvFGVPIHDTWWQTET-GSIMIANYp 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 435 -NNYRLLSCGKILTGCKNMLFQQNKDGI-----GEICL---WGRhIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGF 505
Cdd:cd05969  254 cMPIKPGSMGKPLPGVKAAVVDENGNELppgtkGILALkpgWPS-MFRGIWNDEERYKNSFID-GWYLTGDLAYRDEDGY 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 506 LYVTGHIKEILITAgGENVPPIPVETLVKKKiPIISNAMLVG--DKLK--FLSMLLTLKcemnqmSG-EPLDKLNFEAIN 580
Cdd:cd05969  332 FWFVGRADDIIKTS-GHRVGPFEVESALMEH-PAVAEAGVIGkpDPLRgeIIKAFISLK------EGfEPSDELKEEIIN 403
                        410
                 ....*....|
gi 574584557 581 FCR-GLGSQA 589
Cdd:cd05969  404 FVRqKLGAHV 413
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
108-325 1.64e-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: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  108 VGILGFNSAeWFITAVGAIL-AGGLCVGIYATNSAEVCQYVITHAKVNILLVenDQQLQkilsiPQSSLEPLKAIIqyrl 186
Cdd:TIGR01733  28 VAVLLERSA-ELVVAILAVLkAGAAYVPLDPAYPAERLAFILEDAGARLLLT--DSALA-----SRLAGLVLPVIL---- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  187 pmkknnnlyswDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVTKDFKLTDkhE 265
Cdd:TIGR01733  96 -----------LDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLvNLLAWLARRYGLDPD--D 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574584557  266 TVVSYLPLSHIAAqMMDIWVPIKIGALTYFAQADALKGTLVST---LKEVKPTVFIGVPQIWE 325
Cdd:TIGR01733 163 RVLQFASLSFDAS-VEEIFGALLAGATLVVPPEDEERDDAALLaalIAEHPVTVLNLTPSLLA 224
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
225-540 3.93e-10

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 62.84  E-value: 3.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSH----DNITWIAGAVtkdfKLTDKHETVVSYLPLSHIAAQMMdIWVPikigaltyfaqadA 300
Cdd:PRK12476 196 SHLQYTSGSTRPPVGVEITHravgTNLVQMILSI----DLLDRNTHGVSWLPLYHDMGLSM-IGFP-------------A 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 301 LKG---TLVStlkevkPTVFIGVPQIWekIHEMVKKNSAKSM--GLKKKAFVWARNIGFKVN------SKKMLGKYNTPV 369
Cdd:PRK12476 258 VYGghsTLMS------PTAFVRRPQRW--IKALSEGSRTGRVvtAAPNFAYEWAAQRGLPAEgddidlSNVVLIIGSEPV 329
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 370 SyrMAKTLVFSK-----------VKTSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSgPHTISNqnnyr 438
Cdd:PRK12476 330 S--IDAVTTFNKafapyglprtaFKPSYGIAEATLFVATIAPDAEPSVVYLDREQLGAGRAVRVAADA-PNAVAH----- 401
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 439 lLSCGKIL-----------TGCknmlfqQNKDG-IGEICLWGRHIFMGYLE--SETETT----------------EAIDD 488
Cdd:PRK12476 402 -VSCGQVArsqwavivdpdTGA------ELPDGeVGEIWLHGDNIGRGYWGrpEETERTfgaklqsrlaegshadGAADD 474
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 574584557 489 EGWLHSGDLG-QLDGLgfLYVTGHIKEiLITAGGENVPPIPVETLVKKKIPII 540
Cdd:PRK12476 475 GTWLRTGDLGvYLDGE--LYITGRIAD-LIVIDGRNHYPQDIEATVAEASPMV 524
PRK08180 PRK08180
feruloyl-CoA synthase; Reviewed
225-642 4.01e-10

feruloyl-CoA synthase; Reviewed


Pssm-ID: 236175 [Multi-domain]  Cd Length: 614  Bit Score: 62.97  E-value: 4.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFK-LTDKHETVVSYLPLSHIaaqmmdiwvpikIGALTYFAQADALKG 303
Cdd:PRK08180 212 AKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPfLAEEPPVLVDWLPWNHT------------FGGNHNLGIVLYNGG 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 304 TL---------------VSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAksmglkkkafvwarnigfkvnskkmlgkyntp 368
Cdd:PRK08180 280 TLyiddgkptpggfdetLRNLREISPTVYFNVPKGWEMLVPALERDAA-------------------------------- 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 369 vsyrMAKTLvFSKVKtslgldhchSFISGTAPLNQETAEfflSLD----------IPIGELYGLSESSGPHTISNQNNYR 438
Cdd:PRK08180 328 ----LRRRF-FSRLK---------LLFYAGAALSQDVWD---RLDrvaeatcgerIRMMTGLGMTETAPSATFTTGPLSR 390
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 439 LLSCGKILTGCKNMLFQQnkDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQL-D----GLGFLYvTGHIK 513
Cdd:PRK08180 391 AGNIGLPAPGCEVKLVPV--GGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFvDpadpERGLMF-DGRIA 467
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 514 EILITAGGE--NVPPIPVEtLVKKKIPIISNAMLVGDKLKFLSMLLtlkcemnqmsgepldklnFEAINFCRGLGSQAST 591
Cdd:PRK08180 468 EDFKLSSGTwvSVGPLRAR-AVSAGAPLVQDVVITGHDRDEIGLLV------------------FPNLDACRRLAGLLAD 528
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 574584557 592 VTEIVKQQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGEL 642
Cdd:PRK08180 529 ASLAEVLAHPAVRAAFRERLARLNAQATGSSTRVARALLLDEPPSLDAGEI 579
ttLC_FACS_like cd05915
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
83-600 4.08e-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: 4.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  83 FNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDq 162
Cdd:cd05915   27 YAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPN- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 163 qlqkILSIPQSSLEPLKAIIQYRLPMKKNNNlysWDDFMELGRsiPDTQleqviESQKANQC--AVLIYTSGTTGIPKGV 240
Cdd:cd05915  106 ----LLPLVEAIRGELKTVQHFVVMDEKAPE---GYLAYEEAL--GEEA-----DPVRVPERaaCGMAYTTGTTGLPKGV 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 241 MLSHDNITWIAGAVTKDFKLTDKHETV-VSYLPLSHIAAQMMdIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIG 319
Cdd:cd05915  172 VYSHRALVLHSLAASLVDGTALSEKDVvLPVVPMFHVNAWCL-PYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 320 VPQIWEKIhemvkKNSAKSMglkKKAFVWARNIgfkvnskkMLGKYNTPVSYRMAKTLVFSKVKTSLGLDHCHSFisGTA 399
Cdd:cd05915  251 VPTVWLAL-----ADYLEST---GHRLKTLRRL--------VVGGSAAPRSLIARFERMGVEVRQGYGLTETSPV--VVQ 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 400 PLNQETAEfflslDIPIGELYGLSESSGPHTISNQNNyrllscgkiLTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESE 479
Cdd:cd05915  313 NFVKSHLE-----SLSEEEKLTLKAKTGLPIPLVRLR---------VADEEGRPVPKDGKALGEVQLKGPWITGGYYGNE 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 480 TETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKiPIISNAMLVG--DKLKFLSMLL 557
Cdd:cd05915  379 EATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDL-IKSGGEWISSVDLENALMGH-PKVKEAAVVAipHPKWQERPLA 456
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 574584557 558 TLKCEMNQMSGEpldklnfEAINFC-RGLGSQASTVTEIVKQQD 600
Cdd:cd05915  457 VVVPRGEKPTPE-------ELNEHLlKAGFAKWQLPDAYVFAEE 493
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
82-547 7.31e-10

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 62.08  E-value: 7.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  82 NFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVenD 161
Cdd:PRK06018  41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT--D 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 162 QQLQKILSIPQSSLEPLKAIIQY----RLPMKKNNNLYSWDDFMELGRSipDTQLEQVIESQKANQCavliYTSGTTGIP 237
Cdd:PRK06018 119 LTFVPILEKIADKLPSVERYVVLtdaaHMPQTTLKNAVAYEEWIAEADG--DFAWKTFDENTAAGMC----YTSGTTGDP 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 238 KGVMLSH-DNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPiKIGALTYFAQADALKGTLVSTLKEVKPTV 316
Cdd:PRK06018 193 KGVLYSHrSNVLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAP-SMGTKLVMPGAKLDGASVYELLDTEKVTF 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 317 FIGVPQIWEKIHEMVKKNSAKSMGLKKKAfvwarnIGFKVNSKKMLG---KYNTPV--SYRMAKTlvfSKVKTSLGLDHC 391
Cdd:PRK06018 272 TAGVPTVWLMLLQYMEKEGLKLPHLKMVV------CGGSAMPRSMIKafeDMGVEVrhAWGMTEM---SPLGTLAALKPP 342
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 392 HSFISGTAPLN----QETAEFFLSLDipigelyglsessgphtISNQNNYRLLSCGKILtgcknmlfqqnkdgiGEICLW 467
Cdd:PRK06018 343 FSKLPGDARLDvlqkQGYPPFGVEMK-----------------ITDDAGKELPWDGKTF---------------GRLKVR 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 468 GRHIFMGYLESETETteaIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:PRK06018 391 GPAVAAAYYRVDGEI---LDDDGFFDTGDVATIDAYGYMRITDRSKDV-IKSGGEWISSIDLENLAVGH-PKVAEAAVIG 465
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
461-547 8.08e-10

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 61.61  E-value: 8.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 461 IGEICLWGRHIFMGYLESETETteAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLVKKKiPII 540
Cdd:PRK13295 392 IGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVIIR-GGENIPVVEIEALLYRH-PAI 467

                 ....*..
gi 574584557 541 SNAMLVG 547
Cdd:PRK13295 468 AQVAIVA 474
PLN02479 PLN02479
acetate-CoA ligase
85-533 1.35e-09

acetate-CoA ligase


Pssm-ID: 178097 [Multi-domain]  Cd Length: 567  Bit Score: 61.01  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  85 QYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGL--CVGIYAtnSAEVCQYVITHAKVNILLVEN-- 160
Cdd:PLN02479  50 QTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVvnCVNIRL--NAPTIAFLLEHSKSEVVMVDQef 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 161 ----DQQLQKILSIPQSSLEPLKAII-----------QYRLpmkkNNNLYSWDDFMELGRsiPDTQLEQvieSQKANQCA 225
Cdd:PLN02479 128 ftlaEEALKILAEKKKSSFKPPLLIVigdptcdpkslQYAL----GKGAIEYEKFLETGD--PEFAWKP---PADEWQSI 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 226 VLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAqmmdiWVpikigaltYFAQADALKGTL 305
Cdd:PLN02479 199 ALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEG-AVYLWTLPMFHCNG-----WC--------FTWTLAALCGTN 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 306 VStLKEVKPTvfigvpqiweKIHEMVKKNSAKSMGlkkKAFVWARNIgfkvnskkmlgkYNTPVSyrmaktlvfskvKTS 385
Cdd:PLN02479 265 IC-LRQVTAK----------AIYSAIANYGVTHFC---AAPVVLNTI------------VNAPKS------------ETI 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 386 LGLDH-CHSFISGTAPlnqeTAEFFLSLDIP---IGELYGLSESSGPHTISN----------QNNYRLLSCGKI----LT 447
Cdd:PLN02479 307 LPLPRvVHVMTAGAAP----PPSVLFAMSEKgfrVTHTYGLSETYGPSTVCAwkpewdslppEEQARLNARQGVryigLE 382
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 448 GCKNMLFQQNK----DG--IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGG 521
Cdd:PLN02479 383 GLDVVDTKTMKpvpaDGktMGEIVMRGNMVMKGYLKNPKANEEAFAN-GWFHSGDLGVKHPDGYIEIKDRSKDIIIS-GG 460
                        490
                 ....*....|..
gi 574584557 522 ENVPPIPVETLV 533
Cdd:PLN02479 461 ENISSLEVENVV 472
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
55-291 5.10e-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: 5.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  55 EFFRESVNRFGTYPALASKNGKkweiLNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEwFITAVGAIL-AGGLCV 133
Cdd:cd12117    1 ELFEEQAARTPDAVAVVYGDRS----LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPE-LVVALLAVLkAGAAYV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 134 GIYATNSAEVCQYVITHAKVNILLVENdqqlqkilSIPQSSLEPLKAIIQYRLPMKKnnnlyswddfmelgrsiPDTQLE 213
Cdd:cd12117   76 PLDPELPAERLAFMLADAGAKVLLTDR--------SLAGRAGGLEVAVVIDEALDAG-----------------PAGNPA 130
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574584557 214 QVIEsqkANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVtkDFKLTDKHETVVSYLPLSHIAAqMMDIWVPIKIGA 291
Cdd:cd12117  131 VPVS---PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNT--NYVTLGPDDRVLQTSPLAFDAS-TFEIWGALLNGA 202
PRK08162 PRK08162
acyl-CoA synthetase; Validated
459-530 5.21e-09

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 59.19  E-value: 5.21e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574584557 459 DG--IGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:PRK08162 384 DGetIGEIMFRGNIVMKGYLKNPKATEEAFAG-GWFHTGDLAVLHPDGYIKIKDRSKDIIIS-GGENISSIEVE 455
PRK05850 PRK05850
acyl-CoA synthetase; Validated
209-520 9.08e-09

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 58.42  E-value: 9.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 209 DTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFkLTDKHE------TVVSYLPLSHIAAQMMD 282
Cdd:PRK05850 147 DSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDY-FGDTGGvpppdtTVVSWLPFYHDMGLVLG 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 283 IWVPIKIGALTYfaqadalkgtLVStlkevkPTVFIGVPQIWekIHeMVKKNSAksmglkkkAFVWARNIGFKVNSKK-- 360
Cdd:PRK05850 226 VCAPILGGCPAV----------LTS------PVAFLQRPARW--MQ-LLASNPH--------AFSAAPNFAFELAVRKts 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 361 ---MLGkyntpvsyrmaktlvfskvktsLGLDHCHSFISGTAPLNQET--------AEFFLSlDIPIGELYGLSE----- 424
Cdd:PRK05850 279 dddMAG----------------------LDLGGVLGIISGSERVHPATlkrfadrfAPFNLR-ETAIRPSYGLAEatvyv 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 425 -----SSGPHTIS---------------NQNNYRLLSCG-------KILTGCKNMlfqQNKDG-IGEICLWGRHIFMGYL 476
Cdd:PRK05850 336 atrepGQPPESVRfdyeklsaghakrceTGGGTPLVSYGsprsptvRIVDPDTCI---ECPAGtVGEIWVHGDNVAAGYW 412
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 574584557 477 E--SETETT--EAIDD------EG-WLHSGDLGQLDGlGFLYVTGHIKEILITAG 520
Cdd:PRK05850 413 QkpEETERTfgATLVDpspgtpEGpWLRTGDLGFISE-GELFIVGRIKDLLIVDG 466
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
99-547 2.12e-08

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 57.28  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  99 KLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITH--AKVNILLVE---------NDQQLQKI 167
Cdd:PRK08314  55 ECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDsgARVAIVGSElapkvapavGNLRLRHV 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 168 LS------IPQSSLEPLKAIIQYR--LPMKKNNNLYSWDDFMELGRSIPDTQLeqviesqKANQCAVLIYTSGTTGIPKG 239
Cdd:PRK08314 135 IVaqysdyLPAEPEIAVPAWLRAEppLQALAPGGVVAWKEALAAGLAPPPHTA-------GPDDLAVLPYTSGTTGVPKG 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 240 VMLSHDNItwIAGAVTKDFKLTDKHETVV-SYLPLSHIAAQMMDIWVPIKIGA-LTYFAQAD-ALKGTLVSTLkevKPTV 316
Cdd:PRK08314 208 CMHTHRTV--MANAVGSVLWSNSTPESVVlAVLPLFHVTGMVHSMNAPIYAGAtVVLMPRWDrEAAARLIERY---RVTH 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 317 figvpqiWEKIHEMVkknsaksmglkkkafvwarnIGFKVNSKkmLGKYNtpvsyrmaktlvFSKVKTSLGldhchsfis 396
Cdd:PRK08314 283 -------WTNIPTMV--------------------VDFLASPG--LAERD------------LSSLRYIGG--------- 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 397 GTAPLNQETAEFFLSL-DIPIGELYGLSESSGPhTISNQNNYRLLSCGKILTgcknmlfqQNKDG--------------- 460
Cdd:PRK08314 313 GGAAMPEAVAERLKELtGLDYVEGYGLTETMAQ-THSNPPDRPKLQCLGIPT--------FGVDArvidpetleelppge 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 461 IGEICLWGRHIFMGYLESETETTEA---IDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKi 537
Cdd:PRK08314 384 VGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKR-MINASGFKVWPAEVENLLYKH- 461
                        490
                 ....*....|
gi 574584557 538 PIISNAMLVG 547
Cdd:PRK08314 462 PAIQEACVIA 471
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
80-533 4.22e-08

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 56.36  E-value: 4.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  80 ILNFNQYYEACRKAAKSLIKLGLERfhgVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVE 159
Cdd:PRK06334  45 KLSYNQVRKAVIALATKVSKYPDQH---IGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTS 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 160 ndQQLQKILSIPQSSLEPLKAIIQYRLPMKKNnnlYSWDDFMELG--RSIPDTQLEQV--IESQKANQCAVLIYTSGTTG 235
Cdd:PRK06334 122 --KQLMQHLAQTHGEDAEYPFSLIYMEEVRKE---LSFWEKCRIGiyMSIPFEWLMRWfgVSDKDPEDVAVILFTSGTEK 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 236 IPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPT 315
Cdd:PRK06334 197 LPKGVPLTHANLLANQRACLKFFSPKED-DVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNPLYPKKIVEMIDEAKVT 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 316 VFIGVPQIWEKIHEMVKKNSAKSMGLKkkaFVWARNIGFKvnskkmlgkyntpvsyrmaktlvfskvktslgldhcHSfi 395
Cdd:PRK06334 276 FLGSTPVFFDYILKTAKKQESCLPSLR---FVVIGGDAFK------------------------------------DS-- 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 396 sgtapLNQETAEFFLSLDIPIGelYGLSESSGPHTISNQNNYRLLSC-GKILTGCKNMLFQQ------NKDGIGEICLWG 468
Cdd:PRK06334 315 -----LYQEALKTFPHIQLRQG--YGTTECSPVITINTVNSPKHESCvGMPIRGMDVLIVSEetkvpvSSGETGLVLTRG 387
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574584557 469 RHIFMGYL-ESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLV 533
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 ...
79-248 4.50e-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: 4.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  79 EILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEwFITAVGAIL-AGGLCVGIYATNSAEVCQYVITHAKVNILL 157
Cdd:cd17656   12 QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAE-MIVGILGILkAGGAFVPIDPEYPEERRIYIMLDSGVRVVL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 158 VENDQQlqkilsipqSSLEPLKAIIqyrlpmkknnnLYSWDDfmelgrsIPDTQLEQVIESQKANQCAVLIYTSGTTGIP 237
Cdd:cd17656   91 TQRHLK---------SKLSFNKSTI-----------LLEDPS-------ISQEDTSNIDYINNSDDLLYIIYTSGTTGKP 143
                        170
                 ....*....|.
gi 574584557 238 KGVMLSHDNIT 248
Cdd:cd17656  144 KGVQLEHKNMV 154
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
79-520 5.60e-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: 5.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  79 EILNFNQYYEACRKAAKSLIKLGLERfhG--VGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNIL 156
Cdd:COG0365   38 RTLTYAELRREVNRFANALRALGVKK--GdrVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 157 LVENDQ-------QLQKILSIPQSSLEPLKAIIQYRLPMKKNN--NLYSWDDFMELGRSIPDTqleqviESQKANQCAVL 227
Cdd:COG0365  116 ITADGGlrggkviDLKEKVDEALEELPSLEHVIVVGRTGADVPmeGDLDWDELLAAASAEFEP------EPTDADDPLFI 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 228 IYTSGTTGIPKGVMLSHdniTWIAGAVTKDFKLT-DKHE-------------TVVSYL---PLSHIAAQ-MMDiwvpiki 289
Cdd:COG0365  190 LYTSGTTGKPKGVVHTH---GGYLVHAATTAKYVlDLKPgdvfwctadigwaTGHSYIvygPLLNGATVvLYE------- 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 290 GALTYfaqADAlkGTLVSTLKEVKPTVFIGVPQIWekihemvkknsaksMGLKKKAFVWARnigfkvnskkmlgKYNtpv 369
Cdd:COG0365  260 GRPDF---PDP--GRLWELIEKYGVTVFFTAPTAI--------------RALMKAGDEPLK-------------KYD--- 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 370 syrmaktlvFSKVKtslgldHChsfisGTA--PLNQETAEFFLS-LDIPIGELYGLSESSGpHTISnqnNYRLL-----S 441
Cdd:COG0365  305 ---------LSSLR------LL-----GSAgePLNPEVWEWWYEaVGVPIVDGWGQTETGG-IFIS---NLPGLpvkpgS 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 442 CGKILTGCKNMLFqqNKDG-------IGEICL---W-GrhIFMGYLESETETTEAI--DDEGWLHSGDLGQLDGLGFLYV 508
Cdd:COG0365  361 MGKPVPGYDVAVV--DEDGnpvppgeEGELVIkgpWpG--MFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWI 436
                        490
                 ....*....|..
gi 574584557 509 TGHIKEILITAG 520
Cdd:COG0365  437 LGRSDDVINVSG 448
PRK06164 PRK06164
acyl-CoA synthetase; Validated
90-547 7.87e-08

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 55.52  E-value: 7.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  90 CRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYAT-NSAEVcQYVITHAKVNILLVE---NDQQLQ 165
Cdd:PRK06164  45 VDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRyRSHEV-AHILGRGRARWLVVWpgfKGIDFA 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 166 KILS-IPQSSLEPLKAIIQYRLPMKKNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSH 244
Cdd:PRK06164 124 AILAaVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQ 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 245 DNITWIAGAVTKDFKLTDKHETVVSyLPLShiaaqmmdiwvpikiGALTYFAQADALKGtlvstlkevkptvfiGVPQIW 324
Cdd:PRK06164 204 ATLLRHARAIARAYGYDPGAVLLAA-LPFC---------------GVFGFSTLLGALAG---------------GAPLVC 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 325 EKIHEMVKknSAKSMGLKKKAFVWARNIGFKvnskKMLGKYNTPVSYRMAKTLVFSkvktslgldhchSFISGTAplnqE 404
Cdd:PRK06164 253 EPVFDAAR--TARALRRHRVTHTFGNDEMLR----RILDTAGERADFPSARLFGFA------------SFAPALG----E 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 405 TAEFFLSLDIPIGELYGLSE-----SSGPHTISNQnnYRLLSCGKILTGCKNMLFQQNKDG-------IGEICLWGRHIF 472
Cdd:PRK06164 311 LAALARARGVPLTGLYGSSEvqalvALQPATDPVS--VRIEGGGRPASPEARVRARDPQDGallpdgeSGEIEIRAPSLM 388
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574584557 473 MGYLESETETTEAIDDEGWLHSGDLGQLDGLG-FLYVT--GHIkeilITAGGENVPPIPVETLVkKKIPIISNAMLVG 547
Cdd:PRK06164 389 RGYLDNPDATARALTDDGYFRTGDLGYTRGDGqFVYQTrmGDS----LRLGGFLVNPAEIEHAL-EALPGVAAAQVVG 461
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
225-533 8.11e-08

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 55.74  E-value: 8.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  225 AVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVTK-DFKLTDKhetVVSYLPLSHiaaqmmdiwvpiKIGaLTyfaqadalK 302
Cdd:PRK06814  796 AVILFTSGSEGTPKGVVLSHRNLlANRAQVAARiDFSPEDK---VFNALPVFH------------SFG-LT--------G 851
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  303 GTLVSTLKEVkPTVFIGVPQIWEKIHEMVkknsaksmglkkkafvwarnigFKVNSKKMLG---------KYNTPVSYRM 373
Cdd:PRK06814  852 GLVLPLLSGV-KVFLYPSPLHYRIIPELI----------------------YDTNATILFGtdtflngyaRYAHPYDFRS 908
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  374 AKtLVFskvktslgldhchsfiSGTAPLNQETAEFFLS-LDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNM 452
Cdd:PRK06814  909 LR-YVF----------------AGAEKVKEETRQTWMEkFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYR 971
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  453 LfqQNKDGI---GEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIK---EIlitaGGENVPP 526
Cdd:PRK06814  972 L--EPVPGIdegGRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKrfaKI----AGEMISL 1045

                  ....*..
gi 574584557  527 IPVETLV 533
Cdd:PRK06814 1046 AAVEELA 1052
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
91-530 8.28e-08

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 55.48  E-value: 8.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  91 RKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEndqqlqkilsi 170
Cdd:PRK07008  50 KQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD----------- 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 171 pqSSLEPLKAIIQYRLPMKKNNNLYSWDDFMELGrSIPDTQLEQVIESQKA---------NQCAVLIYTSGTTGIPKGVM 241
Cdd:PRK07008 119 --LTFLPLVDALAPQCPNVKGWVAMTDAAHLPAG-STPLLCYETLVGAQDGdydwprfdeNQASSLCYTSGTTGNPKGAL 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 242 LSHDNITWIA-GAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIkIGALTYFAqADALKGTLVSTLKEVKPTVF-IG 319
Cdd:PRK07008 196 YSHRSTVLHAyGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLP-GPDLDGKSLYELIEAERVTFsAG 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 320 VPQIWEKIHEMVKKNSAKSMGLKkkafvwarnigfkvnsKKMLGKYNTPVSyrMAKTLvfskvKTSLGLDHCHSF-ISGT 398
Cdd:PRK07008 274 VPTVWLGLLNHMREAGLRFSTLR----------------RTVIGGSACPPA--MIRTF-----EDEYGVEVIHAWgMTEM 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 399 APLNQETAEFFLSLDIPIGELYGLSESSGpHTIsnqnnyrllsCG---KILTGCKNMLfqqNKDGI--GEICLWGRHIFM 473
Cdd:PRK07008 331 SPLGTLCKLKWKHSQLPLDEQRKLLEKQG-RVI----------YGvdmKIVGDDGREL---PWDGKafGDLQVRGPWVID 396
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 574584557 474 GYLESETETTeaidDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGENVPPIPVE 530
Cdd:PRK07008 397 RYFRGDASPL----VDGWFPTGDVATIDADGFMQITDRSKDV-IKSGGEWISSIDIE 448
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
416-547 9.55e-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: 9.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 416 IGELYGLSESSGPHTISNQNnyrLL----SCGKILTGCKNMLfqqNKDG-------IGEICLWGRHIFMgYLESETETTE 484
Cdd:cd05929  272 IWEYYGGTEGQGLTIINGEE---WLthpgSVGRAVLGKVHIL---DEDGnevppgeIGEVYFANGPGFE-YTNDPEKTAA 344
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574584557 485 AIDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:cd05929  345 ARNEGGWSTLGDVGYLDEDGYLYLTDR-RSDMIISGGVNIYPQEIENALIAH-PKVLDAAVVG 405
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
43-325 1.13e-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: 55.25  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557   43 HGPGHETP--MTIPEFFRESVNRFGTYPALASKNGKkweiLNfnqYYEACRKA---AKSLIKLGLERFHGVGILGFNSAE 117
Cdd:COG1020   466 NATAAPYPadATLHELFEAQAARTPDAVAVVFGDQS----LT---YAELNARAnrlAHHLRALGVGPGDLVGVCLERSLE 538
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  118 wFITAVGAIL-AGGLCVGIYATNSAEVCQYVITHAKVNILLVenDQQLQKILsiPQSSLEPLkaiiqyrlpmkknnnlyS 196
Cdd:COG1020   539 -MVVALLAVLkAGAAYVPLDPAYPAERLAYMLEDAGARLVLT--QSALAARL--PELGVPVL-----------------A 596
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  197 WDDfmELGRSIPDTQLEQVIESQkanQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDkHETVVSYLPLSHI 276
Cdd:COG1020   597 LDA--LALAAEPATNPPVPVTPD---DLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGP-GDRVLQFASLSFD 670
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 574584557  277 AAqMMDIWVPIKIGALTYFAQADALKGT--LVSTLKEVKPTVFIGVPQIWE 325
Cdd:COG1020   671 AS-VWEIFGALLSGATLVLAPPEARRDPaaLAELLARHRVTVLNLTPSLLR 720
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
225-525 1.59e-07

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 54.35  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLSHIAAQMMdIWVPIKIGAltYFaqadalkgT 304
Cdd:PRK07769 183 AYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEG-QEGDRGVSWLPFFHDMGLIT-VLLPALLGH--YI--------T 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 305 LVStlkevkPTVFIGVPQIWekIHEMVKKNsaksmGLKKKAFVWARNIGFKVNSKKMLGKYNTPvsyrmaktlvfskvkt 384
Cdd:PRK07769 251 FMS------PAAFVRRPGRW--IRELARKP-----GGTGGTFSAAPNFAFEHAAARGLPKDGEP---------------- 301
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 385 SLGLDHCHSFISGTAPLNQETAEFFLSLDIPIG-------ELYGLSE-----SSGPHTISNQ---------NNYRLL--- 440
Cdd:PRK07769 302 PLDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGlpptaikPSYGMAEatlfvSTTPMDEEPTviyvdrdelNAGRFVevp 381
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 441 ----------SCGKIL-----------TGcknmlfQQNKDG-IGEICLWGRHIFMGYLESETETTE-------------- 484
Cdd:PRK07769 382 adapnavaqvSAGKVGvsewavivdpeTA------SELPDGqIGEIWLHGNNIGTGYWGKPEETAAtfqnilksrlsesh 455
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 574584557 485 ---AIDDEGWLHSGDLGQ-LDglGFLYVTGHIKEILITAGGENVP 525
Cdd:PRK07769 456 aegAPDDALWVRTGDYGVyFD--GELYITGRVKDLVIIDGRNHYP 498
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
51-530 2.07e-07

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 53.99  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  51 MTIPEFFRESVNRFGTYPaLASKNGKKWeilNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGG 130
Cdd:PRK06155  21 RTLPAMLARQAERYPDRP-LLVFGGTRW---TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 131 LCVGIYATNSAEVCQYVITHAKVNILLVENDqqlqkilsipqsSLEPLKAIIQYRLPMKK-----NNNLYSWDDFMELGR 205
Cdd:PRK06155  97 IAVPINTALRGPQLEHILRNSGARLLVVEAA------------LLAALEAADPGDLPLPAvwlldAPASVSVPAGWSTAP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 206 SIPDTQLEQVIESQKANQCAVLiYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAAQMMdiwv 285
Cdd:PRK06155 165 LPPLDAPAPAAAVQPGDTAAIL-YTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGAD-DVLYTTLPLFHTNALNA---- 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 286 pikigaltyFAQADALKGTLVSTlkevkptvfigvpqiwekihemvKKNSAKSMglkkkafvWARnigfkvnskkmLGKY 365
Cdd:PRK06155 239 ---------FFQALLAGATYVLE-----------------------PRFSASGF--------WPA-----------VRRH 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 366 NTPVSY---RMAKTLVFSKVKTSlglDHCHSFISGTAP--LNQETAEFFLSLDIPIGELYGLSESSGP--HTISNQnnyR 438
Cdd:PRK06155 268 GATVTYllgAMVSILLSQPARES---DRAHRVRVALGPgvPAALHAAFRERFGVDLLDGYGSTETNFViaVTHGSQ---R 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 439 LLSCGKILTGCKNMLFQQNKDGI-----GEICLWGR--HIFM-GYLESETETTEAIDDEgWLHSGDLGQLDGLGFLYVTG 510
Cdd:PRK06155 342 PGSMGRLAPGFEARVVDEHDQELpdgepGELLLRADepFAFAtGYFGMPEKTVEAWRNL-WFHTGDRVVRDADGWFRFVD 420
                        490       500
                 ....*....|....*....|
gi 574584557 511 HIKEIlITAGGENVPPIPVE 530
Cdd:PRK06155 421 RIKDA-IRRRGENISSFEVE 439
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
223-547 2.53e-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: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 223 QCAVLIYTSGTTGIPKGVMLSHDNI-TWIAGAVTKDFKLTDKHETVVSYLPLSHIaaqmmdiwvpikIGALTYFAQADAL 301
Cdd:cd05923  151 QPAFVFYTSGTTGLPKGAVIPQRAAeSRVLFMSTQAGLRHGRHNVVLGLMPLYHV------------IGFFAVLVAALAL 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 302 KGTLVsTLKEVKPtvfigvpqiwekihemvkknsaksmglkKKAFVWarnigfkVNSKKMLGKYNTPVSYrmaKTLVFSK 381
Cdd:cd05923  219 DGTYV-VVEEFDP----------------------------ADALKL-------IEQERVTSLFATPTHL---DALAAAA 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 382 VKTSLGLDHCHSFISGTAPLNQ---ETAEFFLSldIPIGELYGLSESSgpHTISNQN-------------NYRLLSCGki 445
Cdd:cd05923  260 EFAGLKLSSLRHVTFAGATMPDavlERVNQHLP--GEKVNIYGTTEAM--NSLYMRDartgtemrpgffsEVRIVRIG-- 333
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 446 ltGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVP 525
Cdd:cd05923  334 --GSPDEALANGEEGELIVAAAADAAFTGYLNQPEATAKKLQD-GWYRTGDVGYVDPSGDVRILGRVDDMIIS-GGENIH 409
                        330       340
                 ....*....|....*....|..
gi 574584557 526 PIPVETLVKKKiPIISNAMLVG 547
Cdd:cd05923  410 PSEIERVLSRH-PGVTEVVVIG 430
PRK05691 PRK05691
peptide synthase; Validated
220-540 2.72e-07

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 54.40  E-value: 2.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  220 KANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKL-TDKHETVVSYLPLSHiaaqmmDIWVpikIGALtyfaqa 298
Cdd:PRK05691  164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIdLNPDDVIVSWLPLYH------DMGL---IGGL------ 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  299 dalkgtlvstlkeVKPtVFIGVPQIwekihemvkknsaksmgLKKKAFVWARnigfKVNSKKMLGKYNTPVS------YR 372
Cdd:PRK05691  229 -------------LQP-IFSGVPCV-----------------LMSPAYFLER----PLRWLEAISEYGGTISggpdfaYR 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  373 MAKTLVFSKVKTSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIG-------ELYGLSESS----------GPHTIS--- 432
Cdd:PRK05691  274 LCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGfdpdsffASYGLAEATlfvsggrrgqGIPALElda 353
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  433 ---NQNNYR------LLSCGK------ILTGCKNMLFQQNKDGIGEICLWGRHIFMGYL---ESETETTEAIDDEGWLHS 494
Cdd:PRK05691  354 ealARNRAEpgtgsvLMSCGRsqpghaVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWrnpEASAKTFVEHDGRTWLRT 433
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 574584557  495 GDLGQLDGlGFLYVTGHIKEILITAgGENVPPIPVETLVKKKIPII 540
Cdd:PRK05691  434 GDLGFLRD-GELFVTGRLKDMLIVR-GHNLYPQDIEKTVEREVEVV 477
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
146-522 2.99e-07

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 53.63  E-value: 2.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 146 YVITHAKVNILLVenDQQLQKILSIPQSSLEPLKAII--------QYRLPMKKNNNLYSWDDFMElGRSI----PDtqle 213
Cdd:PRK05620 105 HIINHAEDEVIVA--DPRLAEQLGEILKECPCVRAVVfigpsdadSAAAHMPEGIKVYSYEALLD-GRSTvydwPE---- 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 214 qviesQKANQCAVLIYTSGTTGIPKGVMLSHDNItWIAGA---VTKDFKLTDKhETVVSYLPLSHIAAqmmdiW-VPIKI 289
Cdd:PRK05620 178 -----LDETTAAAICYSTGTTGAPKGVVYSHRSL-YLQSLslrTTDSLAVTHG-ESFLCCVPIYHVLS-----WgVPLAA 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 290 ---GALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLkKKAFV------------WARNIGF 354
Cdd:PRK05620 246 fmsGTPLVFPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSL-QEIYVggsavppilikaWEERYGV 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 355 KVNSkkmlgkyntpvSYRMAKTLVFSKVKtslgldHCHSFISGTAPLNqetaefflsldipigelYGLSESSGPHTIsnq 434
Cdd:PRK05620 325 DVVH-----------VWGMTETSPVGTVA------RPPSGVSGEARWA-----------------YRVSQGRFPASL--- 367
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 435 nNYRLLSCGKILTGcknmlfqqNKDGIGEICLWGRHIFMGYLESETETT---------EAIDDE-------GWLHSGDLG 498
Cdd:PRK05620 368 -EYRIVNDGQVMES--------TDRNEGEIQVRGNWVTASYYHSPTEEGggaastfrgEDVEDAndrftadGWLRTGDVG 438
                        410       420
                 ....*....|....*....|....
gi 574584557 499 QLDGLGFLYVTGHIKEIlITAGGE 522
Cdd:PRK05620 439 SVTRDGFLTIHDRARDV-IRSGGE 461
PRK09192 PRK09192
fatty acyl-AMP ligase;
460-533 3.82e-07

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 53.09  E-value: 3.82e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 574584557 460 GIGEICLWGRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGlGFLYVTGHIKEiLITAGGENVPPIPVETLV 533
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 ...
227-547 4.22e-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: 4.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 227 LIYTSGTTGIPKGVMLSHDNI-------TWIAGAVTKDFKLTDkHETVVSYLPLSHIAAQMMDiwvpikiGALTYFAQAD 299
Cdd:cd05924    8 ILYTGGTTGMPKGVMWRQEDIfrmlmggADFGTGEFTPSEDAH-KAAAAAAGTVMFPAPPLMH-------GTGSWTAFGG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 300 ALKGTLVstlkeVKPTVFIGVPQIWEKIHEMvkknsaksmglkkkafvwarnigfKVNSKKMLGKyntpvsyRMAKTLV- 378
Cdd:cd05924   80 LLGGQTV-----VLPDDRFDPEEVWRTIEKH------------------------KVTSMTIVGD-------AMARPLId 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 379 -FSKVKTsLGLDHCHSFISGTAPLNQETAEFFLSL--DIPIGELYGLSESSGPHTISNQNN------YRLLSCGKILTGC 449
Cdd:cd05924  124 aLRDAGP-YDLSSLFAISSGGALLSPEVKQGLLELvpNITLVDAFGSSETGFTGSGHSAGSgpetgpFTRANPDTVVLDD 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 450 KNMLFQQNKDGIGEICLWGrHIFMGYLESETETTEA---IDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPP 526
Cdd:cd05924  203 DGRVVPPGSGGVGWIARRG-HIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGR-GSVCINTGGEKVFP 280
                        330       340
                 ....*....|....*....|.
gi 574584557 527 IPVETLVKKKiPIISNAMLVG 547
Cdd:cd05924  281 EEVEEALKSH-PAVYDVLVVG 300
PRK05851 PRK05851
long-chain-fatty acid--ACP ligase MbtM;
210-531 4.36e-07

long-chain-fatty acid--ACP ligase MbtM;


Pssm-ID: 180289 [Multi-domain]  Cd Length: 525  Bit Score: 52.85  E-value: 4.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 210 TQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHiaaqmmDIwvpiki 289
Cdd:PRK05851 140 TNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSWLPLYH------DM------ 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 290 gALTyFAQADALKGTlvsTLKEVKPTVFIGVPQIWekihemvkknsAKSMGLKKKAFVWARNIGFKvnskkMLGKYNTPV 369
Cdd:PRK05851 208 -GLA-FLLTAALAGA---PLWLAPTTAFSASPFRW-----------LSWLSDSRATLTAAPNFAYN-----LIGKYARRV 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 370 SYRMAKTLVFSkvktslgldhchsfISGTAPLNQETAEFFLSLDIPIG-------ELYGLSESSGPHTIS---------- 432
Cdd:PRK05851 267 SDVDLGALRVA--------------LNGGEPVDCDGFERFATAMAPFGfdagaaaPSYGLAESTCAVTVPvpgiglrvde 332
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 433 -----NQNNYRLLSCGKILTG------CKNMLFQQNKDGIGEICLWGRHIFMGYLESETetteaIDDEGWLHSGDLGQLd 501
Cdd:PRK05851 333 vttddGSGARRHAVLGNPIPGmevrisPGDGAAGVAGREIGEIEIRGASMMSGYLGQAP-----IDPDDWFPTGDLGYL- 406
                        330       340       350
                 ....*....|....*....|....*....|
gi 574584557 502 GLGFLYVTGHIKEiLITAGGENVPPIPVET 531
Cdd:PRK05851 407 VDGGLVVCGRAKE-LITVAGRNIFPTEIER 435
PRK07638 PRK07638
acyl-CoA synthetase; Validated
458-547 5.91e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 52.47  E-value: 5.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 458 KDGIGEICLWGRHIFMGYLeSETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETlVKKKI 537
Cdd:PRK07638 330 KGEIGTVYVKSPQFFMGYI-IGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILF-GGINIFPEEIES-VLHEH 406
                         90
                 ....*....|
gi 574584557 538 PIISNAMLVG 547
Cdd:PRK07638 407 PAVDEIVVIG 416
PRK12316 PRK12316
peptide synthase; Provisional
57-291 8.75e-07

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 52.65  E-value: 8.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557   57 FRESVNRFGTYPALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWfITAVGAIL-AGGLCVGI 135
Cdd:PRK12316  517 FEEQVERTPEAPALAFGE----ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEM-VVALLAILkAGGAYVPL 591
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  136 YATNSAEVCQYVITHAKVNILLveNDQQLQKILSIPQSSLEPLKAIIQYRLPMKKNNNlyswddfmelgrsiPDTQLEqv 215
Cdd:PRK12316  592 DPEYPAERLAYMLEDSGVQLLL--SQSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEEN--------------PGTELN-- 653
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574584557  216 iesqkANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLtDKHETVVSYLPLShIAAQMMDIWVPIKIGA 291
Cdd:PRK12316  654 -----PENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGL-GVGDTVLQKTPFS-FDVSVWEFFWPLMSGA 722
PRK07445 PRK07445
O-succinylbenzoic acid--CoA ligase; Reviewed
412-533 1.49e-06

O-succinylbenzoic acid--CoA ligase; Reviewed


Pssm-ID: 236019 [Multi-domain]  Cd Length: 452  Bit Score: 51.15  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 412 LDIPIGELYGLSESSG------PHTISNQNNyrllSCGKILTGCKNMLFQQNkdgIGEICLWGRHIFMGYLEsetettEA 485
Cdd:PRK07445 253 LQLRLAPTYGMTETASqiatlkPDDFLAGNN----SSGQVLPHAQITIPANQ---TGNITIQAQSLALGYYP------QI 319
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 574584557 486 IDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVETLV 533
Cdd:PRK07445 320 LDSQGIFETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAI 366
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
221-547 2.29e-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: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 221 ANQCAVLIYTSGTTGIPKGVMlsHdnitwiagavtkdfkltdKHETVVSYLPLSHIAAQMMDiwvpiKIGALtYFAQAD- 299
Cdd:cd05971   87 SDDPALIIYTSGTTGPPKGAL--H------------------AHRVLLGHLPGVQFPFNLFP-----RDGDL-YWTPADw 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 300 ALKGTLVSTLKevkPTVFIGVPQIwekIHEMVKKNSAKSMglkkkafvwarnigfkvnskKMLGKYN------TPVSYRM 373
Cdd:cd05971  141 AWIGGLLDVLL---PSLYFGVPVL---AHRMTKFDPKAAL--------------------DLMSRYGvttaflPPTALKM 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 374 AKtlvFSKVKTSLGLDHCHSFISGTAPLNQE-TAEFFLSLDIPIGELYGLSESSgpHTISNQNNY---RLLSCGKILTGC 449
Cdd:cd05971  195 MR---QQGEQLKHAQVKLRAIATGGESLGEElLGWAREQFGVEVNEFYGQTECN--LVIGNCSALfpiKPGSMGKPIPGH 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 450 KNMLFQQN-----KDGIGEICLW--GRHIFMGYLESEtETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEIlITAGGE 522
Cdd:cd05971  270 RVAIVDDNgtplpPGEVGEIAVElpDPVAFLGYWNNP-SATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDV-ITSSGY 347
                        330       340
                 ....*....|....*....|....*
gi 574584557 523 NVPPIPVETLVKKKiPIISNAMLVG 547
Cdd:cd05971  348 RIGPAEIEECLLKH-PAVLMAAVVG 371
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
89-246 2.46e-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: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  89 ACRKAAKsLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKIL 168
Cdd:cd12114   22 ARRVAGA-LKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDGPDAQLDVA 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574584557 169 sIPQSSLEPLKAIIQyrlpmkknnnlyswddfmelgrsiPDTQLEQVIESQkanQCAVLIYTSGTTGIPKGVMLSHDN 246
Cdd:cd12114  101 -VFDVLILDLDALAA------------------------PAPPPPVDVAPD---DLAYVIFTSGSTGTPKGVMISHRA 150
PRK13382 PRK13382
bile acid CoA ligase;
454-530 2.57e-06

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 50.53  E-value: 2.57e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574584557 454 FQQNKDG-IGEICLWGRHIFMGYLESETETTEaiddEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVE 530
Cdd:PRK13382 383 FREVPTGeVGTIFVRNDTQFDGYTSGSTKDFH----DGFMASGDVGYLDENGRLFVVGRDDE-MIVSGGENVYPIEVE 455
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
48-278 3.28e-06

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 50.26  E-value: 3.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  48 ETPMTIPEFFRESVNRFGTYPALASkNGKKWEILNFNQYyeaCRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAIL 127
Cdd:PRK08279  34 DSKRSLGDVFEEAAARHPDRPALLF-EDQSISYAELNAR---ANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAK 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 128 AGGlCVGIYATN-SAEVCQYVITHAKVNILLVENDQqLQKILSIPQsslEPLKAIIQYRLPMKKNNNLYSWDDFMELGRS 206
Cdd:PRK08279 110 LGA-VVALLNTQqRGAVLAHSLNLVDAKHLIVGEEL-VEAFEEARA---DLARPPRLWVAGGDTLDDPEGYEDLAAAAAG 184
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574584557 207 IPDTQLEqVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNIT----WIAGavtkdfkLTDKHETVVSY--LPLSHIAA 278
Cdd:PRK08279 185 APTTNPA-SRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLkamgGFGG-------LLRLTPDDVLYccLPLYHNTG 254
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
214-262 3.35e-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: 3.35e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 574584557 214 QVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTD 262
Cdd:cd05918   98 KVVLTSSPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTS 146
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
461-547 3.90e-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: 3.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 461 IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVkKKIPII 540
Cdd:cd05920  335 EGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKD-QINRGGEKIAAEEVENLL-LRHPAV 412

                 ....*..
gi 574584557 541 SNAMLVG 547
Cdd:cd05920  413 HDAAVVA 419
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
461-547 4.07e-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: 4.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 461 IGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEiLITAGGENVPPIPVETLVKKKiPII 540
Cdd:COG1021  380 VGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKD-QINRGGEKIAAEEVENLLLAH-PAV 457

                 ....*..
gi 574584557 541 SNAMLVG 547
Cdd:COG1021  458 HDAAVVA 464
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
202-547 4.53e-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: 4.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 202 ELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQM- 280
Cdd:cd05910   65 NLKQCLQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPALg 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 281 MDIWVPikigALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEmvkknsaksmglkkkafvWARNIGFKVNSKK 360
Cdd:cd05910  145 LTSVIP----DMDPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVAR------------------YCAQHGITLPSLR 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 361 MLGKYNTPVsyRMAKTLVFSK-------VKTSLGLDHC--------HSFISGTAPLNQETAEFFLSLDIPIGELYGLSES 425
Cdd:cd05910  203 RVLSAGAPV--PIALAARLRKmlsdeaeILTPYGATEAlpvssigsRELLATTTAATSGGAGTCVGRPIPGVRVRIIEID 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 426 SGPhtISNQNNYRLLSCGkiltgcknmlfqqnkdGIGEICLWGRHIFMGYLESETETTEA-IDDEG---WLHSGDLGQLD 501
Cdd:cd05910  281 DEP--IAEWDDTLELPRG----------------EIGEITVTGPTVTPTYVNRPVATALAkIDDNSegfWHRMGDLGYLD 342
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 574584557 502 GLGFLYVTGHIKEILITAGGeNVPPIPVETlVKKKIPIISNAMLVG 547
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) ...
225-261 4.59e-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: 4.59e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT 261
Cdd:cd17652   96 AYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVG 132
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
178-291 5.77e-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: 5.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 178 LKAIIQYRLPMKKNNNLYSW--------DDFMELGRSIPDTQLEQVIESQKANQC----AVLIYTSGTTGIPKGVMLSHD 245
Cdd:cd05938   88 LQEAVEEVLPALRADGVSVWylshtsntEGVISLLDKVDAASDEPVPASLRAHVTikspALYIYTSGTTGLPKAARISHL 167
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 574584557 246 NItWIAGAVTKDFKLTdKHETVVSYLPLSHIAAQMMDIWVPIKIGA 291
Cdd:cd05938  168 RV-LQCSGFLSLCGVT-ADDVIYITLPLYHSSGFLLGIGGCIELGA 211
PRK07867 PRK07867
acyl-CoA synthetase; Validated
88-286 5.80e-06

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 49.29  E-value: 5.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  88 EACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEV---------CQYVITHAKVNILLv 158
Cdd:PRK07867  37 GSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAAlardiahadCQLVLTESAHAELL- 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 159 enDQQLQKILSIPQSSLEPLKAIIQYRlpmkknnnlyswDDFMELGRSIPDTQLeqviesqkanqcaVLIYTSGTTGIPK 238
Cdd:PRK07867 116 --DGLDPGVRVINVDSPAWADELAAHR------------DAEPPFRVADPDDLF-------------MLIFTSGTSGDPK 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 574584557 239 GVMLSHDNITWIAGAVTKDFKLTdkhETVVSYL--PLSHIAAQMMDiWVP 286
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 ...
220-248 8.42e-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: 8.42e-06
                         10        20
                 ....*....|....*....|....*....
gi 574584557 220 KANQCAVLIYTSGTTGIPKGVMLSHDNIT 248
Cdd:cd17653  103 SPDDLAYIIFTSGSTGIPKGVMVPHRGVL 131
PRK12467 PRK12467
peptide synthase; Provisional
68-261 9.29e-06

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 49.39  E-value: 9.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557   68 PALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYV 147
Cdd:PRK12467  529 PALVFGE----QVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYM 604
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  148 ITHAKVNILLveNDQQLQKILSIPqssleplkaiiqyrlpmkknnnlyswDDFMELGRSIPDTQLEQVIE-----SQKAN 222
Cdd:PRK12467  605 LDDSGVRLLL--TQSHLLAQLPVP--------------------------AGLRSLCLDEPADLLCGYSGhnpevALDPD 656
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 574584557  223 QCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT 261
Cdd:PRK12467  657 NLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLA 695
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
228-283 1.11e-05

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: 1.11e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 574584557 228 IYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIAAQMMDI 283
Cdd:cd05939  110 IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMR-PEDVVYDCLPLYHSAGGIMGV 164
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
221-262 1.15e-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: 1.15e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 574584557 221 ANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTD 262
Cdd:cd17643   92 PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNE 133
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
81-313 1.72e-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: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  81 LNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEn 160
Cdd:cd17650   13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLTQ- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 161 dqqlqkilsipqssleplkaiiqyrlpmkknnnlyswddfmelgrsiPDtqleqviesqkanQCAVLIYTSGTTGIPKGV 240
Cdd:cd17650   92 -----------------------------------------------PE-------------DLAYVIYTSGTTGKPKGV 111
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574584557 241 MLSHDNITWIAGAVTKDFKLTDKhetvvsylplSHIAAQMMDIWVPIKIGAltyFAQADALKGTLVSTLKEVK 313
Cdd:cd17650  112 MVEHRNVAHAAHAWRREYELDSF----------PVRLLQMASFSFDVFAGD---FARSLLNGGTLVICPDEVK 171
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
108-324 2.26e-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: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 108 VGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDqqlqkilsipqsSLEPLKAIIqyrlp 187
Cdd:cd12116   40 VAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDDA------------LPDRLPAGL----- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 188 mkknnnlyswdDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT--DKHE 265
Cdd:cd12116  103 -----------PVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGpgDRLL 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 574584557 266 TVVSYlpLSHIAAqmMDIWVPIKIGALTYFAQADALK--GTLVSTLKEVKPTVFIGVPQIW 324
Cdd:cd12116  172 AVTTY--AFDISL--LELLLPLLAGARVVIAPRETQRdpEALARLIEAHSITVMQATPATW 228
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
88-287 2.27e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 47.33  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  88 EACRKAAkSLIKL--GLERFHgVGILGFNSAEwFITAV-GAILAGGLCVGIYATN-----SAEV----CQYVITHAK--- 152
Cdd:PRK13388  35 EAAARAA-ALIALadPDRPLH-VGVLLGNTPE-MLFWLaAAALGGYVLVGLNTTRrgaalAADIrradCQLLVTDAEhrp 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 153 ---------VNILLVENDQQLQKILsiPQSSLEPLKAIIqyrlpmkknnnlyswddfmelgrsiPDTQLeqviesqkanq 223
Cdd:PRK13388 112 lldgldlpgVRVLDVDTPAYAELVA--AAGALTPHREVD-------------------------AMDPF----------- 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 574584557 224 caVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdkhETVVSYL--PLSHIAAqMMDIWVPI 287
Cdd:PRK13388 154 --MLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLT---RDDVCYVsmPLFHSNA-VMAGWAPA 213
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
218-538 2.44e-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: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 218 SQKANQCAVLIYTSGTTGIPKGVMLSHDN-------ITWIAgavtkDFKLTDKhetVVSYLPLSHIAAQMMDIWVPIKIG 290
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSllanveqIKTIA-----DFTPNDR---FMSALPLFHSFGLTVGLFTPLLTG 432
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 291 AltyfaqadalkgtlvstlkevkpTVFIgvpqiwekihemvkknsaksmglkkkafvwarnigfkvnskkmlgkYNTPVS 370
Cdd:PRK08043 433 A-----------------------EVFL----------------------------------------------YPSPLH 443
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 371 YRMAKTLVFSK-----VKTSLGLDHCHSF------------ISGTAPLNQETAEFFL-SLDIPIGELYGLSESSGPHTIS 432
Cdd:PRK08043 444 YRIVPELVYDRnctvlFGTSTFLGNYARFanpydfarlryvVAGAEKLQESTKQLWQdKFGLRILEGYGVTECAPVVSIN 523
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 433 NQNNYRLLSCGKILTGCKNMLFqqNKDGI---GEICLWGRHIFMGYLESE---------TETTEAIDDEGWLHSGDLGQL 500
Cdd:PRK08043 524 VPMAAKPGTVGRILPGMDARLL--SVPGIeqgGRLQLKGPNIMNGYLRVEkpgvlevptAENARGEMERGWYDTGDIVRF 601
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 574584557 501 DGLGFLYVTGHIKEILITAgGENVPPIPVETLVKKKIP 538
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) ...
57-244 2.64e-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: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  57 FRESVNRFGTYPALASkNGKKWEilnfnqYYEACRKA---AKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCV 133
Cdd:cd17651    1 FERQAARTPDAPALVA-EGRRLT------YAELDRRAnrlAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 134 GIYATNSAEVCQYVITHAKVNILLVENDqqlqkilsiPQSSLEPLKAIIqyrlpmkknnnlysWDDFMELGRSIPDTqlE 213
Cdd:cd17651   74 PLDPAYPAERLAFMLADAGPVLVLTHPA---------LAGELAVELVAV--------------TLLDQPGAAAGADA--E 128
                        170       180       190
                 ....*....|....*....|....*....|.
gi 574584557 214 QVIESQKANQcAVLIYTSGTTGIPKGVMLSH 244
Cdd:cd17651  129 PDPALDADDL-AYVIYTSGSTGRPKGVVMPH 158
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
228-260 3.99e-05

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 46.81  E-value: 3.99e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 574584557 228 IYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKL 260
Cdd:PRK04813 149 IFTSGTTGKPKGVQISHDNLVSFTNWMLEDFAL 181
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
209-247 4.14e-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: 4.14e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 574584557 209 DTQLEQVIESQKanQCAVLIYTSGTTGIPKGVMLSHDNI 247
Cdd:cd17648   83 DTGARVVITNST--DLAYAIYTSGTTGKPKGVLVEHGSV 119
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
79-532 5.91e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 46.22  E-value: 5.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  79 EILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEwFITAVGAILAGGL---CVGIYATnsAEVCQYVITHAKVNI 155
Cdd:PRK13391  23 EVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLR-YLEVCWAAERSGLyytCVNSHLT--PAEAAYIVDDSGARA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 156 LLVENDQqlqkiLSIPQSSLEPLKAIiQYRLPMKKNNNLYSWDDFMELGRSIPDTqleqVIESQKANQcaVLIYTSGTTG 235
Cdd:PRK13391 100 LITSAAK-----LDVARALLKQCPGV-RHRLVLDGDGELEGFVGYAEAVAGLPAT----PIADESLGT--DMLYSSGTTG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 236 IPKGVM--LSHDNI---TWIAGAVTKDFKLTDkhETVvsYL---PLSHIAAQMmdiWVPIKIgaltyfaqadALKGTLVs 307
Cdd:PRK13391 168 RPKGIKrpLPEQPPdtpLPLTAFLQRLWGFRS--DMV--YLspaPLYHSAPQR---AVMLVI----------RLGGTVI- 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 308 TLKEVKPTVFIGVPQIWEKIHEMVkknsAKSMglkkkaFVwarnigfkvnskKMLgkyNTPVSYRMAKTLvfSKVKTSlg 387
Cdd:PRK13391 230 VMEHFDAEQYLALIEEYGVTHTQL----VPTM------FS------------RML---KLPEEVRDKYDL--SSLEVA-- 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 388 ldhchsfISGTAPLNQETAEFFLSLDIP-IGELYGLSESSGPHTI-SNQNNYRLLSCGKILTGCKNMLFQQNKD----GI 461
Cdd:PRK13391 281 -------IHAAAPCPPQVKEQMIDWWGPiIHEYYAATEGLGFTACdSEEWLAHPGTVGRAMFGDLHILDDDGAElppgEP 353
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 574584557 462 GEICLWGRHIFMgYLESETETTEAID-DEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETL 532
Cdd:PRK13391 354 GTIWFEGGRPFE-YLNDPAKTAEARHpDGTWSTVGDIGYVDEDGYLYLTDR-AAFMIISGGVNIYPQEAENL 423
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
441-545 6.73e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 46.14  E-value: 6.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 441 SCGKILTGCKNMLFQQNKDGIGEIcLWGRHIFMGYLESETETT---EAIDDeGWLHSGDLGQLDGLGFLYVTGHiKEILI 517
Cdd:PRK13383 346 TVGKPVAGCPVRILDRNNRPVGPR-VTGRIFVGGELAGTRYTDgggKAVVD-GMTSTGDMGYLDNAGRLFIVGR-EDDMI 422
                         90       100
                 ....*....|....*....|....*...
gi 574584557 518 TAGGENVPPIPVETLVKKKIPIISNAML 545
Cdd:PRK13383 423 ISGGENVYPRAVENALAAHPAVADNAVI 450
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
209-261 8.79e-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: 8.79e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 574584557 209 DTQLeQVIESQKANqCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT 261
Cdd:cd17644   95 DAQI-SVLLTQPEN-LAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGIT 145
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
92-240 9.52e-05

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 45.46  E-value: 9.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  92 KAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVEND--QQLQKIL- 168
Cdd:PRK12406  23 RAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADllHGLASALp 102
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 574584557 169 -SIPQSSLEPLKAIIQ-YRLP---MKKNNNLYSWDDFMELGRSIPDTQLEQViesqkanqcAVLIYTSGTTGIPKGV 240
Cdd:PRK12406 103 aGVTVLSVPTPPEIAAaYRISpalLTPPAGAIDWEGWLAQQEPYDGPPVPQP---------QSMIYTSGTTGHPKGV 170
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
69-262 9.54e-05

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 45.66  E-value: 9.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  69 ALASKNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAE-VCQYV 147
Cdd:PRK04319  62 ALRYLDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEaVRDRL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 148 -ITHAKVnilLVENDQQLQKIlsiPQSSLEPLKAIIQYRLPMKKNNNLYSWDDFMELGrsipDTQLEqvIESQKANQCAV 226
Cdd:PRK04319 142 eDSEAKV---LITTPALLERK---PADDLPSLKHVLLVGEDVEEGPGTLDFNALMEQA----SDEFD--IEWTDREDGAI 209
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 574584557 227 LIYTSGTTGIPKGVMLSHDNIT--WIAGAVTKDFKLTD 262
Cdd:PRK04319 210 LHYTSGSTGKPKGVLHVHNAMLqhYQTGKYVLDLHEDD 247
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
218-261 1.20e-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: 1.20e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 574584557 218 SQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLT 261
Cdd:cd17649   90 THHPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLT 133
PRK07798 PRK07798
acyl-CoA synthetase; Validated
94-280 1.23e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 45.26  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  94 AKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGI-YATNSAEVcQYVITHAKVNILLVEnDQQLQKILSIPq 172
Cdd:PRK07798  42 AHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnYRYVEDEL-RYLLDDSDAVALVYE-REFAPRVAEVL- 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557 173 SSLEPLKAIIQYrlpmkknnnlyswDDFMELGRSIPDTQLEQVIESQKANQCAV--------LIYTSGTTGIPKGVMLSH 244
Cdd:PRK07798 119 PRLPKLRTLVVV-------------EDGSGNDLLPGAVDYEDALAAGSPERDFGerspddlyLLYTGGTTGMPKGVMWRQ 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 574584557 245 DNItWIAGAVTKDF----KLTDKHETVVSYL-----------PLSHIAAQM 280
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 ...
208-247 1.25e-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: 1.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 574584557 208 PDTQLEQVIESQKAnqcAVLIYTSGTTGIPKGVMLSHDNI 247
Cdd:cd17646  127 PATPPLVPPRPDNL---AYVIYTSGSTGRPKGVMVTHAGI 163
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
225-280 1.44e-04

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 44.65  E-value: 1.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNItWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQM 280
Cdd:cd05940   84 ALYIYTSGTTGLPKAAIISHRRA-WRGGAFFAGSGGALPSDVLYTCLPLYHSTALI 138
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
221-257 2.10e-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: 2.10e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 574584557 221 ANQCAVLIYTSGTTGIPKGVMLSHDN----ITWIAGAVTKD 257
Cdd:cd12115  104 PDDLAYVIYTSGSTGRPKGVAIEHRNaaafLQWAAAAFSAE 144
PRK12316 PRK12316
peptide synthase; Provisional
55-309 2.70e-04

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 44.56  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557   55 EFFRESVNRFGTYPALASKNgkkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVG 134
Cdd:PRK12316 3061 RLFEEQVERTPDAVALAFGE----QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVP 3136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  135 IYATNSAEVCQYVITHAKVNILLVendqqlQKILSIPQSsleplkaiiqyrlpmKKNNNLYSWDDFMELGRSIPDTQLEq 214
Cdd:PRK12316 3137 LDPEYPEERLAYMLEDSGAQLLLS------QSHLRLPLA---------------QGVQVLDLDRGDENYAEANPAIRTM- 3194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  215 viesqkANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTdKHETVVSYLPLSHIAAQMMDIWVPIKIGALTY 294
Cdd:PRK12316 3195 ------PENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLG-VGDRVLQFTTFSFDVFVEELFWPLMSGARVVL 3267
                         250
                  ....*....|....*
gi 574584557  295 FAQADALKGTLVSTL 309
Cdd:PRK12316 3268 AGPEDWRDPALLVEL 3282
PRK12316 PRK12316
peptide synthase; Provisional
86-244 3.86e-04

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 44.18  E-value: 3.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557   86 YYEACRKA---AKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDq 162
Cdd:PRK12316 2031 YAELDSRAnrlAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRH- 2109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  163 qLQKILSIPQSSLeplkaiiqyRLPMKKNNNLYSWDDFMELGRSIPDTqleqviesqkanqCAVLIYTSGTTGIPKGVML 242
Cdd:PRK12316 2110 -LLERLPLPAGVA---------RLPLDRDAEWADYPDTAPAVQLAGEN-------------LAYVIYTSGSTGLPKGVAV 2166

                  ..
gi 574584557  243 SH 244
Cdd:PRK12316 2167 SH 2168
PRK05691 PRK05691
peptide synthase; Validated
225-258 6.07e-04

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 43.23  E-value: 6.07e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 574584557  225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDF 258
Cdd:PRK05691 2336 AYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERF 2369
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
227-299 6.97e-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: 6.97e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 574584557 227 LIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHEtvvsYLPLSHIAAQMM--DIWVPIKIGALTYFAQAD 299
Cdd:cd17647  114 LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDK----FTMLSGIAHDPIqrDMFTPLFLGAQLLVPTQD 184
PRK12467 PRK12467
peptide synthase; Provisional
86-292 1.05e-03

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 42.46  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557   86 YYEACRKA---AKSLIKLGL--ERFhgVGILGFNSAEwFITAVGAIL-AGGLCVGIYATNSAEVCQYVITHAKVNILLVE 159
Cdd:PRK12467 3123 YAELNRRAnrlAHRLIAIGVgpDVL--VGVAVERSVE-MIVALLAVLkAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQ 3199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  160 ndqqlqkilsipQSSLEplkaiiqyRLPMKKNNNLYSWDDFMELGrsIPDTQLEQVIESQkanQCAVLIYTSGTTGIPKG 239
Cdd:PRK12467 3200 ------------AHLLE--------QLPAPAGDTALTLDRLDLNG--YSENNPSTRVMGE---NLAYVIYTSGSTGKPKG 3254
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 574584557  240 VMLSHDNIT----WIAGAvtkdfKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGAL 292
Cdd:PRK12467 3255 VGVRHGALAnhlcWIAEA-----YELDANDRVLLFMSFSFDGAQERFLWTLICGGCL 3306
PRK05857 PRK05857
fatty acid--CoA ligase;
473-530 1.69e-03

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 41.53  E-value: 1.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 574584557 473 MGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILITaGGENVPPIPVE 530
Cdd:PRK05857 386 LGYWNNPERTAEVLID-GWVNTGDLLERREDGFFYIKGRSSEMIIC-GGVNIAPDEVD 441
PRK12467 PRK12467
peptide synthase; Provisional
35-247 1.77e-03

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 41.69  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557   35 EVLLRLSKHGPGHETPMTIPEFFRESVNRfgTYPALASKNGKkwEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFN 114
Cdd:PRK12467 1558 QILEGWNATHTGYPLARLVHQLIEDQAAA--TPEAVALVFGE--QELTYGELNRRANRLAHRLIALGVGPEVLVGIAVER 1633
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557  115 SAEwFITAVGAIL-AGGLCVGIYATNSAEVCQYVITHAKVNILLVendqqlqkilsipQSSLEPlkaiiqyRLPMKKNNN 193
Cdd:PRK12467 1634 SLE-MVVGLLAILkAGGAYVPLDPEYPRERLAYMIEDSGIELLLT-------------QSHLQA-------RLPLPDGLR 1692
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 574584557  194 LYSWDDFMELGRSIPDTQLEQVIESQkanQCAVLIYTSGTTGIPKGVMLSHDNI 247
Cdd:PRK12467 1693 SLVLDQEDDWLEGYSDSNPAVNLAPQ---NLAYVIYTSGSTGRPKGAGNRHGAL 1743
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
225-247 1.88e-03

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 41.57  E-value: 1.88e-03
                          10        20
                  ....*....|....*....|...
gi 574584557  225 AVLIYTSGTTGIPKGVMLSHDNI 247
Cdd:PRK10252  601 AYIIFTSGSTGRPKGVMVGQTAI 623
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
225-278 2.13e-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: 2.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 574584557 225 AVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKhETVVSYLPLSHIAA 278
Cdd:cd05937   90 AILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNG-DRTYTCMPLYHGTA 142
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
227-316 2.52e-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: 2.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584557   227 LIYTSGTTGIPKGVMLSHDNIT----WIAgavtKDFKLTDKHEtvvsYLPLSHIAAQMM--DIWVPIKIGALTYFAQADA 300
Cdd:TIGR03443  420 LSFTSGSEGIPKGVLGRHFSLAyyfpWMA----KRFGLSENDK----FTMLSGIAHDPIqrDMFTPLFLGAQLLVPTADD 491
                           90
                   ....*....|....*...
gi 574584557   301 L--KGTLVSTLKEVKPTV 316
Cdd:TIGR03443  492 IgtPGRLAEWMAKYGATV 509
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
221-247 3.16e-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: 3.16e-03
                         10        20
                 ....*....|....*....|....*..
gi 574584557 221 ANQCAVLIYTSGTTGIPKGVMLSHDNI 247
Cdd:cd17645  103 PDDLAYVIYTSGSTGLPKGVMIEHHNL 129
PRK07867 PRK07867
acyl-CoA synthetase; Validated
459-530 4.74e-03

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 40.05  E-value: 4.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 574584557 459 DGIGEIC-LWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHIKEILiTAGGENVPPIPVE 530
Cdd:PRK07867 350 EAIGELVnTAGPGGFEGYYNDPEADAERMRG-GVYWSGDLAYRDADGYAYFAGRLGDWM-RVDGENLGTAPIE 420
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
462-530 6.22e-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: 6.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574584557 462 GEICLWGRHIFMGYLESETETTEAIDDeGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVE 530
Cdd:cd17636  190 GEIVARGPTVMAGYWNRPEVNARRTRG-GWHHTNDLGRREPDGSLSFVGP-KTRMIKSGAENIYPAEVE 256
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
475-532 6.96e-03

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 39.50  E-value: 6.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 574584557 475 YLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHiKEILITAGGENVPPIPVETL 532
Cdd:PRK08276 354 YHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDR-KSDMIISGGVNIYPQEIENL 410
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH