|
Name |
Accession |
Description |
Interval |
E-value |
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
16-671 |
0e+00 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 1165.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 16 QVMWEPDS--KKDTQMDRFRAAVGTACGLALGNYNDLYHWSVRSYMDFWAEFWKFSGIVYSRMYDEVVDTSKGIADVpeW 93
Cdd:TIGR01217 4 QPLWQPDAqrIAQARMTRFQAWAGEHHGAAEGGYDALHRWSVDELDTFWKAVWEWFDVRFSTPCARVVDDRTMPGAQ--W 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 94 FRGSRLNYAENLLRHKENDRVALYVAREgrEEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAA 173
Cdd:TIGR01217 82 FPGARLNYAENLLRAAGTEPALLYVDET--HEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 174 ASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEAVVYNGKEHGHLEKLQRVVKGLPDLQRVVLIPYVLPREKIDIsKI 253
Cdd:TIGR01217 160 ASVGAIWSSCSPDFGARGVLDRFQQIEPKLLFTVDGYRYNGKEHDRRDKVAEVRKELPTLRAVVHIPYLGPRETEAP-KI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 254 PNSVFLDDFLAsgtGAQAPQLEFEQLPFSHPLFIMFSSGTTGAPKCMVHSAGGTLIQHLKEHMLHGNMTSSDILLYYTTV 333
Cdd:TIGR01217 239 DGALDLEDFTA---AAQAAELVFEQLPFDHPLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTTT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 334 GWMMWNWMVSALATGASLVLYDGSPLVPTPNVLWDLVDRIGITILGTGAKWLSVLEEKDMKPVETHNLHTLHTILSTGSP 413
Cdd:TIGR01217 316 GWMMWNWLVSGLATGATLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVASTGSP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 414 LKAQSYEYVYRCIKSSVLLGSISGGTDIISCFMGQNSSIPVYKGEIQARNLGMAVEAWDEEGKAVWGASGELVCTKPIPC 493
Cdd:TIGR01217 396 LPPDGFRWVYDEIKADVWLASISGGTDICSCFAGANPTLPVHIGEIQAPGLGTAVQSWDPEGKPVTGEVGELVCTNPMPS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 494 QPTHFWNDENGSKYRKAYFSKFPGVWAHGDYCRINPkTGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVP 573
Cdd:TIGR01217 476 MPIRFWNDPDGSKYRDAYFDTYPGVWRHGDWITLTP-RGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIG 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 574 QYNRDGEERVVLFLKMASGHTFQPDLVKRIRDAIRLGLSARHVPSLILETRGIPYTLNGKKVEVAVKQVMAGRTVEHRGA 653
Cdd:TIGR01217 555 QEQPDGGYRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKRVLQGTPVDNPGA 634
|
650
....*....|....*...
gi 21313520 654 FSNPETLDLYRDIPELQD 671
Cdd:TIGR01217 635 IDNPELLDLYEELAELRS 652
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
29-663 |
0e+00 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 1134.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 29 MDRFRAAVGTACGLALGNYNDLYHWSVRSYMDFWAEFWKFSGIVYSRMYDeVVDTSKGIADVPEWFRGSRLNYAENLLRH 108
Cdd:cd05943 1 MDAFRRWVNARHGLSLADYAALHRWSVDDPGAFWAAVWDFSGVRGSKPYD-VVVVSGRIMPGARWFPGARLNYAENLLRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 109 KEN-DRVALYVAREGreEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDF 187
Cdd:cd05943 80 ADAdDPAAIYAAEDG--ERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 188 GVNGVLDRFSQIQPKLIFSVEAVVYNGKEHGHLEKLQRVVKGLPDLQRVVLIPYVLPREKIDISKIPNSVFLDDFLASGt 267
Cdd:cd05943 158 GVPGVLDRFGQIEPKVLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVVVVPYTVAAGQPDLSKIAKALTLEDFLATG- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 268 gaQAPQLEFEQLPFSHPLFIMFSSGTTGAPKCMVHSAGGTLIQHLKEHMLHGNMTSSDILLYYTTVGWMMWNWMVSALAT 347
Cdd:cd05943 237 --AAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNWLVSGLAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 348 GASLVLYDGSPLVPTPNVLWDLVDRIGITILGTGAKWLSVLEEKDMKPVETHNLHTLHTILSTGSPLKAQSYEYVYRCIK 427
Cdd:cd05943 315 GATIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 428 SSVLLGSISGGTDIISCFMGQNSSIPVYKGEIQARNLGMAVEAWDEEGKAVWGASGELVCTKPIPCQPTHFWNDENGSKY 507
Cdd:cd05943 395 PDVLLASISGGTDIISCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPVWGEKGELVCTKPFPSMPVGFWNDPDGSRY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 508 RKAYFSKFPGVWAHGDYCRINPKtGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFL 587
Cdd:cd05943 475 RAAYFAKYPGVWAHGDWIEITPR-GGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFV 553
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21313520 588 KMASGHTFQPDLVKRIRDAIRLGLSARHVPSLILETRGIPYTLNGKKVEVAVKQVMAGRTVEHRGAFSNPETLDLY 663
Cdd:cd05943 554 KLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGRPVKNAGALANPESLDLF 629
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
16-671 |
0e+00 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 932.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 16 QVMWEPDS--KKDTQMDRFRAAVGTACGLALGNYNDLYHWSVRSYMDFWAEFWKFSGIVYSRMYDEVVDTskgiADVP-- 91
Cdd:PRK03584 3 DPLWTPSAerIAASRMTAFIRWLAARRGLSFDDYAALWRWSVEDLEAFWQSVWDFFGVIGSTPYTVVLAG----RRMPga 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 92 EWFRGSRLNYAENLLRHKENDRVALYVAREGREEiVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAML 171
Cdd:PRK03584 79 RWFPGARLNYAENLLRHRRDDRPAIIFRGEDGPR-RELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAML 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 172 AAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEAVVYNGKEHGHLEKLQRVVKGLPDLQRVVLIPYVlpREKIDIS 251
Cdd:PRK03584 158 ATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDRRAKVAELRAALPSLEHVVVVPYL--GPAAAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 252 KIPNSVFLDDFLASgtgAQAPQLEFEQLPFSHPLFIMFSSGTTGAPKCMVHSAGGTLIQHLKEHMLHGNMTSSDILLYYT 331
Cdd:PRK03584 236 ALPGALLWEDFLAP---AEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDRFFWYT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 332 TVGWMMWNWMVSALATGASLVLYDGSPLVPTPNVLWDLVDRIGITILGTGAKWLSVLEEKDMKPVETHNLHTLHTILSTG 411
Cdd:PRK03584 313 TCGWMMWNWLVSGLLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 412 SPLKAQSYEYVYRCIKSSVLLGSISGGTDIISCFMGQNSSIPVYKGEIQARNLGMAVEAWDEEGKAVWGASGELVCTKPI 491
Cdd:PRK03584 393 SPLPPEGFDWVYEHVKADVWLASISGGTDICSCFVGGNPLLPVYRGEIQCRGLGMAVEAWDEDGRPVVGEVGELVCTKPF 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 492 PCQPTHFWNDENGSKYRKAYFSKFPGVWAHGDYCRINPkTGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLC 571
Cdd:PRK03584 473 PSMPLGFWNDPDGSRYRDAYFDTFPGVWRHGDWIEITE-HGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLV 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 572 VPQYNRDGEERVVLFLKMASGHTFQPDLVKRIRDAIRLGLSARHVPSLILETRGIPYTLNGKKVEVAVKQVMAGRTVEH- 650
Cdd:PRK03584 552 IGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVELPVKKLLHGRPVKKa 631
|
650 660
....*....|....*....|...
gi 21313520 651 --RGAFSNPETLDLYRDIPELQD 671
Cdd:PRK03584 632 vnRDALANPEALDWFADLAELRA 654
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
92-665 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 572.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 92 EWFRGSRLNYAENLL-RHKE--NDRVALYVAREGREEiVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVE 168
Cdd:COG0365 1 RWFVGGRLNIAYNCLdRHAEgrGDKVALIWEGEDGEE-RTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 169 AMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEAVVYNGKEHGHLEKLQRVVKGLPDLQRVVlipyVLPREKI 248
Cdd:COG0365 80 AMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSLEHVI----VVGRTGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 249 DISkIPNSVFLDDFLAsgtgAQAPQLEFEQLPFSHPLFIMFSSGTTGAPKCMVHSAGGTLIQHLKEHMLHGNMTSSDILL 328
Cdd:COG0365 156 DVP-MEGDLDWDELLA----AASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 329 YYTTVGWMM--WNWMVSALATGASLVLYDGSPLVPTPNVLWDLVDRIGITILGTGAKWLSVLEEKDMKPVETHNLHTLHT 406
Cdd:COG0365 231 CTADIGWATghSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 407 ILSTGSPLKAQSYEYVYRCIKssVLLGSISGGTDIISCFMGQNSSIPVYKGEIQARNLGMAVEAWDEEGKAV-WGASGEL 485
Cdd:COG0365 311 LGSAGEPLNPEVWEWWYEAVG--VPIVDGWGQTETGGIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVpPGEEGEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 486 VCTKPIPCQPTHFWNDEngSKYRKAYFSKFPGVWAHGDYCRINPKtGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDE 565
Cdd:COG0365 389 VIKGPWPGMFRGYWNDP--ERYRETYFGRFPGWYRTGDGARRDED-GYFWILGRSDDVINVSGHRIGTAEIESALVSHPA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 566 VEDSLCVPQYNRDGEERVVLFLKMASGHTFQPDLVKRIRDAIRLGLSARHVPSLILETRGIPYTLNGKKVEVAVKQVMAG 645
Cdd:COG0365 466 VAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEG 545
|
570 580
....*....|....*....|
gi 21313520 646 RTVEHRGAFSNPETLDLYRD 665
Cdd:COG0365 546 RPLGDTSTLEDPEALDEIKE 565
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
42-657 |
1.61e-94 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 304.41 E-value: 1.61e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 42 LALGNYNDLYHWSVRSYMDFWAEFWKFSGIVYSRMYDEVVDTSKGIaDVPEWFRGSRLNYAENLL-RHKENDRVALYVAR 120
Cdd:cd05968 4 LGIPDLEAFLERSAEDNAWFWGEFVKDVGIEWYEPPYQTLDLSGGK-PWAAWFVGGRMNIVEQLLdKWLADTRTRPALRW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 121 EGREEIVK-VTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQI 199
Cdd:cd05968 83 EGEDGTSRtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 200 QPKLIFSVEAVVYNGKEHGHLEKLQRVVKGLPDLQRVVlipyVLPREKIDISKIP-NSVFLDDFLASgtgaqaPQLEFEQ 278
Cdd:cd05968 163 EAKALITADGFTRRGREVNLKEEADKACAQCPTVEKVV----VVRHLGNDFTPAKgRDLSYDEEKET------AGDGAER 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 279 LPFSHPLFIMFSSGTTGAPKCMVHSAGGTLIQHLKEHMLHGNMTSSDILLYYTTVGWMMWNWMV-SALATGASLVLYDGS 357
Cdd:cd05968 233 TESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIfGGLILGATMVLYDGA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 358 PLVPTPNVLWDLVDRIGITILGTGAKWLSVLEEKDMKPVETHNLHTLHTILSTGSPLKAQSYEYVYRCI-KSSVLLGSIS 436
Cdd:cd05968 313 PDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVgKGRNPIINYS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 437 GGTDIISCFMGQNSSIPVYKGEIQARNLGMAVEAWDEEGKAVWGASGELVCTKPIPCQPTHFWNDENgsKYRKAYFSKFP 516
Cdd:cd05968 393 GGTEISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARPEVGELVLLAPWPGMTRGFWRDED--RYLETYWSRFD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 517 GVWAHGDYCRINPKtGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMASGHTFQ 596
Cdd:cd05968 471 NVWVHGDFAYYDEE-GYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPT 549
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21313520 597 PDLVKRIRDAIRLGLSARHVPSLILETRGIPYTLNGKKVEVAVKQVMAGRTVEHRGAFSNP 657
Cdd:cd05968 550 EALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKELGDLSSLENP 610
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
47-633 |
5.02e-78 |
|
acetate-CoA ligase; This family 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: 341289 [Multi-domain] Cd Length: 587 Bit Score: 260.20 E-value: 5.02e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 47 YNDLYHWSVRSYMDFWAEFWKFSGIVYSRMYDEVVDTSKGiADVPEWFRGSRLNYAENLL-RHKEN--DRVALYVAREGR 123
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQKVKNTSFAPG-APSIKWFEDATLNLAANALdRHLREngDRTAIIYEGDDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 124 EEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKL 203
Cdd:cd17634 80 SQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 204 IFSVEAvvynGKEHGHLEKLQRVVKGLPDLQ----RVVLipyVLPREKIDISKIPNSVF-LDDFLAsgtgAQAPQLEFEQ 278
Cdd:cd17634 160 LITADG----GVRAGRSVPLKKNVDDALNPNvtsvEHVI---VLKRTGSDIDWQEGRDLwWRDLIA----KASPEHQPEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 279 LPFSHPLFIMFSSGTTGAPKCMVHSAGGTLIqHLKEHMLHG-NMTSSDILLYYTTVGWMMWN-WMV-SALATGASLVLYD 355
Cdd:cd17634 229 MNAEDPLFILYTSGTTGKPKGVLHTTGGYLV-YAATTMKYVfDYGPGDIYWCTADVGWVTGHsYLLyGPLACGATTLLYE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 356 GSPLVPTPNVLWDLVDRIGITILGTGAKWLSVLEEKDMKPVETHNLHTLHTILSTGSPLKAQSYEYVYRCI-KSSVLLGS 434
Cdd:cd17634 308 GVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIgKEKCPVVD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 435 ISGGTDiISCFMGQN--SSIPVYKGEIQARNLGMAVEAWDEEGKAV-WGASGELVCTKPIPCQPTHFWNDENgsKYRKAY 511
Cdd:cd17634 388 TWWQTE-TGGFMITPlpGAIELKAGSATRPVFGVQPAVVDNEGHPQpGGTEGNLVITDPWPGQTRTLFGDHE--RFEQTY 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 512 FSKFPGVWAHGDYCRINpKTGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMAS 591
Cdd:cd17634 465 FSTFKGMYFSGDGARRD-EDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNH 543
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 21313520 592 GHTFQPDLVKRIRDAIRLGLSARHVPSLILETRGIPYTLNGK 633
Cdd:cd17634 544 GVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGK 585
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
47-633 |
1.77e-70 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) 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 widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 240.54 E-value: 1.77e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 47 YNDLYHWSVRSYMDFWAEfwKFSGIVYSRMYDEVVDTSKGIADVpEWFRGSRLNYAENLL-RHKEN--DRVALYVAREGR 123
Cdd:cd05966 3 YKELYKQSIEDPEEFWGE--IAKELDWFKPWDKVLDWSKGPPFI-KWFEGGKLNISYNCLdRHLKErgDKVAIIWEGDEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 124 EEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKL 203
Cdd:cd05966 80 DQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 204 IFSVEAVVYNGKEHGHLEKLQRVVKGLPDLQRVVlipyVLPREKIDISKIPN-SVFLDDFLASgtgaQAPQLEFEQLPFS 282
Cdd:cd05966 160 VITADGGYRGGKVIPLKEIVDEALEKCPSVEKVL----VVKRTGGEVPMTEGrDLWWHDLMAK----QSPECEPEWMDSE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 283 HPLFIMFSSGTTGAPKCMVHSAGGtliqhlkeHMLHGNMTS--------SDIllYYTT--VGWMM-WNWMVSA-LATGAS 350
Cdd:cd05966 232 DPLFILYTSGSTGKPKGVVHTTGG--------YLLYAATTFkyvfdyhpDDI--YWCTadIGWITgHSYIVYGpLANGAT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 351 LVLYDGSPLVPTPNVLWDLVDRIGITILGTGAKWLSVLEEKDMKPVETHNLHTLHTILSTGSPLKAQSYEYVYRCI---K 427
Cdd:cd05966 302 TVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIgkeR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 428 SSVL-------LGSIsggtdIISCFMGqnsSIPVYKGEIQARNLGMAVEAWDEEGKAVWG-ASGELVCTKPIPCQPTHFW 499
Cdd:cd05966 382 CPIVdtwwqteTGGI-----MITPLPG---ATPLKPGSATRPFFGIEPAILDEEGNEVEGeVEGYLVIKRPWPGMARTIY 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 500 NDEngSKYRKAYFSKFPGVWAHGDYCRINpKTGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDG 579
Cdd:cd05966 454 GDH--ERYEDTYFSKFPGYYFTGDGARRD-EDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIK 530
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 21313520 580 EERVVLFLKMASGHTFQPDLVKRIRDAIRLGLSARHVPSLILETRGIPYTLNGK 633
Cdd:cd05966 531 GEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGK 584
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
47-556 |
4.63e-48 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 179.18 E-value: 4.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 47 YNDLYHWSVRSYMDFWAEFWKfsGIVYSRMYDEVVDTSKGIAdvpEWFRGSRLNYAENLL-RHKEN--DRVALYVAREGR 123
Cdd:PRK00174 19 YKALYQESVEDPEGFWAEQAK--RLDWFKPFDTVLDWNAPFI---KWFEDGELNVSYNCLdRHLKTrgDKVAIIWEGDDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 124 EEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKL 203
Cdd:PRK00174 94 GDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 204 IFSVEAVVYNGKEHghleKLQRVV----KGLPDLQRVVlipyVLPREKIDISKIPN-SVFLDDFLASgtgaQAPQLEFEQ 278
Cdd:PRK00174 174 VITADEGVRGGKPI----PLKANVdealANCPSVEKVI----VVRRTGGDVDWVEGrDLWWHELVAG----ASDECEPEP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 279 LPFSHPLFIMFSSGTTGAPKCMVHSAGGtliqhlkeHMLHGNMT--------SSDIllYYTT--VGWmmwnwmVSA---- 344
Cdd:PRK00174 242 MDAEDPLFILYTSGSTGKPKGVLHTTGG--------YLVYAAMTmkyvfdykDGDV--YWCTadVGW------VTGhsyi 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 345 ----LATGASLVLYDGSPLVPTPNVLWDLVDRIGITILGTGAKWLSVLeekdMK----PVETHNLHTLHTILSTGSPLKA 416
Cdd:PRK00174 306 vygpLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRAL----MKegdeHPKKYDLSSLRLLGSVGEPINP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 417 QSYEYVYRCIKSS---------------VLLGSISGGTDII--SC---FMGqnssipvykgeIQArnlgmavEAWDEEGK 476
Cdd:PRK00174 382 EAWEWYYKVVGGErcpivdtwwqtetggIMITPLPGATPLKpgSAtrpLPG-----------IQP-------AVVDEEGN 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 477 AVWGA-SGELVCTKPIPCQPTHFWNDENgsKYRKAYFSKFPGVWAHGDYCRINpKTGGIIMLGRSDGTLNPNGVRFGSSE 555
Cdd:PRK00174 444 PLEGGeGGNLVIKDPWPGMMRTIYGDHE--RFVKTYFSTFKGMYFTGDGARRD-EDGYYWITGRVDDVLNVSGHRLGTAE 520
|
.
gi 21313520 556 I 556
Cdd:PRK00174 521 I 521
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
47-661 |
6.67e-48 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 178.28 E-value: 6.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 47 YNDLYHWSVRSYMDFWAEFWKfsGIVYSRMYDEVVDTSKgiADVPEWFRGSRLNYAENLL-RHKEN---DRVAL-YVARE 121
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQAR--LIDWFKPPEKILDNSN--PPFTRWFVGGRLNTCYNALdRHVEAgrgDQIALiYDSPV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 122 gREEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQP 201
Cdd:cd05967 77 -TGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 202 KLIFSVEAvvynGKEHGhleklqRVVKGLPDLQRVVLI-----PYVLPREKIDISKIPNSVfLDDFLASGTGAQAPQLEF 276
Cdd:cd05967 156 KLIVTASC----GIEPG------KVVPYKPLLDKALELsghkpHHVLVLNRPQVPADLTKP-GRDLDWSELLAKAEPVDC 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 277 EQLPFSHPLFIMFSSGTTGAPKCMVHSAGGTLIQhLKEHMLH-GNMTSSDILLYYTTVGWMM-WNWMVSA-LATGASLVL 353
Cdd:cd05967 225 VPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVA-LNWSMRNiYGIKPGDVWWAASDVGWVVgHSYIVYGpLLHGATTVL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 354 YDGSPL-VPTPNVLWDLVDRIGITILGTGAKWLSVL--EEKDMKPVETHNLHTLHTILSTGSPLKAQSYEYVYRCIKSSV 430
Cdd:cd05967 304 YEGKPVgTPDPGAFWRVIEKYQVNALFTAPTAIRAIrkEDPDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 431 L--LGSISGGTDIISCFMGQnSSIPVYKGEIQARNLGMAVEAWDEEGKAVW-GASGELVCTKPIP--CQPTHFWNDEngs 505
Cdd:cd05967 384 IdhWWQTETGWPITANPVGL-EPLPIKAGSPGKPVPGYQVQVLDEDGEPVGpNELGNIVIKLPLPpgCLLTLWKNDE--- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 506 KYRKAYFSKFPGVWAHGDYCRINpKTGGIIMLGRSDGTLNPNGVRFGSSEIY-------NIVE-AFDEVEDSLcvpqynr 577
Cdd:cd05967 460 RFKKLYLSKFPGYYDTGDAGYKD-EDGYLFIMGRTDDVINVAGHRLSTGEMEesvlshpAVAEcAVVGVRDEL------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 578 DGEERVVLFLKMASG----HTFQPDLVKRIRDAIrlGLSARhvPSLILETRGIPYTLNGKKVEVAVKQVMAGRTVEHRGA 653
Cdd:cd05967 532 KGQVPLGLVVLKEGVkitaEELEKELVALVREQI--GPVAA--FRLVIFVKRLPKTRSGKILRRTLRKIADGEDYTIPST 607
|
....*...
gi 21313520 654 FSNPETLD 661
Cdd:cd05967 608 IEDPSVLD 615
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
47-655 |
9.32e-44 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 167.38 E-value: 9.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 47 YNDLYHWSVRSYMDFWAE-----FWKfSGIVYSRMYDEVVDTSKGIADVpEWFRGSRLNYAENLL-RHKEN---DRVALY 117
Cdd:PLN02654 32 YMEMYKRSVDDPAGFWSDiasqfYWK-QKWEGDEVCSENLDVRKGPISI-EWFKGGKTNICYNCLdRNVEAgngDKIAIY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 118 vaREGREEIV--KVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDR 195
Cdd:PLN02654 110 --WEGNEPGFdaSLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 196 FSQIQPKLIFSVEAVvyngKEHGHLEKLQRVVKGLPD--LQRVVLIPYVLPREKIDISKIPNS-------VFLDDFLASg 266
Cdd:PLN02654 188 IVDCKPKVVITCNAV----KRGPKTINLKDIVDAALDesAKNGVSVGICLTYENQLAMKREDTkwqegrdVWWQDVVPN- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 267 tgaQAPQLEFEQLPFSHPLFIMFSSGTTGAPKCMVHSAGGTLIQHLKEHMLHGNMTSSDILLYYTTVGWMMWNWMVS--A 344
Cdd:PLN02654 263 ---YPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTygP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 345 LATGASLVLYDGSPLVPTPNVLWDLVDRIGITILGTGAKWLSVLEEKDMKPVETHNLHTLHTILSTGSPLKAQSYEYVY- 423
Cdd:PLN02654 340 MLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFn 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 424 -----RCIKSSVLLGSISGGTdIISCFMGqnsSIPVYKGEIQARNLGMAVEAWDEEGKAVWG-ASGELVCTKPIPCQPTH 497
Cdd:PLN02654 420 vvgdsRCPISDTWWQTETGGF-MITPLPG---AWPQKPGSATFPFFGVQPVIVDEKGKEIEGeCSGYLCVKKSWPGAFRT 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 498 FWNDEngSKYRKAYFSKFPGVWAHGDYCRINpKTGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNR 577
Cdd:PLN02654 496 LYGDH--ERYETTYFKPFAGYYFSGDGCSRD-KDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHE 572
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21313520 578 DGEERVVLFLKMASGHTFQPDLVKRIRDAIRLGLSARHVPSLILETRGIPYTLNGKKVEVAVKQVmAGRTVEHRGAFS 655
Cdd:PLN02654 573 VKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI-ASRQLDELGDTS 649
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
46-665 |
7.26e-37 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 146.25 E-value: 7.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 46 NYNDLYHWSVRSYMDFWAEFWKFsgIVYSRMYDEVVDTSKgiadvP---EWFRGSRLNYAENLL-RH--KENDRVAL-YV 118
Cdd:PRK10524 3 SYSEFYQRSIDDPEAFWAEQARR--IDWQTPFTQVLDYSN-----PpfaRWFVGGRTNLCHNAVdRHlaKRPEQLALiAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 119 AREGREEIVkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQ 198
Cdd:PRK10524 76 STETDEERT-YTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 199 IQPKLIFSVEAVVYNGKehghleklqrvvkglpdlqrvvLIPYV-LPREKIDISKI-PNSVFL-DDFLASGT-------- 267
Cdd:PRK10524 155 AKPVLIVSADAGSRGGK----------------------VVPYKpLLDEAIALAQHkPRHVLLvDRGLAPMArvagrdvd 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 268 ---------GAQAPqleFEQLPFSHPLFIMFSSGTTGAPKCMVHSAGG---TLIQHLKeHMLHGN-----MTSSDIllyy 330
Cdd:PRK10524 213 yatlraqhlGARVP---VEWLESNEPSYILYTSGTTGKPKGVQRDTGGyavALATSMD-TIFGGKagetfFCASDI---- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 331 ttvGWMM-WNWMVSA-LATGASLVLYDGSPLVPTPNVLWDLVDRIGITILGTGAKWLSVLEEKDMKPVETHNLHTLHTIL 408
Cdd:PRK10524 285 ---GWVVgHSYIVYApLLAGMATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALF 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 409 STGSPLKAQSYEYVYRCIKSSVL-----------LGSISGGTDIISCFMGqNSSIPVYKGEIQARNlgmavEAWDEEGKA 477
Cdd:PRK10524 362 LAGEPLDEPTASWISEALGVPVIdnywqtetgwpILAIARGVEDRPTRLG-SPGVPMYGYNVKLLN-----EVTGEPCGP 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 478 vwGASGELVCTKPIP--CQPThFWNDEngSKYRKAYFSKF-PGVWAHGDYCrINPKTGGIIMLGRSDGTLNPNGVRFGSS 554
Cdd:PRK10524 436 --NEKGVLVIEGPLPpgCMQT-VWGDD--DRFVKTYWSLFgRQVYSTFDWG-IRDADGYYFILGRTDDVINVAGHRLGTR 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 555 EIY-------NIVE-AFDEVEDSL--------CVPQYNRDGEERvvlflkmASGHTFQPDLVKRIRDaiRLGLSARhvPS 618
Cdd:PRK10524 510 EIEesisshpAVAEvAVVGVKDALkgqvavafVVPKDSDSLADR-------EARLALEKEIMALVDS--QLGAVAR--PA 578
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 21313520 619 LILETRGIPYTLNGKKVEVAVKQVMAGR------TVEhrgafsNPETLDLYRD 665
Cdd:PRK10524 579 RVWFVSALPKTRSGKLLRRAIQAIAEGRdpgdltTIE------DPAALQQIRQ 625
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
46-548 |
3.59e-33 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 135.64 E-value: 3.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 46 NYNDLYHWSVRSYMDFWAEFWKfSGIVYSRMYDEVVdTSKGIadVPEWFRGSRLNYAENLL-RHKEN----DRVALYVAR 120
Cdd:PTZ00237 9 DYENDSNYANSNPESFWDEVAK-KYVHWDKMYDKVY-SGDEI--YPDWFKGGELNTCYNVLdIHVKNplkrDQDALIYEC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 121 EGREEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQ 200
Cdd:PTZ00237 85 PYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETIT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 201 PKLIFSVEAVVYNgkehghleklQRVVKGLPDLQRVVLIPYVLPREKI-----------------DISKIPNSVFLDDFL 263
Cdd:PTZ00237 165 PKLIITTNYGILN----------DEIITFTPNLKEAIELSTFKPSNVItlfrnditsesdlkkieTIPTIPNTLSWYDEI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 264 AS-GTGAQAPQLEFEQLPFSHPLFIMFSSGTTGAPKCMVHSAGGTL--IQHLKEHMLHGNMTSsdILLYYTTVGWMMW-N 339
Cdd:PTZ00237 235 KKiKENNQSPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLvgLKYYWRSIIEKDIPT--VVFSHSSIGWVSFhG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 340 WMVSALATGASLVLYDGSPLVPT--PNVLWDLVDRIGITILGTGAKWLSVLEEKDMKPVETH---NLHTLHTILSTGSPL 414
Cdd:PTZ00237 313 FLYGSLSLGNTFVMFEGGIIKNKhiEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRskyDLSNLKEIWCGGEVI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 415 KAQSYEYVYRCIK--SSVLLGSISGGTDIISCFmgQNSSIPVYKGEIQARNLGMAVeaWDEEGKAV-WGASGELVCTKPI 491
Cdd:PTZ00237 393 EESIPEYIENKLKikSSRGYGQTEIGITYLYCY--GHINIPYNATGVPSIFIKPSI--LSEDGKELnVNEIGEVAFKLPM 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21313520 492 PcqP----THFWNDEngsKYRKaYFSKFPGVWAHGDYCRINpKTGGIIMLGRSDGTLNPNG 548
Cdd:PTZ00237 469 P--PsfatTFYKNDE---KFKQ-LFSKFPGYYNSGDLGFKD-ENGYYTIVSRSDDQIKISG 522
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
112-414 |
1.17e-32 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 130.90 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALYVAregreEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNG 191
Cdd:pfam00501 10 DKTALEVG-----EGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 VLDRFSQIQPKLIFSVEAvvyngkehghlEKLQRVVKGLPDLQRVVLIPyvlprekidISKIPNSVFLDDFLASGTGAQA 271
Cdd:pfam00501 85 LAYILEDSGAKVLITDDA-----------LKLEELLEALGKLEVVKLVL---------VLDRDPVLKEEPLPEEAKPADV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 272 PQLEFEQLPFSHPLFIMFSSGTTGAPKCMVHSAGG---TLIQHLKEHMLHGNMTSSDILLYYTTVGWMM-WNWMV-SALA 346
Cdd:pfam00501 145 PPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNlvaNVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFgLSLGLlGPLL 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21313520 347 TGASLVLYDGSPLvPTPNVLWDLVDRIGITIL-GTGAKWLSVLEEKDMKPVEthnLHTLHTILSTGSPL 414
Cdd:pfam00501 225 AGATVVLPPGFPA-LDPAALLELIERYKVTVLyGVPTLLNMLLEAGAPKRAL---LSSLRLVLSGGAPL 289
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
46-603 |
1.40e-32 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 134.05 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 46 NYNDLYHWSVRSYMDFWAEFWKFSGIVYSRMYDEVVDTSKGIADVPEWFRGSRLNYAENLL---RHKENDRVALYVAREG 122
Cdd:PLN03052 121 SFSEFQRFSVENPEVYWSIVLDELSLVFSVPPRCILDTSDESNPGGQWLPGAVLNVAECCLtpkPSKTDDSIAIIWRDEG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 123 REE--IVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQ 200
Cdd:PLN03052 201 SDDlpVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISK 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 201 PKLIFSVEAVVYNGKEhghLEKLQRVVKGLPdlQRVVLIP------YVLPREKiDISkipnsvfLDDFLASGTGAQAPQl 274
Cdd:PLN03052 281 AKAIFTQDVIVRGGKS---IPLYSRVVEAKA--PKAIVLPadgksvRVKLREG-DMS-------WDDFLARANGLRRPD- 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 275 EFE--QLPFSHPLFIMFSSGTTGAPKCM--VHSaggTLIQHLKEHMLHGNMTSSDILLYYTTVGWMMWNWMV-SALATGA 349
Cdd:PLN03052 347 EYKavEQPVEAFTNILFSSGTTGEPKAIpwTQL---TPLRAAADAWAHLDIRKGDIVCWPTNLGWMMGPWLVyASLLNGA 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 350 SLVLYDGSPLVPTpnvLWDLVDRIGITILGT----GAKWlsvleeKDMKPVETHNLHTLHTILSTGSP--------LKAQ 417
Cdd:PLN03052 424 TLALYNGSPLGRG---FAKFVQDAKVTMLGTvpsiVKTW------KNTNCMAGLDWSSIRCFGSTGEAssvddylwLMSR 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 418 -SYEYVYRCikssvllgsiSGGTDIISCFMGQNSSIPVYKGEIQARNLGMAVEAWDEEGKAVwgaSGELVCTKPIPCQPT 496
Cdd:PLN03052 495 aGYKPIIEY----------CGGTELGGGFVTGSLLQPQAFAAFSTPAMGCKLFILDDSGNPY---PDDAPCTGELALFPL 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 497 HFWNDE---NGSKYrKAYFSKFPgVWA------HGDycrINPKTGG--IIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDE 565
Cdd:PLN03052 562 MFGASStllNADHY-KVYFKGMP-VFNgkilrrHGD---IFERTSGgyYRAHGRADDTMNLGGIKVSSVEIERVCNAADE 636
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 21313520 566 --VED-SLCVPQYNrDGEERVVLF--LKMASGHTFQPDLVKRI 603
Cdd:PLN03052 637 svLETaAIGVPPPG-GGPEQLVIAavLKDPPGSNPDLNELKKI 678
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
112-633 |
1.77e-31 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 128.00 E-value: 1.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALYvaREGREeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNG 191
Cdd:COG0318 14 DRPALV--FGGRR----LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 VLDRFSQIQPKLIFSVeavvyngkehghleklqrvvkglpdlqrvvlipyvlprekidiskipnsvflddflasgtgaqa 271
Cdd:COG0318 88 LAYILEDSGARALVTA---------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 272 pqlefeqlpfshplFIMFSSGTTGAPKCMVHSAGGtLIQHLKEHMLHGNMTSSDILL-----YYTTvGWMMwnWMVSALA 346
Cdd:COG0318 104 --------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLvalplFHVF-GLTV--GLLAPLL 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 347 TGASLVLYDGsplvPTPNVLWDLVDRIGITIL-GTGAKWLSVLEEKDmkpVETHNLHTLHTILSTGSPLKAQSYEYVYRC 425
Cdd:COG0318 166 AGATLVLLPR----FDPERVLELIERERVTVLfGVPTMLARLLRHPE---FARYDLSSLRLVVSGGAPLPPELLERFEER 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 426 IkssvllgsisgGTDIISCF-----MGQNSSIPVYKGEIQARNLGMA---VEAW--DEEGKAV-WGASGELvCTKPiPCQ 494
Cdd:COG0318 239 F-----------GVRIVEGYgltetSPVVTVNPEDPGERRPGSVGRPlpgVEVRivDEDGRELpPGEVGEI-VVRG-PNV 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 495 PTHFWNDENGSKyrkayfSKFPGVWAH-GDYCRINPkTGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVP 573
Cdd:COG0318 306 MKGYWNDPEATA------EAFRDGWLRtGDLGRLDE-DGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVG 378
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 574 QYNRDGEERVVLFLKMASGHTFQPDlvkRIRDAIRLGLSARHVPSLILETRGIPYTLNGK 633
Cdd:COG0318 379 VPDEKWGERVVAFVVLRPGAELDAE---ELRAFLRERLARYKVPRRVEFVDELPRTASGK 435
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
283-633 |
1.01e-26 |
|
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: 111.61 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 283 HPLFIMFSSGTTGAPKCMVHSAGGtLIQHLKEHMLHGNMTSSDILLYYTTVGWM-MWNWMVSALATGASLVLYDGSPlvp 361
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRN-LLAAAAALAASGGLTEGDVFLSTLPLFHIgGLFGLLGALLAGGTVVLLPKFD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 362 tPNVLWDLVDRIGITILG---TGAKWLSVLEEKDmkpveTHNLHTLHTILSTGSPLKAQSYEYVYRCIKssVLLGSISGG 438
Cdd:cd04433 77 -PEAALELIEREKVTILLgvpTLLARLLKAPESA-----GYDLSSLRALVSGGAPLPPELLERFEEAPG--IKLVNGYGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 439 TDIISCFmgqnSSIPVYKGEIQARNLG-----MAVEAWDEEGKAVW-GASGELVCTKPIPcqPTHFWNDEngskyRKAYF 512
Cdd:cd04433 149 TETGGTV----ATGPPDDDARKPGSVGrpvpgVEVRIVDPDGGELPpGEIGELVVRGPSV--MKGYWNNP-----EATAA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 513 SKFPGVWAHGDYCRINPKtGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMASG 592
Cdd:cd04433 218 VDEDGWYRTGDLGRLDED-GYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPG 296
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 21313520 593 HTFQPDlvkRIRDAIRLGLSARHVPSLILETRGIPYTLNGK 633
Cdd:cd04433 297 ADLDAE---ELRAHVRERLAPYKVPRRVVFVDALPRTASGK 334
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
127-420 |
6.04e-25 |
|
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: 108.84 E-value: 6.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 127 VKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFS 206
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 207 veavvyngkEHGHLEKLQRVVKGLPDLQRVVLIPyVLPREKIDISKIPNSVFLDDFlasgtgaqAPQLEFEQLPFSHPLF 286
Cdd:cd05911 89 ---------DPDGLEKVKEAAKELGPKDKIIVLD-DKPDGVLSIEDLLSPTLGEED--------EDLPPPLKDGKDDTAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 287 IMFSSGTTGAPK--CMVHSaggTLIQHLK--EHMLHGNMTSSDILLYYTTVGWMM-WNWMVSALATGASLVLYDGsplvP 361
Cdd:cd05911 151 ILYSSGTTGLPKgvCLSHR---NLIANLSqvQTFLYGNDGSNDVILGFLPLYHIYgLFTTLASLLNGATVIIMPK----F 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 362 TPNVLWDLVDRIGITILGTgAKWLSVLEEKDmkP-VETHNLHTLHTILSTGSPLKAQSYE 420
Cdd:cd05911 224 DSELFLDLIEKYKITFLYL-VPPIAAALAKS--PlLDKYDLSSLRVILSGGAPLSKELQE 280
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
160-633 |
3.31e-23 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 103.74 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 160 LPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEAVVYNGKEhghLEKLQRVVKGLPdlQRVVLI 239
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRA---LPLYSKVVEAAP--AKAIVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 240 PYVlpREKIDISKIPNSVFLDDFLASGTGA-QAPQLEFEQ--LPFSHPLFIMFSSGTTGAPKCM--VHSaggTLIQHLKE 314
Cdd:PLN03051 76 PAA--GEPVAVPLREQDLSWCDFLGVAAAQgSVGGNEYSPvyAPVESVTNILFSSGTTGEPKAIpwTHL---SPLRCASD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 315 HMLHGNMTSSDILLYYTTVGWMMWNW-MVSALATGASLVLYDGSPLVPTpnvLWDLVDRIGITILGTGAKWLSVLEEKDM 393
Cdd:PLN03051 151 GWAHMDIQPGDVVCWPTNLGWMMGPWlLYSAFLNGATLALYGGAPLGRG---FGKFVQDAGVTVLGLVPSIVKAWRHTGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 394 KPVETHNLHTLHTILSTGSPLKAQSYEY--VYRCIKSSVLlgSISGGTDIISCFMGQNSSIPVYKGEIQARNLGMAVEAW 471
Cdd:PLN03051 228 FAMEGLDWSKLRVFASTGEASAVDDVLWlsSVRGYYKPVI--EYCGGTELASGYISSTLLQPQAPGAFSTASLGTRFVLL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 472 DEEGKAV---WGASGELVCTKPIPCQPTHFWNDENGSKYRKA---YFSKFPGVWAHGDYCRINPkTGGIIMLGRSDGTLN 545
Cdd:PLN03051 306 NDNGVPYpddQPCVGEVALAPPMLGASDRLLNADHDKVYYKGmpmYGSKGMPLRRHGDIMKRTP-GGYFCVQGRADDTMN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 546 PNGVRFGSSEIYNIVEAFDE--VED-SLCVPQYNrDGEERVVLFLKMAS-GHTFQ----PDLVKRIRDAIRLGLSARHVP 617
Cdd:PLN03051 385 LGGIKTSSVEIERACDRAVAgiAETaAVGVAPPD-GGPELLVIFLVLGEeKKGFDqarpEALQKKFQEAIQTNLNPLFKV 463
|
490
....*....|....*.
gi 21313520 618 SLILETRGIPYTLNGK 633
Cdd:PLN03051 464 SRVKIVPELPRNASNK 479
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
130-640 |
1.19e-20 |
|
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: 95.26 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 130 TFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEA 209
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 210 VvyngkehghleklqrvvkglpdlqrvvlipyvlpREKIDISKipnsvflddflasgtgaqapqlefeqlpfshPLFIMF 289
Cdd:cd05969 82 L----------------------------------YERTDPED-------------------------------PTLLHY 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 290 SSGTTGAPKCMVHSAgGTLIQHLKEHMLHGNMTSSDILLYYTTVGWM--MWNWMVSALATGASLVLYDGSplvPTPNVLW 367
Cdd:cd05969 97 TSGTTGTPKGVLHVH-DAMIFYYFTGKYVLDLHPDDIYWCTADPGWVtgTVYGIWAPWLNGVTNVVYEGR---FDAESWY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 368 DLVDRIGITILGTGAKWLSVLEEKDMKPVETHNLHTLHTILSTGSPLKAQSYEYVYRCIKSSVL--LGSISGGTDIISCF 445
Cdd:cd05969 173 GIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHdtWWQTETGSIMIANY 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 446 MGQnssipvykgEIQARNLGM---AVEAW--DEEGKAVW-GASGELVCTKPIPCQPTHFWNDEngSKYRKAyfskFPGVW 519
Cdd:cd05969 253 PCM---------PIKPGSMGKplpGVKAAvvDENGNELPpGTKGILALKPGWPSMFRGIWNDE--ERYKNS----FIDGW 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 520 -AHGDYCRINpKTGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMASGHTFQPD 598
Cdd:cd05969 318 yLTGDLAYRD-EDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDE 396
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 21313520 599 LVKRIRDAIRLGLSARHVPSLILETRGIPYTLNGKKVEVAVK 640
Cdd:cd05969 397 LKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
92-414 |
4.48e-20 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 94.58 E-value: 4.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 92 EWFRGSRLNYA-ENLLRHKEN---DRVALYVAREGREEivKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAV 167
Cdd:PRK04319 35 SWLETGKVNIAyEAIDRHADGgrkDKVALRYLDASRKE--KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 168 EAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEAVvyngkehghlekLQRVVKG-LPDLQRVVLIpyvlpre 246
Cdd:PRK04319 113 FALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPAL------------LERKPADdLPSLKHVLLV------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 247 KIDISKIPNSVFLDDFLASGtgaqAPQLEFEQLPFSHPLFIMFSSGTTGAPKCMVHsAGGTLIQH---------LKEhml 317
Cdd:PRK04319 174 GEDVEEGPGTLDFNALMEQA----SDEFDIEWTDREDGAILHYTSGSTGKPKGVLH-VHNAMLQHyqtgkyvldLHE--- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 318 hgnmtsSDIllYYTTV--GWM--MWNWMVSALATGASLVLYDGSplvPTPNVLWDLVDRIGITILGTGAKWLSVLEEKDM 393
Cdd:PRK04319 246 ------DDV--YWCTAdpGWVtgTSYGIFAPWLNGATNVIDGGR---FSPERWYRILEDYKVTVWYTAPTAIRMLMGAGD 314
|
330 340
....*....|....*....|.
gi 21313520 394 KPVETHNLHTLHTILSTGSPL 414
Cdd:PRK04319 315 DLVKKYDLSSLRHILSVGEPL 335
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
128-633 |
2.67e-19 |
|
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: 90.95 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 128 KVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSV 207
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 208 EAvvyngkehghleklqrvvkglpdlqrvvlipyvlprekidiskipnsvflDDflasgtgaqapqlefeqlpfshPLFI 287
Cdd:cd05971 86 GS--------------------------------------------------DD----------------------PALI 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 288 MFSSGTTGAPKCMVHsAGGTLIQHLKEHMLHGNMTSSDILLYYTTVGwmmWNWmVSALATGASLVLYDGSPLVP------ 361
Cdd:cd05971 94 IYTSGTTGPPKGALH-AHRVLLGHLPGVQFPFNLFPRDGDLYWTPAD---WAW-IGGLLDVLLPSLYFGVPVLAhrmtkf 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 362 TPNVLWDLVDRIGITilgtgAKWLSVLEEKDMKPVETHNLHT---LHTILSTGSPLKAQSYEYVYRCIKSSVllGSISGG 438
Cdd:cd05971 169 DPKAALDLMSRYGVT-----TAFLPPTALKMMRQQGEQLKHAqvkLRAIATGGESLGEELLGWAREQFGVEV--NEFYGQ 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 439 TDiISCFMGQNSSI-PVYKGEIQARNLGMAVEAWDEEGKAV-WGASGELVCTKPIPCQPTHFWNDENGSKyrkayfSKFP 516
Cdd:cd05971 242 TE-CNLVIGNCSALfPIKPGSMGKPIPGHRVAIVDDNGTPLpPGEVGEIAVELPDPVAFLGYWNNPSATE------KKMA 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 517 GVW-AHGDYCRINpKTGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMASGHTF 595
Cdd:cd05971 315 GDWlLTGDLGRKD-SDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETP 393
|
490 500 510
....*....|....*....|....*....|....*...
gi 21313520 596 QPDLVKRIRDAIRLGLSARHVPSLILETRGIPYTLNGK 633
Cdd:cd05971 394 SDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGK 431
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
112-300 |
3.44e-19 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 91.70 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALYVAREGREeiVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGA----IWSSTSPDf 187
Cdd:COG1022 26 DRVALREKEDGIW--QSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAvtvpIYPTSSAE- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 188 gvngvldrfsQIQ-------PKLIFsVEavvyngkEHGHLEKLQRVVKGLPDLQRVVLIpyvlprEKIDISKIPNSVFLD 260
Cdd:COG1022 103 ----------EVAyilndsgAKVLF-VE-------DQEQLDKLLEVRDELPSLRHIVVL------DPRGLRDDPRLLSLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21313520 261 DFLASGTGAQAPQlEFEQLP----FSHPLFIMFSSGTTGAPK-CM 300
Cdd:COG1022 159 ELLALGREVADPA-ELEARRaavkPDDLATIIYTSGTTGRPKgVM 202
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
112-633 |
1.16e-18 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 89.23 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALyvaregREEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVng 191
Cdd:cd05945 6 DRPAV------VEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 vlDRFSQI----QPKLIFSVEAVVYngkehghleklqrvvkglpdlqrvvlipyvlprekidiskipnsvflddflasgt 267
Cdd:cd05945 78 --ERIREIldaaKPALLIADGDDNA------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 268 gaqapqlefeqlpfshplFIMFSSGTTGAPKCMVHSAGGtlIQHLKEHML-HGNMTSSDILL-------------YYTtv 333
Cdd:cd05945 101 ------------------YIIFTSGSTGRPKGVQISHDN--LVSFTNWMLsDFPLGPGDVFLnqapfsfdlsvmdLYP-- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 334 gwmmwnwmvsALATGASLVLydgsplVP---TPNVLwDLVDRI---GITIlgtgakWLSV-------LEEKDMKPvetHN 400
Cdd:cd05945 159 ----------ALASGATLVP------VPrdaTADPK-QLFRFLaehGITV------WVSTpsfaamcLLSPTFTP---ES 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 401 LHTLHTILSTGSPLKAQSYEYVYRCIKSSVLL---------GSISGgTDIISCFMGQNSSIPVykGEIQArnlGMAVEAW 471
Cdd:cd05945 213 LPSLRHFLFCGEVLPHKTARALQQRFPDARIYntygpteatVAVTY-IEVTPEVLDGYDRLPI--GYAKP---GAKLVIL 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 472 DEEGKAVW-GASGELVCTKPipCQPTHFWNDENgsKYRKAYFsKFPGVWAH--GDYCRINPkTGGIIMLGRSDGTLNPNG 548
Cdd:cd05945 287 DEDGRPVPpGEKGELVISGP--SVSKGYLNNPE--KTAAAFF-PDEGQRAYrtGDLVRLEA-DGLLFYRGRLDFQVKLNG 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 549 VRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMASGHTFQpdLVKRIRDAIRLGLSARHVPSLILETRGIPY 628
Cdd:cd05945 361 YRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAG--LTKAIKAELAERLPPYMIPRRFVYLDELPL 438
|
....*
gi 21313520 629 TLNGK 633
Cdd:cd05945 439 NANGK 443
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
129-633 |
2.29e-18 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 88.16 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 129 VTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKlifsve 208
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAK------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 209 AVVYNgkehghleklqrvvkglpdlqrvvlipyvlprekidiskipnsvfLDDflasgtgaqapqlefeqlpfshPLFIM 288
Cdd:cd05972 75 AIVTD---------------------------------------------AED----------------------PALIY 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 289 FSSGTTGAPKCMVHSAgGTLIQHLKEHMLHGNMTSSDIllYYTTV--GWMMWNW--MVSALATGASLVLYDGSPLvpTPN 364
Cdd:cd05972 88 FTSGTTGLPKGVLHTH-SYPLGHIPTAAYWLGLRPDDI--HWNIAdpGWAKGAWssFFGPWLLGATVFVYEGPRF--DAE 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 365 VLWDLVDRIGITILGTGAKWLSVLEEKDMkpvETHNLHTLHTILSTGSPLKAQSYEYVYRCIKSSVLLGsiSGGTDiISC 444
Cdd:cd05972 163 RILELLERYGVTSFCGPPTAYRMLIKQDL---SSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDG--YGQTE-TGL 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 445 FMGQNSSIPVYKGEIQARNLGMAVEAWDEEGKAVW-GASGELVCTKPIPCQPTHFWNDEngskyrKAYFSKFPGVWAH-G 522
Cdd:cd05972 237 TVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPpGEEGDIAIKLPPPGLFLGYVGDP------EKTEASIRGDYYLtG 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 523 DYCRINPKtGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMASGHTFQPDLVKR 602
Cdd:cd05972 311 DRAYRDED-GYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEE 389
|
490 500 510
....*....|....*....|....*....|.
gi 21313520 603 IRDAIRLGLSARHVPSLILETRGIPYTLNGK 633
Cdd:cd05972 390 LQGHVKKVLAPYKYPREIEFVEELPKTISGK 420
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
113-633 |
3.92e-18 |
|
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: 87.52 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 113 RVALYVAREgreeivKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIwsstspdfgvngv 192
Cdd:cd05919 1 KTAFYAADR------SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAI------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 193 ldrfsqiqpklifsveAVVYNGKEHGhleklQRVVKGLPDLQRVVLIpyvlpREKIDISkipnsvflddflasgtgaqap 272
Cdd:cd05919 62 ----------------AVVINPLLHP-----DDYAYIARDCEARLVV-----TSADDIA--------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 273 qlefeqlpfshplFIMFSSGTTGAPKCMVHS-AGGTLIQHLKEHMLHGnMTSSDIL-----LYYttvGWMMWNWMVSALA 346
Cdd:cd05919 95 -------------YLLYSSGTTGPPKGVMHAhRDPLLFADAMAREALG-LTPGDRVfssakMFF---GYGLGNSLWFPLA 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 347 TGASLVLYDGSplvPTPNVLWDLVDRIGITIL-GTGAKWLSVLEEKDMKPvetHNLHTLHTILSTGSPLKAQSYEYVYRC 425
Cdd:cd05919 158 VGASAVLNPGW---PTAERVLATLARFRPTVLyGVPTFYANLLDSCAGSP---DALRSLRLCVSAGEALPRGLGERWMEH 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 426 IKSSVLLGsiSGGTDIISCFMgqnSSIPvykGEIQARNLGMAVEAW-----DEEGKAVW-GASGELVCTKpiPCQPTHFW 499
Cdd:cd05919 232 FGGPILDG--IGATEVGHIFL---SNRP---GAWRLGSTGRPVPGYeirlvDEEGHTIPpGEEGDLLVRG--PSAAVGYW 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 500 NdeNGSKYRKAyfskFPGVW-AHGD-YCRInpKTGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNR 577
Cdd:cd05919 302 N--NPEKSRAT----FNGGWyRTGDkFCRD--ADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPES 373
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 21313520 578 DGEERVVLFLKMASGHTFQPDLVKRIRDAIRLGLSARHVPSLILETRGIPYTLNGK 633
Cdd:cd05919 374 TGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGK 429
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
128-298 |
6.56e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 87.27 E-value: 6.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 128 KVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFG---VNGVLDRfsqIQPKLI 204
Cdd:PRK07656 30 RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTadeAAYILAR---GDAKAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 205 FSVEAVvyngkehghLEKLQRVVKGLPDLQRVVLIPYVLPREkidisKIPNSVFLDDFLASGTGA-QAPQLEFEQlpfsh 283
Cdd:PRK07656 107 FVLGLF---------LGVDYSATTRLPALEHVVICETEEDDP-----HTEKMKTFTDFLAAGDPAeRAPEVDPDD----- 167
|
170
....*....|....*
gi 21313520 284 PLFIMFSSGTTGAPK 298
Cdd:PRK07656 168 VADILFTSGTTGRPK 182
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
104-414 |
2.01e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 85.62 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 104 NLLRH---KENDRVALYvaREGReeivKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAI- 179
Cdd:PRK06187 10 RILRHgarKHPDKEAVY--FDGR----RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 180 ----WSSTSPDFG--VNGVLDRFsqiqpkLIFSVEavvyngkehghLEKLQRVVKGLPDLQRVVLIPYVLPREkidiSKI 253
Cdd:PRK06187 84 hpinIRLKPEEIAyiLNDAEDRV------VLVDSE-----------FVPLLAAILPQLPTVRTVIVEGDGPAA----PLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 254 PNSVFLDDFLAsgtgAQAPQLEFEQLPFSHPLFIMFSSGTTGAPKCMVHSAgGTLIQHLKEHMLHGNMTSSDILLYYTTV 333
Cdd:PRK06187 143 PEVGEYEELLA----AASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSH-RNLFLHSLAVCAWLKLSRDDVYLVIVPM 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 334 GWMM-WNWMVSALATGASLVL---YDgsplvptPNVLWDLVDRIGITIL-GTGAKWLSVLEEKDMKPvetHNLHTLHTIL 408
Cdd:PRK06187 218 FHVHaWGLPYLALMAGAKQVIprrFD-------PENLLDLIETERVTFFfAVPTIWQMLLKAPRAYF---VDFSSLRLVI 287
|
....*.
gi 21313520 409 STGSPL 414
Cdd:PRK06187 288 YGGAAL 293
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
105-298 |
1.09e-16 |
|
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: 83.44 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 105 LLRHKENDRVALYVAREGREeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTS 184
Cdd:cd05904 13 LFASAHPSRPALIDAATGRA----LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTAN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 185 PDFGVNGVLDRFSQIQPKLIFSVEAVVyngkehghlEKLQRVVkglpdlQRVVLIPyvlprekidiSKIPNSVFLDDFLA 264
Cdd:cd05904 89 PLSTPAEIAKQVKDSGAKLAFTTAELA---------EKLASLA------LPVVLLD----------SAEFDSLSFSDLLF 143
|
170 180 190
....*....|....*....|....*....|....
gi 21313520 265 SGTGAQAPQLEFEQlpfSHPLFIMFSSGTTGAPK 298
Cdd:cd05904 144 EADEAEPPVVVIKQ---DDVAALLYSSGTTGRSK 174
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
130-633 |
1.30e-15 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 79.48 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 130 TFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLifsvea 209
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARL------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 210 VVYNGKEhghleklqrvvkglpdlqrvvlipyvlpREKIDiskipnsvflddflasgtgaqapqlefeqlpfSHPLFIMF 289
Cdd:cd05973 76 VVTDAAN----------------------------RHKLD--------------------------------SDPFVMMF 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 290 SSGTTGAPKCMVH--SAGGTLIQHLKEHMlhgNMTSSDILLYYTTVGWM--MWNWMVSALATGASLVLYDGSPLVPTpnv 365
Cdd:cd05973 96 TSGTTGLPKGVPVplRALAAFGAYLRDAV---DLRPEDSFWNAADPGWAygLYYAITGPLALGHPTILLEGGFSVES--- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 366 LWDLVDRIGITILgTGAKWLSVLEEKDMKPVETHNLHTLHTILSTGSPLKAQSYEYVYRCIksSVLLGSISGGTDiISCF 445
Cdd:cd05973 170 TWRVIERLGVTNL-AGSPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAAL--GVPIHDHYGQTE-LGMV 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 446 MGQNSSI--PVYKGEIQARNLGMAVEAWDEEGKavwgasgelvctKPIPCQPTHFWNDENGSK------YRKAYFSKFPG 517
Cdd:cd05973 246 LANHHALehPVHAGSAGRAMPGWRVAVLDDDGD------------ELGPGEPGRLAIDIANSPlmwfrgYQLPDTPAIDG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 518 VW-AHGDYCRINPKtGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMASGHTFQ 596
Cdd:cd05973 314 GYyLTGDTVEFDPD-GSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGT 392
|
490 500 510
....*....|....*....|....*....|....*..
gi 21313520 597 PDLVKRIRDAIRLGLSARHVPSLILETRGIPYTLNGK 633
Cdd:cd05973 393 PALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGK 429
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
112-414 |
1.55e-14 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 76.92 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVAL-YVAREGR-EEIVKVTFEELRQQVALFAAAMRKMGVKKGDrVVGY-LPNSAHAVEAMLAAASIGAIwsstspdFG 188
Cdd:PRK07529 40 DAPALsFLLDADPlDRPETWTYAELLADVTRTANLLHSLGVGPGD-VVAFlLPNLPETHFALWGGEAAGIA-------NP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 189 VNGVLDRfSQIQPKLIFS-VEAVVYNGKEHGH--LEKLQRVVKGLPDLQRVVLI---PYVLPREKIDIS----KIPNSVF 258
Cdd:PRK07529 112 INPLLEP-EQIAELLRAAgAKVLVTLGPFPGTdiWQKVAEVLAALPELRTVVEVdlaRYLPGPKRLAVPlirrKAHARIL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 259 ldDFLASGTGAQAPQLEFEQLPFSHPLFIMF-SSGTTGAPKCMVHSAGGTLIQHLKEHMLHGNMTSSDIL----LYYttV 333
Cdd:PRK07529 191 --DFDAELARQPGDRLFSGRPIGPDDVAAYFhTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFcglpLFH--V 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 334 GWMMWNWMvSALATGASLVLydGSPL-VPTPNV---LWDLVDRIGITILGTGAKWLSVLeekdMK-PVETHNLHTLHTIL 408
Cdd:PRK07529 267 NALLVTGL-APLARGAHVVL--ATPQgYRGPGVianFWKIVERYRINFLSGVPTVYAAL----LQvPVDGHDISSLRYAL 339
|
....*.
gi 21313520 409 STGSPL 414
Cdd:PRK07529 340 CGAAPL 345
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
99-414 |
3.61e-14 |
|
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: 75.36 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 99 LNYAENLLRHKEndrvalYVAREGREEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGA 178
Cdd:cd12119 2 LEHAARLHGDRE------IVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 179 IWSST----SPD---FGVNGVLDRFSQIQPKLIFSVEAVVyngkehGHLEKLQRVVKGLPDlqrvvlipyvlprEKIDIS 251
Cdd:cd12119 76 VLHTInprlFPEqiaYIINHAEDRVVFVDRDFLPLLEAIA------PRLPTVEHVVVMTDD-------------AAMPEP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 252 KIPNSVFLDDFLAsgtgAQAPQLEFEQLPFSHPLFIMFSSGTTGAPKCMVHSAGGTLIQHLKEHMLHG-NMTSSDILLYY 330
Cdd:cd12119 137 AGVGVLAYEELLA----AESPEYDWPDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGlGLSESDVVLPV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 331 TTvgwmM-----WNWMVSALATGASLVLYDGSplvPTPNVLWDLVDRIGITI-LGTGAKWLSVLEEKDMKPVEthnLHTL 404
Cdd:cd12119 213 VP----MfhvnaWGLPYAAAMVGAKLVLPGPY---LDPASLAELIEREGVTFaAGVPTVWQGLLDHLEANGRD---LSSL 282
|
330
....*....|
gi 21313520 405 HTILSTGSPL 414
Cdd:cd12119 283 RRVVIGGSAV 292
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
283-633 |
8.92e-14 |
|
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: 73.94 E-value: 8.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 283 HPLFIMFSSGTTGAPKCMVHSAGgTLIQHLKEHMLHGNMTSSDILLYYTTVGW--MMWNWMVsALATGASLVLyDGSPLV 360
Cdd:cd17649 95 QLAYVIYTSGSTGTPKGVAVSHG-PLAAHCQATAERYGLTPGDRELQFASFNFdgAHEQLLP-PLICGACVVL-RPDELW 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 361 PTPNVLWDLVDRIGITILG-TGAKWLSVLEEkdMKPVETHNLHTLHTILSTGsplKAQSYEYVYRCIKSSVLLGSISGGT 439
Cdd:cd17649 172 ASADELAEMVRELGVTVLDlPPAYLQQLAEE--ADRTGDGRPPSLRLYIFGG---EALSPELLRRWLKAPVRLFNAYGPT 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 440 DIISCFMgqnssipVYKGEIQARNLGMAVEAwdeeGKAVWGASGELVCTKPIPCQPthfwnDENGSKY------RKAYFS 513
Cdd:cd17649 247 EATVTPL-------VWKCEAGAARAGASMPI----GRPLGGRSAYILDADLNPVPV-----GVTGELYiggeglARGYLG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 514 KfPGVWAH-----------------GDYCRINpKTGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQyN 576
Cdd:cd17649 311 R-PELTAErfvpdpfgapgsrlyrtGDLARWR-DDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-D 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 21313520 577 RDGEERVVLFLKMASGHTfQPDLVKRIRDAIRLGLSARHVPSLILETRGIPYTLNGK 633
Cdd:cd17649 388 GAGGKQLVAYVVLRAAAA-QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGK 443
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
97-633 |
4.57e-13 |
|
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: 72.02 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 97 SRLNYAENLLRHK---ENDRVALYvaregrEEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAA 173
Cdd:cd05959 1 EKYNAATLVDLNLnegRGDKTAFI------DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 174 ASIGAIwsstsPdFGVNGVLDrfsqiQPKLIFSVE-----AVVYNGKEHGHLEklQRVVKGLPDLQRVVLipyvlpreki 248
Cdd:cd05959 75 IRAGIV-----P-VPVNTLLT-----PDDYAYYLEdsrarVVVVSGELAPVLA--AALTKSEHTLVVLIV---------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 249 diskipnsvflddflASGTGAQAPQLEFEQLPFSH-------------PLFIMFSSGTTGAPKCMVHSAGGtlIQHLKEH 315
Cdd:cd05959 132 ---------------SGGAGPEAGALLLAELVAAEaeqlkpaathaddPAFWLYSSGSTGRPKGVVHLHAD--IYWTAEL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 316 ----MLHgnMTSSDILLYYTTV--GWMMWNWMVSALATGASLVLYdgsPLVPTPNVLWDLVDRIGITIL-GTGAKWLSVL 388
Cdd:cd05959 195 yarnVLG--IREDDVCFSAAKLffAYGLGNSLTFPLSVGATTVLM---PERPTPAAVFKRIRRYRPTVFfGVPTLYAAML 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 389 EEKDMKpveTHNLHTLHTILSTGSPLKAQSYEYVYRCIKSSVLLGsiSGGTDIISCFMgqnSSIP--VYKGEIQARNLGM 466
Cdd:cd05959 270 AAPNLP---SRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDG--IGSTEMLHIFL---SNRPgrVRYGTTGKPVPGY 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 467 AVEAWDEEGKAVW-GASGELVCTKpiPCQPTHFWNDENGSKyrkayfSKFPGVWAH-GD-YCRiNPKtGGIIMLGRSDGT 543
Cdd:cd05959 342 EVELRDEDGGDVAdGEPGELYVRG--PSSATMYWNNRDKTR------DTFQGEWTRtGDkYVR-DDD-GFYTYAGRADDM 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 544 LNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMASGHTFQPDLVKRIRDAIRLGLSARHVPSLILET 623
Cdd:cd05959 412 LKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFV 491
|
570
....*....|
gi 21313520 624 RGIPYTLNGK 633
Cdd:cd05959 492 DELPKTATGK 501
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
124-654 |
4.88e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 72.08 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 124 EEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKL 203
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 204 ifsveaVVYNGKEHG--HLEKLQRVVKG-LPDLQRVVLIpyvlpreKIDISKIPNSVFLDDFLASGTGAQAPQ--LEFEQ 278
Cdd:PRK06164 111 ------LVVWPGFKGidFAAILAAVPPDaLPPLRAIAVV-------DDAADATPAPAPGARVQLFALPDPAPPaaAGERA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 279 LPFSHPLFIMFSSGTTGAPKCMVHSAgGTLIQHLKEHMLHGNMTSSDILLYYTTV-GWMMWNWMVSALATGASLVL---Y 354
Cdd:PRK06164 178 ADPDAGALLFTTSGTTSGPKLVLHRQ-ATLLRHARAIARAYGYDPGAVLLAALPFcGVFGFSTLLGALAGGAPLVCepvF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 355 DGSPLVptpnvlwDLVDRIGIT-ILGTGAKWLSVLEEKDMKPvethNLHTLHtILSTGSPLKAqSYEYVYRCIKSSVLLG 433
Cdd:PRK06164 257 DAARTA-------RALRRHRVThTFGNDEMLRRILDTAGERA----DFPSAR-LFGFASFAPA-LGELAALARARGVPLT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 434 SISGGTDIISCFMGQNSSIPVykgeiQARNLG--------MAVEAWDEEGKAVW--GASGELVCTKpipcqPTHFWN-DE 502
Cdd:PRK06164 324 GLYGSSEVQALVALQPATDPV-----SVRIEGggrpaspeARVRARDPQDGALLpdGESGEIEIRA-----PSLMRGyLD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 503 NGSKYRKAYFSKfpGVWAHGDYCRINPkTGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVpQYNRDGEER 582
Cdd:PRK06164 394 NPDATARALTDD--GYFRTGDLGYTRG-DGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVV-GATRDGKTV 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21313520 583 VVLFLKMASGHTFQPdlvKRIRDAIRLGLSARHVPSLILETRGIPYTL--NGKKVEVAVKQVMAGRTVEHRGAF 654
Cdd:PRK06164 470 PVAFVIPTDGASPDE---AGLMAACREALAGFKVPARVQVVEAFPVTEsaNGAKIQKHRLREMAQARLAAERAA 540
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
101-298 |
7.32e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 71.57 E-value: 7.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 101 YAENLLRHKenDRVALYVAreGREeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIW 180
Cdd:PRK05605 38 YDNAVARFG--DRPALDFF--GAT----TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 181 SSTSPDFGVNGVLDRFSQIQPKLifsveAVVYNgKEHGHLEKLQR-----------VVKGLPDLQRVVL-IPyvLP---- 244
Cdd:PRK05605 110 VEHNPLYTAHELEHPFEDHGARV-----AIVWD-KVAPTVERLRRttpletivsvnMIAAMPLLQRLALrLP--IPalrk 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21313520 245 -REKIDiSKIPNSVFLDDFLASGTGAQAPQLEFEQLPFSHPLFIMFSSGTTGAPK 298
Cdd:PRK05605 182 aRAALT-GPAPGTVPWETLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPK 235
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
130-420 |
1.63e-12 |
|
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: 69.60 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 130 TFEELRQQVALFAAAMRKM-GVKKGDRVVGYLPNSAHAVEAMLAAASIGAIW---SSTSPdfgvngvLDRFSQI----QP 201
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYvplDPAYP-------AERLAFIledaGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 202 KLIFSveavvyngkEHGHLEKLQRVVkglpdlQRVVLIPyvlprekidiskipnsvfLDDFLASGTGAQAPQLEFEQLPf 281
Cdd:TIGR01733 74 RLLLT---------DSALASRLAGLV------LPVILLD------------------PLELAALDDAPAPPPPDAPSGP- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 282 SHPLFIMFSSGTTGAPKCMVHSAGGtLIQHLKEHMLHGNMTSSDILLYYTTVGWMMWNW-MVSALATGASLVLYDGSPLV 360
Cdd:TIGR01733 120 DDLAYVIYTSGSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDRVLQFASLSFDASVEeIFGALLAGATLVVPPEDEER 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21313520 361 PTPNVLWDLVDRIGITIL-GTGAKWLSVLEEKDMKpvethnLHTLHTILSTGSPLKAQSYE 420
Cdd:TIGR01733 199 DDAALLAALIAEHPVTVLnLTPSLLALLAAALPPA------LASLRLVILGGEALTPALVD 253
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
77-641 |
2.85e-12 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 69.45 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 77 YDEVVDTSKgiADVPEWFrgsrlNYAENLL---RHKENDRVAL-YVAREGREEIVkvTFEELRQQVALFAAAMRKMGVKK 152
Cdd:cd05970 1 YEDFHNNFS--INVPENF-----NFAYDVVdamAKEYPDKLALvWCDDAGEERIF--TFAELADYSDKTANFFKAMGIGK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 153 GDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEavvyngkEHGHLEKLQRVVKGLPD 232
Cdd:cd05970 72 GDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIA-------EDNIPEEIEKAAPECPS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 233 LQRVVLIPYVLPREKIDISKIpnsvfLDDFLASGTGAQAPQLEFEQlpfsHPLFIMFSSGTTGAPKcMV---------HS 303
Cdd:cd05970 145 KPKLVWVGDPVPEGWIDFRKL-----IKNASPDFERPTANSYPCGE----DILLVYFSSGTTGMPK-MVehdftyplgHI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 304 AGGTLIQHLKEHMLHgnMTSSDillyyttVGW--MMWNWMVSALATGASLVLYDGSPLvpTPNVLWDLVDRIGITILGTG 381
Cdd:cd05970 215 VTAKYWQNVREGGLH--LTVAD-------TGWgkAVWGKIYGQWIAGAAVFVYDYDKF--DPKALLEKLSKYGVTTFCAP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 382 AKWLSVLEEKDMkpvETHNLHTLHTILSTGSPLKAQSYEYVYRCIKSSVLLGsiSGGTDIISCfMGQNSSIPVYKGEIQA 461
Cdd:cd05970 284 PTIYRFLIREDL---SRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEG--FGQTETTLT-IATFPWMEPKPGSMGK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 462 RNLGMAVEAWDEEGKAV-WGASGElVCTKPIPCQPTHFWND--ENGSKYRKAYFSkfpGVWAHGDYCRINpKTGGIIMLG 538
Cdd:cd05970 358 PAPGYEIDLIDREGRSCeAGEEGE-IVIRTSKGKPVGLFGGyyKDAEKTAEVWHD---GYYHTGDAAWMD-EDGYLWFVG 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 539 RSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLC--VPQYNRDgeERVVLFLKMASGHTFQPDLVKRIRDAIRLGLSARHV 616
Cdd:cd05970 433 RTDDLIKSSGYRIGPFEVESALIQHPAVLECAVtgVPDPIRG--QVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKY 510
|
570 580
....*....|....*....|....*
gi 21313520 617 PSLILETRGIPYTLNGKKVEVAVKQ 641
Cdd:cd05970 511 PRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
112-413 |
7.54e-12 |
|
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: 68.02 E-value: 7.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALyvaregREEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWsstspdfgvng 191
Cdd:cd17631 10 DRTAL------VFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVF----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 vldrfsqiqpklifsveavvyngkehghleklqrvvkglpdlqrvVLIPYVL-PREKIDIskipnsvfLDDFLASgtgaq 270
Cdd:cd17631 73 ---------------------------------------------VPLNFRLtPPEVAYI--------LADSGAK----- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 271 apqlefeqLPFSHPLFIMFSSGTTGAPKCMVHSAGGTLIQHLKeHMLHGNMTSSDIL-----LYYTTVGWMmwnWMVSAL 345
Cdd:cd17631 95 --------VLFDDLALLMYTSGTTGRPKGAMLTHRNLLWNAVN-ALAALDLGPDDVLlvvapLFHIGGLGV---FTLPTL 162
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21313520 346 ATGASLVLYDGsplvPTPNVLWDLVDRIGIT-ILGTGAKWLSVLEEKDMkpvETHNLHTLHTILSTGSP 413
Cdd:cd17631 163 LRGGTVVILRK----FDPETVLDLIERHRVTsFFLVPTMIQALLQHPRF---ATTDLSSLRAVIYGGAP 224
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
94-395 |
1.17e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 67.49 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 94 FRGSRLNYAENLLRHKEN--DRVALyvaregREEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAML 171
Cdd:PRK07786 12 YLARRQNWVNQLARHALMqpDAPAL------RFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 172 AAASIGAIwsstspdfgvnGVLDRFSQIQPKLIFSVE-----AVVYNGKehghLEKLQRVVKGL-PDLQRVVLipyvlpr 245
Cdd:PRK07786 86 AANMLGAI-----------AVPVNFRLTPPEIAFLVSdcgahVVVTEAA----LAPVATAVRDIvPLLSTVVV------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 246 ekIDISKIPNSVFLDDFLASGTGAQAPQlefeQLPFSHPLFIMFSSGTTGAPKCMVHSaggtliqhlkehmlHGNMTSSD 325
Cdd:PRK07786 144 --AGGSSDDSVLGYEDLLAEAGPAHAPV----DIPNDSPALIMYTSGTTGRPKGAVLT--------------HANLTGQA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 326 ILLYYTT-------VGWMM--------WNWMVSALATGASLVLYdgsPL-VPTPNVLWDLVDRIGIT-ILGTGAKWLSVL 388
Cdd:PRK07786 204 MTCLRTNgadinsdVGFVGvplfhiagIGSMLPGLLLGAPTVIY---PLgAFDPGQLLDVLEAEKVTgIFLVPAQWQAVC 280
|
....*..
gi 21313520 389 EEKDMKP 395
Cdd:PRK07786 281 AEQQARP 287
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
112-633 |
1.25e-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: 67.17 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALyVAREGReeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFgvng 191
Cdd:cd05930 2 DAVAV-VDGDQS-----LTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSY---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 vldrfsqiqPKlifsveavvyngkehghlEKLQRVVKglpDLQRVVLIpyvlprekidiskipnsvflddflasgTGAqa 271
Cdd:cd05930 72 ---------PA------------------ERLAYILE---DSGAKLVL---------------------------TDP-- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 272 pqlefeqlpfSHPLFIMFSSGTTGAPKcmvhsagGTLIQH------LKEHMLHGNMTSSDILLYYTTVG-----WMMWnw 340
Cdd:cd05930 93 ----------DDLAYVIYTSGSTGKPK-------GVMVEHrglvnlLLWMQEAYPLTPGDRVLQFTSFSfdvsvWEIF-- 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 341 mvSALATGASLVLYDGSpLVPTPNVLWDLVDRIGITIL-GTGAKWLSVLEEKDMKpvethNLHTLHTILSTGSPLKAQSY 419
Cdd:cd05930 154 --GALLAGATLVVLPEE-VRKDPEALADLLAEEGITVLhLTPSLLRLLLQELELA-----ALPSLRLVLVGGEALPPDLV 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 420 EYVYRcIKSSVLLGSISGGTD--IISCFMgqnssiPVYKGEIQARNL-------GMAVEAWDEEGKAV-WGASGELVCT- 488
Cdd:cd05930 226 RRWRE-LLPGARLVNLYGPTEatVDATYY------RVPPDDEEDGRVpigrpipNTRVYVLDENLRPVpPGVPGELYIGg 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 489 ---------KPipcqpthfwnDENGSKYRKAYFskFPGVWAH--GDYCRINPkTGGIIMLGRSDGTLNPNGVRFGSSEIY 557
Cdd:cd05930 299 aglargylnRP----------ELTAERFVPNPF--GPGERMYrtGDLVRWLP-DGNLEFLGRIDDQVKIRGYRIELGEIE 365
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21313520 558 NIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMASGHTFQPDlvkRIRDAIRLGLSARHVPSLILETRGIPYTLNGK 633
Cdd:cd05930 366 AALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEE---ELRAHLAERLPDYMVPSAFVVLDALPLTPNGK 438
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
112-424 |
1.32e-11 |
|
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: 67.96 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALyVAREGReeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIW---SSTSPDfg 188
Cdd:COG1020 491 DAVAV-VFGDQS-----LTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYvplDPAYPA-- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 189 vngvlDRFSQI----QPKLIFSVEAVVyngkehghleklqrvvKGLPDLQRVVLipyvlprekidiskipnsvFLDDFLA 264
Cdd:COG1020 563 -----ERLAYMledaGARLVLTQSALA----------------ARLPELGVPVL-------------------ALDALAL 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 265 SGTGAQAPQLEFEqlPfSHPLFIMFSSGTTGAPK--CMVHSAggtLIQHLKEHMLHGNMTSSDILLYYTTVG-----WMM 337
Cdd:COG1020 603 AAEPATNPPVPVT--P-DDLAYVIYTSGSTGRPKgvMVEHRA---LVNLLAWMQRRYGLGPGDRVLQFASLSfdasvWEI 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 338 WnwmvSALATGASLVLYDGSpLVPTPNVLWDLVDRIGITILgtgakWL--SVLEEkdMKPVETHNLHTLHTILSTGSPLK 415
Cdd:COG1020 677 F----GALLSGATLVLAPPE-ARRDPAALAELLARHRVTVL-----NLtpSLLRA--LLDAAPEALPSLRLVLVGGEALP 744
|
....*....
gi 21313520 416 AQSYEYVYR 424
Cdd:COG1020 745 PELVRRWRA 753
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
112-633 |
1.62e-11 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 66.93 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVAlyVAREGREeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVng 191
Cdd:cd12116 2 DATA--VRDDDRS----LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 vlDRFSQI----QPKLIFSVEAvvyngkehghleklqrvvkgLPD--LQRVVLIPYVLPREKidiskipnsvflddflAS 265
Cdd:cd12116 74 --DRLRYIledaEPALVLTDDA--------------------LPDrlPAGLPVLLLALAAAA----------------AA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 266 GTGAQAPQlefeqlPFSHPLFIMFSSGTTGAPKCMVHSAGGTLiqhlkeHMLHG-----NMTSSDILLYYTTVGW----- 335
Cdd:cd12116 116 PAAPRTPV------SPDDLAYVIYTSGSTGRPKGVVVSHRNLV------NFLHSmrerlGLGPGDRLLAVTTYAFdisll 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 336 -MMWnwmvsALATGASLVLYDGSpLVPTPNVLWDLVDRIGITIL-GTGAKWLSVL--EEKDMKPVethnlhtlhTILSTG 411
Cdd:cd12116 184 eLLL-----PLLAGARVVIAPRE-TQRDPEALARLIEAHSITVMqATPATWRMLLdaGWQGRAGL---------TALCGG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 412 SPLKAQSYEYVyrCIKSSVLLgSISGGTD--IISCFM---GQNSSIPVykGEiqaRNLGMAVEAWDEEGKAV-WGASGEL 485
Cdd:cd12116 249 EALPPDLAARL--LSRVGSLW-NLYGPTEttIWSTAArvtAAAGPIPI--GR---PLANTQVYVLDAALRPVpPGVPGEL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 486 VctkpI--PCQPTHFWND--------------ENGSK-YRKayfskfpgvwahGDYCRINPKtGGIIMLGRSDGTLNPNG 548
Cdd:cd12116 321 Y----IggDGVAQGYLGRpaltaerfvpdpfaGPGSRlYRT------------GDLVRRRAD-GRLEYLGRADGQVKIRG 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 549 VRFGSSEIYNIVEAFDEVEDSLCVPQYNrDGEERVVLFLKMASGHTFQPDlvkRIRDAIRLGLSARHVPSLILETRGIPY 628
Cdd:cd12116 384 HRIELGEIEAALAAHPGVAQAAVVVRED-GGDRRLVAYVVLKAGAAPDAA---ALRAHLRATLPAYMVPSAFVRLDALPL 459
|
....*
gi 21313520 629 TLNGK 633
Cdd:cd12116 460 TANGK 464
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
112-633 |
2.16e-11 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 66.46 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALyVAREGReeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVng 191
Cdd:cd12117 12 DAVAV-VYGDRS-----LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPA-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 vlDRFSQI----QPKLIFSveavvyngkehghleklQRVVKGLPDLQRVVLIPYVLPRekidiskipnsvflddflASGT 267
Cdd:cd12117 84 --ERLAFMladaGAKVLLT-----------------DRSLAGRAGGLEVAVVIDEALD------------------AGPA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 268 GAQAPQLEFEQLPFshplfIMFSSGTTGAPKcmvhsagGTLIQH-----LKEHMLHGNMTSSDILLYYTTVGW-----MM 337
Cdd:cd12117 127 GNPAVPVSPDDLAY-----VMYTSGSTGRPK-------GVAVTHrgvvrLVKNTNYVTLGPDDRVLQTSPLAFdastfEI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 338 WnwmvSALATGASLVLYDGSPLVpTPNVLWDLVDRIGITILgtgakWLS-------VLEEKDMkpvethnLHTLHTILST 410
Cdd:cd12117 195 W----GALLNGARLVLAPKGTLL-DPDALGALIAEEGVTVL-----WLTaalfnqlADEDPEC-------FAGLRELLTG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 411 GSPLKAQSYEYVYRcikssvllgsISGGTDIISCF-----MGQNSSIPVYKGEIQARNL-------GMAVEAWDEEGKAV 478
Cdd:cd12117 258 GEVVSPPHVRRVLA----------ACPGLRLVNGYgptenTTFTTSHVVTELDEVAGSIpigrpiaNTRVYVLDEDGRPV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 479 -WGASGEL------VCTKpipcqpthFWNDENGSKYRKAYFSKFPGVWAH--GDYCRINPkTGGIIMLGRSDGTLNPNGV 549
Cdd:cd12117 328 pPGVPGELyvggdgLALG--------YLNRPALTAERFVADPFGPGERLYrtGDLARWLP-DGRLEFLGRIDDQVKIRGF 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 550 RFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLkmASGHTFQPDLVkriRDAIRLGLSARHVPSLILETRGIPYT 629
Cdd:cd12117 399 RIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYV--VAEGALDAAEL---RAFLRERLPAYMVPAAFVVLDELPLT 473
|
....
gi 21313520 630 LNGK 633
Cdd:cd12117 474 ANGK 477
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
112-311 |
3.33e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 66.33 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALYVaregREEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNG 191
Cdd:PRK12583 33 DREALVV----RHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 VLDRFSQIQPKLIFSVEAVvyngKEHGHLEKLQRVVKGLPDLQRVVLIPYVLPREK----IDISKIPNSVFLDDFLASGT 267
Cdd:PRK12583 109 LEYALGQSGVRWVICADAF----KTSDYHAMLQELLPGLAEGQPGALACERLPELRgvvsLAPAPPPGFLAWHELQARGE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21313520 268 GAQAPQLEFEQLPFSH--PLFIMFSSGTTGAPKcmvhsaGGTLIQH 311
Cdd:PRK12583 185 TVSREALAERQASLDRddPINIQYTSGTTGFPK------GATLSHH 224
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
112-414 |
3.33e-11 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 66.23 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALYVAREGREEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFgvng 191
Cdd:PRK13295 39 DKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIF---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 vldRFSQIQPKLIFSVEAVVYNGKE---HGHLEKLQRVVKGLPDLQRVVLIpyvlprekidiskipNSVFLDDFLASGTG 268
Cdd:PRK13295 115 ---RERELSFMLKHAESKVLVVPKTfrgFDHAAMARRLRPELPALRHVVVV---------------GGDGADSFEALLIT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 269 AqapqlEFEQLPFSHPLF------------IMFSSGTTGAPKCMVHSAgGTLIQHLKEHMLHGNMTSSDILLYYTTVGWM 336
Cdd:PRK13295 177 P-----AWEQEPDAPAILarlrpgpddvtqLIYTSGTTGEPKGVMHTA-NTLMANIVPYAERLGLGADDVILMASPMAHQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 337 ---MWNWMVsALATGASLVLYDgsplVPTPNVLWDLVDRIGITILGTGAKWLS----VLEEKDmkpvetHNLHTLHTILS 409
Cdd:PRK13295 251 tgfMYGLMM-PVMLGATAVLQD----IWDPARAAELIRTEGVTFTMASTPFLTdltrAVKESG------RPVSSLRTFLC 319
|
....*
gi 21313520 410 TGSPL 414
Cdd:PRK13295 320 AGAPI 324
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
112-311 |
4.06e-11 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 65.99 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALYVAREGReeivKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNG 191
Cdd:PRK08315 31 DREALVYRDQGL----RWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 VLDRFSQIQPKLIFSVEAVvyngKEHGHLEKLQRVVKGLPDLQRVVLIPYVLPREK----IDISKIPNSVFLDDFLASGT 267
Cdd:PRK08315 107 LEYALNQSGCKALIAADGF----KDSDYVAMLYELAPELATCEPGQLQSARLPELRrvifLGDEKHPGMLNFDELLALGR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21313520 268 GAQAPQLEF--EQLPFSHPLFIMFSSGTTGAPKcmvhsaGGTLIQH 311
Cdd:PRK08315 183 AVDDAELAArqATLDPDDPINIQYTSGTTGFPK------GATLTHR 222
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
129-633 |
4.74e-11 |
|
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: 65.41 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 129 VTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIfsve 208
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 209 aVVYNGKEHGHLEKLQRVVKGLPDLQRVVLIPYVLPREkidiSKIPNSVFLDDFLASGTGAQAPQLefeqlpfshpLFIM 288
Cdd:cd05926 91 -LTPKGELGPASRAASKLGLAILELALDVGVLIRAPSA----ESLSNLLADKKNAKSEGVPLPDDL----------ALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 289 FSSGTTGAPKcMV---H---SAGGTLIQhlKEHMLhgnmTSSDILLyyttvgwmmwNWM------------VSALATGAS 350
Cdd:cd05926 156 HTSGTTGRPK-GVpltHrnlAASATNIT--NTYKL----TPDDRTL----------VVMplfhvhglvaslLSTLAAGGS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 351 LVLYDGSplvpTPNVLWDLVDRIGITilgtgakWLSVLEE------KDMKPVETHNLHTLHTILSTGSPLKAQSYEYVYR 424
Cdd:cd05926 219 VVLPPRF----SASTFWPDVRDYNAT-------WYTAVPTihqillNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 425 CIKSSVL-----------------------LGS--ISGGTDIisCFMGQNSSI--PVYKGEIQARnlgmaveawdeeGKA 477
Cdd:cd05926 288 TFGAPVLeaygmteaahqmtsnplppgprkPGSvgKPVGVEV--RILDEDGEIlpPGVVGEICLR------------GPN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 478 VwgasgelvctkpipcqpTH-FWNDEngsKYRKAYFSKFPgvWAH-GDYCRINPKtGGIIMLGRSDGTLNPNGVRFGSSE 555
Cdd:cd05926 354 V-----------------TRgYLNNP---EANAEAAFKDG--WFRtGDLGYLDAD-GYLFLTGRIKELINRGGEKISPLE 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 556 IYNIVEAFDEVEDSLCV----PQYnrdGEErVVLFLKMASGHTFqpdLVKRIRDAIRLGLSARHVPSLILETRGIPYTLN 631
Cdd:cd05926 411 VDGVLLSHPAVLEAVAFgvpdEKY---GEE-VAAAVVLREGASV---TEEELRAFCRKHLAAFKVPKKVYFVDELPKTAT 483
|
..
gi 21313520 632 GK 633
Cdd:cd05926 484 GK 485
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
112-633 |
5.13e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 65.68 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALyVAREGReeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIwsstspDFGVNG 191
Cdd:PRK07798 18 DRVAL-VCGDRR-----LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAV------PVNVNY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 vldRFSQIQPKLIFS---VEAVVYngkEHGHLEKLQRVVKGLPDLQRVVLIPyvlprEKIDISKIPNSVFLDDFLASGTG 268
Cdd:PRK07798 86 ---RYVEDELRYLLDdsdAVALVY---EREFAPRVAEVLPRLPKLRTLVVVE-----DGSGNDLLPGAVDYEDALAAGSP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 269 AQapqlefeqlPFSHP----LFIMFSSGTTGAPKCMV--HS------------AGGTLIQHLKEHMLHGNMTSSDILLyy 330
Cdd:PRK07798 155 ER---------DFGERspddLYLLYTGGTTGMPKGVMwrQEdifrvllggrdfATGEPIEDEEELAKRAAAGPGMRRF-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 331 tTVGWMM-----WNWMvSALATGASLVLYDGSPLVPTPnvLWDLVDRIGITILG-TG---AKWLsvLEEKDMKpvETHNL 401
Cdd:PRK07798 224 -PAPPLMhgagqWAAF-AALFSGQTVVLLPDVRFDADE--VWRTIEREKVNVITiVGdamARPL--LDALEAR--GPYDL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 402 HTLHTILSTGSPLKAQSYEYVYRCIKSSVLLGSIsGGTDiiSCFMGqnsSIPVYKGEIQAR----NLGMAVEAWDEEGKA 477
Cdd:PRK07798 296 SSLFAIASGGALFSPSVKEALLELLPNVVLTDSI-GSSE--TGFGG---SGTVAKGAVHTGgprfTIGPRTVVLDEDGNP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 478 VWGASGE---LVCTKPIpcqPTHFWNDEngSKYRKAYFSkFPGV-WA-HGDYCRINPKtGGIIMLGRSDGTLNPNGVRFG 552
Cdd:PRK07798 370 VEPGSGEigwIARRGHI---PLGYYKDP--EKTAETFPT-IDGVrYAiPGDRARVEAD-GTITLLGRGSVCINTGGEKVF 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 553 SSEIYNIVEAFDEVEDSLCVPqynRDGE---ERVVLFLKMASGHTFQPDlvkRIRDAIRLGLSARHVPSLILETRGIPYT 629
Cdd:PRK07798 443 PEEVEEALKAHPDVADALVVG---VPDErwgQEVVAVVQLREGARPDLA---ELRAHCRSSLAGYKVPRAIWFVDEVQRS 516
|
....
gi 21313520 630 LNGK 633
Cdd:PRK07798 517 PAGK 520
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
112-404 |
5.13e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 65.72 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALyvaregREEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWsstspdFGVNG 191
Cdd:PRK08316 26 DKTAL------VFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVH------VPVNF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 VLDR------FSQIQPKLIFSVEAVVyngkehGHLEKLQRVVKGLPDLQRVVLIPYVLPREKIDiskipnsvFLDDFLAS 265
Cdd:PRK08316 94 MLTGeelayiLDHSGARAFLVDPALA------PTAEAALALLPVDTLILSLVLGGREAPGGWLD--------FADWAEAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 266 GTGAQAPQLEFEQLpfshpLFIMFSSGTTGAPKCMVHSAGGTLIQHLKEhMLHGNMTSSDIL-----LYYTTvgwMMWNW 340
Cdd:PRK08316 160 SVAEPDVELADDDL-----AQILYTSGTESLPKGAMLTHRALIAEYVSC-IVAGDMSADDIPlhalpLYHCA---QLDVF 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21313520 341 MVSALATGASLVLYDGsplvPTPNVLWDLVDRIGITIL-GTGAKWLSVLEEKDMkpvETHNLHTL 404
Cdd:PRK08316 231 LGPYLYVGATNVILDA----PDPELILRTIEAERITSFfAPPTVWISLLRHPDF---DTRDLSSL 288
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
112-298 |
1.12e-10 |
|
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: 64.40 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALyVAREGReeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIwsstsPdfgVNG 191
Cdd:COG1021 40 DRIAV-VDGERR-----LSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI-----P---VFA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 V-------LDRF-SQIQPKLIfsVEAVVYNGkeHGHLEKLQRVVKGLPDLQRVVlipyVL--PREKIDiskipnsvfLDD 261
Cdd:COG1021 106 LpahrraeISHFaEQSEAVAY--IIPDRHRG--FDYRALARELQAEVPSLRHVL----VVgdAGEFTS---------LDA 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 21313520 262 FLASGTGAQAPQLEFEQlpfshPLFIMFSSGTTGAPK 298
Cdd:COG1021 169 LLAAPADLSEPRPDPDD-----VAFFQLSGGTTGLPK 200
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
112-633 |
1.20e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 64.21 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALyVAREGReeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDfgvng 191
Cdd:cd12114 2 DATAV-ICGDGT-----LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDID----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 vldrfsqiQPKlifsveavvyngkehghlEKLQRVvkgLPDLQ-RVVLIPYVLPREKIDiskiPNSVFLDDFLASGTGAQ 270
Cdd:cd12114 71 --------QPA------------------ARREAI---LADAGaRLVLTDGPDAQLDVA----VFDVLILDLDALAAPAP 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 271 APQLEFEQlpfSHPLFIMFSSGTTGAPKCMV--HSAGGTLIQHLKEHMlhgNMTSSDILLYYTTVGWMMWNWMV-SALAT 347
Cdd:cd12114 118 PPPVDVAP---DDLAYVIFTSGSTGTPKGVMisHRAALNTILDINRRF---AVGPDDRVLALSSLSFDLSVYDIfGALSA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 348 GASLVLYDGSpLVPTPNVLWDLVDRIGITIlgtgakWLSVLEEKDM----KPVETHNLHTLHTILSTGS------PLKaq 417
Cdd:cd12114 192 GATLVLPDEA-RRRDPAHWAELIERHGVTL------WNSVPALLEMlldvLEAAQALLPSLRLVLLSGDwipldlPAR-- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 418 syeyvYRCIKSSVLLGSISGGTD--IIScfmgqN-----------SSIPvYkgeiqARNL-GMAVEAWDEEGKAV--WGA 481
Cdd:cd12114 263 -----LRALAPDARLISLGGATEasIWS-----IyhpidevppdwRSIP-Y-----GRPLaNQRYRVLDPRGRDCpdWVP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 482 sGELvctkpipcqptH---------FWNDENgskyRKAyfSKFPGVWAH------GDYCRINPKtGGIIMLGRSDGTLNP 546
Cdd:cd12114 327 -GEL-----------WiggrgvalgYLGDPE----LTA--ARFVTHPDGerlyrtGDLGRYRPD-GTLEFLGRRDGQVKV 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 547 NGVRFGSSEIYNIVEAFDEVEdSLCVPQYNRDGEERVVLFLKMASGHTfqPDLVKRIRDAIRLGLSARHVPSLILETRGI 626
Cdd:cd12114 388 RGYRIELGEIEAALQAHPGVA-RAVVVVLGDPGGKRLAAFVVPDNDGT--PIAPDALRAFLAQTLPAYMIPSRVIALEAL 464
|
....*..
gi 21313520 627 PYTLNGK 633
Cdd:cd12114 465 PLTANGK 471
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
112-633 |
2.14e-10 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 63.52 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALyVAREGReeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDfgvng 191
Cdd:cd17651 10 DAPAL-VAEGRR-----LTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 vldrfsqiQPKlifsveavvyngkehghlEKLQRVVKglpDLQRVVLIPYvlPREKIDISKIPNSVFLDDFLASGTGAQA 271
Cdd:cd17651 79 --------YPA------------------ERLAFMLA---DAGPVLVLTH--PALAGELAVELVAVTLLDQPGAAAGADA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 272 PQleFEQLPFSHPLFIMFSSGTTGAPKCMVHSaGGTLIQHLKEHMLHGNMTSSDILLYYTTVGWMMWNWMV-SALATGAS 350
Cdd:cd17651 128 EP--DPALDADDLAYVIYTSGSTGRPKGVVMP-HRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIfSTLCAGAT 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 351 LVLydgsplvPTPNV------LWDLVDRIGITILGTGAKWLSVLEEkDMKPVETHnLHTLHTILSTGSPLKAQSyeyvyr 424
Cdd:cd17651 205 LVL-------PPEEVrtdppaLAAWLDEQRISRVFLPTVALRALAE-HGRPLGVR-LAALRYLLTGGEQLVLTE------ 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 425 ciKSSVLLGSISGGTDIiscfmgqNSSIPVYKGEIQARNLGMAVEAWDEE---GKAVWGAS----------------GEL 485
Cdd:cd17651 270 --DLREFCAGLPGLRLH-------NHYGPTETHVVTALSLPGDPAAWPAPppiGRPIDNTRvyvldaalrpvppgvpGEL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 486 V----------CTKPipcQPTH--FWND---ENGSKYRKayfskfpgvwahGDYCRINPkTGGIIMLGRSDGTLNPNGVR 550
Cdd:cd17651 341 YiggaglargyLNRP---ELTAerFVPDpfvPGARMYRT------------GDLARWLP-DGELEFLGRADDQVKIRGFR 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 551 FGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMASGHtfqPDLVKRIRDAIRLGLSARHVPSLILETRGIPYTL 630
Cdd:cd17651 405 IELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEA---PVDAAELRAALATHLPEYMVPSAFVLLDALPLTP 481
|
...
gi 21313520 631 NGK 633
Cdd:cd17651 482 NGK 484
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
112-353 |
7.10e-10 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 62.20 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALyvaREGREEIvkvTFEELRQQVALFAAAMRKMGVKKGDrVVG-YLPNSAHAVEAMLAAASIGAIwsstspdfgvn 190
Cdd:PRK08279 52 DRPAL---LFEDQSI---SYAELNARANRYAHWAAARGVGKGD-VVAlLMENRPEYLAAWLGLAKLGAV----------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 191 GVLDRFSQIQPKLIFSVEAVvyngkEHGHL----EKLQRVVKGLPDLQRVVLIPYVLPREKIDISKIPNsvfLDDfLASG 266
Cdd:PRK08279 114 VALLNTQQRGAVLAHSLNLV-----DAKHLivgeELVEAFEEARADLARPPRLWVAGGDTLDDPEGYED---LAA-AAAG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 267 TGAQAPQLEfEQLPFSHPLFIMFSSGTTGAPK----------CMVHSAGGTLiqhlkehmlhgNMTSSDIL-----LYYT 331
Cdd:PRK08279 185 APTTNPASR-SGVTAKDTAFYIYTSGTTGLPKaavmshmrwlKAMGGFGGLL-----------RLTPDDVLycclpLYHN 252
|
250 260
....*....|....*....|..
gi 21313520 332 TVGWMMWNwmvSALATGASLVL 353
Cdd:PRK08279 253 TGGTVAWS---SVLAAGATLAL 271
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
118-414 |
1.23e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 61.21 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 118 VAREGREEIVKV------TFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSpdfgvng 191
Cdd:PRK07470 16 AARRFPDRIALVwgdrswTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 vldrFSQIQPKLIFSVE-----AVVYNGKEHGHLEKLQRVVkglPDLQRVVLIPyvLPREKIDIskipnsvflDDFLASG 266
Cdd:PRK07470 89 ----FRQTPDEVAYLAEasgarAMICHADFPEHAAAVRAAS---PDLTHVVAIG--GARAGLDY---------EALVARH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 267 TGAQAPQLEFEQlpfSHPLFIMFSSGTTGAPKCMV--HSAGGTLI-QHLKEHMlhGNMTSSDILLyytTVGWMMWNWMVS 343
Cdd:PRK07470 151 LGARVANAAVDH---DDPCWFFFTSGTTGRPKAAVltHGQMAFVItNHLADLM--PGTTEQDASL---VVAPLSHGAGIH 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21313520 344 AL---ATGASLVLYDGSPLVPTpnVLWDLVDRIGITILGTGAKWLSVLEEKdmKPVETHNLHTLHTILSTGSPL 414
Cdd:PRK07470 223 QLcqvARGAATVLLPSERFDPA--EVWALVERHRVTNLFTVPTILKMLVEH--PAVDRYDHSSLRYVIYAGAPM 292
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
47-104 |
2.28e-09 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 53.63 E-value: 2.28e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 21313520 47 YNDLYHWSVRSYMDFWAEFWKFsgIVYSRMYDEVVDTSKGiaDVPEWFRGSRLNYAEN 104
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKE--LDWFKPFDKVLDGSNG--PFAKWFVGGKLNVCYN 54
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
128-376 |
6.04e-09 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 59.67 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 128 KVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGvNGVLDR-FSQIQPKLIFS 206
Cdd:PRK10252 483 QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYP-DDRLKMmLEDARPSLLIT 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 207 VEAVvyngkehghlekLQRvvkgLPDLQRVVLIPYVLPrekidiskipnsvflddfLAsgtgAQAPQLEFEQLPfSHPLF 286
Cdd:PRK10252 562 TADQ------------LPR----FADVPDLTSLCYNAP------------------LA----PQGAAPLQLSQP-HHTAY 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 287 IMFSSGTTGAPK-CMV-HSAggtLIQHLKEHMLHGNMTSSDILLYYTTVG-----W-MMWNWMVsalatGASLVLydgSP 358
Cdd:PRK10252 603 IIFTSGSTGRPKgVMVgQTA---IVNRLLWMQNHYPLTADDVVLQKTPCSfdvsvWeFFWPFIA-----GAKLVM---AE 671
|
250 260
....*....|....*....|..
gi 21313520 359 lvPT----PNVLWDLVDRIGIT 376
Cdd:PRK10252 672 --PEahrdPLAMQQFFAEYGVT 691
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
112-414 |
8.45e-09 |
|
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: 58.34 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALYVarEGReeivKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPdfgvng 191
Cdd:cd05936 14 DKTALIF--MGR----KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 vldrfsqiqpklifsveavVYNGKEHGHLeklqrvvkgLPDLQRVVLIpyvlprekidiskipNSVFLDDFLASGTGAQA 271
Cdd:cd05936 82 -------------------LYTPRELEHI---------LNDSGAKALI---------------VAVSFTDLLAAGAPLGE 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 272 PQlefeQLPFSHPLFIMFSSGTTGAPKcmvhsagGTLIqhlkehmLHGNMTS---------------SDILL----YYTT 332
Cdd:cd05936 119 RV----ALTPEDVAVLQYTSGTTGVPK-------GAML-------THRNLVAnalqikawledllegDDVVLaalpLFHV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 333 VGWMMwnWMVSALATGASLVlydgspLVPTP---NVLwDLVDRIGITIL-GTGAKWLSVLEEKDmkpVETHNLHTLHTIL 408
Cdd:cd05936 181 FGLTV--ALLLPLALGATIV------LIPRFrpiGVL-KEIRKHRVTIFpGVPTMYIALLNAPE---FKKRDFSSLRLCI 248
|
....*.
gi 21313520 409 STGSPL 414
Cdd:cd05936 249 SGGAPL 254
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
112-633 |
3.57e-08 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 56.51 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVAlyVAREGREeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVng 191
Cdd:cd17646 13 DAPA--VVDEGRT----LTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPA-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 vlDRFSQI----QPKLIFSVEavvyngkehghleklqRVVKGLPDLQRVVLIPYVLPREkidiskipnsvflddflASGT 267
Cdd:cd17646 85 --DRLAYMladaGPAVVLTTA----------------DLAARLPAGGDVALLGDEALAA-----------------PPAT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 268 GAQAPqlefeqLPFSHPLFIMFSSGTTGAPK-CMV-HSAGGTLIQHLKEHMLHGnmtSSDILLYYTTVG-----WMMWnW 340
Cdd:cd17646 130 PPLVP------PRPDNLAYVIYTSGSTGRPKgVMVtHAGIVNRLLWMQDEYPLG---PGDRVLQKTPLSfdvsvWELF-W 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 341 mvsALATGASLVLydgspLVP----TPNVLWDLVDRIGITILGTGAKWLSV-LEEKDmkpVETHNlhTLHTILSTGSPLK 415
Cdd:cd17646 200 ---PLVAGARLVV-----ARPgghrDPAYLAALIREHGVTTCHFVPSMLRVfLAEPA---AGSCA--SLRRVFCSGEALP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 416 AQSYEYVYRciKSSVLLGSISGGTDiiscfmgqnSSIPVYKGEIQAR-------------NLGMAVeaWDEEGKAV-WGA 481
Cdd:cd17646 267 PELAARFLA--LPGAELHNLYGPTE---------AAIDVTHWPVRGPaetpsvpigrpvpNTRLYV--LDDALRPVpVGV 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 482 SGELVCTkpipcqpthfwndenGSKYRKAYF-------SKF------PG--VWAHGDYCRINPKtGGIIMLGRSDGTLNP 546
Cdd:cd17646 334 PGELYLG---------------GVQLARGYLgrpaltaERFvpdpfgPGsrMYRTGDLARWRPD-GALEFLGRSDDQVKI 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 547 NGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMASGHtfQPDLVKRIRDAIRLGLSARHVPSLILETRGI 626
Cdd:cd17646 398 RGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGA--AGPDTAALRAHLAERLPEYMVPAAFVVLDAL 475
|
....*..
gi 21313520 627 PYTLNGK 633
Cdd:cd17646 476 PLTANGK 482
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
129-633 |
4.13e-08 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 56.04 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 129 VTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIwsstspdfgvngVLDRFSQIQPKlifsve 208
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV------------VIPATTLLTPD------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 209 avvyngkehghleklqrvvkglpDLqrvvlipyvlpREKIDIskipnsvflddflasGTGAQAPQLEFEQLpfSHPLFIM 288
Cdd:cd05974 63 -----------------------DL-----------RDRVDR---------------GGAVYAAVDENTHA--DDPMLLY 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 289 FSSGTTGAPKCMVHSAGGTLIQHLKEhMLHGNMTSSDILLYYTTVGWM--MWNWMVSALATGASLVLYDGSPLVPTpnVL 366
Cdd:cd05974 92 FTSGTTSKPKLVEHTHRSYPVGHLST-MYWIGLKPGDVHWNISSPGWAkhAWSCFFAPWNAGATVFLFNYARFDAK--RV 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 367 WDLVDRIGITILGTGAKWLSVLEEKDMKPVEThnlhTLHTILSTGSPLKAQSYEYVYRCIKSSVLLGsiSGGTDiISCFM 446
Cdd:cd05974 169 LAALVRYGVTTLCAPPTVWRMLIQQDLASFDV----KLREVVGAGEPLNPEVIEQVRRAWGLTIRDG--YGQTE-TTALV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 447 GQNSSIPVYKGEIQARNLGMAVEAWDEEGKAVwgASGELVC----TKPIPCQpTHFWNDENGSKYRKAyfskfPGVWAHG 522
Cdd:cd05974 242 GNSPGQPVKAGSMGRPLPGYRVALLDPDGAPA--TEGEVALdlgdTRPVGLM-KGYAGDPDKTAHAMR-----GGYYRTG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 523 DYCRiNPKTGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPqyNRDGEERVV--LFLKMASGHTFQPDLV 600
Cdd:cd05974 314 DIAM-RDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVP--SPDPVRLSVpkAFIVLRAGYEPSPETA 390
|
490 500 510
....*....|....*....|....*....|....
gi 21313520 601 KRIRDAIRLGLSA-RHVPSliLETRGIPYTLNGK 633
Cdd:cd05974 391 LEIFRFSRERLAPyKRIRR--LEFAELPKTISGK 422
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
121-303 |
5.07e-08 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 55.94 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 121 EGREEIvkvTFEELRQQVALFAAAMR-KMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQI 199
Cdd:PRK05620 34 AEQEQT---TFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 200 QPKLIFSVEAVVyngkehghlEKLQRVVKGLPDLQRVVLIpyvlPREKIDI--SKIPNSVFLDDFLASGTGaQAPQLEFE 277
Cdd:PRK05620 111 EDEVIVADPRLA---------EQLGEILKECPCVRAVVFI----GPSDADSaaAHMPEGIKVYSYEALLDG-RSTVYDWP 176
|
170 180
....*....|....*....|....*.
gi 21313520 278 QLPFSHPLFIMFSSGTTGAPKCMVHS 303
Cdd:PRK05620 177 ELDETTAAAICYSTGTTGAPKGVVYS 202
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
85-633 |
5.25e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 56.20 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 85 KGIADVPEWFRGSR--LNYaenlLRH---KENDRVAL--YvareGREeivkVTFEELRQQVALFAAAMRKMGVKKGDRVV 157
Cdd:PRK06178 20 AGIPREPEYPHGERplTEY----LRAwarERPQRPAIifY----GHV----ITYAELDELSDRFAALLRQRGVGAGDRVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 158 GYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEAvvyngkehghLEKLQRVVKGLPDLQRVV 237
Cdd:PRK06178 88 VFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQ----------LAPVVEQVRAETSLRHVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 238 LIPY--VLPRE-------KIDISKIPNSVFLDDFLASGTGAQAPQLEFEQLpfSHPLFIMFSSGTTGAPKCMVHSAGGTL 308
Cdd:PRK06178 158 VTSLadVLPAEptlplpdSLRAPRLAAAGAIDLLPALRACTAPVPLPPPAL--DALAALNYTGGTTGMPKGCEHTQRDMV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 309 IQHLKEHMLHGNMTSSDILLYYTTVGWmmwnwmVSALATGASLVLYDGSPLVptpnVL--WD------LVDRIGITIlgT 380
Cdd:PRK06178 236 YTAAAAYAVAVVGGEDSVFLSFLPEFW------IAGENFGLLFPLFSGATLV----LLarWDavafmaAVERYRVTR--T 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 381 GAKWLSVLEEKDMKPVETHNLHTLHTILSTGSPLKAQ-SYEYVYRCIKSSVLLGSISGGT-----DIISCFMGQN----S 450
Cdd:PRK06178 304 VMLVDNAVELMDHPRFAEYDLSSLRQVRVVSFVKKLNpDYRQRWRALTGSVLAEAAWGMTethtcDTFTAGFQDDdfdlL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 451 SIPVYKGeiqarnL---GMAVEAWDEEGKAV--WGASGELVCTKpiPCQPTHFWNDENGSKyrkayfSKFPGVWAH-GDY 524
Cdd:PRK06178 384 SQPVFVG------LpvpGTEFKICDFETGELlpLGAEGEIVVRT--PSLLKGYWNKPEATA------EALRDGWLHtGDI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 525 CRINPKtGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMASGHTFQPDlvkRIR 604
Cdd:PRK06178 450 GKIDEQ-GFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAA---ALQ 525
|
570 580 590
....*....|....*....|....*....|
gi 21313520 605 DAIRLGLSARHVPSL-ILETrgIPYTLNGK 633
Cdd:PRK06178 526 AWCRENMAVYKVPEIrIVDA--LPMTATGK 553
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
107-301 |
6.20e-08 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 55.62 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 107 RHKENDRVALYVAREGreeiVKVTFEELRQQVALFAAAMRK-MGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSP 185
Cdd:PLN02574 49 HHNHNGDTALIDSSTG----FSISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 186 DFGVNGVLDRFSQIQPKLIFSVEAVVyngkehghlEKLQRVvkGLPdlqrVVLIPYVLpreKIDISKIPNSVFLDDFLAS 265
Cdd:PLN02574 125 SSSLGEIKKRVVDCSVGLAFTSPENV---------EKLSPL--GVP----VIGVPENY---DFDSKRIEFPKFYELIKED 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 21313520 266 GTGAQAPQLEFEQLPfshplFIMFSSGTTGAPKCMV 301
Cdd:PLN02574 187 FDFVPKPVIKQDDVA-----AIMYSSGTTGASKGVV 217
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
286-633 |
1.14e-07 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. 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: 341309 [Multi-domain] Cd Length: 449 Bit Score: 54.79 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 286 FIMFSSGTTGAPKC--MVHSAGGTLIQHLKEHMlhgNMTSSDILLYyTTVgwMMWNWMVS----ALATGASLVLYDGSPL 359
Cdd:cd17654 122 YVIHTSGTTGTPKIvaVPHKCILPNIQHFRSLF---NITSEDILFL-TSP--LTFDPSVVeiflSLSSGATLLIVPTSVK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 360 VpTPNVLWDLVD-RIGITILGTGAKWLSVLEEKDMKPVETHNLHTLHTILSTGSPLKaqsyeyvyrcikSSVLLGSISG- 437
Cdd:cd17654 196 V-LPSKLADILFkRHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFP------------SLVILSSWRGk 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 438 ----------GTDIISCFMGQNSsIPVYKGEIQARN--LGMAVEAWDEEGKAVwgaSGELvctkpipcqpthFWNDENGS 505
Cdd:cd17654 263 gnrtrifniyGITEVSCWALAYK-VPEEDSPVQLGSplLGTVIEVRDQNGSEG---TGQV------------FLGGLNRV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 506 KYRKAYFSKFPGVW-AHGDYCRInpKTGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEdSLCVPQYNrdgEERVV 584
Cdd:cd17654 327 CILDDEVTVPKGTMrATGDFVTV--KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVE-SCAVTLSD---QQRLI 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 21313520 585 LFlkmasgHTFQPdLVKRIRDAIRLGLSARH-VPSLILETRGIPYTLNGK 633
Cdd:cd17654 401 AF------IVGES-SSSRIHKELQLTLLSSHaIPDTFVQIDKLPLTSHGK 443
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
112-353 |
1.25e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 54.93 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALyVAREGReeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFG--- 188
Cdd:PRK07788 64 DRAAL-IDERGT-----LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSgpq 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 189 VNGVLDRfsqiqpkliFSVEAVVYNGKEHGHLEKLQrvvkglPDLQRVVLIPYVLPREKIDISKIPNsvfLDDFLASGTG 268
Cdd:PRK07788 138 LAEVAAR---------EGVKALVYDDEFTDLLSALP------PDLGRLRAWGGNPDDDEPSGSTDET---LDDLIAGSST 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 269 AQAPqlefeqLPFSHPLFIMFSSGTTGAPKCMVHSA------GGTLIQHL----KEHMLhgnMTSSdilLYYTTvGWMMW 338
Cdd:PRK07788 200 APLP------KPPKPGGIVILTSGTTGTPKGAPRPEpsplapLAGLLSRVpfraGETTL---LPAP---MFHAT-GWAHL 266
|
250
....*....|....*
gi 21313520 339 NwmvSALATGASLVL 353
Cdd:PRK07788 267 T---LAMALGSTVVL 278
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
128-633 |
1.33e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 54.22 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 128 KVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIwsstspdfgvngvldrfsqiqpklifsv 207
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAV---------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 208 eAVVYNgkehghleklqrvvkglPDLQRVVLiPYVLPRekidiskipnsvflddflasgtgAQApqlefeQLPFSHPLFI 287
Cdd:cd05934 55 -LVPIN-----------------TALRGDEL-AYIIDH-----------------------SGA------QLVVVDPASI 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 288 MFSSGTTGAPKcmvhsagGTLIQHLKEHML------HGNMTSSDIllYYTT-----VGWMMWNWMvSALATGASLVlydg 356
Cdd:cd05934 87 LYTSGTTGPPK-------GVVITHANLTFAgyysarRFGLGEDDV--YLTVlplfhINAQAVSVL-AALSVGATLV---- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 357 spLVP--TPNVLWDLVDRIGITILGTGAKWLSVLEEKDMKPVETHnlHTLHTILSTGSPlKAQSYEYVYRCiksSVLLGS 434
Cdd:cd05934 153 --LLPrfSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRA--HRLRAAYGAPNP-PELHEEFEERF---GVRLLE 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 435 ISGGTDIISCFMGQNSSiPVYKGEIQARNLGMAVEAWDEEGKAV-WGASGELVCT-KPIPCQPTHFWNDENGSkyRKAyf 512
Cdd:cd05934 225 GYGMTETIVGVIGPRDE-PRRPGSIGRPAPGYEVRIVDDDGQELpAGEPGELVIRgLRGWGFFKGYYNMPEAT--AEA-- 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 513 skFPGVWAH-GDYCRINPKtGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMAS 591
Cdd:cd05934 300 --MRNGWFHtGDLGYRDAD-GFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRP 376
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 21313520 592 GHTFQPDlvkRIRDAIRLGLSARHVPSLILETRGIPYTLNGK 633
Cdd:cd05934 377 GETLDPE---ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEK 415
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
96-427 |
1.46e-07 |
|
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: 54.46 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 96 GSRLNYAenLLRHKE-NDRVALYVAREGreeiVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAA 174
Cdd:cd17642 17 GEQLHKA--MKRYASvPGTIAFTDAHTG----VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 175 SIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEAVvyngkehghLEKLQRVVKGLPDLQRVVLIPyvlprEKIDISKIP 254
Cdd:cd17642 91 FIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKG---------LQKVLNVQKKLKIIKTIIILD-----SKEDYKGYQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 255 NsvfLDDFLASGTGAQAPQLEFEQLPFSHP---LFIMFSSGTTGAPK--CMVHSAGGTLIQHLKEHMLhGNMTSSDILLy 329
Cdd:cd17642 157 C---LYTFITQNLPPGFNEYDFKPPSFDRDeqvALIMNSSGSTGLPKgvQLTHKNIVARFSHARDPIF-GNQIIPDTAI- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 330 YTTVGWMMWNWMVSALAT---GASLVLYdgsPLVPTPNVLWDLVD-RIGITILgtGAKWLSVLEEKDMkpVETHNLHTLH 405
Cdd:cd17642 232 LTVIPFHHGFGMFTTLGYlicGFRVVLM---YKFEEELFLRSLQDyKVQSALL--VPTLFAFFAKSTL--VDKYDLSNLH 304
|
330 340
....*....|....*....|..
gi 21313520 406 TILSTGSPLKAQSYEYVYRCIK 427
Cdd:cd17642 305 EIASGGAPLSKEVGEAVAKRFK 326
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
112-298 |
1.50e-07 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 54.60 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALYVAREGREeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNG 191
Cdd:PLN02246 38 DRPCLIDGATGRV----YTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 VLDRFSQIQPKLIFSVEAVVyngkehghlEKLqrvvKGLPDLQRVVLIPYVLPREkidiskipNSVFLDDFLASGTGAqA 271
Cdd:PLN02246 114 IAKQAKASGAKLIITQSCYV---------DKL----KGLAEDDGVTVVTIDDPPE--------GCLHFSELTQADENE-L 171
|
170 180 190
....*....|....*....|....*....|..
gi 21313520 272 PQLEFE-----QLPfshplfimFSSGTTGAPK 298
Cdd:PLN02246 172 PEVEISpddvvALP--------YSSGTTGLPK 195
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
262-633 |
1.84e-07 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 53.94 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 262 FLASGTGAQAPQLEFEQLPFshplfIMFSSGTTGAPKCMVHSAGGT--LIQHLKEhmLHGNMTSSD--ILLYYTTVGWMM 337
Cdd:cd17648 79 FILEDTGARVVITNSTDLAY-----AIYTSGTTGKPKGVLVEHGSVvnLRTSLSE--RYFGRDNGDeaVLFFSNYVFDFF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 338 WNWMVSALATGASLVLYDGSpLVPTPNVLWDLVDRIGITIL-GTGakwlSVLEEKDMKpvethNLHTLHTILSTGSPLKA 416
Cdd:cd17648 152 VEQMTLALLNGQKLVVPPDE-MRFDPDRFYAYINREKVTYLsGTP----SVLQQYDLA-----RLPHLKRVDAAGEEFTA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 417 QSYEYVYRCIKSSVLLG---SISGGTDIISCFMGQ---NSSI--PVYKGEIQARNLGMaveawdeegKAV-WGASGEL-- 485
Cdd:cd17648 222 PVFEKLRSRFAGLIINAygpTETTVTNHKRFFPGDqrfDKSLgrPVRNTKCYVLNDAM---------KRVpVGAVGELyl 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 486 --VCTKPipcqptHFWNDENGSKYR----------KAYFSKFPGVWAHGDYCRINPkTGGIIMLGRSDGTLNPNGVRFGS 553
Cdd:cd17648 293 ggDGVAR------GYLNRPELTAERflpnpfqteqERARGRNARLYKTGDLVRWLP-SGELEYLGRNDFQVKIRGQRIEP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 554 SEIYNIVEAFDEVEDSLCVPQY-----NRDGEERVVLFLKMASGHTFQPDlvkrIRDAIRLGLSARHVPSLILETRGIPY 628
Cdd:cd17648 366 GEVEAALASYPGVRECAVVAKEdasqaQSRIQKYLVGYYLPEPGHVPESD----LLSFLRAKLPRYMVPARLVRLEGIPV 441
|
....*
gi 21313520 629 TLNGK 633
Cdd:cd17648 442 TINGK 446
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
286-633 |
4.31e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.81 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 286 FIMFSSGTTGAPKCmVHSAGGTLIQHLKEHMLHGNMTSSDILLYYTTVGW--MMWNWMvSALATGASLVLYDGSplVPTP 363
Cdd:PRK12316 4698 YVIYTSGSTGRPKG-VAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFdgSHEGLY-HPLINGASVVIRDDS--LWDP 4773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 364 NVLWDLVDRIGITILG-TGAKWLSVLEEkdmkPVETHNLHTLHTILSTGSPLKAQSYEYVYRCIKS-------------- 428
Cdd:PRK12316 4774 ERLYAEIHEHRVTVLVfPPVYLQQLAEH----AERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPvylfngygptettv 4849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 429 SVLLGSISGGTDIISCFM--GQ---NSSIPVYKGEIQARNLGMAVEAW---DEEGKAVW---GASGELVCTKPIpcqpth 497
Cdd:PRK12316 4850 TVLLWKARDGDACGAAYMpiGTplgNRSGYVLDGQLNPLPVGVAGELYlggEGVARGYLerpALTAERFVPDPF------ 4923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 498 fwnDENGSK-YRKayfskfpgvwahGDYCRINPKtGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYN 576
Cdd:PRK12316 4924 ---GAPGGRlYRT------------GDLARYRAD-GVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEG 4987
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21313520 577 RDGEERVVLFL----KMASGHTFQPDLVKRIRDAIRLGLSARHVPSLILETRGIPYTLNGK 633
Cdd:PRK12316 4988 AVGKQLVGYVVpqdpALADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGK 5048
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
90-558 |
6.31e-07 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 52.47 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 90 VPEWFrgsrlNYAENLLRH-----KENDRVAL----YVAREGREeiVKVTFEELRQQVALFAAAMRKM-GVKKGDRVVGY 159
Cdd:cd05928 1 VPEYF-----NFASDVLDQwadkeKAGKRPPNpalwWVNGKGDE--VKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 160 LPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEAVVyngkehghlEKLQRVVKGLPDLQRVVLI 239
Cdd:cd05928 74 LPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELA---------PEVDSVASECPSLKTKLLV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 240 PYVlPREK-IDISKIPNSVFlDDFLASGTGAQapqlefeqlpfsHPLFIMFSSGTTGAPKCMVHSAGGTLIQHLKEHMLH 318
Cdd:cd05928 145 SEK-SRDGwLNFKELLNEAS-TEHHCVETGSQ------------EPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYW 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 319 GNMTSSDILLYYTTVGWMM--WNWMVSALATGASLVLYdgspLVPT--PNVLWDLVDRIGITILGTGAKWLSVLEEKDMK 394
Cdd:cd05928 211 LDLTASDIMWNTSDTGWIKsaWSSLFEPWIQGACVFVH----HLPRfdPLVILKTLSSYPITTFCGAPTVYRMLVQQDLS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 395 pveTHNLHTLHTILSTGSPL--------KAQSYEYVYRCIKSS--VLLGSISGGTDIISCFMGQNSsiPVYKgeiqarnl 464
Cdd:cd05928 287 ---SYKFPSLQHCVTGGEPLnpevlekwKAQTGLDIYEGYGQTetGLICANFKGMKIKPGSMGKAS--PPYD-------- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 465 gmaVEAWDEEGKAV-WGASGEL-VCTKPIpcQPTHFWNDENGSKYRKAyfSKFPG-VWAHGDYCRINpKTGGIIMLGRSD 541
Cdd:cd05928 354 ---VQIIDDNGNVLpPGTEGDIgIRVKPI--RPFGLFSGYVDNPEKTA--ATIRGdFYLTGDRGIMD-EDGYFWFMGRAD 425
|
490
....*....|....*..
gi 21313520 542 GTLNPNGVRFGSSEIYN 558
Cdd:cd05928 426 DVINSSGYRIGPFEVES 442
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
108-572 |
9.56e-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: 51.74 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 108 HKENDRVALYVAREGreeiVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPdf 187
Cdd:cd05923 12 SRAPDACAIADPARG----LRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINP-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 188 gvngvldrfsQIQPKLIfsvEAVVYNGKEHghleklqrvvkglpdlqRVVLIPYVLPREKIDISKIpNSVFLDDFLASGT 267
Cdd:cd05923 86 ----------RLKAAEL---AELIERGEMT-----------------AAVIAVDAQVMDAIFQSGV-RVLALSDLVGLGE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 268 GAQA-PQLEFEQLPFSHPLFIMFSSGTTGAPKCMV----HSAGGTLIQHLKEHMLHG--NMTSSDILLYYtTVGWmmWNW 340
Cdd:cd05923 135 PESAgPLIEDPPREPEQPAFVFYTSGTTGLPKGAVipqrAAESRVLFMSTQAGLRHGrhNVVLGLMPLYH-VIGF--FAV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 341 MVSALAtgaslvlYDGSPLVPT---PNVLWDLVDRIGITIL-GTGAKWLSVLEEKDMKPVethNLHTLHTILSTGSPLKA 416
Cdd:cd05923 212 LVAALA-------LDGTYVVVEefdPADALKLIEQERVTSLfATPTHLDALAAAAEFAGL---KLSSLRHVTFAGATMPD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 417 QSYEYVYRCIKSSVLlgSISGGTDIISCFMGQNSSI-----PVYKGEIQ-ARNLGMAVEAwdeegkAVWGASGELVCTKP 490
Cdd:cd05923 282 AVLERVNQHLPGEKV--NIYGTTEAMNSLYMRDARTgtemrPGFFSEVRiVRIGGSPDEA------LANGEEGELIVAAA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 491 IPCQPTHFWNDENGSKYRKA---YFSKFPGVWaHGDycrinpktGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVE 567
Cdd:cd05923 354 ADAAFTGYLNQPEATAKKLQdgwYRTGDVGYV-DPS--------GDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVT 424
|
....*
gi 21313520 568 DSLCV 572
Cdd:cd05923 425 EVVVI 429
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
69-317 |
3.34e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 50.23 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 69 SGIVYSRMY--DEVVDTSKGIADVPEWFRGSRLNYAENLL---RHKENDRVALYVAregreeivkVTFEELRQQVALFAA 143
Cdd:PLN02861 22 AGPVYRSIYakDGLLDLPADIDSPWQFFSDAVKKYPNNQMlgrRQVTDSKVGPYVW---------LTYKEVYDAAIRIGS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 144 AMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEAvvyngkehghleKL 223
Cdd:PLN02861 93 AIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQES------------KI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 224 QRVVKGLP----DLQRVVLIPYVLPREKIDISKIPNSVF-LDDFlasgtgAQAPQLEFEqLPFSHP---LFIMFSSGTTG 295
Cdd:PLN02861 161 SSILSCLPkcssNLKTIVSFGDVSSEQKEEAEELGVSCFsWEEF------SLMGSLDCE-LPPKQKtdiCTIMYTSGTTG 233
|
250 260
....*....|....*....|...
gi 21313520 296 APKCMVHSAGGTLIQHLK-EHML 317
Cdd:PLN02861 234 EPKGVILTNRAIIAEVLStDHLL 256
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
112-298 |
3.34e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 49.96 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALYVAREgreeivKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIwsstspdfgvnG 191
Cdd:PRK03640 17 DRTAIEFEEK------KVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAV-----------A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 VLdrfsqIQPKLifSVEAVVYNgkehghleklqrvvkgLPDLQRVVLI--PYVLPREKIDIskipnSVFLDDFLASGTGA 269
Cdd:PRK03640 80 VL-----LNTRL--SREELLWQ----------------LDDAEVKCLItdDDFEAKLIPGI-----SVKFAELMNGPKEE 131
|
170 180
....*....|....*....|....*....
gi 21313520 270 QAPQLEFeqlPFSHPLFIMFSSGTTGAPK 298
Cdd:PRK03640 132 AEIQEEF---DLDEVATIMYTSGTTGKPK 157
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
130-424 |
3.42e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 50.73 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 130 TFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFgvngvldrfsqiqPKlifsvEA 209
Cdd:PRK12316 2030 SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY-------------PA-----ER 2091
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 210 VVYNGKEHG-HLEKLQRvvkglpDLQRVVLIPYVLPREKIDISkipnsvflDDFLASGTGAQAPQLEFEQLPFshplfIM 288
Cdd:PRK12316 2092 LAYMLEDSGaALLLTQR------HLLERLPLPAGVARLPLDRD--------AEWADYPDTAPAVQLAGENLAY-----VI 2152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 289 FSSGTTGAPKCmVHSAGGTLIQHLKEHMLHGNMTSSDILLYYTTVGW--MMWNWMVSaLATGASLVLYDGSplVPTPNVL 366
Cdd:PRK12316 2153 YTSGSTGLPKG-VAVSHGALVAHCQAAGERYELSPADCELQFMSFSFdgAHEQWFHP-LLNGARVLIRDDE--LWDPEQL 2228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 21313520 367 WDLVDRIGITILGTGAKWLSVLEEKDMKPVETHNLHTLHTilsTGSPLKAQSYEYVYR 424
Cdd:PRK12316 2229 YDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCF---GGEAVPAASLRLAWE 2283
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
131-298 |
3.68e-06 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 50.08 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 131 FEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFsveav 210
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 211 vyngkehGHLEKLQRVVKGLPDLQRVVLI---PYVLPREKIDISKI---PNSVFLDDFLAsgtgAQAPQlefEQLPFSHP 284
Cdd:PRK12406 89 -------AHADLLHGLASALPAGVTVLSVptpPEIAAAYRISPALLtppAGAIDWEGWLA----QQEPY---DGPPVPQP 154
|
170
....*....|....
gi 21313520 285 LFIMFSSGTTGAPK 298
Cdd:PRK12406 155 QSMIYTSGTTGHPK 168
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
112-633 |
3.95e-06 |
|
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: 49.61 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVAlyVAREGREeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVng 191
Cdd:cd17643 2 EAVA--VVDEDRR----LTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPV-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 vlDRFSQIqpklifsveavvyngkehghleklqrvvkgLPDLQRVVLIpyvlprekidiskipnsvflddflasGTGAQa 271
Cdd:cd17643 74 --ERIAFI------------------------------LADSGPSLLL--------------------------TDPDD- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 272 pqlefeqlpfshPLFIMFSSGTTGAPKcmvhsagGTLIQH-----LKEHMLHG-NMTSSDILLYYTTVG-----WMMWnw 340
Cdd:cd17643 95 ------------LAYVIYTSGSTGRPK-------GVVVSHanvlaLFAATQRWfGFNEDDVWTLFHSYAfdfsvWEIW-- 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 341 mvSALATGASLVlydgspLVP-----TPNVLWDLVDRIGITILG-TGAKWLSVLEEKDMKPVETHNLHtlHTILStGSPL 414
Cdd:cd17643 154 --GALLHGGRLV------VVPyevarSPEDFARLLRDEGVTVLNqTPSAFYQLVEAADRDGRDPLALR--YVIFG-GEAL 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 415 KAQSYE-YVYRCIKSSVLLGSISGGTD--------IIScfmgqNSSIPVYKGEIQARNL-GMAVEAWDEEGKAVW-GASG 483
Cdd:cd17643 223 EAAMLRpWAGRFGLDRPQLVNMYGITEttvhvtfrPLD-----AADLPAAAASPIGRPLpGLRVYVLDADGRPVPpGVVG 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 484 ELVCTKPIPCQPTHFWNDENGSKYRKAYFSKfPGVWAH--GDYCRINPkTGGIIMLGRSDGTLNPNGVRFGSSEIYNIVE 561
Cdd:cd17643 298 ELYVSGAGVARGYLGRPELTAERFVANPFGG-PGSRMYrtGDLARRLP-DGELEYLGRADEQVKIRGFRIELGEIEAALA 375
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21313520 562 AFDEVEDSLCVPQYNRDGEERVVLFLKMASGhtfQPDLVKRIRDAIRLGLSARHVPSLILETRGIPYTLNGK 633
Cdd:cd17643 376 THPSVRDAAVIVREDEPGDTRLVAYVVADDG---AAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGK 444
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
124-179 |
6.11e-06 |
|
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: 49.13 E-value: 6.11e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 21313520 124 EEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAI 179
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAV 56
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
117-633 |
6.95e-06 |
|
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: 49.20 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 117 YVAREGREEIVkvTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPdfgvngvldrf 196
Cdd:cd05906 30 YIDADGSEEFQ--SYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTV----------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 197 sqiqpklifsveAVVYNGKEHGhLEKLQRVVKGLPD---LQRVVLIPYVLPREKIDISKIPNSVFLDDFLASGTGAQAPQ 273
Cdd:cd05906 97 ------------PPTYDEPNAR-LRKLRHIWQLLGSpvvLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLPQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 274 LEFEQlpfshPLFIMFSSGTTGAPKCMVHSAgGTLIQHLKEHMLHGNMTSSDILLyyttvgwmmwNWMvsALATGASLVL 353
Cdd:cd05906 164 SRPDD-----LALLMLTSGSTGFPKAVPLTH-RNILARSAGKIQHNGLTPQDVFL----------NWV--PLDHVGGLVE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 354 YDGSPL--------VPTPNVL-----W-DLVDRIGITIlgTGA------KWLSVLEEKDMKpveTHNLHTLHTILSTGSP 413
Cdd:cd05906 226 LHLRAVylgcqqvhVPTEEILadplrWlDLIDRYRVTI--TWApnfafaLLNDLLEEIEDG---TWDLSSLRYLVNAGEA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 414 LKAQS----------YEYVYRCIKSSvlLG---SISGGTDIISC----------FMGQNSSIPvykgeiqarnlGMAVEA 470
Cdd:cd05906 301 VVAKTirrllrllepYGLPPDAIRPA--FGmteTCSGVIYSRSFptydhsqaleFVSLGRPIP-----------GVSMRI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 471 WDEEGKAV-WGASGEL-VCTkpiPCQPTHFWNDENGSkyrKAYFSKfPGVWAHGDYCRInpKTGGIIMLGRSDGTLNPNG 548
Cdd:cd05906 368 VDDEGQLLpEGEVGRLqVRG---PVVTKGYYNNPEAN---AEAFTE-DGWFRTGDLGFL--DNGNLTITGRTKDTIIVNG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 549 VRFGSSEIYNIVEAFDEVEDSLCVPQYNRD---GEERVVLFLKMASGHTFQPD-LVKRIRDAIRL--GLSARHVpsLILE 622
Cdd:cd05906 439 VNYYSHEIEAAVEEVPGVEPSFTAAFAVRDpgaETEELAIFFVPEYDLQDALSeTLRAIRSVVSRevGVSPAYL--IPLP 516
|
570
....*....|.
gi 21313520 623 TRGIPYTLNGK 633
Cdd:cd05906 517 KEEIPKTSLGK 527
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
129-298 |
7.70e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 48.88 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 129 VTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVE 208
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 209 AV---VYNGKEHGHLEKL--QRVVKGLPdLQRVVLIPYVLPREKIDISKIPNSVFLdDFLASGTGAQAPQLEFEQLPFSH 283
Cdd:PRK06710 130 LVfprVTNVQSATKIEHVivTRIADFLP-FPKNLLYPFVQKKQSNLVVKVSESETI-HLWNSVEKEVNTGVEVPCDPEND 207
|
170
....*....|....*
gi 21313520 284 PLFIMFSSGTTGAPK 298
Cdd:PRK06710 208 LALLQYTGGTTGFPK 222
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
129-355 |
1.26e-05 |
|
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: 48.15 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 129 VTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIwsstspdfgVNGVLdrfsqiqpklifsve 208
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAV---------TNPIL--------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 209 aVVYNGKEHGHLekLQRVvkglpdLQRVVLIPyvlprekidiskipnSVFlddflasgtgaqaPQLEFEQLPFShPLFIM 288
Cdd:cd05903 58 -PFFREHELAFI--LRRA------KAKVFVVP---------------ERF-------------RQFDPAAMPDA-VALLL 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 289 FSSGTTGAPKCMVHSAgGTLIQHLKEHMLHGNMTSSDILLYYTTVGW---MMWNWMVSALAtGASLVLYD 355
Cdd:cd05903 100 FTSGTTGEPKGVMHSH-NTLSASIRQYAERLGLGPGDVFLVASPMAHqtgFVYGFTLPLLL-GAPVVLQD 167
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
118-353 |
1.61e-05 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 47.82 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 118 VAREGREEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFS 197
Cdd:PRK06018 29 VTRSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIIN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 198 QIQPKLIFSveavvyngkEHGHLEKLQRVVKGLPDLQRVVLIPyvlPREKIDISKIPNSVFLDDFLASGTGaqapQLEFE 277
Cdd:PRK06018 109 HAEDRVVIT---------DLTFVPILEKIADKLPSVERYVVLT---DAAHMPQTTLKNAVAYEEWIAEADG----DFAWK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 278 QLPFSHPLFIMFSSGTTGAPKCMVHSAGGTLIQHLKEHMLHG-NMTSSDILLyytTVGWMM----WNWMVSALATGASLV 352
Cdd:PRK06018 173 TFDENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANNGDAlGTSAADTML---PVVPLFhansWGIAFSAPSMGTKLV 249
|
.
gi 21313520 353 L 353
Cdd:PRK06018 250 M 250
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
112-324 |
1.93e-05 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 47.67 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALYVAREGReeivKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNG 191
Cdd:PLN02330 43 DKVAFVEAVTGK----AVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 192 VLDRFSQIQPKLIfsveavVYNGKEHGHLEKLqrvvkGLPDLqrvvlipyVLPREKIDiskipNSVFLDDFLASGTGAqA 271
Cdd:PLN02330 119 IKKQAEAAGAKLI------VTNDTNYGKVKGL-----GLPVI--------VLGEEKIE-----GAVNWKELLEAADRA-G 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21313520 272 PQLEFEQLPFSHPLFIMFSSGTTGAPKcmvhsagGTLIQHLKehmLHGNMTSS 324
Cdd:PLN02330 174 DTSDNEEILQTDLCALPFSSGTTGISK-------GVMLTHRN---LVANLCSS 216
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
112-315 |
4.01e-05 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 46.82 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALYVAReGREEIVKV-----TFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPD 186
Cdd:PRK09274 21 DQLAVAVPG-GRGADGKLaydelSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 187 FGVNGVLDRFSQIQPklifsvEAVVYNGKEHghlekLQRVVKGLPDLQRVVLIPyvlprekIDISKIPNSVFLDDFLASG 266
Cdd:PRK09274 100 MGIKNLKQCLAEAQP------DAFIGIPKAH-----LARRLFGWGKPSVRRLVT-------VGGRLLWGGTTLATLLRDG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21313520 267 TGAqapqlEFE--QLPFSHPLFIMFSSGTTGAPKCMVHSAGGTL--IQHLKEH 315
Cdd:PRK09274 162 AAA-----PFPmaDLAPDDMAAILFTSGSTGTPKGVVYTHGMFEaqIEALRED 209
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
93-179 |
1.03e-04 |
|
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: 45.40 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 93 WFRGSRLnyAENLLRHKEN--DRVALyVAREGReeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAM 170
Cdd:cd05920 11 YWQDEPL--GDLLARSAARhpDRIAV-VDGDRR-----LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLF 82
|
....*....
gi 21313520 171 LAAASIGAI 179
Cdd:cd05920 83 FALLRLGAV 91
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
129-179 |
1.19e-04 |
|
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: 45.16 E-value: 1.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 21313520 129 VTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAI 179
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAV 52
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
112-363 |
1.29e-04 |
|
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: 45.12 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVALyVAREGREEIVKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSA-HAVEAmLAAASIGAIWSSTSPDFGVN 190
Cdd:cd05921 10 DRTWL-AEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIeHALMA-LAAMYAGVPAAPVSPAYSLM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 191 GV-LDR----FSQIQPKLIFSVEAvvyngkehghlEKLQRVVKGLPDLQRVVLIPYVLPREKidiskipNSVFLDDFLAS 265
Cdd:cd05921 88 SQdLAKlkhlFELLKPGLVFAQDA-----------APFARALAAIFPLGTPLVVSRNAVAGR-------GAISFAELAAT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 266 GTGAQAPQLEFEQLPFSHPLFiMFSSGTTGAPKCMVHSaggtliqhlkehmlHGNMTSSDILLYYT----------TVGW 335
Cdd:cd05921 150 PPTAAVDAAFAAVGPDTVAKF-LFTSGSTGLPKAVINT--------------QRMLCANQAMLEQTypffgeeppvLVDW 214
|
250 260 270
....*....|....*....|....*....|...
gi 21313520 336 MMWNWMVSALAtGASLVLYDGSPLV-----PTP 363
Cdd:cd05921 215 LPWNHTFGGNH-NFNLVLYNGGTLYiddgkPMP 246
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
129-353 |
1.37e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 44.95 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 129 VTFEELRQQVALFAAAM-RKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSP------------DFGVNGVL-- 193
Cdd:PRK08314 36 ISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPmnreeelahyvtDSGARVAIvg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 194 -DRFSQIQPklifsveavvYNGKEHghlekLQRVVKG-----LPDLQRVVLIPYVLPREKIDISKIPNSVFLDDFLASgt 267
Cdd:PRK08314 116 sELAPKVAP----------AVGNLR-----LRHVIVAqysdyLPAEPEIAVPAWLRAEPPLQALAPGGVVAWKEALAA-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 268 GAQAPQLEfeqlpfSHP--LFIM-FSSGTTGAPK-CMvHSAgGTLIQHLKEHMLHGNMTSSDILL----YYTTVGwmMWN 339
Cdd:PRK08314 179 GLAPPPHT------AGPddLAVLpYTSGTTGVPKgCM-HTH-RTVMANAVGSVLWSNSTPESVVLavlpLFHVTG--MVH 248
|
250
....*....|....
gi 21313520 340 WMVSALATGASLVL 353
Cdd:PRK08314 249 SMNAPIYAGATVVL 262
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
115-173 |
2.24e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 44.12 E-value: 2.24e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 21313520 115 ALYVAREGREeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAA 173
Cdd:PRK08276 2 AVIMAPSGEV----VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAA 56
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
282-417 |
3.41e-04 |
|
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: 43.40 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 282 SHPLFIMFSSGTTGAPKCMV--HSAGGTLIQHLKEHMlhgNMTSSDILLYYTTVGW--MMWNWmVSALATGASLVLYDGS 357
Cdd:cd17652 93 DNLAYVIYTSGSTGRPKGVVvtHRGLANLAAAQIAAF---DVGPGSRVLQFASPSFdaSVWEL-LMALLAGATLVLAPAE 168
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21313520 358 PLVPtPNVLWDLVDRIGIT--ILGTGAkwLSVLEEKDMKPvethnlhtLHTILSTGSPLKAQ 417
Cdd:cd17652 169 ELLP-GEPLADLLREHRIThvTLPPAA--LAALPPDDLPD--------LRTLVVAGEACPAE 219
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
532-633 |
4.62e-04 |
|
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: 42.78 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 532 GGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMASghtfqpdLVKR-IRDAIRLG 610
Cdd:cd17633 222 GYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDK-------LTYKqLKRFLKQK 294
|
90 100
....*....|....*....|...
gi 21313520 611 LSARHVPSLILETRGIPYTLNGK 633
Cdd:cd17633 295 LSRYEIPKKIIFVDSLPYTSSGK 317
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
112-348 |
4.82e-04 |
|
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: 43.21 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 112 DRVAL-YVAREGR-------------EEIVKVTFEELRQQV-ALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASI 176
Cdd:cd17632 37 DRPALgQRATELVtdpatgrttlrllPRFETITYAELWERVgAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 177 GAIWSSTSPDFGVNGVLDRFSQIQPKLIfsveAVvyngkEHGHLEKLQRVVKGLPDLQRVVLIPYVLP----REKIDISK 252
Cdd:cd17632 117 GAVSVPLQAGASAAQLAPILAETEPRLL----AV-----SAEHLDLAVEAVLEGGTPPRLVVFDHRPEvdahRAALESAR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 253 -----IPNSVFLDDFLASGTGAQAPQLEFEQLPFSHPL-FIMFSSGTTGAPKCMVHSAGGTLIQHLKEHMLHGNMTSSDI 326
Cdd:cd17632 188 erlaaVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDDPLaLLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASI 267
|
250 260
....*....|....*....|...
gi 21313520 327 LLYYTTVGWMMW-NWMVSALATG 348
Cdd:cd17632 268 TLNFMPMSHIAGrISLYGTLARG 290
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
128-179 |
5.66e-04 |
|
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: 42.72 E-value: 5.66e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 21313520 128 KVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAI 179
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAE 52
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
128-179 |
6.36e-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: 42.73 E-value: 6.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 21313520 128 KVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAI 179
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV 54
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
105-298 |
9.23e-04 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 42.28 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 105 LLRHKENDRVALyVAREGReeivkVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAH---AVEAMLAA--ASIGAI 179
Cdd:PRK10946 31 LTRHAASDAIAV-ICGERQ-----FSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEfyiTFFALLKLgvAPVNAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 180 WSSTSPDfgvngvLDRF-SQIQPKL-IFSVEAVVYNGKEHghlekLQRVVKGLPDLQRVVLIPYVLPREKIDISKIPNsv 257
Cdd:PRK10946 105 FSHQRSE------LNAYaSQIEPALlIADRQHALFSDDDF-----LNTLVAEHSSLRVVLLLNDDGEHSLDDAINHPA-- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 21313520 258 flDDFLASGTGAQapQLEFEQLpfshplfimfSSGTTGAPK 298
Cdd:PRK10946 172 --EDFTATPSPAD--EVAFFQL----------SGGSTGTPK 198
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
130-440 |
9.68e-04 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 42.43 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 130 TFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEA 209
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 210 VvyngKEHGHLEKLQRVVKGLPDLQRVVLIPYVLPREkidiskipNSVFLDDFLASGTgaqapqlefeqlPFSHPLF--- 286
Cdd:PRK06087 131 F----KQTRPVDLILPLQNQLPQLQQIVGVDKLAPAT--------SSLSLSQIIADYE------------PLTTAITthg 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 287 -----IMFSSGTTGAPKcmvhsagGTLIQhlkehmlHGNMTSSDilLYYTTVGWMMWN---WMVSAL--AT--------- 347
Cdd:PRK06087 187 delaaVLFTSGTEGLPK-------GVMLT-------HNNILASE--RAYCARLNLTWQdvfMMPAPLghATgflhgvtap 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 348 ---GASLVLYDgsplVPTPNVLWDLVDRIGIT-ILGTGAKWLSVLEEKDMKPVEthnLHTLHTILSTGSPLKAqsyEYVY 423
Cdd:PRK06087 251 fliGARSVLLD----IFTPDACLALLEQQRCTcMLGATPFIYDLLNLLEKQPAD---LSALRFFLCGGTTIPK---KVAR 320
|
330
....*....|....*..
gi 21313520 424 RCIKSSVLLGSISGGTD 440
Cdd:PRK06087 321 ECQQRGIKLLSVYGSTE 337
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
70-298 |
1.51e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 41.93 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 70 GIVYSRMY--DEVVDTSKGIADVPEWFRGSRLNYAENLL---RHKENDRVALYVARegreeivkvTFEELRQQVALFAAA 144
Cdd:PLN02614 25 GPVYRSIFakDGFPNPIEGMDSCWDVFRMSVEKYPNNPMlgrREIVDGKPGKYVWQ---------TYQEVYDIVIKLGNS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 145 MRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFSVEavvyngkehghlEKLQ 224
Cdd:PLN02614 96 LRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEE------------KKIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 225 RVVKGLPD----LQRVVLIPYVLPREKIDISKIPNSVF-LDDFLASGTGAQApqlefeQLPFSHP---LFIMFSSGTTGA 296
Cdd:PLN02614 164 ELFKTCPNsteyMKTVVSFGGVSREQKEEAETFGLVIYaWDEFLKLGEGKQY------DLPIKKKsdiCTIMYTSGTTGD 237
|
..
gi 21313520 297 PK 298
Cdd:PLN02614 238 PK 239
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
522-633 |
2.88e-03 |
|
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: 40.76 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 522 GDYCRINPKtGGIIMLGRSDGTLNPNGVRFGSSEIYNIVEAFDEVEDSLCVPQYNRDGEERVVLFLKMASGhtfQPDLVK 601
Cdd:cd12115 334 GDLVRWRPD-GLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPG---AAGLVE 409
|
90 100 110
....*....|....*....|....*....|..
gi 21313520 602 RIRDAIRLGLSARHVPSLILETRGIPYTLNGK 633
Cdd:cd12115 410 DLRRHLGTRLPAYMVPSRFVRLDALPLTPNGK 441
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
127-219 |
6.37e-03 |
|
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: 39.73 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313520 127 VKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAIWSSTSPDFGVNGVLDRFSQIQPKLIFS 206
Cdd:cd05914 6 EPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90
....*....|....*...
gi 21313520 207 -----VEAVVYNGKEHGH 219
Cdd:cd05914 86 sdeddVALINYTSGTTGN 103
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
127-179 |
6.84e-03 |
|
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: 39.26 E-value: 6.84e-03
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gi 21313520 127 VKVTFEELRQQVALFAAAMRKMGVKKGDRVVGYLPNSAHAVEAMLAAASIGAI 179
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAV 56
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