|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
5-652 |
0e+00 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 1069.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 5 TPLWVPSQDRIKASNLNQFIEHINMQ-GEAIESYSQLHLWSVAERKQFWLEVWQFCDVIGFRGNCIYGEGiarwDDFTAA 83
Cdd:PRK03584 3 DPLWTPSAERIAASRMTAFIRWLAARrGLSFDDYAALWRWSVEDLEAFWQSVWDFFGVIGSTPYTVVLAG----RRMPGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 84 RdtiWFPQAQLNYAENLLSYAfqQPEGIAVWFKNENGQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETL 163
Cdd:PRK03584 79 R---WFPGARLNYAENLLRHR--RDDRPAIIFRGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 164 VAMLATTSLGAVWTSTSPDFGVDSVVERFGQVQPKILFCCNGYTFNGKTHLMEEKNGQIADAISSLHNICQIEYLHQRSl 243
Cdd:PRK03584 154 VAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDRRAKVAELRAALPSLEHVVVVPYLGPAA- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 244 TADFNDAFSDWNAILASYLPRGLRYERVSFNDPLFILYSSGTTGKPKCIAHSVGGTILNHLKEHQLHCDIQPGDRVFYYT 323
Cdd:PRK03584 233 AAAALPGALLWEDFLAPAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDRFFWYT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 324 TCGWMMWNWHVSALASGATLVIYDGSPMYPQPGVLWDLAEEANITLFGTSAKYLEALQKTAYSPSDYYPLSSLKTLCSTG 403
Cdd:PRK03584 313 TCGWMMWNWLVSGLLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 404 SVLYPKQFDYVYANIKADLHLASISGGTDICGCFVLGNPISPVYRGECQGAGLGLDVAVFNDLGQPVIQQRGELVCRNSF 483
Cdd:PRK03584 393 SPLPPEGFDWVYEHVKADVWLASISGGTDICSCFVGGNPLLPVYRGEIQCRGLGMAVEAWDEDGRPVVGEVGELVCTKPF 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 484 PNQPIGFWHD-DGQRYHDAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAV 562
Cdd:PRK03584 473 PSMPLGFWNDpDGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVI 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 563 GQKI-DNDEQIILFVQLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLVELAVKQLLHGETVK--- 638
Cdd:PRK03584 553 GQEWpDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVELPVKKLLHGRPVKkav 632
|
650
....*....|....
gi 1067526515 639 NLGAIANPHVLEEI 652
Cdd:PRK03584 633 NRDALANPEALDWF 646
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
20-650 |
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: 850.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 20 LNQFIEHIN-MQGEAIESYSQLHLWSVAERKQFWLEVWQFCDVIGFRGNCIYGEGIARWDDftaARdtiWFPQAQLNYAE 98
Cdd:cd05943 1 MDAFRRWVNaRHGLSLADYAALHRWSVDDPGAFWAAVWDFSGVRGSKPYDVVVVSGRIMPG---AR---WFPGARLNYAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 99 NLLSYAfqQPEGIAVWFKNENGQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTS 178
Cdd:cd05943 75 NLLRHA--DADDPAAIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 179 TSPDFGVDSVVERFGQVQPKILFCCNGYTFNGKTHLMEEKNGQIADAISSLHNICQIEYLHQR-SLTADFNDAFSDWNAI 257
Cdd:cd05943 153 CSPDFGVPGVLDRFGQIEPKVLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVVVVPYTVAAgQPDLSKIAKALTLEDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 258 LASYLPRGLRYERVSFNDPLFILYSSGTTGKPKCIAHSVGGTILNHLKEHQLHCDIQPGDRVFYYTTCGWMMWNWHVSAL 337
Cdd:cd05943 233 LATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNWLVSGL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 338 ASGATLVIYDGSPMYPQPGVLWDLAEEANITLFGTSAKYLEALQKTAYSPSDYYPLSSLKTLCSTGSVLYPKQFDYVYAN 417
Cdd:cd05943 313 AVGATIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 418 IKADLHLASISGGTDICGCFVLGNPISPVYRGECQGAGLGLDVAVFNDLGQPVIQQRGELVCRNSFPNQPIGFWHD-DGQ 496
Cdd:cd05943 393 IKPDVLLASISGGTDIISCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPVWGEKGELVCTKPFPSMPVGFWNDpDGS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 497 RYHDAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKI-DNDEQIILF 575
Cdd:cd05943 473 RYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWkDGDERVILF 552
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067526515 576 VQLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLVELAVKQLLHGETVKNLGAIANPHVLE 650
Cdd:cd05943 553 VKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGRPVKNAGALANPESLD 627
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
6-650 |
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: 739.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 6 PLWVPSQDRIKASNLNQFIEHINMQ-GEAIESYSQLHLWSVAERKQFWLEVWQFCDVIGFRGNciygegiARWDDFTAAR 84
Cdd:TIGR01217 5 PLWQPDAQRIAQARMTRFQAWAGEHhGAAEGGYDALHRWSVDELDTFWKAVWEWFDVRFSTPC-------ARVVDDRTMP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 85 DTIWFPQAQLNYAENLLSYAFQQPegiAVWFKNENGQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLV 164
Cdd:TIGR01217 78 GAQWFPGARLNYAENLLRAAGTEP---ALLYVDETHEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 165 AMLATTSLGAVWTSTSPDFGVDSVVERFGQVQPKILFCCNGYTFNGKTHLMEEKNGQIADAISSLHNICQIEYLHQRSLT 244
Cdd:TIGR01217 155 AMLATASVGAIWSSCSPDFGARGVLDRFQQIEPKLLFTVDGYRYNGKEHDRRDKVAEVRKELPTLRAVVHIPYLGPRETE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 245 ADFNDAFSDWNAILASYLPRGLRYERVSFNDPLFILYSSGTTGKPKCIAHSVGGTILNHLKEHQLHCDIQPGDRVFYYTT 324
Cdd:TIGR01217 235 APKIDGALDLEDFTAAAQAAELVFEQLPFDHPLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 325 CGWMMWNWHVSALASGATLVIYDGSPMYPQPGVLWDLAEEANITLFGTSAKYLEALQKTAYSPSDYYPLSSLKTLCSTGS 404
Cdd:TIGR01217 315 TGWMMWNWLVSGLATGATLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVASTGS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 405 VLYPKQFDYVYANIKADLHLASISGGTDICGCFVLGNPISPVYRGECQGAGLGLDVAVFNDLGQPVIQQRGELVCRNSFP 484
Cdd:TIGR01217 395 PLPPDGFRWVYDEIKADVWLASISGGTDICSCFAGANPTLPVHIGEIQAPGLGTAVQSWDPEGKPVTGEVGELVCTNPMP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 485 NQPIGFWHD-DGQRYHDAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVG 563
Cdd:TIGR01217 475 SMPIRFWNDpDGSKYRDAYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIG 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 564 Q-KIDNDEQIILFVQLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLVELAVKQLLHGETVKNLGA 642
Cdd:TIGR01217 555 QeQPDGGYRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKRVLQGTPVDNPGA 634
|
....*...
gi 1067526515 643 IANPHVLE 650
Cdd:TIGR01217 635 IDNPELLD 642
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
88-652 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 620.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 88 WFPQAQLNYAENLL-SYAFQQPEGIAVWFKNENGQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAM 166
Cdd:COG0365 2 WFVGGRLNIAYNCLdRHAEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 167 LATTSLGAVWTSTSPDFGVDSVVERFGQVQPKILFCCNGYTFNGKTHLMEEKNGQIADAISSLHNIcqieYLHQRSLTAD 246
Cdd:COG0365 82 LACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSLEHV----IVVGRTGADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 247 FNDAFSDWNAILASyLPRGLRYERVSFNDPLFILYSSGTTGKPKCIAHSVGGTILNHLKEHQLHCDIQPGDRVFYYTTCG 326
Cdd:COG0365 158 PMEGDLDWDELLAA-ASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 327 WMM--WNWHVSALASGATLVIYDGSPMYPQPGVLWDLAEEANITLFGTSAKYLEALQKTAYSPSDYYPLSSLKTLCSTGS 404
Cdd:COG0365 237 WATghSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 405 VLYPKQFDYVYANIKadLHLASISGGTDICGCFVLGNPISPVYRGECQGAGLGLDVAVFNDLGQPVIQ-QRGELVCRNSF 483
Cdd:COG0365 317 PLNPEVWEWWYEAVG--VPIVDGWGQTETGGIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPgEEGELVIKGPW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 484 PNQPIGFWHDDgQRYHDAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVG 563
Cdd:COG0365 395 PGMFRGYWNDP-ERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 564 QKID-NDEQIILFVQLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLVELAVKQLLHGETVKNLGA 642
Cdd:COG0365 474 VPDEiRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRPLGDTST 553
|
570
....*....|
gi 1067526515 643 IANPHVLEEI 652
Cdd:COG0365 554 LEDPEALDEI 563
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
29-646 |
9.49e-105 |
|
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: 330.61 E-value: 9.49e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 29 MQGEAIESYSQLHLWSVAERKQFWLEvwqFCDVIGfrgnciygegIARWDDFTAARD-------TIWFPQAQLNYAENLL 101
Cdd:cd05968 1 MASLGIPDLEAFLERSAEDNAWFWGE---FVKDVG----------IEWYEPPYQTLDlsggkpwAAWFVGGRMNIVEQLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 102 -SYAFQQPEGIAVWFKNENGQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTS 180
Cdd:cd05968 68 dKWLADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 181 PDFGVDSVVERFGQVQPKILFCCNGYTFNGKTHLMEEKNGQIADAISSLHNICQIEYLHQRSLTADFNDAFsdWNAILAS 260
Cdd:cd05968 148 SGFGKEAAATRLQDAEAKALITADGFTRRGREVNLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLS--YDEEKET 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 261 YLPRglrYERVSFNDPLFILYSSGTTGKPKCIAHSVGGTILNHLKEHQLHCDIQPGDRVFYYTTCGWMMWNWHV-SALAS 339
Cdd:cd05968 226 AGDG---AERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIfGGLIL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 340 GATLVIYDGSPMYPQPGVLWDLAEEANITLFGTSAKYLEALQKTAYSPSDYYPLSSLKTLCSTGSVLYPKQFDYVYANI- 418
Cdd:cd05968 303 GATMVLYDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVg 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 419 KADLHLASISGGTDICGCFVLGNPISPVYRGECQGAGLGLDVAVFNDLGQPVIQQRGELVCRNSFPNQPIGFWHDDgQRY 498
Cdd:cd05968 383 KGRNPIINYSGGTEISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARPEVGELVLLAPWPGMTRGFWRDE-DRY 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 499 HDAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKID-NDEQIILFVQ 577
Cdd:cd05968 462 LETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPvKGEAIVCFVV 541
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067526515 578 LAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLVELAVKQLLHGETVKNLGAIANP 646
Cdd:cd05968 542 LKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKELGDLSSLENP 610
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
51-624 |
8.99e-83 |
|
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: 272.53 E-value: 8.99e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 51 FWLEVWQFCDVIGfrgnciYGEGIARWDDFTAARDTIWFPQAQLNYAENLLSYAFQQ-PEGIAVWFKNENG-QSKKLTWQ 128
Cdd:cd17634 15 FWGEAGKILDWIT------PYQKVKNTSFAPGAPSIKWFEDATLNLAANALDRHLREnGDRTAIIYEGDDTsQSRTISYR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 129 QLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDSVVERFGQVQPKILFCCNGYTF 208
Cdd:cd17634 89 ELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 209 NGKTHLMEEKNGQIADA-ISSLHNIC-----QIEYlhQRSLTADFndafsDWNAILASYLPRgLRYERVSFNDPLFILYS 282
Cdd:cd17634 169 AGRSVPLKKNVDDALNPnVTSVEHVIvlkrtGSDI--DWQEGRDL-----WWRDLIAKASPE-HQPEAMNAEDPLFILYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 283 SGTTGKPKCIAHSVGGTILnHLKEHQLHC-DIQPGDRVFYYTTCGWMMWN-WHV-SALASGATLVIYDGSPMYPQPGVLW 359
Cdd:cd17634 241 SGTTGKPKGVLHTTGGYLV-YAATTMKYVfDYGPGDIYWCTADVGWVTGHsYLLyGPLACGATTLLYEGVPNWPTPARMW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 360 DLAEEANITLFGTSAKYLEALQKTAYSPSDYYPLSSLKTLCSTGSVLYPKQFDYVYANI-KADLHLASISGGTDICGCFV 438
Cdd:cd17634 320 QVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIgKEKCPVVDTWWQTETGGFMI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 439 LGNPISPVYRGECQ-GAGLGLDVAVFNDLGQPV-IQQRGELVCRNSFPNQPIGFWHDDgQRYHDAYWSKFSGVWHHGDEV 516
Cdd:cd17634 400 TPLPGAIELKAGSAtRPVFGVQPAVVDNEGHPQpGGTEGNLVITDPWPGQTRTLFGDH-ERFEQTYFSTFKGMYFSGDGA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 517 EWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKIDNDEQ-IILFVQLAPQCELNTLLVNTIKQR 595
Cdd:cd17634 479 RRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQaPYAYVVLNHGVEPSPELYAELRNW 558
|
570 580
....*....|....*....|....*....
gi 1067526515 596 LRENCSPRHVPAQIHSISDVPRTKSGKLV 624
Cdd:cd17634 559 VRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
35-641 |
3.97e-72 |
|
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: 244.39 E-value: 3.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 35 ESYSQLHLWSVAERKQFWLEV-----W--QFCDVigfrgnciygegiarWDDFTAARDTIWFPQAQLNYAENLLSY-AFQ 106
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIakeldWfkPWDKV---------------LDWSKGPPFIKWFEGGKLNISYNCLDRhLKE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 107 QPEGIA-VWFKNENGQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGV 185
Cdd:cd05966 66 RGDKVAiIWEGDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 186 DSVVERFGQVQPKILFCCNGYTFNGKThlMEEKngQIADAisSLHNICQIEY---LHQRSLTADFNDAFS-DWNAILASY 261
Cdd:cd05966 146 ESLADRINDAQCKLVITADGGYRGGKV--IPLK--EIVDE--ALEKCPSVEKvlvVKRTGGEVPMTEGRDlWWHDLMAKQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 262 LPrglrY---ERVSFNDPLFILYSSGTTGKPKCIAHSVGGTILNHLKEHQLHCDIQPGDRVFYYTTCGWMMWNWHV--SA 336
Cdd:cd05966 220 SP----EcepEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIvyGP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 337 LASGATLVIYDGSPMYPQPGVLWDLAEEANITLFGTSAKYLEALQKTAYSPSDYYPLSSLKTLCSTGSVLYPKQFDYVYA 416
Cdd:cd05966 296 LANGATTVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 417 NIK------ADLHLASISGG---TDICGCFvlgnPISPvyrGECQGAGLGLDVAVFNDLGQPV-IQQRGELVCRNSFPNQ 486
Cdd:cd05966 376 VIGkercpiVDTWWQTETGGimiTPLPGAT----PLKP---GSATRPFFGIEPAILDEEGNEVeGEVEGYLVIKRPWPGM 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 487 PIGFWHDDgQRYHDAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGqkI 566
Cdd:cd05966 449 ARTIYGDH-ERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVG--R 525
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067526515 567 DND---EQIILFVQLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLVELAVKQLLHGEtvKNLG 641
Cdd:cd05966 526 PHDikgEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGE--EELG 601
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
35-655 |
8.97e-59 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 209.37 E-value: 8.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 35 ESYSQLHLWSVAERKQFWLEVW-QFCDVIGFRGNCIYGEGIarwdDFTAARDTI-WFPQAQLNYAENLLSYAFQQPEG-- 110
Cdd:PLN02654 30 QQYMEMYKRSVDDPAGFWSDIAsQFYWKQKWEGDEVCSENL----DVRKGPISIeWFKGGKTNICYNCLDRNVEAGNGdk 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 111 IAV-WFKNENGQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDSVV 189
Cdd:PLN02654 106 IAIyWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 190 ERFGQVQPKILFCCNGYTFNGKTHLMEE----------KNGQIADAISSLHNicQIEYLHQRSLTADFNDAFsdWNAILA 259
Cdd:PLN02654 186 QRIVDCKPKVVITCNAVKRGPKTINLKDivdaaldesaKNGVSVGICLTYEN--QLAMKREDTKWQEGRDVW--WQDVVP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 260 SYlPRGLRYERVSFNDPLFILYSSGTTGKPKCIAHSVGGTILNHLKEHQLHCDIQPGDRVFYYTTCGWMMWNWHVS--AL 337
Cdd:PLN02654 262 NY-PTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTygPM 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 338 ASGATLVIYDGSPMYPQPGVLWDLAEEANITLFGTSAKYLEALQKTAYSPSDYYPLSSLKTLCSTGSVLYPKQFDYVYAN 417
Cdd:PLN02654 341 LNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNV 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 418 IK------ADLHLASISGG---TDICGCFvlgnPISPvyrGECQGAGLGLDVAVFNDLGQPVIQQ-RGELVCRNSFPNqP 487
Cdd:PLN02654 421 VGdsrcpiSDTWWQTETGGfmiTPLPGAW----PQKP---GSATFPFFGVQPVIVDEKGKEIEGEcSGYLCVKKSWPG-A 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 488 IGFWHDDGQRYHDAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGqkID 567
Cdd:PLN02654 493 FRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVG--IE 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 568 ND---EQIILFVQLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGK-----LVELAVKQLlhgETVKN 639
Cdd:PLN02654 571 HEvkgQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKimrriLRKIASRQL---DELGD 647
|
650
....*....|....*.
gi 1067526515 640 LGAIANPHVLEEIHAL 655
Cdd:PLN02654 648 TSTLADPGVVDQLIAL 663
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
37-652 |
2.37e-58 |
|
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: 207.17 E-value: 2.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 37 YSQLHLWSVAERKQFWLEVwqfcdvigfrgnciyGEGIArWD-------DFTAARDTIWFPQAQLNYAENLLSYAFQQPE 109
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQ---------------ARLID-WFkppekilDNSNPPFTRWFVGGRLNTCYNALDRHVEAGR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 110 G--IAV-WFKNENGQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVD 186
Cdd:cd05967 65 GdqIALiYDSPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 187 SVVERFGQVQPKILFCCNGYTFNGK----THLMEEKngqIADAISSLHNICQIeylhQRSL-TADFNDAFS--DWNAILA 259
Cdd:cd05967 145 ELASRIDDAKPKLIVTASCGIEPGKvvpyKPLLDKA---LELSGHKPHHVLVL----NRPQvPADLTKPGRdlDWSELLA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 260 SYLPRGlrYERVSFNDPLFILYSSGTTGKPKCIAHSVGGTILnHLKEHQLHC-DIQPGDRVFYYTTCGWMMWNWHV--SA 336
Cdd:cd05967 218 KAEPVD--CVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAV-ALNWSMRNIyGIKPGDVWWAASDVGWVVGHSYIvyGP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 337 LASGATLVIYDGSPM-YPQPGVLWDLAEEANITLFGTSAKYLEALQK--TAYSPSDYYPLSSLKTLCSTGSVLYPKQFDY 413
Cdd:cd05967 295 LLHGATTVLYEGKPVgTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKedPDGKYIKKYDLSSLRTLFLAGERLDPPTLEW 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 414 VYANIKADL--HLASISGGTDICGCFV--------LGNPISPVYrgecqgaglGLDVAVFNDLGQPV-IQQRGELVCRNS 482
Cdd:cd05967 375 AENTLGVPVidHWWQTETGWPITANPVgleplpikAGSPGKPVP---------GYQVQVLDEDGEPVgPNELGNIVIKLP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 483 FPnqP---IGFWHDDGqRYHDAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDS 559
Cdd:cd05967 446 LP--PgclLTLWKNDE-RFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAEC 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 560 VAVGQKIDNDEQIIL-FVQLAPQCELNT-LLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLVELAVKQLLHGETV 637
Cdd:cd05967 523 AVVGVRDELKGQVPLgLVVLKEGVKITAeELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDY 602
|
650
....*....|....*
gi 1067526515 638 KNLGAIANPHVLEEI 652
Cdd:cd05967 603 TIPSTIEDPSVLDEI 617
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
26-652 |
1.02e-50 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 186.50 E-value: 1.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 26 HINMqgeaiESYSQLHLWSVAERKQFWLEVwqfcdvigfrGNCIygEGIARWD-DFTAARDTI-WFPQAQLNYAENLLS- 102
Cdd:PRK00174 13 LIDM-----EQYKALYQESVEDPEGFWAEQ----------AKRL--DWFKPFDtVLDWNAPFIkWFEDGELNVSYNCLDr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 103 YAFQQPEGIAVWFKNEN-GQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVwtsTSP 181
Cdd:PRK00174 76 HLKTRGDKVAIIWEGDDpGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAV---HSV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 182 DFG---VDSVVERFGQVQPKILFCCNGYTFNGKTHLMEEkngqIAD-AISSLHNI----------CQIEYLHQRSLtaDF 247
Cdd:PRK00174 153 VFGgfsAEALADRIIDAGAKLVITADEGVRGGKPIPLKA----NVDeALANCPSVekvivvrrtgGDVDWVEGRDL--WW 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 248 NDAFSDWNAILASylprglryERVSFNDPLFILYSSGTTGKPKCIAHSVGGTILNHLKEHQLHCDIQPGDrVFYYTT-CG 326
Cdd:PRK00174 227 HELVAGASDECEP--------EPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGD-VYWCTAdVG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 327 WmmwnwhVSA--------LASGATLVIYDGSPMYPQPGVLWDLAEEANITLFGTSAKYLEALQKTAYSPSDYYPLSSLKT 398
Cdd:PRK00174 298 W------VTGhsyivygpLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 399 LCSTGSVLYPKQFDYVYANIkadlhlasisgGTDIC-----------GCFVL-----GNPISPvyrGECQGAGLGLDVAV 462
Cdd:PRK00174 372 LGSVGEPINPEAWEWYYKVV-----------GGERCpivdtwwqtetGGIMItplpgATPLKP---GSATRPLPGIQPAV 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 463 FNDLGQPV-IQQRGELVCRNSFPNQPIGFWHDDgQRYHDAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRI 541
Cdd:PRK00174 438 VDEEGNPLeGGEGGNLVIKDPWPGMMRTIYGDH-ERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRL 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 542 GTAEIYQQVNSFPEIQDSVAVGqKIDN--DEQIILFVQLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTK 619
Cdd:PRK00174 517 GTAEIESALVAHPKVAEAAVVG-RPDDikGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTR 595
|
650 660 670
....*....|....*....|....*....|....*.
gi 1067526515 620 SGKLVELAVKQLLHGETvkNLGAI---ANPHVLEEI 652
Cdd:PRK00174 596 SGKIMRRILRKIAEGEE--ILGDTstlADPSVVEKL 629
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
275-622 |
8.97e-49 |
|
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: 174.01 E-value: 8.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 275 DPLFILYSSGTTGKPKCIAHSvGGTILNHLKEHQLHCDIQPGDRVFYYT-TCGWMMWNWHVSALASGATLVIYDGSPmyp 353
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLS-HRNLLAAAAALAASGGLTEGDVFLSTLpLFHIGGLFGLLGALLAGGTVVLLPKFD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 354 qPGVLWDLAEEANITLFGTSAKYLEALQKTAYSPSdyYPLSSLKTLCSTGSVLYPKQFDYVYANIKADLHlaSISGGTDI 433
Cdd:cd04433 77 -PEAALELIEREKVTILLGVPTLLARLLKAPESAG--YDLSSLRALVSGGAPLPPELLERFEEAPGIKLV--NGYGLTET 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 434 CGCFVLGNPISPVYRGECQG-AGLGLDVAVFNDLGQPV-IQQRGELVCRNsfPNQPIGFWHDDGQRYHDaywsKFSGVWH 511
Cdd:cd04433 152 GGTVATGPPDDDARKPGSVGrPVPGVEVRIVDPDGGELpPGEIGELVVRG--PSVMKGYWNNPEATAAV----DEDGWYR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 512 HGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGqkIDND---EQIILFVQLAPQCelnTLL 588
Cdd:cd04433 226 TGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVG--VPDPewgERVVAVVVLRPGA---DLD 300
|
330 340 350
....*....|....*....|....*....|....
gi 1067526515 589 VNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGK 622
Cdd:cd04433 301 AEELRAHVRERLAPYKVPRRVVFVDALPRTASGK 334
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
97-623 |
2.60e-40 |
|
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: 153.43 E-value: 2.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 97 AENLLSYAFQQPEGIAVWFknengQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVW 176
Cdd:COG0318 2 ADLLRRAAARHPDRPALVF-----GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 177 TSTSPDFGVDSVVERFGQVQPKILFCCngytfngkthlmeekngqiadaisslhnicqieylhqrsltadfndafsdwna 256
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALVTA----------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 257 ilasylprglryervsfndplFILYSSGTTGKPKCIAHSvGGTILNHLKEHQLHCDIQPGDRV-----FYYTTcGWMMWN 331
Cdd:COG0318 104 ---------------------LILYTSGTTGRPKGVMLT-HRNLLANAAAIAAALGLTPGDVVlvalpLFHVF-GLTVGL 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 332 WhvSALASGATLVIYDGspmyPQPGVLWDLAEEANITLFGTSAKYLEALqkTAYSPSDYYPLSSLKTLCSTGSVLYPKqf 411
Cdd:COG0318 161 L--APLLAGATLVLLPR----FDPERVLELIERERVTVLFGVPTMLARL--LRHPEFARYDLSSLRLVVSGGAPLPPE-- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 412 dyVYANIKADLHLASIS--GGTDiCGCFVLGNPISPVYRGE-CQG-AGLGLDVAVFNDLGQPV-IQQRGELVCRNsfPNQ 486
Cdd:COG0318 231 --LLERFEERFGVRIVEgyGLTE-TSPVVTVNPEDPGERRPgSVGrPLPGVEVRIVDEDGRELpPGEVGEIVVRG--PNV 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 487 PIGFWHDDgqryhDAYWSKFSGVWHH-GDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQK 565
Cdd:COG0318 306 MKGYWNDP-----EATAEAFRDGWLRtGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVP 380
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1067526515 566 IDN-DEQIILFVQLAPQCELNtllVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:COG0318 381 DEKwGERVVAFVVLRPGAELD---AEELRAFLRERLARYKVPRRVEFVDELPRTASGKI 436
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
35-652 |
3.63e-40 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 155.88 E-value: 3.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 35 ESYSQLHLWSVAERKQFWLEV-----WQ--FcdvigfrgnciygEGIARWDDFTAARdtiWFPQAQLNYAENLLS-YAFQ 106
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQarridWQtpF-------------TQVLDYSNPPFAR---WFVGGRTNLCHNAVDrHLAK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 107 QPEGIA-VWFKNENGQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGV 185
Cdd:PRK10524 66 RPEQLAlIAVSTETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFAS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 186 DSVVERFGQVQPKILFCCNGYTFNGK----THLMEEkngqiadAISslhnicQIEYLHQRSLTADFNDAFS--------D 253
Cdd:PRK10524 146 HSLAARIDDAKPVLIVSADAGSRGGKvvpyKPLLDE-------AIA------LAQHKPRHVLLVDRGLAPMarvagrdvD 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 254 WNAILASYLPRGLRYERVSFNDPLFILYSSGTTGKPKCIAHSVGG------TILNHLkehqlhCDIQPGDRVFYYTTCGW 327
Cdd:PRK10524 213 YATLRAQHLGARVPVEWLESNEPSYILYTSGTTGKPKGVQRDTGGyavalaTSMDTI------FGGKAGETFFCASDIGW 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 328 MMWNWHV--SALASGATLVIYDGSPMYPQPGVLWDLAEEANITLFGTSAKYLEALQKtaySPSDY---YPLSSLKTLCST 402
Cdd:PRK10524 287 VVGHSYIvyAPLLAGMATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKK---QDPALlrkHDLSSLRALFLA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 403 GSVLypkqfdyvyanikaDLHLAS-ISGGTD------------------ICGCF-----VLGNPISPVYrgecqgaglGL 458
Cdd:PRK10524 364 GEPL--------------DEPTASwISEALGvpvidnywqtetgwpilaIARGVedrptRLGSPGVPMY---------GY 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 459 DVAVFNDL-GQPV-IQQRGELVCRnsfPNQPIGF----WHDDgQRYHDAYWSKFsgvwhhGDEVEWTDNGGIR----FY- 527
Cdd:PRK10524 421 NVKLLNEVtGEPCgPNEKGVLVIE---GPLPPGCmqtvWGDD-DRFVKTYWSLF------GRQVYSTFDWGIRdadgYYf 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 528 --GRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKidnDE---QIIL-FVQL---------APQCELNTLLVNTI 592
Cdd:PRK10524 491 ilGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVK---DAlkgQVAVaFVVPkdsdsladrEARLALEKEIMALV 567
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067526515 593 KQRL----RencsprhvPAQIHSISDVPRTKSGKLVELAVKQLLHGETVKNLGAIANPHVLEEI 652
Cdd:PRK10524 568 DSQLgavaR--------PARVWFVSALPKTRSGKLLRRAIQAIAEGRDPGDLTTIEDPAALQQI 623
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
6-623 |
2.37e-37 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 148.69 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 6 PLWVPSQDRIKASNLNQFIEHINMQ--GEA----IESYSQLHLWSVAERKQFWLEVWQFCDVIgF--RGNCIygegiarW 77
Cdd:PLN03052 85 PAWFPSPEIAKLTNLGRLLEARGKEllGSKykdpISSFSEFQRFSVENPEVYWSIVLDELSLV-FsvPPRCI-------L 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 78 DDFTAAR-DTIWFPQAQLNYAENLLSYAFQQP-EGIAVWFKNENGQS---KKLTWQQLSDQVSIIQQWLKQNGVEKGDVV 152
Cdd:PLN03052 157 DTSDESNpGGQWLPGAVLNVAECCLTPKPSKTdDSIAIIWRDEGSDDlpvNRMTLSELRSQVSRVANALDALGFEKGDAI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 153 AGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDSVVERFGQVQPKILFCCNGYTFNGKTHLME----EKNGQIADAISS 228
Cdd:PLN03052 237 AIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYsrvvEAKAPKAIVLPA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 229 LHNICQIEyLHQRSLTadfndafsdWNAIL--ASYLPRGLRYERVSFNDPLF--ILYSSGTTGKPKCIAHsvggTILNHL 304
Cdd:PLN03052 317 DGKSVRVK-LREGDMS---------WDDFLarANGLRRPDEYKAVEQPVEAFtnILFSSGTTGEPKAIPW----TQLTPL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 305 K---EHQLHCDIQPGDRVFYYTTCGWMMWNWHV-SALASGATLVIYDGSPMYPQPGvlwDLAEEANITLFGTSAKYLEAL 380
Cdd:PLN03052 383 RaaaDAWAHLDIRKGDIVCWPTNLGWMMGPWLVyASLLNGATLALYNGSPLGRGFA---KFVQDAKVTMLGTVPSIVKTW 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 381 QKTaySPSDYYPLSSLKTLCSTGSVlypkqfdyvyANIKADLHLASIS---------GGTDICGCFVLGNPISPVYRGEC 451
Cdd:PLN03052 460 KNT--NCMAGLDWSSIRCFGSTGEA----------SSVDDYLWLMSRAgykpiieycGGTELGGGFVTGSLLQPQAFAAF 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 452 QGAGLGLDVAVFNDLGQPVIQqrgELVCRNSFPNQPIGFWHDDGQRYHDAYWSKFSG--VWH------HGDEVEWTDNGG 523
Cdd:PLN03052 528 STPAMGCKLFILDDSGNPYPD---DAPCTGELALFPLMFGASSTLLNADHYKVYFKGmpVFNgkilrrHGDIFERTSGGY 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 524 IRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPE-IQDSVAVGQKIDND--EQIILFVQLAP----QCELNTL--LVNTIKQ 594
Cdd:PLN03052 605 YRAHGRADDTMNLGGIKVSSVEIERVCNAADEsVLETAAIGVPPPGGgpEQLVIAAVLKDppgsNPDLNELkkIFNSAIQ 684
|
650 660
....*....|....*....|....*....
gi 1067526515 595 RlreNCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:PLN03052 685 K---KLNPLFKVSAVVIVPSFPRTASNKV 710
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
104-531 |
8.75e-32 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 128.20 E-value: 8.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 104 AFQQPEGIAVwfknENGQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDF 183
Cdd:pfam00501 5 AARTPDKTAL----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 184 GVDSVVERFGQVQPKILFCCNgytfngkthlmeekngqiADAISSLHNICQIEYLHQRSLTADFNDAFSDWNAILASYLP 263
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDD------------------ALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 264 RGLRYERVSF--NDPLFILYSSGTTGKPKCIAHSVGGTI--LNHLKEHQLHCDIQPGDRVFY-YTTCGWMM-WNWHV-SA 336
Cdd:pfam00501 143 DVPPPPPPPPdpDDLAYIIYTSGTTGKPKGVMLTHRNLVanVLSIKRVRPRGFGLGPDDRVLsTLPLFHDFgLSLGLlGP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 337 LASGATLVIYDGSPMYPqPGVLWDLAEEANITLFGTSAKYLEALqkTAYSPSDYYPLSSLKTLCSTGSVLYPKQFDYVYA 416
Cdd:pfam00501 223 LLAGATVVLPPGFPALD-PAALLELIERYKVTVLYGVPTLLNML--LEAGAPKRALLSSLRLVLSGGAPLPPELARRFRE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 417 niKADLHLASISGGTDICGCFVLGNPISP--VYRGECQGAGLGLDVAVFNDL-GQPVIQ-QRGELVCRNsfPNQPIGFWH 492
Cdd:pfam00501 300 --LFGGALVNGYGLTETTGVVTTPLPLDEdlRSLGSVGRPLPGTEVKIVDDEtGEPVPPgEPGELCVRG--PGVMKGYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1067526515 493 DdgqryHDAYWSKF-SGVWHH-GDEVEWTDNGGIRFYGRSD 531
Cdd:pfam00501 376 D-----PELTAEAFdEDGWYRtGDLGRRDEDGYLEIVGRKK 411
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
259-638 |
3.61e-31 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 127.62 E-value: 3.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 259 ASYLPRGLRYERV--SFNDPLFILYSSGTTGKPKCI--AHSvggTILNHLKEHQLHCDIQPGDRVFYYTTCGWMMWNWHV 334
Cdd:PLN03051 102 AQGSVGGNEYSPVyaPVESVTNILFSSGTTGEPKAIpwTHL---SPLRCASDGWAHMDIQPGDVVCWPTNLGWMMGPWLL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 335 -SALASGATLVIYDGSPMYPQPGvlwDLAEEANITLFGTSAKYLEALQKTAYSPSDYYPLSSLKTLCSTGSVLYPKqfDY 413
Cdd:PLN03051 179 ySAFLNGATLALYGGAPLGRGFG---KFVQDAGVTVLGLVPSIVKAWRHTGAFAMEGLDWSKLRVFASTGEASAVD--DV 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 414 VY-ANIKADLH-LASISGGTDICGCFVLGNPISPVYRGECQGAGLGLDVAVFNDLG------QPVIqqrGELVCRNSFpn 485
Cdd:PLN03051 254 LWlSSVRGYYKpVIEYCGGTELASGYISSTLLQPQAPGAFSTASLGTRFVLLNDNGvpypddQPCV---GEVALAPPM-- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 486 qpIG-----FWHDDGQRYHDA---YWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPE-I 556
Cdd:PLN03051 329 --LGasdrlLNADHDKVYYKGmpmYGSKGMPLRRHGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRAVAgI 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 557 QDSVAVGQKIDND--EQIILFV-----QLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLVELAVK 629
Cdd:PLN03051 407 AETAAVGVAPPDGgpELLVIFLvlgeeKKGFDQARPEALQKKFQEAIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
410
....*....|
gi 1067526515 630 -QLLHGETVK 638
Cdd:PLN03051 487 dQLKKELSGR 496
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
125-629 |
2.02e-30 |
|
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: 124.54 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 125 LTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDSVVERfgqvqpkilfccn 204
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 205 gytfngkthlMEEKNGQIADAISSLhnicqieylhqrsltadfndafsdwnailasylprglrYERVSFNDPLFILYSSG 284
Cdd:cd05969 68 ----------LENSEAKVLITTEEL--------------------------------------YERTDPEDPTLLHYTSG 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 285 TTGKPKCIAHSVGGTILNHLKEHQlHCDIQPGDrVFYYTT-CGWM------MWnwhvSALASGATLVIYDGSpmyPQPGV 357
Cdd:cd05969 100 TTGTPKGVLHVHDAMIFYYFTGKY-VLDLHPDD-IYWCTAdPGWVtgtvygIW----APWLNGVTNVVYEGR---FDAES 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 358 LWDLAEEANITLFGTSAKYLEALQKTAYSPSDYYPLSSLKTLCSTGSVLYPKQFDYVYANIKADLH---LASISGGTDIC 434
Cdd:cd05969 171 WYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHdtwWQTETGSIMIA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 435 GCfvLGNPISPvyrGECQGAGLGLDVAVFNDLGQPVIQQR-GELVCRNSFPNQPIGFWHDDGQryhdaYWSKFSGVWH-H 512
Cdd:cd05969 251 NY--PCMPIKP---GSMGKPLPGVKAAVVDENGNELPPGTkGILALKPGWPSMFRGIWNDEER-----YKNSFIDGWYlT 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 513 GDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGqKID--NDEQIILFVQL----APQCELNT 586
Cdd:cd05969 321 GDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIG-KPDplRGEIIKAFISLkegfEPSDELKE 399
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1067526515 587 LLVNTIKQRLRENCSPRhvpaQIHSISDVPRTKSGKLVELAVK 629
Cdd:cd05969 400 EIINFVRQKLGAHVAPR----EIEFVDNLPKTRSGKIMRRVLK 438
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
108-623 |
6.47e-29 |
|
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: 119.94 E-value: 6.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 108 PEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDS 187
Cdd:cd05930 1 PDAVAVVDGDQ-----SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 188 VVERFGQVQPKILfccngytfngkthlmeekngqiadaisslhnicqieylhqrsLTADfndafsdwnailasylprglr 267
Cdd:cd05930 76 LAYILEDSGAKLV------------------------------------------LTDP--------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 268 yervsfNDPLFILYSSGTTGKPK--CIAHsvgGTILNHLKEHQLHCDIQPGDRVFYYTT-----CGWMMWnwhvSALASG 340
Cdd:cd05930 93 ------DDLAYVIYTSGSTGKPKgvMVEH---RGLVNLLLWMQEAYPLTPGDRVLQFTSfsfdvSVWEIF----GALLAG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 341 ATLVIYDGSPMYPqPGVLWDLAEEANITLFGTSAKYLEALQKTAYSPsdyyPLSSLKTLCSTGSVLYPKQFDYVYANIKa 420
Cdd:cd05930 160 ATLVVLPEEVRKD-PEALADLLAEEGITVLHLTPSLLRLLLQELELA----ALPSLRLVLVGGEALPPDLVRRWRELLP- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 421 DLHLASISG---GTDICGCFVL------------GNPISpvyrgecqgaglGLDVAVFNDLGQPV-IQQRGELV------ 478
Cdd:cd05930 234 GARLVNLYGpteATVDATYYRVppddeedgrvpiGRPIP------------NTRVYVLDENLRPVpPGVPGELYiggagl 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 479 ---CRN-------SFPNQPigfwHDDGQRYHdaywskfsgvwHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQ 548
Cdd:cd05930 302 argYLNrpeltaeRFVPNP----FGPGERMY-----------RTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 366
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067526515 549 QVNSFPEIQDSVAVGQK-IDNDEQIILFVQLAPQCELNTllvNTIKQRLRENcSPRH-VPAQIHSISDVPRTKSGKL 623
Cdd:cd05930 367 ALLAHPGVREAAVVAREdGDGEKRLVAYVVPDEGGELDE---EELRAHLAER-LPDYmVPSAFVVLDALPLTPNGKV 439
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
125-626 |
1.65e-28 |
|
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: 118.59 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 125 LTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDSVVERFGQVQPKILfccn 204
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAI---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 205 gytfngkthlmeekngqIADAisslhnicqieylhqrsltadfndafsdwnailasylprglryervsfNDPLFILYSSG 284
Cdd:cd05972 77 -----------------VTDA------------------------------------------------EDPALIYFTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 285 TTGKPKCIAHSVgGTILNHLKEHQLHCDIQPGDRVFYYTTCGWMMWNWH--VSALASGATLVIYDGSPMYPQpgVLWDLA 362
Cdd:cd05972 92 TTGLPKGVLHTH-SYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSsfFGPWLLGATVFVYEGPRFDAE--RILELL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 363 EEANITLFGTSAKYLEALQKTAyspSDYYPLSSLKTLCSTGSVLYPKQFDYVYANIKADLHlaSISGGTDiCGcFVLGN- 441
Cdd:cd05972 169 ERYGVTSFCGPPTAYRMLIKQD---LSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIR--DGYGQTE-TG-LTVGNf 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 442 PISPVYRGECQGAGLGLDVAVFNDLGQPVIQ-QRGELVCRNSFPNQPIGFWHDDgqryhDAYWSKFSGVWHH-GDEVEWT 519
Cdd:cd05972 242 PDMPVKPGSMGRPTPGYDVAIIDDDGRELPPgEEGDIAIKLPPPGLFLGYVGDP-----EKTEASIRGDYYLtGDRAYRD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 520 DNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKIDNDEQII-LFVQLAPQCELNTLLVNTIKQRLRE 598
Cdd:cd05972 317 EDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVkAFVVLTSGYEPSEELAEELQGHVKK 396
|
490 500 510
....*....|....*....|....*....|
gi 1067526515 599 NCSPRHVPAQIHSISDVPRTKSGKL--VEL 626
Cdd:cd05972 397 VLAPYKYPREIEFVEELPKTISGKIrrVEL 426
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
119-624 |
1.33e-27 |
|
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: 115.99 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 119 NGQSKKLTWQQL---SDQVSiiqQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDSVVERFGQV 195
Cdd:cd05971 1 KGTPEKVTFKELktaSNRFA---NVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 196 QPKILfccngytfngkthlmeekngqIADAisslhnicqieylhqrsltadfndafSDwnailasylprglryervsfnD 275
Cdd:cd05971 78 GASAL---------------------VTDG--------------------------SD---------------------D 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 276 PLFILYSSGTTGKPKCI--AHSVggtILNHLKEHQLHCDIQPGDRVFYYTTCGWmMW-----NWHVSALASGATLVIYDG 348
Cdd:cd05971 90 PALIIYTSGTTGPPKGAlhAHRV---LLGHLPGVQFPFNLFPRDGDLYWTPADW-AWiggllDVLLPSLYFGVPVLAHRM 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 349 SPMypQPGVLWDLAEEANITLFGTSAKYLEaLQKTAYSPSDYYPLsSLKTLCSTGSVLYPKQFDYVYANIKADLHlaSIS 428
Cdd:cd05971 166 TKF--DPKAALDLMSRYGVTTAFLPPTALK-MMRQQGEQLKHAQV-KLRAIATGGESLGEELLGWAREQFGVEVN--EFY 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 429 GGTDicGCFVLGN--PISPVYRGECQGAGLGLDVAVFNDLGQPV-IQQRGELVCRNSFPNQPIGFWHDDgqryhDAYWSK 505
Cdd:cd05971 240 GQTE--CNLVIGNcsALFPIKPGSMGKPIPGHRVAIVDDNGTPLpPGEVGEIAVELPDPVAFLGYWNNP-----SATEKK 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 506 FSGVWHHGDEVEWTDNGG-IRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGqKID--NDEQIILFVQLAPQC 582
Cdd:cd05971 313 MAGDWLLTGDLGRKDSDGyFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVG-IPDpiRGEIVKAFVVLNPGE 391
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1067526515 583 ELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLV 624
Cdd:cd05971 392 TPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIR 433
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
271-629 |
1.25e-24 |
|
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: 107.16 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 271 VSFNDPLFILYSSGTTGKPKCIAHSvggtilnhLKEHQLHCD--------IQPGDRVF-----YYttcGWMMWNWHVSAL 337
Cdd:cd05919 88 TSADDIAYLLYSSGTTGPPKGVMHA--------HRDPLLFADamarealgLTPGDRVFssakmFF---GYGLGNSLWFPL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 338 ASGATLVIYDGSPMypQPGVLWDLAEEANITLFGTSAKYLEALQKTAYSPSDyypLSSLKTLCSTGSVLyPKQFDYVYAN 417
Cdd:cd05919 157 AVGASAVLNPGWPT--AERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDA---LRSLRLCVSAGEAL-PRGLGERWME 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 418 ikadlhlasiSGGTDIC---GC-----FVLGNPISPVYRGECQGAGLGLDVAVFNDLGQPVIQQR-GELVCRNsfPNQPI 488
Cdd:cd05919 231 ----------HFGGPILdgiGAtevghIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGHTIPPGEeGDLLVRG--PSAAV 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 489 GFWHD-DGQRyhdaywSKFSGVWHH-GDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGqkI 566
Cdd:cd05919 299 GYWNNpEKSR------ATFNGGWYRtGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVA--V 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067526515 567 DNDEQII---LFVQLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLVELAVK 629
Cdd:cd05919 371 PESTGLSrltAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
125-623 |
1.90e-24 |
|
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: 106.83 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 125 LTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDSVVERFGQVQPKILFCcn 204
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 205 gytfngkthlmeekngqiaDAisslhnicqieylHQRSLTADfndafsdwnailasylprglryervsfnDPLFILYSSG 284
Cdd:cd05973 79 -------------------DA-------------ANRHKLDS----------------------------DPFVMMFTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 285 TTGKPKCIAHSVGGtILNHLKEHQLHCDIQPGDRVFYYTTCGWM--MWNWHVSALASGATLVIYDGSPmypQPGVLWDLA 362
Cdd:cd05973 99 TTGLPKGVPVPLRA-LAAFGAYLRDAVDLRPEDSFWNAADPGWAygLYYAITGPLALGHPTILLEGGF---SVESTWRVI 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 363 EEANITLFGTSAKYLEALqKTAYSPSDYYPLSSLKTLCSTGSVLYPKQFDYVYANIKADLHlasisggtDICGCFVLGNP 442
Cdd:cd05973 175 ERLGVTNLAGSPTAYRLL-MAAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIH--------DHYGQTELGMV 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 443 IS-------PVYRGECQGAGLGLDVAVFNDLG-QPVIQQRGELV--CRNS----FPnqpiGFWHDDGqryhdaywSKFSG 508
Cdd:cd05973 246 LAnhhalehPVHAGSAGRAMPGWRVAVLDDDGdELGPGEPGRLAidIANSplmwFR----GYQLPDT--------PAIDG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 509 VWH-HGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKIDNDEQII-LFVQLAPQCELNT 586
Cdd:cd05973 314 GYYlTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVkAFVVLRGGHEGTP 393
|
490 500 510
....*....|....*....|....*....|....*..
gi 1067526515 587 LLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd05973 394 ALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKI 430
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
125-623 |
2.72e-24 |
|
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: 106.59 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 125 LTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDfgvdsvverfgqvQPKilfccn 204
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDID-------------QPA------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 205 gytfngkthlmEEKNGQIADAISSLHNICQiEYLHQRSLTADFNDAFSDWNAILASYLPRglryeRVSFNDPLFILYSSG 284
Cdd:cd12114 74 -----------ARREAILADAGARLVLTDG-PDAQLDVAVFDVLILDLDALAAPAPPPPV-----DVAPDDLAYVIFTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 285 TTGKPKCIAHSVGGTIlNHLKEHQLHCDIQPGDRVFYYTTCGWMMWNWHV-SALASGATLVIYDGSPMyPQPGVLWDLAE 363
Cdd:cd12114 137 STGTPKGVMISHRAAL-NTILDINRRFAVGPDDRVLALSSLSFDLSVYDIfGALSAGATLVLPDEARR-RDPAHWAELIE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 364 EANITLFGTSAKYLEALqkTAYSPSDYYPLSSLK------------------------TLCSTG--------SVLYPKQf 411
Cdd:cd12114 215 RHGVTLWNSVPALLEML--LDVLEAAQALLPSLRlvllsgdwipldlparlralapdaRLISLGgateasiwSIYHPID- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 412 dyvyaniKADLHLASISGGTDICG--CFVL---GNPISPVYRGECQGAGLGLDVAVFNDlgqpviqqrGELVCRnSFPNq 486
Cdd:cd12114 292 -------EVPPDWRSIPYGRPLANqrYRVLdprGRDCPDWVPGELWIGGRGVALGYLGD---------PELTAA-RFVT- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 487 pigfwHDDGQRyhdAYWSkfsgvwhhGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKI 566
Cdd:cd12114 354 -----HPDGER---LYRT--------GDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGD 417
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1067526515 567 DNDEQIILFVqlAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd12114 418 PGGKRLAAFV--VPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKV 472
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
106-623 |
2.86e-23 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 103.16 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 106 QQPEGIAVWFKnengqSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTspDFGV 185
Cdd:cd17653 9 AHPDAVAVESL-----GGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL--DAKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 186 DSvvERfgqvqpkilfccngytfngKTHLMEEKNGQIAdaisslhnicqieylhqrsLTADfndafsdwnailasylprg 265
Cdd:cd17653 82 PS--AR-------------------IQAILRTSGATLL-------------------LTTD------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 266 lryervSFNDPLFILYSSGTTGKPK--CIAHSvggTILNHLKEHQLHCDIQPGDRV-----FYYTTCGWMMWnwhvSALA 338
Cdd:cd17653 103 ------SPDDLAYIIFTSGSTGIPKgvMVPHR---GVLNYVSQPPARLDVGPGSRVaqvlsIAFDACIGEIF----STLC 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 339 SGATLVIYDgsPMYPqpgvLWDLAEEANITLFGTSAkyleaLQKtaYSPSDYyplSSLKTLCSTGSVLYPKQFDYVYANI 418
Cdd:cd17653 170 NGGTLVLAD--PSDP----FAHVARTVDALMSTPSI-----LST--LSPQDF---PNLKTIFLGGEAVPPSLLDRWSPGR 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 419 KadlhLASISGGTDI-CGCF----------VLGNPISpvyrgecqgaglGLDVAVFNDLGQPV-IQQRGEL------VCR 480
Cdd:cd17653 234 R----LYNAYGPTECtISSTmtellpgqpvTIGKPIP------------NSTCYILDADLQPVpEGVVGEIcisgvqVAR 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 481 NSFPNQ--------PIGFWHddGQRyhdaywskfsgVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNS 552
Cdd:cd17653 298 GYLGNPaltaskfvPDPFWP--GSR-----------MYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQ 364
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067526515 553 FPEIQDSVAVgqkIDNDEQIILFVqlAPQcelnTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd17653 365 SQPEVTQAAA---IVVNGRLVAFV--TPE----TVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKV 426
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
95-630 |
3.51e-23 |
|
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: 103.73 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 95 NYAENLL-SYAFQQPEGIAVWFKNENGQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLG 173
Cdd:cd05970 17 NFAYDVVdAMAKEYPDKLALVWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 174 AVWTSTSPDFGVDSVVERFGQVQPKILFCcngytfNGKTHLMEekngQIADAISSLHNICQIEYLHqrsltADFNDAFSD 253
Cdd:cd05970 97 AIAIPATHQLTAKDIVYRIESADIKMIVA------IAEDNIPE----EIEKAAPECPSKPKLVWVG-----DPVPEGWID 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 254 WNAILASYLPRGLRYERVSF---NDPLFILYSSGTTGKPKCIAHsVGGTILNHLKEHQLHCDIQPGDRVFYYTTCGW--M 328
Cdd:cd05970 162 FRKLIKNASPDFERPTANSYpcgEDILLVYFSSGTTGMPKMVEH-DFTYPLGHIVTAKYWQNVREGGLHLTVADTGWgkA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 329 MWNWHVSALASGATLVIYDGSPMYPQPgvLWDLAEEANITLF---GTSAKYL--EALQKtayspsdyYPLSSLKTLCSTG 403
Cdd:cd05970 241 VWGKIYGQWIAGAAVFVYDYDKFDPKA--LLEKLSKYGVTTFcapPTIYRFLirEDLSR--------YDLSSLRYCTTAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 404 SVLYPKQFDYV-----------YANIKADLHLASISGGTDICGCFVLGNPispvyrgecqgaglGLDVAVFNDLGQPV-I 471
Cdd:cd05970 311 EALNPEVFNTFkektgiklmegFGQTETTLTIATFPWMEPKPGSMGKPAP--------------GYEIDLIDREGRSCeA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 472 QQRGELVCRNSfPNQPIGF---WHDDGQRYHDAYwskFSGVWHHGDeVEWTDNGG-IRFYGRSDTTLNPGGVRIGTAEIY 547
Cdd:cd05970 377 GEEGEIVIRTS-KGKPVGLfggYYKDAEKTAEVW---HDGYYHTGD-AAWMDEDGyLWFVGRTDDLIKSSGYRIGPFEVE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 548 QQVNSFPEIQDSVAVGQKIDNDEQII-LFVQLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLVEL 626
Cdd:cd05970 452 SALIQHPAVLECAVTGVPDPIRGQVVkATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRV 531
|
....
gi 1067526515 627 AVKQ 630
Cdd:cd05970 532 EIRE 535
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
126-561 |
2.91e-22 |
|
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: 99.65 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 126 TWQQLSDQVSIIQQWLKQN-GVEKGDVVAGYLPYMTETLVAMLATTSLGAVWT---STSPdfgvdsvVERFGQVqpkilf 201
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVpldPAYP-------AERLAFI------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 202 ccngytfngkthlmeekngqIADAISSLHnICQIEYLHQRSLTADFNDAFS-DWNAILASYLPRGLRYERVSFNDPLFIL 280
Cdd:TIGR01733 68 --------------------LEDAGARLL-LTDSALASRLAGLVLPVILLDpLELAALDDAPAPPPPDAPSGPDDLAYVI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 281 YSSGTTGKPKCIAHSvGGTILNHLKEHQLHCDIQPGDRVFYYTT-----CGWMMWnwhvSALASGATLVIYDGSPMYPQP 355
Cdd:TIGR01733 127 YTSGSTGRPKGVVVT-HRSLVNLLAWLARRYGLDPDDRVLQFASlsfdaSVEEIF----GALLAGATLVVPPEDEERDDA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 356 GVLWDLAEEANITLFGTSAKYLEALqktaySPSDYYPLSSLKTLCSTGSVLYPKQFDYVYANIKaDLHLASISG---GTD 432
Cdd:TIGR01733 202 ALLAALIAEHPVTVLNLTPSLLALL-----AAALPPALASLRLVILGGEALTPALVDRWRARGP-GARLINLYGpteTTV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 433 ICGCFVLgnPISPVYRGECQGAGLGLD---VAVFNDLGQPV-IQQRGEL------VCRnsfpnqpiGFWHDDG---QRY- 498
Cdd:TIGR01733 276 WSTATLV--DPDDAPRESPVPIGRPLAntrLYVLDDDLRPVpVGVVGELyiggpgVAR--------GYLNRPEltaERFv 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067526515 499 HDAYWSKFSGVWHH-GDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVA 561
Cdd:TIGR01733 346 PDPFAGGDGARLYRtGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
122-494 |
1.05e-21 |
|
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: 98.82 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 122 SKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDSVVERFGQVQPKILF 201
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 202 CCNGYTFNGKTHLMEEKNGQ----IADAISSLHNICQIeyLHQRSLTADfndafsdwnailaSYLPrglRYERVSFNDPL 277
Cdd:cd05911 88 TDPDGLEKVKEAAKELGPKDkiivLDDKPDGVLSIEDL--LSPTLGEED-------------EDLP---PPLKDGKDDTA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 278 FILYSSGTTGKPK--CIAHSvggTILNHLKEHQLH--CDIQPGDRVFYYTTCGWMM-WNWHVSALASGATLVIYDGspmy 352
Cdd:cd05911 150 AILYSSGTTGLPKgvCLSHR---NLIANLSQVQTFlyGNDGSNDVILGFLPLYHIYgLFTTLASLLNGATVIIMPK---- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 353 PQPGVLWDLAEEANITLFGTSAKYLEALQKtaySPS-DYYPLSSLKTLCSTGSVLYPKqfdyVYANIKADLHLASIS--- 428
Cdd:cd05911 223 FDSELFLDLIEKYKITFLYLVPPIAAALAK---SPLlDKYDLSSLRVILSGGAPLSKE----LQELLAKRFPNATIKqgy 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067526515 429 GGTDiCGCFVLGNPISPVYRGECQGAGLGLDVAVFNDLGQPV--IQQRGELVCRNsfPNQPIGFWHDD 494
Cdd:cd05911 296 GMTE-TGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSlgPNEPGEICVRG--PQVMKGYYNNP 360
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
88-657 |
3.02e-21 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 98.28 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 88 WFPQAQLNYAENLLSYAFQQPEGiavwfKNENG---------QSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPY 158
Cdd:PTZ00237 52 WFKGGELNTCYNVLDIHVKNPLK-----RDQDAliyecpylkKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMAN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 159 MTETLVAMLATTSLGAVWTSTSPDFGVDSVVERFGQVQPKILFCCNGYTFNGkthlmeekngQIADAISSLHNICQIEYL 238
Cdd:PTZ00237 127 TLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGILND----------EIITFTPNLKEAIELSTF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 239 HQRSLTADF-ND--AFSDWNAILA-SYLPRGL------------------RYERVSFNDPLFILYSSGTTGKPKCIAHSV 296
Cdd:PTZ00237 197 KPSNVITLFrNDitSESDLKKIETiPTIPNTLswydeikkikennqspfyEYVPVESSHPLYILYTSGTTGNSKAVVRSN 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 297 GGTILNhLKEHQLHCDIQPGD-RVFYYTTCGWMMW-NWHVSALASGATLVIYDGSPMYPQ--PGVLWDLAEEANITLFGT 372
Cdd:PTZ00237 277 GPHLVG-LKYYWRSIIEKDIPtVVFSHSSIGWVSFhGFLYGSLSLGNTFVMFEGGIIKNKhiEDDLWNTIEKHKVTHTLT 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 373 SAKYLEALQKT---AYSPSDYYPLSSLKTLCSTGSVLYPKQFDYVYANIKA---DLHLASISGGTDICGCFVLGNPISpv 446
Cdd:PTZ00237 356 LPKTIRYLIKTdpeATIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIkssRGYGQTEIGITYLYCYGHINIPYN-- 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 447 yrgECQGAGLGLDVAVFNDLGQPV-IQQRGELVCRNSFPNQ-PIGFWHDDgQRYHDAYwSKFSGVWHHGDeVEWTDNGGi 524
Cdd:PTZ00237 434 ---ATGVPSIFIKPSILSEDGKELnVNEIGEVAFKLPMPPSfATTFYKND-EKFKQLF-SKFPGYYNSGD-LGFKDENG- 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 525 rFYG---RSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVG---------------QKIDNDEQIILFVQLapQCELNT 586
Cdd:PTZ00237 507 -YYTivsRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGiydpdcynvpigllvLKQDQSNQSIDLNKL--KNEINN 583
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067526515 587 LLVNTIkqrlrENCSprhVPAQIHSISDVPRTKSGKLVELAVKQLLHGETVKNLGAIANPHVLEEIHALFT 657
Cdd:PTZ00237 584 IITQDI-----ESLA---VLRKIIIVNQLPKTKTGKIPRQIISKFLNDSNYQLPDNVNDSEIFYKIKELYM 646
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
104-623 |
8.72e-21 |
|
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: 95.37 E-value: 8.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 104 AFQQPEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTstspdf 183
Cdd:cd17631 5 ARRHPDRTALVFGGR-----SLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFV------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 184 gvdsvverfgqvqPkilfccngytfngkthlmeekngqiadaisslhnicqieyLHQRsLTADfndafsDWNAILASYLP 263
Cdd:cd17631 74 -------------P----------------------------------------LNFR-LTPP------EVAYILADSGA 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 264 RglryerVSFNDPLFILYSSGTTGKPKCIAHSvGGTILNHLKEHQLHCDIQPGDRVF-----YYTTCGWMMWnwhVSALA 338
Cdd:cd17631 94 K------VLFDDLALLMYTSGTTGRPKGAMLT-HRNLLWNAVNALAALDLGPDDVLLvvaplFHIGGLGVFT---LPTLL 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 339 SGATLVIYDGspmyPQPGVLWDLAEEANIT-LFGTSAKYLEALQKTAYSPSDyypLSSLKTLCSTGSvlyPKQFDYVYAN 417
Cdd:cd17631 164 RGGTVVILRK----FDPETVLDLIERHRVTsFFLVPTMIQALLQHPRFATTD---LSSLRAVIYGGA---PMPERLLRAL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 418 IKADLHLASISGGTDIC-GCFVL------------GNPISPVyrgecqgaglglDVAVFNDLGQPV-IQQRGELVCRNsf 483
Cdd:cd17631 234 QARGVKFVQGYGMTETSpGVTFLspedhrrklgsaGRPVFFV------------EVRIVDPDGREVpPGEVGEIVVRG-- 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 484 PNQPIGFWHDDgqryhDAYWSKFSGVWHH-GDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAV 562
Cdd:cd17631 300 PHVMAGYWNRP-----EATAAAFRDGWFHtGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVI 374
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067526515 563 GqkIDND---EQIILFVQLAPQCELntllvntIKQRLRENCSPR----HVPAQIHSISDVPRTKSGKL 623
Cdd:cd17631 375 G--VPDEkwgEAVVAVVVPRPGAEL-------DEDELIAHCRERlaryKIPKSVEFVDALPRNATGKI 433
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
104-623 |
6.24e-20 |
|
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: 93.42 E-value: 6.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 104 AFQQPEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDF 183
Cdd:cd12117 7 AARTPDAVAVVYGDR-----SLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 184 GVDSVVERFGQVQPKILFCCNGYTFNGKTHLMeekngqiadaisslhnicqieylhqRSLTADFNDAFSDWNAILAsylp 263
Cdd:cd12117 82 PAERLAFMLADAGAKVLLTDRSLAGRAGGLEV-------------------------AVVIDEALDAGPAGNPAVP---- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 264 rglryerVSFNDPLFILYSSGTTGKPK--CIAH-SVGGTILNhlkehQLHCDIQPGDRVFYYTTCGW-----MMWnwhvS 335
Cdd:cd12117 133 -------VSPDDLAYVMYTSGSTGRPKgvAVTHrGVVRLVKN-----TNYVTLGPDDRVLQTSPLAFdastfEIW----G 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 336 ALASGATLVIYDGSPMYpQPGVLWDLAEEANIT-LFGTSAKYLEAlqktayspSDYYP--LSSLKTLCSTGSVLYPKQFD 412
Cdd:cd12117 197 ALLNGARLVLAPKGTLL-DPDALGALIAEEGVTvLWLTAALFNQL--------ADEDPecFAGLRELLTGGEVVSPPHVR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 413 YVYAnIKADLHLASISG---GTDICGCFVL------------GNPISpvyrgecqgaglGLDVAVFNDLGQPV-IQQRGE 476
Cdd:cd12117 268 RVLA-ACPGLRLVNGYGpteNTTFTTSHVVteldevagsipiGRPIA------------NTRVYVLDEDGRPVpPGVPGE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 477 L------VCRnsfpnqpiGFWHDDG---QRYHDAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIY 547
Cdd:cd12117 335 LyvggdgLAL--------GYLNRPAltaERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIE 406
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067526515 548 QQVNSFPEIQDSVAVGQKIDNDE-QIILFVQLAPqcelnTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd12117 407 AALRAHPGVREAVVVVREDAGGDkRLVAYVVAEG-----ALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKV 478
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
275-622 |
1.90e-19 |
|
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: 91.20 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 275 DPLFILYSSGTTGKPKciahsvgGTILNHLKEHQL------HCDIQPGDRvfYYTTcgwmMWNWHVSALASGATLVIYDG 348
Cdd:cd05934 82 DPASILYTSGTTGPPK-------GVVITHANLTFAgyysarRFGLGEDDV--YLTV----LPLFHINAQAVSVLAALSVG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 349 SPMYPQP----GVLWDLAEEANITLFGTSAKYLEALQKTAYSPSDYYplsslktlcstgsvlYPKQFDYVYANIKADLH- 423
Cdd:cd05934 149 ATLVLLPrfsaSRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRA---------------HRLRAAYGAPNPPELHEe 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 424 --------LASISGGTDICGCfVLGNPISPVYRGECQGAGLGLDVAVFNDLGQPV-IQQRGELVCRnsfPNQPIGFWHDd 494
Cdd:cd05934 214 feerfgvrLLEGYGMTETIVG-VIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELpAGEPGELVIR---GLRGWGFFKG- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 495 gqrYH---DAYWSKFSGVWHH-GDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKID-ND 569
Cdd:cd05934 289 ---YYnmpEATAEAMRNGWFHtGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEvGE 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1067526515 570 EQIILFVQLAPQcelNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGK 622
Cdd:cd05934 366 DEVKAVVVLRPG---ETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEK 415
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
106-627 |
1.52e-18 |
|
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: 90.30 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 106 QQPEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGV 185
Cdd:COG1020 488 RTPDAVAVVFGDQ-----SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPA 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 186 dsvvERFGQVqpkilfccngytfngkthlmeekngqIADAisslhnicQIEY-LHQRSLTADFNDAFSDW---NAILASY 261
Cdd:COG1020 563 ----ERLAYM--------------------------LEDA--------GARLvLTQSALAARLPELGVPVlalDALALAA 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 262 LPRGLRYERVSFNDPLFILYSSGTTGKPK--CIAHsvgGTILNHLKEHQLHCDIQPGDRVFYYTTCG-----WMMWnwhv 334
Cdd:COG1020 605 EPATNPPVPVTPDDLAYVIYTSGSTGRPKgvMVEH---RALVNLLAWMQRRYGLGPGDRVLQFASLSfdasvWEIF---- 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 335 SALASGATLVIYDGSPMYPqPGVLWDLAEEANITLFGTSAKYLEALQKTAYSpsdyyPLSSLKTLCSTGSVLYPKQFDYV 414
Cdd:COG1020 678 GALLSGATLVLAPPEARRD-PAALAELLARHRVTVLNLTPSLLRALLDAAPE-----ALPSLRLVLVGGEALPPELVRRW 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 415 YANIK-ADLH-------------LASISGGTDICGCFVLGNPISpvyrgecqgaglGLDVAVFNDLGQPV-IQQRGEL-- 477
Cdd:COG1020 752 RARLPgARLVnlygptettvdstYYEVTPPDADGGSVPIGRPIA------------NTRVYVLDAHLQPVpVGVPGELyi 819
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 478 ----VCRnsfpnqpiGFWHD---------------DGQRyhdAYWSkfsgvwhhGDEVEWTDNGGIRFYGRSDTTLNPGG 538
Cdd:COG1020 820 ggagLAR--------GYLNRpeltaerfvadpfgfPGAR---LYRT--------GDLARWLPDGNLEFLGRADDQVKIRG 880
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 539 VRIGTAEIYQQVNSFPEIQDSVAVGQKIDNDEQIILFVQLAPQCELNTLLVntIKQRLRENCSPRHVPAQIHSISDVPRT 618
Cdd:COG1020 881 FRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAAL--LRLALALLLPPYMVPAAVVLLLPLPLT 958
|
....*....
gi 1067526515 619 KSGKLVELA 627
Cdd:COG1020 959 GNGKLDRLA 967
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
121-623 |
2.13e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 89.06 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 121 QSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDSVVERFGQVQPKIL 200
Cdd:PRK12583 42 QALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 201 FCCNGYtfngKT---HLMeekngqIADAISSLHNICQIEYLHQR--------SLTADFNDAFSDWNAILASylPRGLRYE 269
Cdd:PRK12583 122 ICADAF----KTsdyHAM------LQELLPGLAEGQPGALACERlpelrgvvSLAPAPPPGFLAWHELQAR--GETVSRE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 270 R-------VSFNDPLFILYSSGTTGKPK--CIAHSvggTILN---------HLKEHQLHCDIQPgdrvfYYTTCGWMMWN 331
Cdd:PRK12583 190 AlaerqasLDRDDPINIQYTSGTTGFPKgaTLSHH---NILNngyfvaeslGLTEHDRLCVPVP-----LYHCFGMVLAN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 332 whVSALASGATLViydgspmYPQP-----GVLWDLAEEANITLFGTSAKYLEALQKTAYSPSDyypLSSLKTLCSTGSVL 406
Cdd:PRK12583 262 --LGCMTVGACLV-------YPNEafdplATLQAVEEERCTALYGVPTMFIAELDHPQRGNFD---LSSLRTGIMAGAPC 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 407 YPKqfdyVYANIKADLHLASIS---GGTDICGCFVLGNPISPV-YRGECQGAGL-GLDVAVFNDLGQPV-IQQRGELVCR 480
Cdd:PRK12583 330 PIE----VMRRVMDEMHMAEVQiayGMTETSPVSLQTTAADDLeRRVETVGRTQpHLEVKVVDPDGATVpRGEIGELCTR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 481 NSfpNQPIGFWHDDgQRYHDAYWSkfSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSV 560
Cdd:PRK12583 406 GY--SVMKGYWNNP-EATAESIDE--DGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQ 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 561 AVG---QKIdnDEQIILFVQLAPQCELNtllvntiKQRLRENCSPR----HVPAQIHSISDVPRTKSGKL 623
Cdd:PRK12583 481 VFGvpdEKY--GEEIVAWVRLHPGHAAS-------EEELREFCKARiahfKVPRYFRFVDEFPMTVTGKV 541
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
125-623 |
3.01e-18 |
|
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: 87.82 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 125 LTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGvdsvverfgqvqpkilfccn 204
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFR-------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 205 gytfngkthlmeekngqiadaisslhnicqieylhQRSLTADFNDAFSdwNAILASYLPRGLRYERVSfNDPLFILYSSG 284
Cdd:cd05903 62 -----------------------------------EHELAFILRRAKA--KVFVVPERFRQFDPAAMP-DAVALLLFTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 285 TTGKPKCIAHSvGGTILNHLKEHQLHCDIQPGDRVFYYTTCGwmmwnwHVSALASGATLVIYDGSPMYPQPgvLWD---- 360
Cdd:cd05903 104 TTGEPKGVMHS-HNTLSASIRQYAERLGLGPGDVFLVASPMA------HQTGFVYGFTLPLLLGAPVVLQD--IWDpdka 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 361 --LAEEANITLFGTSAKYLEALQKTAYSPSDyyPLSSLKTLCSTGSVLYPKQFDYVYANIKAdlHLASISGGTDICGCFV 438
Cdd:cd05903 175 laLMREHGVTFMMGATPFLTDLLNAVEEAGE--PLSRLRTFVCGGATVPRSLARRAAELLGA--KVCSAYGSTECPGAVT 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 439 LGNPISPVYRGECQG-AGLGLDVAVFNDLGQPVIQ-QRGELVCRNsfPNQPIGFwhddgqrYHDAYWSK--FSGVWHH-G 513
Cdd:cd05903 251 SITPAPEDRRLYTDGrPLPGVEIKVVDDTGATLAPgVEGELLSRG--PSVFLGY-------LDRPDLTAdaAPEGWFRtG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 514 DEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKIDN-DEQIILFVQLAPQCELNtllVNTI 592
Cdd:cd05903 322 DLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERlGERACAVVVTKSGALLT---FDEL 398
|
490 500 510
....*....|....*....|....*....|..
gi 1067526515 593 KQRL-RENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd05903 399 VAYLdRQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
74-623 |
7.75e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 88.48 E-value: 7.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 74 IARWDDFTAArdtiwFPqAQLNYAENLLSYAFQQPEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGVEKGDVVA 153
Cdd:PRK12316 4537 VALWNRTDAG-----YP-ATRCVHQLVAERARMTPDAVAVVFDEE-----KLTYAELNRRANRLAHALIARGVGPEVLVG 4605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 154 GYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDSVVERFGQVQPKILFCcngytfngKTHLMEEKngQIADAISSLhnic 233
Cdd:PRK12316 4606 IAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLT--------QSHLLQRL--PIPDGLASL---- 4671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 234 qieylhqrsltadFNDAFSDW-----NAILASYLPRGLRYervsfndplfILYSSGTTGKPKCIAHSVgGTILNHLKEHQ 308
Cdd:PRK12316 4672 -------------ALDRDEDWegfpaHDPAVRLHPDNLAY----------VIYTSGSTGRPKGVAVSH-GSLVNHLHATG 4727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 309 LHCDIQPGDRVFYYTTCGW--MMWNWHvSALASGATLVIYDGSpmYPQPGVLWDLAEEANITLFGTSAKYLEALQKTAYS 386
Cdd:PRK12316 4728 ERYELTPDDRVLQFMSFSFdgSHEGLY-HPLINGASVVIRDDS--LWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAER 4804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 387 PSDYyplSSLKTLCSTGSVLYPKQFDYVYANIKADlHLASISGGT--------------DICGCFV--LGNPISpvyrge 450
Cdd:PRK12316 4805 DGEP---PSLRVYCFGGEAVAQASYDLAWRALKPV-YLFNGYGPTettvtvllwkardgDACGAAYmpIGTPLG------ 4874
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 451 cqgaglGLDVAVFNDLGQPV-IQQRGEL------VCRnsfpnqpiGFWHDDG---QRY-HDAYWSKFSGVWHHGDEVEWT 519
Cdd:PRK12316 4875 ------NRSGYVLDGQLNPLpVGVAGELylggegVAR--------GYLERPAltaERFvPDPFGAPGGRLYRTGDLARYR 4940
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 520 DNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKIDNDEQIILFV-----QLAPQCELNTLLVNTIKQ 594
Cdd:PRK12316 4941 ADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVvpqdpALADADEAQAELRDELKA 5020
|
570 580
....*....|....*....|....*....
gi 1067526515 595 RLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:PRK12316 5021 ALRERLPEYMVPAHLVFLARMPLTPNGKL 5049
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
124-623 |
9.77e-18 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 87.79 E-value: 9.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 124 KLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDSVVERFGQVQPKILFCc 203
Cdd:PRK10252 483 QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLIT- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 204 ngytfngkthlmeekngqiadaisslhnicqieylhqrslTADFNDAFSD--------WNAILASYLPRGLRYERVSfnD 275
Cdd:PRK10252 562 ----------------------------------------TADQLPRFADvpdltslcYNAPLAPQGAAPLQLSQPH--H 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 276 PLFILYSSGTTGKPKCIAhsVGGT-ILNHLKEHQLHCDIQPGDRVFYYTTCG-----WMMWnWhvsALASGATLViydgs 349
Cdd:PRK10252 600 TAYIIFTSGSTGRPKGVM--VGQTaIVNRLLWMQNHYPLTADDVVLQKTPCSfdvsvWEFF-W---PFIAGAKLV----- 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 350 pMYP-----QPGVLWDLAEEANITLFGTSAKYLEALQKTAYSPSDYYPLSSLKTLCSTGSVLYPKQFDYVYANIKADLH- 423
Cdd:PRK10252 669 -MAEpeahrDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHn 747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 424 -----LASI------SGGTDICGcfVLGNPIS---PVYrgecqGAGLgldvAVFNDLGQPV------------IQ-QRGE 476
Cdd:PRK10252 748 lygptEAAVdvswypAFGEELAA--VRGSSVPigyPVW-----NTGL----RILDARMRPVppgvagdlyltgIQlAQGY 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 477 LvCR-----NSFPNQPIGfwhdDGQRyhdaywskfsgVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVN 551
Cdd:PRK10252 817 L-GRpdltaSRFIADPFA----PGER-----------MYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQ 880
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067526515 552 SFPEIQDSVAVGQKIDNDE-------QIILFVQLAPQCELNtllVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:PRK10252 881 ALPDVEQAVTHACVINQAAatggdarQLVGYLVSQSGLPLD---TSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKL 956
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
108-623 |
1.51e-17 |
|
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: 85.81 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 108 PEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDS 187
Cdd:cd12116 1 PDATAVRDDDR-----SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 188 VVERFGQVQPKILFCCNgytfngkthlmEEKNGQIADAISSLHNICQIEYLHQRSLTAdfndafsdwnailasylprglr 267
Cdd:cd12116 76 LRYILEDAEPALVLTDD-----------ALPDRLPAGLPVLLLALAAAAAAPAAPRTP---------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 268 yerVSFNDPLFILYSSGTTGKPKCIAHSVGGTIlnhlkeHQLHC-----DIQPGDRVFYYTTCGW------MMWnwhvsA 336
Cdd:cd12116 123 ---VSPDDLAYVIYTSGSTGRPKGVVVSHRNLV------NFLHSmrerlGLGPGDRLLAVTTYAFdislleLLL-----P 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 337 LASGATLVIYDGSPMYpQPGVLWDLAEEANITLF-GTSAKYLEALQktayspSDYYPLSSLKTLCStGSVLYPKQFDYVY 415
Cdd:cd12116 189 LLAGARVVIAPRETQR-DPEALARLIEAHSITVMqATPATWRMLLD------AGWQGRAGLTALCG-GEALPPDLAARLL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 416 ANIkADLH----------LASISGGTDICGCFVLGNPIspvyrgecqgagLGLDVAVFNDLGQPV-IQQRGEL------V 478
Cdd:cd12116 261 SRV-GSLWnlygptettiWSTAARVTAAAGPIPIGRPL------------ANTQVYVLDAALRPVpPGVPGELyiggdgV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 479 CRnsfpnqpiGFWHDDG---QRY-HDAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFP 554
Cdd:cd12116 328 AQ--------GYLGRPAltaERFvPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHP 399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067526515 555 EIQDSVAVGQKIDNDEQIILFVQLAPQCELNTLLvntIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd12116 400 GVAQAAVVVREDGGDRRLVAYVVLKAGAAPDAAA---LRAHLRATLPAYMVPSAFVRLDALPLTANGKL 465
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
98-630 |
2.02e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 85.73 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 98 ENLLSYAFQQPEGIAVWFknengQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWT 177
Cdd:PRK07656 9 ELLARAARRFGDKEAYVF-----GDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 178 STSPDFGVDSVVERFGQVQPKILFCCNGytFNGKTHLMEEKNGQIADAIsslhnICQIEYlhqrslTADFNDAFSDWNAI 257
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGL--FLGVDYSATTRLPALEHVV-----ICETEE------DDPHTEKMKTFTDF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 258 LASYLPRgLRYERVSFNDPLFILYSSGTTGKPKciahsvgGTILNH---LKEHQLHCD---IQPGDR---------VFYY 322
Cdd:PRK07656 151 LAAGDPA-ERAPEVDPDDVADILFTSGTTGRPK-------GAMLTHrqlLSNAADWAEylgLTEGDRylaanpffhVFGY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 323 TTCgwmmWNwhvSALASGATLVIYdgsPMYpQPGVLWDLAEEANITLF-GTSAKYLEALQKTAYSPSDyypLSSLKtLCS 401
Cdd:PRK07656 223 KAG----VN---APLMRGATILPL---PVF-DPDEVFRLIETERITVLpGPPTMYNSLLQHPDRSAED---LSSLR-LAV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 402 TGSVLYPKQfdyVYANIKADLHLASISGG---TDICG--CFV-LGNPISPVyRGECQGAGLGLDVAVFNDLGQPV-IQQR 474
Cdd:PRK07656 288 TGAASMPVA---LLERFESELGVDIVLTGyglSEASGvtTFNrLDDDRKTV-AGTIGTAIAGVENKIVNELGEEVpVGEV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 475 GELVCRNsfPNQPIGFWHD----------DGqryhdaywskfsgvW-HHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGT 543
Cdd:PRK07656 364 GELLVRG--PNVMKGYYDDpeataaaidaDG--------------WlHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYP 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 544 AEIYQQVNSFPEIQDSVAVGQKIDN-DEQIILFVQLAPQCELNtllvntiKQRLRENCSpRH-----VPAQIHSISDVPR 617
Cdd:PRK07656 428 AEVEEVLYEHPAVAEAAVIGVPDERlGEVGKAYVVLKPGAELT-------EEELIAYCR-EHlakykVPRSIEFLDELPK 499
|
570
....*....|...
gi 1067526515 618 TKSGKLVELAVKQ 630
Cdd:PRK07656 500 NATGKVLKRALRE 512
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
106-642 |
3.18e-17 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 85.18 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 106 QQPEGIAVwfKNENGQSkkLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGV 185
Cdd:PRK06087 35 AMPDKIAV--VDNHGAS--YTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 186 DSVVERFGQVQPKILFCCNGYtfngkthlmeeKNGQIADAISSLHNicQIEYLHQRSLTADFNDAFSD--WNAILASYLP 263
Cdd:PRK06087 111 AELVWVLNKCQAKMFFAPTLF-----------KQTRPVDLILPLQN--QLPQLQQIVGVDKLAPATSSlsLSQIIADYEP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 264 rgLRYE-RVSFNDPLFILYSSGTTGKPK--CIAHS---------VGGT------------ILNHLKEHqLHCDIQP---G 316
Cdd:PRK06087 178 --LTTAiTTHGDELAAVLFTSGTEGLPKgvMLTHNnilaserayCARLnltwqdvfmmpaPLGHATGF-LHGVTAPfliG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 317 DRV-----FYYTT---------CGWMMwnwhvsalasGATLVIYDgspmypqpgvlwdlaeeanitlfgtsakYLEALQK 382
Cdd:PRK06087 255 ARSvlldiFTPDAclalleqqrCTCML----------GATPFIYD----------------------------LLNLLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 383 taySPSDyypLSSLKTLCSTGSVLyPKQF--DYVYANIKadlhLASISGGTDIC-GCFV-LGNPISPVyrGECQG-AGLG 457
Cdd:PRK06087 297 ---QPAD---LSALRFFLCGGTTI-PKKVarECQQRGIK----LLSVYGSTESSpHAVVnLDDPLSRF--MHTDGyAAAG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 458 LDVAVFNDLGQPVIQ-QRGELVCRNsfPNQPIGFWHDDGQ--RYHDAywskfSGVWHHGDEVEWTDNGGIRFYGRSDTTL 534
Cdd:PRK06087 364 VEIKVVDEARKTLPPgCEGEEASRG--PNVFMGYLDEPELtaRALDE-----EGWYYSGDLCRMDEAGYIKITGRKKDII 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 535 NPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKIDN-DEQIILFVQLAPQCelNTLLVNTIKQRL-RENCSPRHVPAQIHSI 612
Cdd:PRK06087 437 VRGGENISSREVEDILLQHPKIHDACVVAMPDERlGERSCAYVVLKAPH--HSLTLEEVVAFFsRKRVAKYKYPEHIVVI 514
|
570 580 590
....*....|....*....|....*....|
gi 1067526515 613 SDVPRTKSGKLvelaVKQLLHGETVKNLGA 642
Cdd:PRK06087 515 DKLPRTASGKI----QKFLLRKDIMRRLTQ 540
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
108-623 |
6.76e-17 |
|
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: 83.57 E-value: 6.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 108 PEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVds 187
Cdd:cd17649 1 PDAVALVFGDQ-----SLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 188 vvERFgqvqpkilfccngytfngktHLMEEKNGQiadaisslhnicqieylhqrsltadfndafsdwnAILASYLPRGLR 267
Cdd:cd17649 74 --ERL--------------------RYMLEDSGA----------------------------------GLLLTHHPRQLA 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 268 YervsfndplfILYSSGTTGKPKCIAHSvGGTILNHLKEHQLHCDIQPGDRVFYYTTCG-------WMmwnwhvSALASG 340
Cdd:cd17649 98 Y----------VIYTSGSTGTPKGVAVS-HGPLAAHCQATAERYGLTPGDRELQFASFNfdgaheqLL------PPLICG 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 341 ATLVIYDGSPMYPqPGVLWDLAEEANITLFGTSAKYL-EALQKTAYSPSDYYPlsSLKTLCSTGSVLypkQFDYVYANIK 419
Cdd:cd17649 161 ACVVLRPDELWAS-ADELAEMVRELGVTVLDLPPAYLqQLAEEADRTGDGRPP--SLRLYIFGGEAL---SPELLRRWLK 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 420 ADLHLASISGGTDICgcfvlgnpISP-VYRGECQGAGLGLDVAvfndLGQPVIQQRGELV--CRNSFPNQPIGFWHDDGQ 496
Cdd:cd17649 235 APVRLFNAYGPTEAT--------VTPlVWKCEAGAARAGASMP----IGRPLGGRSAYILdaDLNPVPVGVTGELYIGGE 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 497 ----RYH------------DAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSV 560
Cdd:cd17649 303 glarGYLgrpeltaerfvpDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAA 382
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067526515 561 AVGQKIDNDEQIILFVQLApQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd17649 383 VVALDGAGGKQLVAYVVLR-AAAAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKL 444
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
104-623 |
1.91e-16 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 82.38 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 104 AFQQPEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDF 183
Cdd:cd17655 7 AEKTPDHTAVVFEDQ-----TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 184 GVD-----------SVVERFGQVQPKILFccngytfNGKTHLMEEKNGQIADAiSSLHNICQieylhqrsltadfndafs 252
Cdd:cd17655 82 PEEriqyiledsgaDILLTQSHLQPPIAF-------IGLIDLLDEDTIYHEES-ENLEPVSK------------------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 253 dwnailasylPRGLRYervsfndplfILYSSGTTGKPKciahsvgGTILNHLKEHQLHCDIQ------PGDRVFYYTTCG 326
Cdd:cd17655 136 ----------SDDLAY----------VIYTSGSTGKPK-------GVMIEHRGVVNLVEWANkviyqgEHLRVALFASIS 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 327 WMMWNWHV-SALASGATLVIYDGSPMYPQPgVLWDLAEEANITLFGTSAKYLEALQktaysPSDYYPLSSLKTLCSTGSV 405
Cdd:cd17655 189 FDASVTEIfASLLSGNTLYIVRKETVLDGQ-ALTQYIRQNRITIIDLTPAHLKLLD-----AADDSEGLSLKHLIVGGEA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 406 LYPKQFDYVYANIKADLHLASISGGTDICGCFVLGNPISPVYRGECQGAGLGLD---VAVFNDLGQPV-IQQRGEL---- 477
Cdd:cd17655 263 LSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLGntrIYILDQYGRPQpVGVAGELyigg 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 478 --VCRnsfpnqpiGFWH----------DD----GQRyhdaywskfsgVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRI 541
Cdd:cd17655 343 egVAR--------GYLNrpeltaekfvDDpfvpGER-----------MYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRI 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 542 GTAEIYQQVNSFPEIQDSVAVGQKiDNDEQIILFVQLAPQCELNTLlvnTIKQRLRENCSPRHVPAQIHSISDVPRTKSG 621
Cdd:cd17655 404 ELGEIEARLLQHPDIKEAVVIARK-DEQGQNYLCAYIVSEKELPVA---QLREFLARELPDYMIPSYFIKLDEIPLTPNG 479
|
..
gi 1067526515 622 KL 623
Cdd:cd17655 480 KV 481
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
91-623 |
3.41e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 81.77 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 91 QAQLNYAENLLSYAFQQPEGIAVWFknengQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAgylpYM----TETLVAM 166
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDKEAVYF-----DGRRTTYAELDERVNRLANALRALGVKKGDRVA----VFdwnsHEYLEAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 167 LATTSLGAVWTST----SPDfgvdsvverfgQV-------QPKILFccngytFNGKthLMEEKNgQIADAISSLHNICQI 235
Cdd:PRK06187 74 FAVPKIGAVLHPInirlKPE-----------EIayilndaEDRVVL------VDSE--FVPLLA-AILPQLPTVRTVIVE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 236 EYLHqRSLTADFNDAFSDWNAILASYLPrglrYERVSFNDPLFILYSSGTTGKPKciahsvgGTILNH--LKEHQLHC-- 311
Cdd:PRK06187 134 GDGP-AAPLAPEVGEYEELLAAASDTFD----FPDIDENDAAAMLYTSGTTGHPK-------GVVLSHrnLFLHSLAVca 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 312 --DIQPGDRVFYYTTCGWMM-WNWHVSALASGATLVI---YDgspmypqPGVLWDLAEEANITLFGTSAKYLEAL--QKT 383
Cdd:PRK06187 202 wlKLSRDDVYLVIVPMFHVHaWGLPYLALMAGAKQVIprrFD-------PENLLDLIETERVTFFFAVPTIWQMLlkAPR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 384 AYsPSDyypLSSLKTLCSTGSVLYP---KQFDYVYaniKADlhLASISGGTDICGCFVL-----GNPISPVYRGEcQG-A 454
Cdd:PRK06187 275 AY-FVD---FSSLRLVIYGGAALPPallREFKEKF---GID--LVQGYGMTETSPVVSVlppedQLPGQWTKRRS-AGrP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 455 GLGLDVAVFNDLGQPV---IQQRGELVCRNsfPNQPIGFWHDdgqryHDAYWSKFSGVW-HHGDEVEWTDNGGIRFYGRS 530
Cdd:PRK06187 345 LPGVEARIVDDDGDELppdGGEVGEIIVRG--PWLMQGYWNR-----PEATAETIDGGWlHTGDVGYIDEDGYLYITDRI 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 531 DTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKIDN-DEQIILFVQLAPQCELNtllVNTIKQRLRENCSPRHVPAQI 609
Cdd:PRK06187 418 KDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKwGERPVAVVVLKPGATLD---AKELRAFLRGRLAKFKLPKRI 494
|
570
....*....|....
gi 1067526515 610 HSISDVPRTKSGKL 623
Cdd:PRK06187 495 AFVDELPRTSVGKI 508
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
270-622 |
4.58e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 81.33 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 270 RVSFNDPLFILYSSGTTGKPKCIAHS----VGGT--ILNHLkehqlhcDIQPGDRVFyytTCGWMMWNWHVS----ALAS 339
Cdd:cd05922 113 EVSHEDLALLLYTSGSTGSPKLVRLShqnlLANArsIAEYL-------GITADDRAL---TVLPLSYDYGLSvlntHLLR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 340 GATLVIYDGSpMYPQPgvLWDLAEEANITLFGTSAKYLEALQKTAYSPSdyyPLSSLKTLCSTGSVLYPkqfdyvyANIK 419
Cdd:cd05922 183 GATLVLTNDG-VLDDA--FWEDLREHGATGLAGVPSTYAMLTRLGFDPA---KLPSLRYLTQAGGRLPQ-------ETIA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 420 AdlhLASISGGTDI------CGCFVLGNPISPVYRGECQGA-GLGL---DVAVFNDLGQPV-IQQRGELVCRNsfPNQPI 488
Cdd:cd05922 250 R---LRELLPGAQVyvmygqTEATRRMTYLPPERILEKPGSiGLAIpggEFEILDDDGTPTpPGEPGEIVHRG--PNVMK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 489 GFWHDDGqryHDAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKIDN 568
Cdd:cd05922 325 GYWNDPP---YRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL 401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1067526515 569 DEQIILFVQLAPQCELNTLLVntikqRLRENCSPRHVPAQIHSISDVPRTKSGK 622
Cdd:cd05922 402 GEKLALFVTAPDKIDPKDVLR-----SLAERLPPYKVPATVRVVDELPLTASGK 450
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
92-623 |
5.48e-16 |
|
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: 81.36 E-value: 5.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 92 AQLNYAENLLSY------AFQQPEGIAVWFKNENGQSKKLTWQQLSDQVSIIQQWLKQN-GVEKGDVVAGYLPYMTETLV 164
Cdd:cd05928 3 EYFNFASDVLDQwadkekAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 165 AMLATTSLGAVWTSTSPDFGVDSVVERFgqvqpkilfccngYTFNGKTHLMEEKNGQIADAISSlhnicQIEYLHQRSLT 244
Cdd:cd05928 83 VNVACIRTGLVFIPGTIQLTAKDILYRL-------------QASKAKCIVTSDELAPEVDSVAS-----ECPSLKTKLLV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 245 ADFN-DAFSDWNAILASYLPRGLRYERVSfNDPLFILYSSGTTGKPKCIAHSVGGTILNHLKEHQLHCDIQPGDRVFYYT 323
Cdd:cd05928 145 SEKSrDGWLNFKELLNEASTEHHCVETGS-QEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 324 TCGWMMWNWH--VSALASGATLVIYDgSPMYPQPGVLWDLAEEANITLFGTSAKYLEALQKTAYSpsdyYPLSSLKTLCS 401
Cdd:cd05928 224 DTGWIKSAWSslFEPWIQGACVFVHH-LPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSS----YKFPSLQHCVT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 402 TGSVLYPKqfdyVYANIKAD--LHLASISGGTD---ICGCFvLGNPISPVYRGEcqgAGLGLDVAVFNDLGQPVIQ-QRG 475
Cdd:cd05928 299 GGEPLNPE----VLEKWKAQtgLDIYEGYGQTEtglICANF-KGMKIKPGSMGK---ASPPYDVQIIDDNGNVLPPgTEG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 476 ELVCRNSfPNQPIGF---WHDDGQRYHDAYWSKFsgvWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNS 552
Cdd:cd05928 371 DIGIRVK-PIRPFGLfsgYVDNPEKTAATIRGDF---YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIE 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067526515 553 FPEIQDSVAVGQKiD--NDEQIILFVQLAPQCELNT--LLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd05928 447 HPAVVESAVVSSP-DpiRGEVVKAFVVLAPQFLSHDpeQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKI 520
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
274-623 |
6.98e-16 |
|
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: 80.88 E-value: 6.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 274 NDPLFILYSSGTTGKPKCIAHsvggtilnhlkehqLHCDIQ--------------PGDRVFYYTTC--GWMMWNWHVSAL 337
Cdd:cd05959 163 DDPAFWLYSSGSTGRPKGVVH--------------LHADIYwtaelyarnvlgirEDDVCFSAAKLffAYGLGNSLTFPL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 338 ASGATLVIYdgsPMYPQPGVLWDLAEEANITLF-GTSAKYlEALQKTAYSPSdyYPLSSLKTLCSTGSVLyPKQfdyVYA 416
Cdd:cd05959 229 SVGATTVLM---PERPTPAAVFKRIRRYRPTVFfGVPTLY-AAMLAAPNLPS--RDLSSLRLCVSAGEAL-PAE---VGE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 417 NIKADLHLASISG--GTDICGCFvLGNPISPVYRGeCQGAGL-GLDVAVFNDLGQPV-IQQRGELVCRNsfPNQPIGFWH 492
Cdd:cd05959 299 RWKARFGLDILDGigSTEMLHIF-LSNRPGRVRYG-TTGKPVpGYEVELRDEDGGDVaDGEPGELYVRG--PSSATMYWN 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 493 ddgqRYHDAYwSKFSGVWHH-GDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGqkIDNDEQ 571
Cdd:cd05959 375 ----NRDKTR-DTFQGEWTRtGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVG--VEDEDG 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1067526515 572 II---LFVQLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd05959 448 LTkpkAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKI 502
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
269-623 |
7.43e-16 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 80.21 E-value: 7.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 269 ERVSFNDPLFIL-YSSGTTGKPKCIAHSvggtilnhLKEHQLHCD--------IQPGDRV-------FYYTTCGWMMWNW 332
Cdd:cd05958 91 HALTASDDICILaFTSGTTGAPKATMHF--------HRDPLASADryavnvlrLREDDRFvgspplaFTFGLGGVLLFPF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 333 HVsalasGATLVIYDGSpmyPQPGVLWDLAEEANITLFGTSAKYLEALQKTAYSPSDyypLSSLKTLCSTGSVLYPKQFD 412
Cdd:cd05958 163 GV-----GASGVLLEEA---TPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPD---LSSLRKCVSAGEALPAALHR 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 413 YVYANIKADLhLASIsGGTDICGCFV-----------LGNPIsPVYRGEcqgaglgldvaVFNDLGQPVIQ-QRGELVCR 480
Cdd:cd05958 232 AWKEATGIPI-IDGI-GSTEMFHIFIsarpgdarpgaTGKPV-PGYEAK-----------VVDDEGNPVPDgTIGRLAVR 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 481 NsfpnqPIGFWHDDGQRYHDAywskFSGVWHH-GDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDS 559
Cdd:cd05958 298 G-----PTGCRYLADKRQRTY----VQGGWNItGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAEC 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067526515 560 VAVGQKIDNDEQII-LFVQLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd05958 369 AVVGHPDESRGVVVkAFVVLRPGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKL 433
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
95-621 |
9.87e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 77.48 E-value: 9.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 95 NYAENLLSYAFQQPEGIAVWfknenGQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGA 174
Cdd:PRK06164 11 TLASLLDAHARARPDAVALI-----DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 175 VWTSTSPDFGVDSVVERFGQVQPKILFCCNGYTfngKTHLMEEKNGQIADAISSLHNICQIEylhqRSLTADFNDAFSDW 254
Cdd:PRK06164 86 TVIAVNTRYRSHEVAHILGRGRARWLVVWPGFK---GIDFAAILAAVPPDALPPLRAIAVVD----DAADATPAPAPGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 255 NAILASYLPRGL--RYERVSFNDPLFILY-SSGTTGKPKCIAHSvGGTILNHLKEHQLHCDIQPGDRVFYYT-TCGWMMW 330
Cdd:PRK06164 159 VQLFALPDPAPPaaAGERAADPDAGALLFtTSGTTSGPKLVLHR-QATLLRHARAIARAYGYDPGAVLLAALpFCGVFGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 331 NWHVSALASGATLVIydgSPMYPQPGVLWDLAEEANITLFGTSAKYLEALQKTAYSPsdyyPLSSLKtLCSTGSVLyPKQ 410
Cdd:PRK06164 238 STLLGALAGGAPLVC---EPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERA----DFPSAR-LFGFASFA-PAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 411 FDYVYANIKADLHLASISGGTDICGCFVLGnPISPVYRGECQGAGL----GLDVAVFNDLGQPVIQ--QRGELVCRNsfP 484
Cdd:PRK06164 309 GELAALARARGVPLTGLYGSSEVQALVALQ-PATDPVSVRIEGGGRpaspEARVRARDPQDGALLPdgESGEIEIRA--P 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 485 NQPIGFWHDDgqryhDAYWSKFS--GVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAV 562
Cdd:PRK06164 386 SLMRGYLDNP-----DATARALTddGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVV 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1067526515 563 GQKIDNDEQIILFVQLAPQCELNTllvNTIKQRLRENCSPRHVPAQIHSISDVPRTKSG 621
Cdd:PRK06164 461 GATRDGKTVPVAFVIPTDGASPDE---AGLMAACREALAGFKVPARVQVVEAFPVTESA 516
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
104-622 |
1.59e-14 |
|
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: 76.13 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 104 AFQQPEGIAVWfknenGQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDF 183
Cdd:cd05945 1 AAANPDRPAVV-----EGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 184 GVdsvverfgqvqpkilfccngytfngkthlmeEKNGQIADAISSlhnicqieylhqrslTADFNDAfsdwnailasylp 263
Cdd:cd05945 76 PA-------------------------------ERIREILDAAKP---------------ALLIADG------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 264 rglryervsfNDPLFILYSSGTTGKPKCIAHSVGGtiLNHLKEHQL-HCDIQPGDR------------VFYYTTcgwmmw 330
Cdd:cd05945 97 ----------DDNAYIIFTSGSTGRPKGVQISHDN--LVSFTNWMLsDFPLGPGDVflnqapfsfdlsVMDLYP------ 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 331 nwhvsALASGATLVIYDgSPMYPQPGVLWDLAEEANITLFgTSAKYLEALQKTaySPSDYYP-LSSLKTLCSTGSVLYPK 409
Cdd:cd05945 159 -----ALASGATLVPVP-RDATADPKQLFRFLAEHGITVW-VSTPSFAAMCLL--SPTFTPEsLPSLRHFLFCGEVLPHK 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 410 QFDYvyanIKADLHLASIS---GGTDICGCfVLGNPIS--------PVYRGECQGaglGLDVAVFNDLGQPVIQ-QRGEL 477
Cdd:cd05945 230 TARA----LQQRFPDARIYntyGPTEATVA-VTYIEVTpevldgydRLPIGYAKP---GAKLVILDEDGRPVPPgEKGEL 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 478 VCRNsfPNQPIGFW-----------HDDGQRyhdaywskfsgvWHH-GDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAE 545
Cdd:cd05945 302 VISG--PSVSKGYLnnpektaaaffPDEGQR------------AYRtGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEE 367
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067526515 546 IYQQVNSFPEIQDSVAVG-QKIDNDEQIILFVQLAPQCELntLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGK 622
Cdd:cd05945 368 IEAALRQVPGVKEAVVVPkYKGEKVTELIAFVVPKPGAEA--GLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGK 443
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
108-637 |
1.93e-14 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 76.63 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 108 PEGIAVW-FKNENGQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVD 186
Cdd:PRK13295 38 PDKTAVTaVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRER 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 187 SVVERFGQVQPKILFCCNgyTFNGKTHlmEEKNGQIADAISSLHNICQIEylhqrSLTAD-FNDAFSDWNAILASYLPRG 265
Cdd:PRK13295 118 ELSFMLKHAESKVLVVPK--TFRGFDH--AAMARRLRPELPALRHVVVVG-----GDGADsFEALLITPAWEQEPDAPAI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 266 LRYERVSFNDPLFILYSSGTTGKPKCIAHSvGGTILNHLKEHQLHCDIQPGDRVFYYTTCGwmmwnwHVSALASGATLVI 345
Cdd:PRK13295 189 LARLRPGPDDVTQLIYTSGTTGEPKGVMHT-ANTLMANIVPYAERLGLGADDVILMASPMA------HQTGFMYGLMMPV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 346 ydgspMYPQPGVL---WD------LAEEANITLFGTSAKYLEALQKTAYSPSdyYPLSSLKTLCSTGSVLYPKQFDYVYA 416
Cdd:PRK13295 262 -----MLGATAVLqdiWDparaaeLIRTEGVTFTMASTPFLTDLTRAVKESG--RPVSSLRTFLCAGAPIPGALVERARA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 417 NIKAdlHLASISGGTDiCGCFVLGNPISPVYR-GECQGAGL-GLDVAVFNDLGQPVIQ-QRGELVCRNsfPNQPIGFWHD 493
Cdd:PRK13295 335 ALGA--KIVSAWGMTE-NGAVTLTKLDDPDERaSTTDGCPLpGVEVRVVDADGAPLPAgQIGRLQVRG--CSNFGGYLKR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 494 DGQRYHDAywskfSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDsVAVGQKIDN--DEQ 571
Cdd:PRK13295 410 PQLNGTDA-----DGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQ-VAIVAYPDErlGER 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067526515 572 IILFVQLAPQCELNtllVNTIKQRLREN-CSPRHVPAQIHSISDVPRTKSGKLVELAVKQLLHGETV 637
Cdd:PRK13295 484 ACAFVVPRPGQSLD---FEEMVEFLKAQkVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGEDA 547
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
106-319 |
7.45e-14 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 74.75 E-value: 7.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 106 QQPEGIAVWFKnENGQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGV 185
Cdd:COG1022 23 RFPDRVALREK-EDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 186 DSVVERFGQVQPKILFCcngytfNGKTHLmeEKNGQIADAISSLHNICQIEylhQRSLTADFN-DAFSDWNAILASYLPR 264
Cdd:COG1022 102 EEVAYILNDSGAKVLFV------EDQEQL--DKLLEVRDELPSLRHIVVLD---PRGLRDDPRlLSLDELLALGREVADP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 265 GL---RYERVSFNDPLFILYSSGTTGKPK--CIAHsvgGTILNHLKEHQLHCDIQPGDRV 319
Cdd:COG1022 171 AEleaRRAAVKPDDLATIIYTSGTTGRPKgvMLTH---RNLLSNARALLERLPLGPGDRT 227
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
120-630 |
1.21e-13 |
|
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: 73.89 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 120 GQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDSVVERFGQVQPKI 199
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 200 LFCcngytfngkthlmeEKNGQIADAISSLHNICQIEYLHQRSLTADFND-----AFSDWNAILASYLPRGLRyervsfN 274
Cdd:cd05926 90 VLT--------------PKGELGPASRAASKLGLAILELALDVGVLIRAPsaeslSNLLADKKNAKSEGVPLP------D 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 275 DPLFILYSSGTTGKPKciahSVGGTILNHL-------KEHQLhcdiQPGDRVFYyttcgwMMWNWHV--------SALAS 339
Cdd:cd05926 150 DLALILHTSGTTGRPK----GVPLTHRNLAasatnitNTYKL----TPDDRTLV------VMPLFHVhglvasllSTLAA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 340 GATLVIydgsPMYPQPGVLWDLAEEANITLFgTSAKYLEALQKTAYSPSDYYPLSSLKTLCSTGSVLYPKqfdyVYANIK 419
Cdd:cd05926 216 GGSVVL----PPRFSASTFWPDVRDYNATWY-TAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPA----VLEALE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 420 ADLHLASIS--GGTDICGCfVLGNPISPVYRGECQ-GAGLGLDVAVFNDLGQPVIQ-QRGELVCRNsfPNQPIGFWHDdg 495
Cdd:cd05926 287 ATFGAPVLEayGMTEAAHQ-MTSNPLPPGPRKPGSvGKPVGVEVRILDEDGEILPPgVVGEICLRG--PNVTRGYLNN-- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 496 qryHDAYWSKFS--GVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKIDN-DEQI 572
Cdd:cd05926 362 ---PEANAEAAFkdGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKyGEEV 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1067526515 573 ILFVQLAPQcelNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLVELAVKQ 630
Cdd:cd05926 439 AAAVVLREG---ASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
259-623 |
1.61e-13 |
|
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: 73.20 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 259 ASYLPRGLRY--ERVSF--------------NDPLFILYSSGTTGKPKCIahsvggtilnhLKEH----QLHCDIQ---- 314
Cdd:cd17648 63 AAYVPIDPSYpdERIQFiledtgarvvitnsTDLAYAIYTSGTTGKPKGV-----------LVEHgsvvNLRTSLSeryf 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 315 ---PGD-RVFYYTTcgwMMWNWHVS----ALASGATLVIYDGSpMYPQPGVLWDLAEEANIT-LFGTSAkyleALQKTay 385
Cdd:cd17648 132 grdNGDeAVLFFSN---YVFDFFVEqmtlALLNGQKLVVPPDE-MRFDPDRFYAYINREKVTyLSGTPS----VLQQY-- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 386 spsDYYPLSSLKTLCSTGSVLYPKQFD-------------Y------VYANIK-------ADLHLASISGGTDicgCFVL 439
Cdd:cd17648 202 ---DLARLPHLKRVDAAGEEFTAPVFEklrsrfagliinaYgptettVTNHKRffpgdqrFDKSLGRPVRNTK---CYVL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 440 GNPISPV---YRGECQGAGLGLDVAVFNdlgqpviqqRGELVcRNSFPNQPIgfwhddgQRYHDAYWSKFSGVWHHGDEV 516
Cdd:cd17648 276 NDAMKRVpvgAVGELYLGGDGVARGYLN---------RPELT-AERFLPNPF-------QTEQERARGRNARLYKTGDLV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 517 EWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKI--DNDEQIILFVQLAPQCELNTLLVNTIKQ 594
Cdd:cd17648 339 RWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDasQAQSRIQKYLVGYYLPEPGHVPESDLLS 418
|
410 420
....*....|....*....|....*....
gi 1067526515 595 RLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd17648 419 FLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
103-623 |
2.04e-13 |
|
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: 73.15 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 103 YAFQQPEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPD 182
Cdd:cd17651 4 QAARTPDAPALVAEGR-----RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 183 FGVDSVVERFGQVQPKILFCCNGYTFngkthlmeekngqiadaisslhnicqieylhqRSLTADFNDAFSDWNAILAsyL 262
Cdd:cd17651 79 YPAERLAFMLADAGPVLVLTHPALAG--------------------------------ELAVELVAVTLLDQPGAAA--G 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 263 PRGLRYERVSFNDPLFILYSSGTTGKPKCIAHSvGGTILNHLKEHQLHCDIQPGDRVFYYTTCGWMMWNWHV-SALASGA 341
Cdd:cd17651 125 ADAEPDPALDADDLAYVIYTSGSTGRPKGVVMP-HRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIfSTLCAGA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 342 TLVIyDGSPMYPQPGVLWDLAEEANITLFGTSAKYLEALQKTAYSPSDYypLSSLKTLCSTGS--VLYPKQFDYVYANIK 419
Cdd:cd17651 204 TLVL-PPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVR--LAALRYLLTGGEqlVLTEDLREFCAGLPG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 420 ADLHLASISGGTDICGCFVLGNPISPVYRGECQGAGL-GLDVAVFNDLGQPV-IQQRGEL------VCRnsfpnqpiGFW 491
Cdd:cd17651 281 LRLHNHYGPTETHVVTALSLPGDPAAWPAPPPIGRPIdNTRVYVLDAALRPVpPGVPGELyiggagLAR--------GYL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 492 HDDG---QRYHDAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDS-VAVGQKID 567
Cdd:cd17651 353 NRPEltaERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAvVLAREDRP 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1067526515 568 NDEQIILFVQLAPQCELNTllvNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd17651 433 GEKRLVAYVVGDPEAPVDA---AELRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
275-622 |
2.50e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 72.03 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 275 DPLFILYSSGTTGKPKCI---AHSVGGTIL---NHLKEHQLHCDIQ-------PGDRVFyyTTCGWM----MWNWhVSAL 337
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVmwrQEDIFRMLMggaDFGTGEFTPSEDAhkaaaaaAGTVMF--PAPPLMhgtgSWTA-FGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 338 ASGATLVIYDgsPMYpQPGVLWDLAEEANITLF-----GTSAKYLEALQKtayspSDYYPLSSLKTLCSTGSVLYPKQFD 412
Cdd:cd05924 81 LGGQTVVLPD--DRF-DPEEVWRTIEKHKVTSMtivgdAMARPLIDALRD-----AGPYDLSSLFAISSGGALLSPEVKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 413 YVYAnIKADLHLasisggTDICGCFVLGNPISPVYRGECQGAG----LGLDVAVFNDLGQPVIQQRGEL--VCRNSfpNQ 486
Cdd:cd05924 153 GLLE-LVPNITL------VDAFGSSETGFTGSGHSAGSGPETGpftrANPDTVVLDDDGRVVPPGSGGVgwIARRG--HI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 487 PIGFWHD-----------DGQRYhdaywsKFSGvwhhgDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPE 555
Cdd:cd05924 224 PLGYYGDeaktaetfpevDGVRY------AVPG-----DRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPA 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067526515 556 IQDSVAVGQKidnDE----QIILFVQLAPQCELNtllvntiKQRLRENCSPR----HVPAQIHSISDVPRTKSGK 622
Cdd:cd05924 293 VYDVLVVGRP---DErwgqEVVAVVQLREGAGVD-------LEELREHCRTRiaryKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
124-623 |
3.04e-13 |
|
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: 72.31 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 124 KLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDfgvdsvverfgqvQPKilfcc 203
Cdd:cd17646 23 TLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG-------------YPA----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 204 ngytfngkthlmEEKNGQIADAISSLhnicqieYLHQRSLTADF---NDAFSDWNAILASYlPRGLRYERVSFNDPLFIL 280
Cdd:cd17646 85 ------------DRLAYMLADAGPAV-------VLTTADLAARLpagGDVALLGDEALAAP-PATPPLVPPRPDNLAYVI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 281 YSSGTTGKPK--CIAHsvgGTILNHLKEHQLHCDIQPGDRVFYYTTCG-----WMMWnWhvsALASGATLVIY--DGspm 351
Cdd:cd17646 145 YTSGSTGRPKgvMVTH---AGIVNRLLWMQDEYPLGPGDRVLQKTPLSfdvsvWELF-W---PLVAGARLVVArpGG--- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 352 YPQPGVLWDLAEEANITL--FGTSAkyLEALQKTAYSPSdyypLSSLKTLCSTGSVLYPKQFDYVYANIKADLH------ 423
Cdd:cd17646 215 HRDPAYLAALIREHGVTTchFVPSM--LRVFLAEPAAGS----CASLRRVFCSGEALPPELAARFLALPGAELHnlygpt 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 424 LASIsggtDICGCFVLGN------PI-SPVYRGEcqgaglgldVAVFNDLGQPV-IQQRGEL------VCRNSFpNQP-- 487
Cdd:cd17646 289 EAAI----DVTHWPVRGPaetpsvPIgRPVPNTR---------LYVLDDALRPVpVGVPGELylggvqLARGYL-GRPal 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 488 -----IGFWHDDGQRyhdaywskfsgVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAV 562
Cdd:cd17646 355 taerfVPDPFGPGSR-----------MYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVV 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067526515 563 GQKI-DNDEQIILFVQLAPQCElnTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd17646 424 ARAApAGAARLVGYVVPAAGAA--GPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKL 483
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
111-622 |
3.99e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 72.24 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 111 IAVWFKNENGQsKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDSVVE 190
Cdd:PRK04319 61 VALRYLDASRK-EKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 191 RFGQVQPKILFCCNGytfngkthLMEEKngqIADAISSLHNICQIEylhqrsLTADFNDAFSDWNAILAsYLPRGLRYER 270
Cdd:PRK04319 140 RLEDSEAKVLITTPA--------LLERK---PADDLPSLKHVLLVG------EDVEEGPGTLDFNALME-QASDEFDIEW 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 271 VSFNDPLFILYSSGTTGKPKCIAHsVGGTILNHLKEHQLHCDIQPGDRvfYYTTC--GWMMWNWH--VSALASGATLVIy 346
Cdd:PRK04319 202 TDREDGAILHYTSGSTGKPKGVLH-VHNAMLQHYQTGKYVLDLHEDDV--YWCTAdpGWVTGTSYgiFAPWLNGATNVI- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 347 DGSPMYPQPgvlW-DLAEEANITLFGTSAKYLEALQKTAYSPSDYYPLSSLKTLCSTGSVLYP-------KQFD------ 412
Cdd:PRK04319 278 DGGRFSPER---WyRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPLNPevvrwgmKVFGlpihdn 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 413 --------YVYANIKA-DLHLASisggtdicgcfvLGNPIsPvyrgecqgaglGLDVAVFNDLGQPVIQQR-GELVCRNS 482
Cdd:PRK04319 355 wwmtetggIMIANYPAmDIKPGS------------MGKPL-P-----------GIEAAIVDDQGNELPPNRmGNLAIKKG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 483 FPNQPIGFWHDDgQRYHdaywSKFSGVWH-HGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVA 561
Cdd:PRK04319 411 WPSMMRGIWNNP-EKYE----SYFAGDWYvSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1067526515 562 VGqKID--NDEQIILFVQLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGK 622
Cdd:PRK04319 486 IG-KPDpvRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGK 547
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
108-623 |
1.25e-12 |
|
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: 70.28 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 108 PEGIAVWFKNengqsKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVwtstspdfgvds 187
Cdd:cd05936 13 PDKTALIFMG-----RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV------------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 188 VVerfgQVQPKilfccngYTFNGKTHLMeeKNGQIADAISslhnicqieylhqrslTADFNDAFSDWnailasylPRGLR 267
Cdd:cd05936 76 VV----PLNPL-------YTPRELEHIL--NDSGAKALIV----------------AVSFTDLLAAG--------APLGE 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 268 YERVSFNDPLFILYSSGTTGKPKciahsvgGTILNH---------LKEHqLHCDIQPGDR---------VFYYTTCGwmm 329
Cdd:cd05936 119 RVALTPEDVAVLQYTSGTTGVPK-------GAMLTHrnlvanalqIKAW-LEDLLEGDDVvlaalplfhVFGLTVAL--- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 330 wnwhVSALASGATLVIydgSPMYPQPGVLWDLAEEaNITLF-GTSAKYLEALQKTAYSPSDyypLSSLKTLCSTGSVLYP 408
Cdd:cd05936 188 ----LLPLALGATIVL---IPRFRPIGVLKEIRKH-RVTIFpGVPTMYIALLNAPEFKKRD---FSSLRLCISGGAPLPV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 409 KqfdyVYANIKADLHLASISG-GTDICGCFVLGNPISPVYR-GECqgaGL---GLDVAVFNDLGQPVIQ-QRGELVCRNs 482
Cdd:cd05936 257 E----VAERFEELTGVPIVEGyGLTETSPVVAVNPLDGPRKpGSI---GIplpGTEVKIVDDDGEELPPgEVGELWVRG- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 483 fPNQPIGFWHDDG---QRYHDaywskfsGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDS 559
Cdd:cd05936 329 -PQVMKGYWNRPEetaEAFVD-------GWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEA 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067526515 560 VAVGQKiDND--EQIILFVQLAPQcelNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd05936 401 AVVGVP-DPYsgEAVKAFVVLKEG---ASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKI 462
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
96-345 |
1.75e-12 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 70.29 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 96 YAENLLSYAFQQ-----PEGIAVWFkneNGQSkkLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATT 170
Cdd:PRK08279 34 DSKRSLGDVFEEaaarhPDRPALLF---EDQS--ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 171 SLGAVwtstspdfgV---------DSVVERFGQVQPKILfccngytfngkthLMEEKNGQIADAISSLHNICQIEYLHQr 241
Cdd:PRK08279 109 KLGAV---------VallntqqrgAVLAHSLNLVDAKHL-------------IVGEELVEAFEEARADLARPPRLWVAG- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 242 SLTADFNDAFSDWNAILASY--LPRGLRyERVSFNDPLFILYSSGTTGKPK----------CIAHSVGGTIlnhlkehql 309
Cdd:PRK08279 166 GDTLDDPEGYEDLAAAAAGAptTNPASR-SGVTAKDTAFYIYTSGTTGLPKaavmshmrwlKAMGGFGGLL--------- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1067526515 310 hcDIQPGDRV-----FYYTTCGWMMWNwhvSALASGATLVI 345
Cdd:PRK08279 236 --RLTPDDVLycclpLYHNTGGTVAWS---SVLAAGATLAL 271
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
108-623 |
4.43e-12 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 68.65 E-value: 4.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 108 PEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFgvds 187
Cdd:cd17656 2 PDAVAVVFENQ-----KLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEY---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 188 vverfgqvqPKilfccngytfngkthlmEEKNGQIADAISSLhnicqieYLHQRSLTADFNDAFS----DWNAIlASYLP 263
Cdd:cd17656 73 ---------PE-----------------ERRIYIMLDSGVRV-------VLTQRHLKSKLSFNKStillEDPSI-SQEDT 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 264 RGLRYErVSFNDPLFILYSSGTTGKPKCIA--HSvggTILNHLKEHQLHCDIQPGDRVFYYTTCGW-MMWNWHVSALASG 340
Cdd:cd17656 119 SNIDYI-NNSDDLLYIIYTSGTTGKPKGVQleHK---NMVNLLHFEREKTNINFSDKVLQFATCSFdVCYQEIFSTLLSG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 341 ATLVIYDGSPMYPQPGvLWDLAEEANI-TLFgtsakYLEALQKTAYSPSDYYP--LSSLKTLCSTGSVLYPKQ-FDYVYA 416
Cdd:cd17656 195 GTLYIIREETKRDVEQ-LFDLVKRHNIeVVF-----LPVAFLKFIFSEREFINrfPTCVKHIITAGEQLVITNeFKEMLH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 417 NIKADLH------------LASISGGTDICGCFVLGNPISPVyrgecqgaglglDVAVFNDLGQPV-IQQRGEL------ 477
Cdd:cd17656 269 EHNVHLHnhygpsethvvtTYTINPEAEIPELPPIGKPISNT------------WIYILDQEQQLQpQGIVGELyisgas 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 478 VCRNSFPNQPIgfwhdDGQRYHDAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQ 557
Cdd:cd17656 337 VARGYLNRQEL-----TAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVS 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067526515 558 DSVAVGQKIDNDEQIIlfvqLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd17656 412 EAVVLDKADDKGEKYL----CAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKV 473
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
256-623 |
7.44e-12 |
|
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: 67.72 E-value: 7.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 256 AIL---ASYLPRGLRY--ERVSF--------------NDPLFILYSSGTTGKPKciahsvgGTILNH------LKEHQLH 310
Cdd:cd17643 56 AILkagGAYVPIDPAYpvERIAFiladsgpsllltdpDDLAYVIYTSGSTGRPK-------GVVVSHanvlalFAATQRW 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 311 CDIQPGDRVFYYTTCG-----WMMWnwhvSALASGATLVI--YDGSpmyPQPGVLWDLAEEANITLFGTSAKYLEALQKT 383
Cdd:cd17643 129 FGFNEDDVWTLFHSYAfdfsvWEIW----GALLHGGRLVVvpYEVA---RSPEDFARLLRDEGVTVLNQTPSAFYQLVEA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 384 AYSPSDyyPLSSLKTLCSTGSVLYPKQFDYVYANIKADL-HLASISGGTDICgCFVLGNPISPVYRGECQ----GAGL-G 457
Cdd:cd17643 202 ADRDGR--DPLALRYVIFGGEALEAAMLRPWAGRFGLDRpQLVNMYGITETT-VHVTFRPLDAADLPAAAaspiGRPLpG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 458 LDVAVFNDLGQPVIQQR-GEL------VCR----------NSFPNQPIGfwhDDGQRYhdaywskfsgvWHHGDEVEWTD 520
Cdd:cd17643 279 LRVYVLDADGRPVPPGVvGELyvsgagVARgylgrpeltaERFVANPFG---GPGSRM-----------YRTGDLARRLP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 521 NGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDsVAVGQKIDNDEQIILFVQLAPQcELNTLLVNTIKQRLRENC 600
Cdd:cd17643 345 DGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRD-AAVIVREDEPGDTRLVAYVVAD-DGAAADIAELRALLKELL 422
|
410 420
....*....|....*....|...
gi 1067526515 601 SPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd17643 423 PDYMVPARYVPLDALPLTVNGKL 445
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
88-632 |
1.41e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 67.33 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 88 WFPqAQLNYAENLLSYAFQQ-----PEGIAVWFKnengqSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTET 162
Cdd:PRK05605 22 WTP-HDLDYGDTTLVDLYDNavarfGDRPALDFF-----GATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 163 LVAMLATTSLGAVwtstspdfgvdsVVERfgqvQPKilfccngYTFNGKTHLMEEKNGQIA---DAISS----------L 229
Cdd:PRK05605 96 IVAFYAVLRLGAV------------VVEH----NPL-------YTAHELEHPFEDHGARVAivwDKVAPtverlrrttpL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 230 HNICQIEY-----LHQR---------------SLTAdFNDAFSDWNAILASYLPR---GLRYERVSFNDPLFILYSSGTT 286
Cdd:PRK05605 153 ETIVSVNMiaampLLQRlalrlpipalrkaraALTG-PAPGTVPWETLVDAAIGGdgsDVSHPRPTPDDVALILYTSGTT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 287 GKPKciahsvgGTILNHLkehQLHC----------DIQPGDRVFY--------Y--TTCGWMmwnwhvsALASGATLVIY 346
Cdd:PRK05605 232 GKPK-------GAQLTHR---NLFAnaaqgkawvpGLGDGPERVLaalpmfhaYglTLCLTL-------AVSIGGELVLL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 347 DgSPMYPQ-------------PGV------LWDLAEEANITLfgTSAKYlealqktAYSPSDYYPLSSLKTLCS-TGSVL 406
Cdd:PRK05605 295 P-APDIDLildamkkhpptwlPGVpplyekIAEAAEERGVDL--SGVRN-------AFSGAMALPVSTVELWEKlTGGLL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 407 ypkqfdyvyanikadlhlasISG-GTDICGCFVLGNPISPVYRgecqgAG-LGL-----DVAVFN--DLG--QPViQQRG 475
Cdd:PRK05605 365 --------------------VEGyGLTETSPIIVGNPMSDDRR-----PGyVGVpfpdtEVRIVDpeDPDetMPD-GEEG 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 476 ELVCRNsfPNQPIGFWHDDgqryhDAYWSKFSGVWHH-GDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFP 554
Cdd:PRK05605 419 ELLVRG--PQVFKGYWNRP-----EETAKSFLDGWFRtGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHP 491
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067526515 555 EIQDSVAVG-QKIDNDEQIILFVQLAPQCELNTllvNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLVELAVKQLL 632
Cdd:PRK05605 492 GVEDAAVVGlPREDGSEEVVAAVVLEPGAALDP---EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREEL 567
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
275-632 |
1.73e-11 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 65.82 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 275 DPLFILYSSGTTGKPKCIAHSVggtiLNHLKE----HQ-LHCDiqPGDRVF-----YYTTCGWMMWNWhvsaLASGATLV 344
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTA----ANLLASaaglHSrLGFG--GGDSWLlslplYHVGGLAILVRS----LLAGAELV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 345 IydgspmypqPGVLWDLAEeaNITLFGTSAKYL--EALQKTAYSPSDYYPLSSLKTLCSTGSVLYPkqfdyVYANIKADL 422
Cdd:cd17630 71 L---------LERNQALAE--DLAPPGVTHVSLvpTQLQRLLDSGQGPAALKSLRAVLLGGAPIPP-----ELLERAADR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 423 HLASISG------GTDICGCFVLGNPISPVYRgecqgAGLGLDVAVFNDlgqPVIQQRGELVCRNSFPNQPIGFWHDDGq 496
Cdd:cd17630 135 GIPLYTTygmtetASQVATKRPDGFGRGGVGV-----LLPGRELRIVED---GEIWVGGASLAMGYLRGQLVPEFNEDG- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 497 ryhdaywskfsgvWHH-GDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKidnD----EQ 571
Cdd:cd17630 206 -------------WFTtKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVP---DeelgQR 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067526515 572 IILFVQLAPQcelntLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLVELAVKQLL 632
Cdd:cd17630 270 PVAVIVGRGP-----ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
107-623 |
2.41e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 67.67 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 107 QPEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVD 186
Cdd:PRK12316 524 TPEAPALAFGEE-----TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAE 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 187 SVverfgqvqpkilfccngytfngkTHLMEEKNGQIadaisslhnicqieYLHQRSL--TADFND-----AFSDWNAILA 259
Cdd:PRK12316 599 RL-----------------------AYMLEDSGVQL--------------LLSQSHLgrKLPLAAgvqvlDLDRPAAWLE 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 260 SYLPRGLRYERVSFNdPLFILYSSGTTGKPK--CIAHSvggTILNHLKEHQLHCDIQPGDRVFYYTTCG-----WMMWnW 332
Cdd:PRK12316 642 GYSEENPGTELNPEN-LAYVIYTSGSTGKPKgaGNRHR---ALSNRLCWMQQAYGLGVGDTVLQKTPFSfdvsvWEFF-W 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 333 hvsALASGATLVIYdGSPMYPQPGVLWDLAEEANITLFGTSAKYLEALQKTAYSPSdyypLSSLKTLCSTGSVLYPKQFD 412
Cdd:PRK12316 717 ---PLMSGARLVVA-APGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVAS----CTSLRRIVCSGEALPADAQE 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 413 YVYANiKADLHLASISGGT----DIC---------------------GCFVL---GNPISPVYRGECQGAGLGLDVAVFn 464
Cdd:PRK12316 789 QVFAK-LPQAGLYNLYGPTeaaiDVThwtcveeggdsvpigrpianlACYILdanLEPVPVGVLGELYLAGRGLARGYH- 866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 465 dlgqpviqQRGELVCRNSFPNqPIGfwhdDGQRyhdaywskfsgVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTA 544
Cdd:PRK12316 867 --------GRPGLTAERFVPS-PFV----AGER-----------MYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELG 922
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067526515 545 EIYQQVNSFPEIQDSVAVGQkidNDEQIILFVqlAPQCELNTlLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:PRK12316 923 EIEARLLEHPWVREAAVLAV---DGKQLVGYV--VLESEGGD-WREALKAHLAASLPEYMVPAQWLALERLPLTPNGKL 995
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
104-623 |
2.55e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 67.49 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 104 AFQQPEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDF 183
Cdd:PRK12467 522 ARQHPERPALVFGEQ-----VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEY 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 184 GVDSVVERFGQVQPKILFccngytfnGKTHLMeeKNGQIADAISSLhnicqieylhQRSLTADFNDAFSDWNAILAsYLP 263
Cdd:PRK12467 597 PQDRLAYMLDDSGVRLLL--------TQSHLL--AQLPVPAGLRSL----------CLDEPADLLCGYSGHNPEVA-LDP 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 264 RGLRYervsfndplfILYSSGTTGKPKCIAHSvGGTILNHLKEHQLHCDIQPGDRVFYYTTCGWMMWNWHV-SALASGAT 342
Cdd:PRK12467 656 DNLAY----------VIYTSGSTGQPKGVAIS-HGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELfGALASGAT 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 343 LVIYDgspmypqPGVLWDLAEeanitlfgtSAKYLEALQKTAYSpsdyYPLSSLKTLCSTGSVLYPKQFDYVYANIKA-- 420
Cdd:PRK12467 725 LHLLP-------PDCARDAEA---------FAALMADQGVTVLK----IVPSHLQALLQASRVALPRPQRALVCGGEAlq 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 421 -DLhLASISGGTDICGCFVLGNPISP---VYRGECQGAGLgldVAVFNDLGQPvIQQRGELV---CRNSFPNQPIGFWHD 493
Cdd:PRK12467 785 vDL-LARVRALGPGARLINHYGPTETtvgVSTYELSDEER---DFGNVPIGQP-LANLGLYIldhYLNPVPVGVVGELYI 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 494 DGQ----RYH------------DAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQ 557
Cdd:PRK12467 860 GGAglarGYHrrpaltaerfvpDPFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVR 939
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067526515 558 DSVAVGQKIDNDEQIILFV--QLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:PRK12467 940 EAVVLAQPGDAGLQLVAYLvpAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKL 1007
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
275-623 |
3.09e-11 |
|
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: 65.12 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 275 DPLFILYSSGTTGKPKCIA---HSVGGTILNHLKEHQLHCD---IQPGDRVFYYTTCGWMmwnwhvSALASGATLVIYDG 348
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYrseRSWIESFVCNEDLFNISGEdaiLAPGPLSHSLFLYGAI------SALYLGGTFIGQRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 349 SpmypQPGVLWDLAEEANITLFGTSAKYLEALQKTayspsdYYPLSSLKTLCSTGSVLYPKQFDyVYANIKADLHLASIS 428
Cdd:cd17633 75 F----NPKSWIRKINQYNATVIYLVPTMLQALART------LEPESKIKSIFSSGQKLFESTKK-KLKNIFPKANLIEFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 429 GGTDIcgcfvlgNPISPVYRGECQGAglgldvavfNDLGQPVIQQRGELvcRNSfPNQPIGFWHDDGQRYHDAYWS-KFS 507
Cdd:cd17633 144 GTSEL-------SFITYNFNQESRPP---------NSVGRPFPNVEIEI--RNA-DGGEIGKIFVKSEMVFSGYVRgGFS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 508 GV--WHHGDEVEWTDNGG-IRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKIDNDEQIILFVqlapqCEL 584
Cdd:cd17633 205 NPdgWMSVGDIGYVDEEGyLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVAL-----YSG 279
|
330 340 350
....*....|....*....|....*....|....*....
gi 1067526515 585 NTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd17633 280 DKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
274-633 |
3.94e-11 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 65.64 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 274 NDPLFILYSSGTTGKPKciahsvgGTILNH------LKEHQLHCDIQPGDRVFYYTTCGW-MMWNWHVSALASGATLVIy 346
Cdd:cd05918 106 SDAAYVIFTSGSTGKPK-------GVVIEHralstsALAHGRALGLTSESRVLQFASYTFdVSILEIFTTLAAGGCLCI- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 347 dgspmypqpgvlwdLAEEANITLFgtsAKYLEALQKTA----------YSPSDyypLSSLKTLCSTGSVLYPKQFD---- 412
Cdd:cd05918 178 --------------PSEEDRLNDL---AGFINRLRVTWafltpsvarlLDPED---VPSLRTLVLGGEALTQSDVDtwad 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 413 -------Y---------VYANIKADLHLASISGGTDiCGCFVL--GNPISPVYRGecqgaglgldvAVfndlGQPVIQqr 474
Cdd:cd05918 238 rvrlinaYgpaectiaaTVSPVVPSTDPRNIGRPLG-ATCWVVdpDNHDRLVPIG-----------AV----GELLIE-- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 475 GELVCRnsfpnqpiGFWHDDGQR----YHDAYWSKFSGVWHH------GDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTA 544
Cdd:cd05918 300 GPILAR--------GYLNDPEKTaaafIEDPAWLKQEGSGRGrrlyrtGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELG 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 545 EIYQQVNSFPEIQDSVAVG--QKIDNDEQIIL--FVQLAP--------------QCELNTLLVNTIKQRLREnCSPRH-V 605
Cdd:cd05918 372 EIEHHLRQSLPGAKEVVVEvvKPKDGSSSPQLvaFVVLDGsssgsgdgdslflePSDEFRALVAELRSKLRQ-RLPSYmV 450
|
410 420
....*....|....*....|....*...
gi 1067526515 606 PAQIHSISDVPRTKSGKLVELAVKQLLH 633
Cdd:cd05918 451 PSVFLPLSHLPLTASGKIDRRALRELAE 478
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
108-623 |
1.70e-10 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 63.64 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 108 PEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFgvds 187
Cdd:cd17650 1 PDAIAVSDATR-----QLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDY---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 188 vverfgqvqPKilfccngytfngkthlmeekngqiadaisslhniCQIEYLhqrsltadfndaFSDWNAILASYLPrglr 267
Cdd:cd17650 72 ---------PA----------------------------------ERLQYM------------LEDSGAKLLLTQP---- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 268 yervsfNDPLFILYSSGTTGKPKC-------IAHSVGG---------TILNHLKEHQLHCDIQPGDrvfyyttcgwmmwn 331
Cdd:cd17650 93 ------EDLAYVIYTSGTTGKPKGvmvehrnVAHAAHAwrreyeldsFPVRLLQMASFSFDVFAGD-------------- 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 332 wHVSALASGATLVIY-DGSPMYPQpgVLWDLAEEANITLFGTSAKYLEALQKtaYSPSDYYPLSSLKTLCSTGSVLYPKQ 410
Cdd:cd17650 153 -FARSLLNGGTLVICpDEVKLDPA--ALYDLILKSRITLMESTPALIRPVMA--YVYRNGLDLSAMRLLIVGSDGCKAQD 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 411 FDYVYANIKADLHLASISGGTDICgcfvlgnpI-SPVYRGECQGAGLGLDVAVfndlGQP-------VIQQR-------- 474
Cdd:cd17650 228 FKTLAARFGQGMRIINSYGVTEAT--------IdSTYYEEGRDPLGDSANVPI----GRPlpntamyVLDERlqpqpvgv 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 475 -GEL------VCRnsfpnqpiGFWHDD---GQRYHDAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTA 544
Cdd:cd17650 296 aGELyiggagVAR--------GYLNRPeltAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELG 367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 545 EIYQQVNSFPEIQDSVAVGQKiDNDEQIILFVQLAPQCELNTllvntikQRLRENCSPR----HVPAQIHSISDVPRTKS 620
Cdd:cd17650 368 EIESQLARHPAIDEAVVAVRE-DKGGEARLCAYVVAAATLNT-------AELRAFLAKElpsyMIPSYYVQLDALPLTPN 439
|
...
gi 1067526515 621 GKL 623
Cdd:cd17650 440 GKV 442
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
256-623 |
2.19e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 63.11 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 256 AIL---ASYLPRGLRY--ERVSF--------------NDPLFILYSSGTTGKPK--CIAHSVGGTILNHLKEHQlhcdiq 314
Cdd:cd12115 68 AVLkagAAYVPLDPAYppERLRFiledaqarlvltdpDDLAYVIYTSGSTGRPKgvAIEHRNAAAFLQWAAAAF------ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 315 PGD---RVFYYTTCGWMMWNWHVSA-LASGATLVIYDGSPmypqpgVLWDLAEEANITLFGTSAKYLEALQKTAYSPSdy 390
Cdd:cd12115 142 SAEelaGVLASTSICFDLSVFELFGpLATGGKVVLADNVL------ALPDLPAAAEVTLINTVPSAAAELLRHDALPA-- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 391 yplsSLKTLCSTGSVLYPKQFDYVYANikadLHLASIsggtdicgcFVLGNP--------ISPVYRGECQGAGLGLDVA- 461
Cdd:cd12115 214 ----SVRVVNLAGEPLPRDLVQRLYAR----LQVERV---------VNLYGPsedttystVAPVPPGASGEVSIGRPLAn 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 462 ----VFNDLGQPV-IQQRGEL------VCRnsfpnqpiGFWHDDGQ---RYHDAYWSKFSGVWHHGDEVEWTDNGGIRFY 527
Cdd:cd12115 277 tqayVLDRALQPVpLGVPGELyiggagVAR--------GYLGRPGLtaeRFLPDPFGPGARLYRTGDLVRWRPDGLLEFL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 528 GRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQK-IDNDEQIILFVQL-APQCELNTLLVNTIKQRLrencsPRH- 604
Cdd:cd12115 349 GRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGdAAGERRLVAYIVAePGAAGLVEDLRRHLGTRL-----PAYm 423
|
410
....*....|....*....
gi 1067526515 605 VPAQIHSISDVPRTKSGKL 623
Cdd:cd12115 424 VPSRFVRLDALPLTPNGKI 442
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
277-623 |
4.66e-10 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 62.45 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 277 LFILYSSGTTGKPK--CIAHSvggTILNHLKEHQLHCDIQPGDRVFYYTTCGwmmwnWHVSA------LASGATLVIYDG 348
Cdd:cd17644 109 AYVIYTSGSTGKPKgvMIEHQ---SLVNLSHGLIKEYGITSSDRVLQFASIA-----FDVAAeeiyvtLLSGATLVLRPE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 349 SpMYPQPGVLWDLAEEANITLFGTSAKYLEALqKTAYSPSDYYPLSSLKTLCSTGSVLYPK-------------QFDYVY 415
Cdd:cd17644 181 E-MRSSLEDFVQYIQQWQLTVLSLPPAYWHLL-VLELLLSTIDLPSSLRLVIVGGEAVQPElvrqwqknvgnfiQLINVY 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 416 ----ANIKADLHLASISGGTDICGcFVLGNPIS--------------PV-YRGECQGAGLGLDVAVFNdlgqpviqqRGE 476
Cdd:cd17644 259 gpteATIAATVCRLTQLTERNITS-VPIGRPIAntqvyildenlqpvPVgVPGELHIGGVGLARGYLN---------RPE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 477 LVcRNSFPNQPigFWHDDGQRYHDAywskfsgvwhhGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEI 556
Cdd:cd17644 329 LT-AEKFISHP--FNSSESERLYKT-----------GDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDV 394
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067526515 557 QDSVAVGQKID-NDEQIILFVqlAPQCElNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd17644 395 KTAVVIVREDQpGNKRLVAYI--VPHYE-ESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKI 459
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
74-623 |
6.05e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.05 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 74 IARWDDFTAArdtiwFPqAQLNYAENLLSYAFQQPEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGVEKGDVVA 153
Cdd:PRK12316 1989 LADWDRTPEA-----YP-RGPGVHQRIAEQAARAPEAIAVVFGDQ-----HLSYAELDSRANRLAHRLRARGVGPEVRVA 2057
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 154 GYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDSVVERFGQVQPKILFCcngytfngKTHLMEEKngQIADAISSLhnic 233
Cdd:PRK12316 2058 IAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT--------QRHLLERL--PLPAGVARL---- 2123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 234 qieylhqrSLTADfnDAFSDWnailasylPRGLRYERVSFNDPLFILYSSGTTGKPKCIAHSvGGTILNHLKEHQLHCDI 313
Cdd:PRK12316 2124 --------PLDRD--AEWADY--------PDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVS-HGALVAHCQAAGERYEL 2184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 314 QPGDRVFYYTTCGW--MMWNWHVSaLASGATLVIYDGSPMYPQPgvLWDLAEEANITLFGTSAKYLEALQKTAYspSDYY 391
Cdd:PRK12316 2185 SPADCELQFMSFSFdgAHEQWFHP-LLNGARVLIRDDELWDPEQ--LYDEMERHGVTILDFPPVYLQQLAEHAE--RDGR 2259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 392 PLsSLKTLCSTGSVLYPKQFDYVYANIKADlHLASISGGT--------------DICGCFvlGNPIspvyrgecqGAGLG 457
Cdd:PRK12316 2260 PP-AVRVYCFGGEAVPAASLRLAWEALRPV-YLFNGYGPTeavvtpllwkcrpqDPCGAA--YVPI---------GRALG 2326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 458 ------LDvAVFNDLGQPVIQQR---GELVCRNSFpNQPigfwHDDGQRY-HDAYWSKFSGVWHHGDEVEWTDNGGIRFY 527
Cdd:PRK12316 2327 nrrayiLD-ADLNLLAPGMAGELylgGEGLARGYL-NRP----GLTAERFvPDPFSASGERLYRTGDLARYRADGVVEYL 2400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 528 GRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKIDNDEQIILFVqlAPQcELNTLLVNTIKQRLRENCSPRHVPA 607
Cdd:PRK12316 2401 GRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYV--VPD-DAAEDLLAELRAWLAARLPAYMVPA 2477
|
570
....*....|....*.
gi 1067526515 608 QIHSISDVPRTKSGKL 623
Cdd:PRK12316 2478 HWVVLERLPLNPNGKL 2493
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
94-316 |
8.37e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 61.60 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 94 LNYAENLLSYAFQQPEGIA-VWfknenGQsKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSL 172
Cdd:PRK07470 7 MNLAHFLRQAARRFPDRIAlVW-----GD-RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 173 GAVWTST----SPDfgvdsVVERFGQVQPKILFCCNGyTFNGktHlmeekngqiADAISSLhnicqiEYLHQRSLTADFN 248
Cdd:PRK07470 81 GAVWVPTnfrqTPD-----EVAYLAEASGARAMICHA-DFPE--H---------AAAVRAA------SPDLTHVVAIGGA 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067526515 249 DAFSDWNAILASYLPRGLRYERVSFNDPLFILYSSGTTGKPKCIA---HSVGGTILNHLkehqlhCDIQPG 316
Cdd:PRK07470 138 RAGLDYEALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVlthGQMAFVITNHL------ADLMPG 202
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
259-623 |
9.28e-10 |
|
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: 61.11 E-value: 9.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 259 ASYLPRGLRY--ERVSF--------------NDPLFILYSSGTTGKPKCIAHSVGGtILNHLKEHQLHCDIQPGDRVFYY 322
Cdd:cd17652 62 AAYLPLDPAYpaERIAYmladarpalllttpDNLAYVIYTSGSTGRPKGVVVTHRG-LANLAAAQIAAFDVGPGSRVLQF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 323 TTCGW--MMWNWhVSALASGATLVIYDGSPMYPQPGvLWDLAEEANITLFGTSAKYLEALqktaysPSDYYPlsSLKTLC 400
Cdd:cd17652 141 ASPSFdaSVWEL-LMALLAGATLVLAPAEELLPGEP-LADLLREHRITHVTLPPAALAAL------PPDDLP--DLRTLV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 401 STGSVLYP---------KQFDYVY----ANIKADLHLASISG-----GTDICG--CFVLG---NPISPVYRGECQGAGLG 457
Cdd:cd17652 211 VAGEACPAelvdrwapgRRMINAYgpteTTVCATMAGPLPGGgvppiGRPVPGtrVYVLDarlRPVPPGVPGELYIAGAG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 458 LDVAVfndLGQPviqqrgELVCRNSFPNqPIGfwhDDGQRyhdaywskfsgVWHHGDEVEWTDNGGIRFYGRSDTTLNPG 537
Cdd:cd17652 291 LARGY---LNRP------GLTAERFVAD-PFG---APGSR-----------MYRTGDLARWRADGQLEFLGRADDQVKIR 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 538 GVRIGTAEIYQQVNSFPEIQDSVAVGQKID-NDEQIILFVQLAPQcelntllVNTIKQRLRENCS---PRH-VPAQIHSI 612
Cdd:cd17652 347 GFRIELGEVEAALTEHPGVAEAVVVVRDDRpGDKRLVAYVVPAPG-------AAPTAAELRAHLAerlPGYmVPAAFVVL 419
|
410
....*....|.
gi 1067526515 613 SDVPRTKSGKL 623
Cdd:cd17652 420 DALPLTPNGKL 430
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
89-622 |
1.57e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 60.83 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 89 FPQAQLNYAENLLSYAFQQPEGIAVWFKnenGQSkkLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLA 168
Cdd:PRK06178 28 YPHGERPLTEYLRAWARERPQRPAIIFY---GHV--ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 169 TTSLGAVWTSTSPDFGVDSVVERFGQVQPKILFCcngytFNGKTHLMEEKNGQIA---DAISSLHNICQIE------YLH 239
Cdd:PRK06178 103 ILKLGAVHVPVSPLFREHELSYELNDAGAEVLLA-----LDQLAPVVEQVRAETSlrhVIVTSLADVLPAEptlplpDSL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 240 Q--RSLTADFNDAFsdwNAILASylPRGLRYERVSFNDPLFILYSSGTTGKPK-CI---AHSVGGTILNHLKEHQLhcdi 313
Cdd:PRK06178 178 RapRLAAAGAIDLL---PALRAC--TAPVPLPPPALDALAALNYTGGTTGMPKgCEhtqRDMVYTAAAAYAVAVVG---- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 314 qPGDRVF--YYTtcgwMMW----NWHV-SALASGATLVI---YDgspmypqPGVLWDLAEEANIT-LFGTSAKYLEALQK 382
Cdd:PRK06178 249 -GEDSVFlsFLP----EFWiageNFGLlFPLFSGATLVLlarWD-------AVAFMAAVERYRVTrTVMLVDNAVELMDH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 383 TAYSPSDyypLSSLKTlcsTGSVLYPKQFDYVYANIKADLH---LASISGG---TDICGCFVLGNPI-------SPVYrg 449
Cdd:PRK06178 317 PRFAEYD---LSSLRQ---VRVVSFVKKLNPDYRQRWRALTgsvLAEAAWGmteTHTCDTFTAGFQDddfdllsQPVF-- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 450 ecqgAGL---GLDVAVFN-DLGQPV-IQQRGELVCRNsfPNQPIGFWhddgqRYHDAYWSKFSGVWHH-GDEVEWTDNGG 523
Cdd:PRK06178 389 ----VGLpvpGTEFKICDfETGELLpLGAEGEIVVRT--PSLLKGYW-----NKPEATAEALRDGWLHtGDIGKIDEQGF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 524 IRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGqKIDND--EQIILFVQLAPQCELNTllvNTIKQRLRENCS 601
Cdd:PRK06178 458 LHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVG-RPDPDkgQVPVAFVQLKPGADLTA---AALQAWCRENMA 533
|
570 580
....*....|....*....|.
gi 1067526515 602 PRHVPaQIHSISDVPRTKSGK 622
Cdd:PRK06178 534 VYKVP-EIRIVDALPMTATGK 553
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
262-623 |
1.58e-09 |
|
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: 60.56 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 262 LPRGLRYERVSFNDPL-----FILYSSGTTGKPKCIAHSVGgTILNHLKEHQLHCDIQPgDRVFYYTTcgwmMWNWHVS- 335
Cdd:cd17654 101 APLSFTPEHRHFNIRTdeclaYVIHTSGTTGTPKIVAVPHK-CILPNIQHFRSLFNITS-EDILFLTS----PLTFDPSv 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 336 -----ALASGATLVIYDGSpMYPQPGVLWD-LAEEANITLFGTSAKYLEALQKTAYSPSDYYPLSSLKTLCSTGSVLYPK 409
Cdd:cd17654 175 veiflSLSSGATLLIVPTS-VKVLPSKLADiLFKRHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFPSL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 410 QFDYVYANIKADLHLASISGGTDICgCFVLGNPIsPVYRGECQgaglgldvavfndLGQPVIQQRGELVCRNSFPNQPIG 489
Cdd:cd17654 254 VILSSWRGKGNRTRIFNIYGITEVS-CWALAYKV-PEEDSPVQ-------------LGSPLLGTVIEVRDQNGSEGTGQV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 490 FwhdDGQR----YHDAYWSKFSGVWHH-GDEVEWTDnGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSF-PEIQDSVAvg 563
Cdd:cd17654 319 F---LGGLnrvcILDDEVTVPKGTMRAtGDFVTVKD-GELFFLGRKDSQIKRRGKRINLDLIQQVIESClGVESCAVT-- 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1067526515 564 qkIDNDEQIILFVqlapqceLNTLLVNTIKQRLRENCSPRH-VPAQIHSISDVPRTKSGKL 623
Cdd:cd17654 393 --LSDQQRLIAFI-------VGESSSSRIHKELQLTLLSSHaIPDTFVQIDKLPLTSHGKV 444
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
275-623 |
4.13e-09 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 58.81 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 275 DPLFILYSSGTTGKPK--CIAHSVGGTILNHLKEHQLHCDIQPGDRVFYYTTCGWMMWnWHVSALASGATLVIYDGSPMY 352
Cdd:cd17635 2 DPLAVIFTSGTTGEPKavLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLW-WILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 353 PQPGVLWDLAEEANITLFGTSAKYLEALQKTA--YSPSdyyplssLKTLCSTGSVLYPK--QFDYVYANIKADLHLASIS 428
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVSELKSAnaTVPS-------LRLIGYGGSRAIAAdvRFIEATGLTNTAQVYGLSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 429 GGTDICGCFVLG----NPISPVYRGecqgaglgLDVAVFNDLGQPVIQ-QRGELVCRNsfPNQPIGFWhDDGQRYHDayw 503
Cdd:cd17635 154 TGTALCLPTDDDsieiNAVGRPYPG--------VDVYLAATDGIAGPSaSFGTIWIKS--PANMLGYW-NNPERTAE--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 504 sKFSGVW-HHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSvAVGQKIDND--EQIILFVQLAP 580
Cdd:cd17635 220 -VLIDGWvNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQEC-ACYEISDEEfgELVGLAVVASA 297
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1067526515 581 qcELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd17635 298 --ELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
95-625 |
7.05e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 58.64 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 95 NYAENLLSYAFQQPEGIAVWFKnenGQSkkLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGA 174
Cdd:PRK07786 18 NWVNQLARHALMQPDAPALRFL---GNT--TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 175 VwtstspdfgvdSVVERFGQVQPKILFccngytfngkthLMEEKNGQIADAISSLHNIC----QIEYLHQRSLTA--DFN 248
Cdd:PRK07786 93 I-----------AVPVNFRLTPPEIAF------------LVSDCGAHVVVTEAALAPVAtavrDIVPLLSTVVVAggSSD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 249 DAFSDWNAILASylpRGLRYERVSF-ND-PLFILYSSGTTGKPKciahsvgGTILNH--LKEHQLHC----DIQPGDRVF 320
Cdd:PRK07786 150 DSVLGYEDLLAE---AGPAHAPVDIpNDsPALIMYTSGTTGRPK-------GAVLTHanLTGQAMTClrtnGADINSDVG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 321 YyttCGWMMwnWHVSALAS-------GATLVIYdgsPMYP-QPGVLWDLAEEANIT-LFGTSAKYLEALQKTAYSPSDYy 391
Cdd:PRK07786 220 F---VGVPL--FHIAGIGSmlpglllGAPTVIY---PLGAfDPGQLLDVLEAEKVTgIFLVPAQWQAVCAEQQARPRDL- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 392 plsSLKTLCSTGSVLYPKQFDYVYANIKADLHLASIsGGTDIcgcfvlgNPISPVYRGECQGAGLGldvavfnDLGQPV- 470
Cdd:PRK07786 291 ---ALRVLSWGAAPASDTLLRQMAATFPEAQILAAF-GQTEM-------SPVTCMLLGEDAIRKLG-------SVGKVIp 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 471 -IQQR--------------GELVCRNsfPNQPIGFWHDDgqryhDAYWSKFSGVW-HHGDEVEWTDNGGIRFYGRSDTTL 534
Cdd:PRK07786 353 tVAARvvdenmndvpvgevGEIVYRA--PTLMSGYWNNP-----EATAEAFAGGWfHSGDLVRQDEEGYVWVVDRKKDMI 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 535 NPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKIDNDEQIILFVqLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISD 614
Cdd:PRK07786 426 ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAV-AAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDA 504
|
570
....*....|.
gi 1067526515 615 VPRTKSGKLVE 625
Cdd:PRK07786 505 LPRNPAGKVLK 515
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
275-622 |
7.37e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 58.06 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 275 DPLFILYSSGTTGKPK--CIAHSvggTILN---HLKEHQlhcDIQPGDRV-----FYYttC-GWMMWNwhVSALASGATL 343
Cdd:cd05917 3 DVINIQFTSGTTGSPKgaTLTHH---NIVNngyFIGERL---GLTEQDRLcipvpLFH--CfGSVLGV--LACLTHGATM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 344 VIydGSPMYPQPGVLWDLAEEANITLFGTSAKYLEALQktaySPS-DYYPLSSLKTLCSTGSVLYPKqfdyVYANIKADL 422
Cdd:cd05917 73 VF--PSPSFDPLAVLEAIEKEKCTALHGVPTMFIAELE----HPDfDKFDLSSLRTGIMAGAPCPPE----LMKRVIEVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 423 HLASIS---GGTDIC-GCFVLGNPISPVYRGECQG-AGLGLDVAVFNDLGQPVIQ--QRGELVCRNSfpNQPIGFWHDDG 495
Cdd:cd05917 143 NMKDVTiayGMTETSpVSTQTRTDDSIEKRVNTVGrIMPHTEAKIVDPEGGIVPPvgVPGELCIRGY--SVMKGYWNDPE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 496 Q--RYHDAywskfsGVWHH-GDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKIDN-DEQ 571
Cdd:cd05917 221 KtaEAIDG------DGWLHtGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERyGEE 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1067526515 572 IILFVQLAPQCElntLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGK 622
Cdd:cd05917 295 VCAWIRLKEGAE---LTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGK 342
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
103-352 |
2.90e-08 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 56.42 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 103 YAFQQPEGIAVwfkNENGQSkkLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPD 182
Cdd:PRK09029 12 WAQVRPQAIAL---RLNDEV--LTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 183 FGVDSVVERFGQVQPKILFCCNGY-TFNGKTHLMeekngqiadaISSLHNICQIEYLHQRsltadfndafsdwnaiLASy 261
Cdd:PRK09029 87 LPQPLLEELLPSLTLDFALVLEGEnTFSALTSLH----------LQLVEGAHAVAWQPQR----------------LAT- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 262 lprglryervsfndplfILYSSGTTGKPKCIAHSVGgtilNHLKEHQLHCDIQPGDRvfyytTCGWM------------- 328
Cdd:PRK09029 140 -----------------MTLTSGSTGLPKAAVHTAQ----AHLASAEGVLSLMPFTA-----QDSWLlslplfhvsgqgi 193
|
250 260
....*....|....*....|....
gi 1067526515 329 MWNWhvsaLASGATLVIYDGSPMY 352
Cdd:PRK09029 194 VWRW----LYAGATLVVRDKQPLE 213
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
109-623 |
3.02e-08 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 56.67 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 109 EGIAVWFKNENGQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDSV 188
Cdd:cd05915 9 GRKEVVSRLHTGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 189 VERFGQVQPKILFCCNGYTfngktHLMEEkngqiadAISSLHNIcqIEYLHQRSLTADFNDAFSDWNAILASYLPrglry 268
Cdd:cd05915 89 AYILNHAEDKVLLFDPNLL-----PLVEA-------IRGELKTV--QHFVVMDEKAPEGYLAYEEALGEEADPVR----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 269 erVSFNDPLFILYSSGTTGKPKCIAHSVGGTILNHLK---EHQLHCDIQPGD--RVFYYTTCGWmMWNWHVSALAsGATL 343
Cdd:cd05915 150 --VPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAaslVDGTALSEKDVVlpVVPMFHVNAW-CLPYAATLVG-AKQV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 344 VIYDgspmYPQPGVLWDLAEEANITLFGTSAKYLEALQKTAYSPSDYYPLSSlkTLCSTGSVlyPKQfdyVYANIK--AD 421
Cdd:cd05915 226 LPGP----RLDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLR--RLVVGGSA--APR---SLIARFerMG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 422 LHLASISGGTDICG----CFVLGN----PISPVYRGECQGaGL-----GLDVAVFNDLGQP-------VIQQRGELVCRn 481
Cdd:cd05915 295 VEVRQGYGLTETSPvvvqNFVKSHleslSEEEKLTLKAKT-GLpiplvRLRVADEEGRPVPkdgkalgEVQLKGPWITG- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 482 sfpnqpiGFWHDDGQRYHDAywskFSGVWHHGDEVEWTD-NGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSV 560
Cdd:cd05915 373 -------GYYGNEEATRSAL----TPDGFFRTGDIAVWDeEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAA 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1067526515 561 AVGQKIDN-DEQIILFVQLAPQCELNTLLVNTIKQRLRencSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd05915 442 VVAIPHPKwQERPLAVVVPRGEKPTPEELNEHLLKAGF---AKWQLPDAYVFAEEIPRTSAGKF 502
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
104-623 |
3.93e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.89 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 104 AFQQPEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDF 183
Cdd:PRK12316 3067 VERTPDAVALAFGEQ-----RLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEY 3141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 184 GVDsvverfgqvqpkilfccngytfngKTHLMEEKNGQIADAISSLHNICQIEYLHQRSLTADFNDAFSDWNAILAsyLP 263
Cdd:PRK12316 3142 PEE------------------------RLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRT--MP 3195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 264 RGLRYervsfndplfILYSSGTTGKPKCIAHSvGGTILNHLKEHQLHCDIQPGDRVFYYTTCGWMMWNWHV-SALASGAT 342
Cdd:PRK12316 3196 ENLAY----------VIYTSGSTGKPKGVGIR-HSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELfWPLMSGAR 3264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 343 LVIYDGSpmypqpgvLWDLAEEANITLFGTSAKYLEALQKT---AYSPSDYYPLSSLKTLCSTGSVLYPKQFDYVYA--- 416
Cdd:PRK12316 3265 VVLAGPE--------DWRDPALLVELINSEGVDVLHAYPSMlqaFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAglp 3336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 417 --NIKADLHLASISGGTDICGCFVLGNPI-SPVYRGECQGAGLGLDVAVFNDLGQPVIQqrGELVCRNSFpNQPigfwHD 493
Cdd:PRK12316 3337 lyNLYGPTEATITVTHWQCVEEGKDAVPIgRPIANRACYILDGSLEPVPVGALGELYLG--GEGLARGYH-NRP----GL 3409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 494 DGQRYHDAYWSKFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGqkIDNDEQII 573
Cdd:PRK12316 3410 TAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA--VDGRQLVA 3487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1067526515 574 LFVQLAPQCELNTLLVNTIKQRLREncspRHVPAQIHSISDVPRTKSGKL 623
Cdd:PRK12316 3488 YVVPEDEAGDLREALKAHLKASLPE----YMVPAHLLFLERMPLTPNGKL 3533
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
104-398 |
7.06e-08 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 55.73 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 104 AFQQPEGIAVWFKNENG---QSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLAT----------- 169
Cdd:PRK07529 35 AARHPDAPALSFLLDADpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGeaagianpinp 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 170 -------TSL----GAVWTST-SPDFGVD------SVVERFGQVQPKILFccngytfNGKTHLMEEKnGQIADAISSLHN 231
Cdd:PRK07529 115 llepeqiAELlraaGAKVLVTlGPFPGTDiwqkvaEVLAALPELRTVVEV-------DLARYLPGPK-RLAVPLIRRKAH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 232 IcqieylhqrsltadfndAFSDWNAILASYL-PRGLRYERVSFNDPLFILYSSGTTGKPKCIAHSVGGTILNHLKEHQLh 310
Cdd:PRK07529 187 A-----------------RILDFDAELARQPgDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALL- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 311 CDIQPGDRVFyyttCGWMMwnWHV--------SALASGATLVIydGSPM-YPQPGV---LWDLAEEANITLFGTSAKYLE 378
Cdd:PRK07529 249 LGLGPGDTVF----CGLPL--FHVnallvtglAPLARGAHVVL--ATPQgYRGPGVianFWKIVERYRINFLSGVPTVYA 320
|
330 340
....*....|....*....|
gi 1067526515 379 ALQKTaysPSDYYPLSSLKT 398
Cdd:PRK07529 321 ALLQV---PVDGHDISSLRY 337
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
275-623 |
7.84e-08 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 55.25 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 275 DPLFILYSSGTTGKPK--CIAHSvggTILNHLKEHQLHCDIQPGDRVFYYTTCGWMMWNWHV-SALASGATLVIYDGSPM 351
Cdd:cd17645 105 DLAYVIYTSGSTGLPKgvMIEHH---NLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIfPHLTAGAALHVVPSERR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 352 YPQPGvLWDLAEEANIT---LFGTSAKYLEALQKTayspsdyyplsSLKTLCSTGSVLY--------------PKQFDYV 414
Cdd:cd17645 182 LDLDA-LNDYFNQEGITisfLPTGAAEQFMQLDNQ-----------SLRVLLTGGDKLKkierkgyklvnnygPTENTVV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 415 YANIKADLHLASISGGTDICGCFVL----GNPISPV-YRGECQGAGLGLDVAVFNdlgqpviqqRGELVcRNSFPNQPig 489
Cdd:cd17645 250 ATSFEIDKPYANIPIGKPIDNTRVYildeALQLQPIgVAGELCIAGEGLARGYLN---------RPELT-AEKFIVHP-- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 490 fwHDDGQRyhdaywskfsgVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSvAVGQKIDND 569
Cdd:cd17645 318 --FVPGER-----------MYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELA-AVLAKEDAD 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1067526515 570 EQIILFVQLAPQCELNtllVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:cd17645 384 GRKYLVAYVTAPEEIP---HEELREWLKNDLPDYMIPTYFVHLKALPLTANGKV 434
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
125-626 |
8.62e-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: 54.88 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 125 LTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDSVVERFGQvqpkilfccn 204
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDR---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 205 gytfnGKthlmeekngqiadaisslHNICQIEylhqrsltadfndafsdwnailasylprglryERVSFNDPLFILYSSG 284
Cdd:cd05974 71 -----GG------------------AVYAAVD--------------------------------ENTHADDPMLLYFTSG 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 285 TTGKPKCIAHSVGGTILNHLKEhQLHCDIQPGDRVFYYTTCGWM--MWNWHVSALASGATLVIYDgspmYPQ--PGVLWD 360
Cdd:cd05974 96 TTSKPKLVEHTHRSYPVGHLST-MYWIGLKPGDVHWNISSPGWAkhAWSCFFAPWNAGATVFLFN----YARfdAKRVLA 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 361 LAEEANITLFgtsakyleALQKTAYSPSDYYPLSSLKT----LCSTGSVLYPKQFDYVyaniKADLHLASISG-GTDICG 435
Cdd:cd05974 171 ALVRYGVTTL--------CAPPTVWRMLIQQDLASFDVklreVVGAGEPLNPEVIEQV----RRAWGLTIRDGyGQTETT 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 436 CFVLGNPISPVYRGECQGAGLGLDVAVFNDLGQPVIQqrGElVCRNSFPNQPIGF---WHDDGQRYHDAYWskfSGVWHH 512
Cdd:cd05974 239 ALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPATE--GE-VALDLGDTRPVGLmkgYAGDPDKTAHAMR---GGYYRT 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 513 GDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSvAVGQKIDNDEQII--LFVQLAPQCELNTLLVN 590
Cdd:cd05974 313 GDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEA-AVVPSPDPVRLSVpkAFIVLRAGYEPSPETAL 391
|
490 500 510
....*....|....*....|....*....|....*...
gi 1067526515 591 TIKQRLRENCSPRHVPAQIhSISDVPRTKSGKL--VEL 626
Cdd:cd05974 392 EIFRFSRERLAPYKRIRRL-EFAELPKTISGKIrrVEL 428
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
94-634 |
1.23e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 54.51 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 94 LNYAENLLSYAFQQPEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLG 173
Cdd:PRK06145 2 FNLSASIAFHARRTPDRAALVYRDQ-----EISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 174 AVWTSTSPDFGVDSVVERFGQVQPKILFccngytfngkthLMEEkngqiADAISSL-HNICQIEYLHQrsltadfndafS 252
Cdd:PRK06145 77 AVFLPINYRLAADEVAYILGDAGAKLLL------------VDEE-----FDAIVALeTPKIVIDAAAQ-----------A 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 253 DWNAILASYLPRGLRYERVSfNDPLFILYSSGTTGKPKCIAHSVGGTilnHLK--EHQLHCDIQPGDRVFyytTCGWMmw 330
Cdd:PRK06145 129 DSRRLAQGGLEIPPQAAVAP-TDLVRLMYTSGTTDRPKGVMHSYGNL---HWKsiDHVIALGLTASERLL---VVGPL-- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 331 nWHVSALASGATLVIYDGSPM-----YPQPGVLWDLAEEAnitlfgTSAKYLEALQKTAY---SPSDYYPLSSLkTLCST 402
Cdd:PRK06145 200 -YHVGAFDLPGIAVLWVGGTLrihreFDPEAVLAAIERHR------LTCAWMAPVMLSRVltvPDRDRFDLDSL-AWCIG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 403 GSVLYPKQFDYVYANIKADLHLASISGGTDICGCFVL---GNPISPVyrGECQGAGLGLDVAVFNDLGQPVI-QQRGELV 478
Cdd:PRK06145 272 GGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLmeaGREIEKI--GSTGRALAHVEIRIADGAGRWLPpNMKGEIC 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 479 CRNsfPNQPIGFWHDDgqryhDAYWSKFSGVWHHGDEVEWTDNGGIRFY-GRSDTTLNPGGVRIGTAEIYQQVNSFPEIQ 557
Cdd:PRK06145 350 MRG--PKVTKGYWKDP-----EKTAEAFYGDWFRSGDVGYLDEEGFLYLtDRKKDMIISGGENIASSEVERVIYELPEVA 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 558 DSVAVGQKIDN-DEQIILFVQLAPQCELnTLlvntikQRLRENCSPR----HVPAQIHSISDVPRTKSGKLVELAVKQLL 632
Cdd:PRK06145 423 EAAVIGVHDDRwGERITAVVVLNPGATL-TL------EALDRHCRQRlasfKVPRQLKVRDELPRNPSGKVLKRVLRDEL 495
|
..
gi 1067526515 633 HG 634
Cdd:PRK06145 496 NG 497
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
97-632 |
1.45e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 54.40 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 97 AENLLSYAFQQPEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGvEKGDVVAGYLPYMTETLVAMLATTSLGAVW 176
Cdd:PRK07638 4 TKEYKKHASLQPNKIAIKENDR-----VLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 177 TSTSPDFGVDSVVERFGQVQPKILFCCNGYtfngKTHLMEEKnGQIADaisslhnicqieylhqrsltadfndaFSDWNA 256
Cdd:PRK07638 78 VPLDIKWKQDELKERLAISNADMIVTERYK----LNDLPDEE-GRVIE--------------------------IDEWKR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 257 ILASYLPRGLRYERVSfNDPLFILYSSGTTGKPKCIA-------HSVGGTilnhlkEHQLHcdIQPGDRV---------- 319
Cdd:PRK07638 127 MIEKYLPTYAPIENVQ-NAPFYMGFTSGSTGKPKAFLraqqswlHSFDCN------VHDFH--MKREDSVliagtlvhsl 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 320 FYYTTcgwmmwnwhVSALASGATLVIydgSPMYPQPGVLwDLAEEANITLFGTSAKYLEALQKtayspSDYYPLSSLKTL 399
Cdd:PRK07638 198 FLYGA---------ISTLYVGQTVHL---MRKFIPNQVL-DKLETENISVMYTVPTMLESLYK-----ENRVIENKMKII 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 400 CSTGSvlYPKQFDYVYANIKADLHLASISGGTDICgcFV--------------LGNPISPVYRGECQGAGlgldvavfnd 465
Cdd:PRK07638 260 SSGAK--WEAEAKEKIKNIFPYAKLYEFYGASELS--FVtalvdeeserrpnsVGRPFHNVQVRICNEAG---------- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 466 lgqpVIQQRGELvcRNSFPNQPIGFwhddgQRY-HDAYWSKFSGV--WHHGDEVEWTDNGG-IRFYGRSDTTLNPGGVRI 541
Cdd:PRK07638 326 ----EEVQKGEI--GTVYVKSPQFF-----MGYiIGGVLARELNAdgWMTVRDVGYEDEEGfIYIVGREKNMILFGGINI 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 542 GTAEIYQQVNSFPEIQDSVAVGqkIDND---EQIILFVQlapqcelNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRT 618
Cdd:PRK07638 395 FPEEIESVLHEHPAVDEIVVIG--VPDSywgEKPVAIIK-------GSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYT 465
|
570
....*....|....
gi 1067526515 619 KSGKLVELAVKQLL 632
Cdd:PRK07638 466 NSGKIARMEAKSWI 479
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
278-624 |
2.81e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 53.78 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 278 FILYSSGTTGKPKCIAHS------VGGTILNH--LKEHQLhcdIQPGDRVFYYTtcGWMMWNwhvSALASGATLV---IY 346
Cdd:PRK07788 211 IVILTSGTTGTPKGAPRPepsplaPLAGLLSRvpFRAGET---TLLPAPMFHAT--GWAHLT---LAMALGSTVVlrrRF 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 347 DgspmyPQpGVLWDLAE---EANITLFGTSAKYLEALQKTayspSDYYPLSSLKTLCSTGSVLYP-------KQFDYVYA 416
Cdd:PRK07788 283 D-----PE-ATLEDIAKhkaTALVVVPVMLSRILDLGPEV----LAKYDTSSLKIIFVSGSALSPelatralEAFGPVLY 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 417 NI--KADLHLASISGGTDICgcfvlgnpISPVYRGEcqgAGLGLDVAVFNDLGQPVIQ-QRGELVCRNSFPNQpiGFWHD 493
Cdd:PRK07788 353 NLygSTEVAFATIATPEDLA--------EAPGTVGR---PPKGVTVKILDENGNEVPRgVVGRIFVGNGFPFE--GYTDG 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 494 DGQRYHDAYWSKfsgvwhhGDEVEWTDNGgiRFY--GRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGqkIDNDE- 570
Cdd:PRK07788 420 RDKQIIDGLLSS-------GDVGYFDEDG--LLFvdGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIG--VDDEEf 488
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1067526515 571 --QIILFVQLAPQCELNtllVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLV 624
Cdd:PRK07788 489 gqRLRAFVVKAPGAALD---EDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVL 541
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
98-635 |
5.16e-07 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 52.70 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 98 ENLLSYAFQQPEGIAVwfKNENGQSKkLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWT 177
Cdd:PRK05857 18 DRVFEQARQQPEAIAL--RRCDGTSA-LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 178 STSPDFGVdSVVERFGQVQPKILFCCNGYTFNGKTHLMEEKNGQIADAIsslhNICQIEYLHQRSLTADFNDAFSDWNAi 257
Cdd:PRK05857 95 MADGNLPI-AAIERFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAV----DIAAVTRESEHSLDAASLAGNADQGS- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 258 lasylprglryervsfNDPLFILYSSGTTGKPKCI--AHSVGGTILNHLKEHQLHcdiqpgdrvfyyttcgWMMWnwhvs 335
Cdd:PRK05857 169 ----------------EDPLAMIFTSGTTGEPKAVllANRTFFAVPDILQKEGLN----------------WVTW----- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 336 alASGATlvIYDGSPMYPQPGVLWDLAEEAN----ITLFGTSAKYLEALQKTAYSPSDYYP--LSSLKTLCSTGSVLYPK 409
Cdd:PRK05857 212 --VVGET--TYSPLPATHIGGLWWILTCLMHgglcVTGGENTTSLLEILTTNAVATTCLVPtlLSKLVSELKSANATVPS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 410 QFDYVYAN---IKADLHLASISG-------GTDICGCFVLGNP-----ISPVYRGECQGAGLGLDVAVFN-DLGQPVIQQ 473
Cdd:PRK05857 288 LRLVGYGGsraIAADVRFIEATGvrtaqvyGLSETGCTALCLPtddgsIVKIEAGAVGRPYPGVDVYLAAtDGIGPTAPG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 474 RGELVCRNSF----PNQPIGFWhDDGQRYHDAYwskFSGVWHHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQ 549
Cdd:PRK05857 368 AGPSASFGTLwiksPANMLGYW-NNPERTAEVL---IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRI 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 550 VNSFPEIQDsvAVGQKIDnDEQIILFVQLA--PQCELNTLLVNTIKQRL-----RENCSPRHvPAQIHSISDVPRTKSGK 622
Cdd:PRK05857 444 AEGVSGVRE--AACYEIP-DEEFGALVGLAvvASAELDESAARALKHTIaarfrRESEPMAR-PSTIVIVTDIPRTQSGK 519
|
570
....*....|...
gi 1067526515 623 LVELAVKQLLHGE 635
Cdd:PRK05857 520 VMRASLAAAATAD 532
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
104-623 |
5.66e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 52.63 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 104 AFQQPEGIAVWFKNEngqskKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGY----LPYmtetLVAMLATTSLGAVWTST 179
Cdd:PRK08316 21 ARRYPDKTALVFGDR-----SWTYAELDAAVNRVAAALLDLGLKKGDRVAALghnsDAY----ALLWLACARAGAVHVPV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 180 SPDFGVDSVVERFGQVQPKILFCcngytfngKTHLMEekngqIADAISSLHNICQIEYLHQRSLTaDFNDAFSDWNAILA 259
Cdd:PRK08316 92 NFMLTGEELAYILDHSGARAFLV--------DPALAP-----TAEAALALLPVDTLILSLVLGGR-EAPGGWLDFADWAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 260 SYLPRGLRyERVSFNDPLFILYSSGTTGKPKCIAHSVGGTIlnhlkeHQ-----LHCDIQPGDRV-----FYYttCGWMm 329
Cdd:PRK08316 158 AGSVAEPD-VELADDDLAQILYTSGTESLPKGAMLTHRALI------AEyvsciVAGDMSADDIPlhalpLYH--CAQL- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 330 wnwHV---SALASGATLVIYDGspmyPQPGVLWDLAEEANIT-LFGTSAKYLEALQKTAYSPSDyypLSSLKTlCSTGSV 405
Cdd:PRK08316 228 ---DVflgPYLYVGATNVILDA----PDPELILRTIEAERITsFFAPPTVWISLLRHPDFDTRD---LSSLRK-GYYGAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 406 LYPKQfdyVYANIKA---DLHLASISGGTDICgcfvlgnPISPVYR--------GECQGAGLGLDVAVFNDLGQPVIQ-Q 473
Cdd:PRK08316 297 IMPVE---VLKELRErlpGLRFYNCYGQTEIA-------PLATVLGpeehlrrpGSAGRPVLNVETRVVDDDGNDVAPgE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 474 RGELVCRNsfPNQPIGFWHDDgQRYHDAywskFSGVW-HHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNS 552
Cdd:PRK08316 367 VGEIVHRS--PQLMLGYWDDP-EKTAEA----FRGGWfHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYT 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 553 FPEIQDsVAV--------------------GQKIDNDEqIILFVqlapqcelntllvntiKQRLrencSPRHVPAQIHSI 612
Cdd:PRK08316 440 HPAVAE-VAViglpdpkwieavtavvvpkaGATVTEDE-LIAHC----------------RARL----AGFKVPKRVIFV 497
|
570
....*....|.
gi 1067526515 613 SDVPRTKSGKL 623
Cdd:PRK08316 498 DELPRNPSGKI 508
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
279-624 |
2.99e-06 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 50.07 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 279 ILYSSGTTGKPKCI--AHSVGGTILNHLKEHQLHCDIQPGDR------VFYYTTCGWMMwnwhvSALASGATLVI---YD 347
Cdd:cd05929 130 MLYSGGTTGRPKGIkrGLPGGPPDNDTLMAAALGFGPGADSVylspapLYHAAPFRWSM-----TALFMGGTLVLmekFD 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 348 gspmypqPGVLWDLAEEANI-------TLFGTSAKYLEALQKTayspsdyYPLSSLKTLCSTGSV-----------LYPK 409
Cdd:cd05929 205 -------PEEFLRLIERYRVtfaqfvpTMFVRLLKLPEAVRNA-------YDLSSLKRVIHAAAPcppwvkeqwidWGGP 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 410 QFDYVYANIKAdlhlasiSGGTDICGCFVLGNPISpVYRgecqgAGLGlDVAVFNDLGQPVIqqrgelvcrnsfPNQP-- 487
Cdd:cd05929 271 IIWEYYGGTEG-------QGLTIINGEEWLTHPGS-VGR-----AVLG-KVHILDEDGNEVP------------PGEIge 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 488 IGFWHDDGQRYHDAY-WSKFS---GVWHHGDEVEWTDNGGIRFYG--RSDTTLNpGGVRIGTAEIYQQVNSFPEIQDSVA 561
Cdd:cd05929 325 VYFANGPGFEYTNDPeKTAAArneGGWSTLGDVGYLDEDGYLYLTdrRSDMIIS-GGVNIYPQEIENALIAHPKVLDAAV 403
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1067526515 562 VGqkIDNDE---QIILFVQLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLV 624
Cdd:cd05929 404 VG--VPDEElgqRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLY 467
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
123-175 |
1.02e-05 |
|
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: 48.50 E-value: 1.02e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1067526515 123 KKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAV 175
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV 54
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
392-631 |
2.99e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 46.91 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 392 PLSSLKTLCSTGSVLYP---KQFDYVYANIkadlhLASISGGTDIcGCFVLGNPISPVYRGECQGAGL-GLDVAVFNDLG 467
Cdd:PRK13383 290 PLPQLRVVMSSGDRLDPtlgQRFMDTYGDI-----LYNGYGSTEV-GIGALATPADLRDAPETVGKPVaGCPVRILDRNN 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 468 QPViqqrGELVCRNSFPNQPIgfwhdDGQRYHDAYWSK-FSGVWHHGDeVEWTDNGGiRFY--GRSDTTLNPGGVRIGTA 544
Cdd:PRK13383 364 RPV----GPRVTGRIFVGGEL-----AGTRYTDGGGKAvVDGMTSTGD-MGYLDNAG-RLFivGREDDMIISGGENVYPR 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 545 EIYQQVNSFPEIQDSVAVGQKidnDEQ----IILFVQLAPQCELNTllvNTIKQRLRENCSPRHVPAQIHSISDVPRTKS 620
Cdd:PRK13383 433 AVENALAAHPAVADNAVIGVP---DERfghrLAAFVVLHPGSGVDA---AQLRDYLKDRVSRFEQPRDINIVSSIPRNPT 506
|
250
....*....|.
gi 1067526515 621 GKLVElavKQL 631
Cdd:PRK13383 507 GKVLR---KEL 514
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
498-624 |
6.19e-05 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 45.90 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 498 YHDAYWSKfsgvwhhGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGqkIDNDE---QIIL 574
Cdd:PRK13382 413 FHDGFMAS-------GDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIG--VDDEQygqRLAA 483
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1067526515 575 FVQLAPQCelnTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLV 624
Cdd:PRK13382 484 FVVLKPGA---SATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKIL 530
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
256-393 |
6.96e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 46.11 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 256 AILASYLPRGLRYERvSFNDPLFILYSSGTTGKPKciahsvgGTILNHlKEHQLHC-------DIQPGDRVFyyttcgwm 328
Cdd:PRK06814 776 GLLAGRFPLVYFCNR-DPDDPAVILFTSGSEGTPK-------GVVLSH-RNLLANRaqvaariDFSPEDKVF-------- 838
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067526515 329 mwN----WHVSALASGATLVIYDGSP--MYPQP---GVLWDLAEEANIT-LFGTSAkYLEALQKTAYsPSDYYPL 393
Cdd:PRK06814 839 --NalpvFHSFGLTGGLVLPLLSGVKvfLYPSPlhyRIIPELIYDTNATiLFGTDT-FLNGYARYAH-PYDFRSL 909
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
436-623 |
7.53e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.31 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 436 CFVLG---NPISPVYRGECQGAGLGLDVAVfndLGQPVIQ-QRgelvcrnsFPNQPIGfwhDDGQRyhdaywskfsgVWH 511
Cdd:PRK05691 1454 CRVLDaelNLLPPGVAGELCIGGAGLARGY---LGRPALTaER--------FVPDPLG---EDGAR-----------LYR 1508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 512 HGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKIDNDEQIILFVQLAPQCELNTLlvnT 591
Cdd:PRK05691 1509 TGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAE---R 1585
|
170 180 190
....*....|....*....|....*....|..
gi 1067526515 592 IKQRLRENCSPRHVPAQIHSISDVPRTKSGKL 623
Cdd:PRK05691 1586 LKAALAAELPEYMVPAQLIRLDQMPLGPSGKL 1617
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
510-632 |
8.01e-05 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 45.83 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 510 W-HHGDEVEWTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVAVGQKID-NDEQIILFVQLAPQcelNTL 587
Cdd:PRK08008 399 WlHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSiRDEAIKAFVVLNEG---ETL 475
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1067526515 588 LVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGKLvelaVKQLL 632
Cdd:PRK08008 476 SEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKI----IKKNL 516
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
537-632 |
1.77e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 44.51 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 537 GGVRIGTAEIYQQVNSFPEIQDSVAVGqkIDND---EQIILFVQLAPQCELNTLLVNTIKQRLRENCSPRHVPAQIHSIS 613
Cdd:PRK08276 398 GGVNIYPQEIENLLVTHPKVADVAVFG--VPDEemgERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFED 475
|
90
....*....|....*....
gi 1067526515 614 DVPRTKSGKLvelaVKQLL 632
Cdd:PRK08276 476 ELPRTPTGKL----YKRRL 490
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
545-622 |
2.29e-04 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 39.84 E-value: 2.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1067526515 545 EIYQQVNSFPEIQDSVAVGQKIDNDEQIIL-FVQLAPQcelNTLLVNTIKQRLRENCSPRHVPAQIHSISDVPRTKSGK 622
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVaFVVLKPG---VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
120-204 |
2.95e-04 |
|
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: 43.97 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 120 GQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETLVAMLATTSLGAVWTSTSPDFGVDSVVERFGQVQPKI 199
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
....*
gi 1067526515 200 LFCCN 204
Cdd:cd05914 83 IFVSD 87
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
457-623 |
3.27e-04 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 43.53 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 457 GLDVAVFNDLGQPVIQ-QRGELVCRnsFPNQPIGFWHDDGQRYHDAYWSKFSGVwhhGDeVEWTDNGGIRFYG--RSDTT 533
Cdd:PRK12406 332 GAELRFVDEDGRPLPQgEIGEIYSR--IAGNPDFTYHNKPEKRAEIDRGGFITS---GD-VGYLDADGYLFLCdrKRDMV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 534 LNpGGVRIGTAEIYQQVNSFPEIQDSVAVGqkI-DND--EQIILFVQLAPQCELNTllvNTIKQRLRENCSPRHVPAQIH 610
Cdd:PRK12406 406 IS-GGVNIYPAEIEAVLHAVPGVHDCAVFG--IpDAEfgEALMAVVEPQPGATLDE---ADIRAQLKARLAGYKVPKHIE 479
|
170
....*....|...
gi 1067526515 611 SISDVPRTKSGKL 623
Cdd:PRK12406 480 IMAELPREDSGKI 492
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
460-624 |
3.70e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 43.52 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 460 VAVFNDLGQPVIQQR-GELVCRNSfPNQPIGFWHD---DGQRYHDaywskfsGVWHHGDeVEWTD-NGGIRFYGRSDTTL 534
Cdd:PRK07867 337 PAEDADGRLLNADEAiGELVNTAG-PGGFEGYYNDpeaDAERMRG-------GVYWSGD-LAYRDaDGYAYFAGRLGDWM 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 535 NPGGVRIGTAEIYQQVNSFPEIQDsVAVGQKIDND--EQIILFVQLAPQCELNtllVNTIKQRLRE--NCSPRHVPAQIH 610
Cdd:PRK07867 408 RVDGENLGTAPIERILLRYPDATE-VAVYAVPDPVvgDQVMAALVLAPGAKFD---PDAFAEFLAAqpDLGPKQWPSYVR 483
|
170
....*....|....
gi 1067526515 611 SISDVPRTKSGKLV 624
Cdd:PRK07867 484 VCAELPRTATFKVL 497
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
518-622 |
1.17e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 41.95 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 518 WTDNGGIRFYGRSDTTLNPGGVRIGTAEIYQQVNSFPEIQDSVaVGQKIDNDEQIILFVQLAPQCELNTLlvnTIKQRLR 597
Cdd:PRK08308 301 KSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAV-VYRGKDPVAGERVKAKVISHEEIDPV---QLREWCI 376
|
90 100
....*....|....*....|....*
gi 1067526515 598 ENCSPRHVPAQIHSISDVPRTKSGK 622
Cdd:PRK08308 377 QHLAPYQVPHEIESVTEIPKNANGK 401
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
529-624 |
2.13e-03 |
|
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: 40.79 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 529 RSDTTLNpGGVRIGTAEIYQQVNSFPEIQDSVAVGQKIDNDEQI-ILFVQLApqcelNTLLVNTIKQRLRENCSPRHVPA 607
Cdd:cd05912 315 RSDLIIS-GGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVpVAFVVSE-----RPISEEELIAYCSEKLAKYKVPK 388
|
90
....*....|....*..
gi 1067526515 608 QIHSISDVPRTKSGKLV 624
Cdd:cd05912 389 KIYFVDELPRTASGKLL 405
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
37-99 |
4.55e-03 |
|
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: 35.53 E-value: 4.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 37 YSQLHLWSVAERKQFWLEVWQFCDvigfrgnciygegiarWD-DFTAARDTI------WFPQAQLNYAEN 99
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELD----------------WFkPFDKVLDGSngpfakWFVGGKLNVCYN 54
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
89-198 |
7.05e-03 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 39.50 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067526515 89 FPQAQLNYAENLLSYAFQQPEGIAV-----WFKNENGQSKKLTWQQLSDQVSIIQQWLKQNGVEKGDVVAGYLPYMTETL 163
Cdd:PRK09274 1 MMASMANIARHLPRAAQERPDQLAVavpggRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFF 80
|
90 100 110
....*....|....*....|....*....|....*
gi 1067526515 164 VAMLATTSLGAVWTSTSPDFGVDSVVERFGQVQPK 198
Cdd:PRK09274 81 ALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPD 115
|
|
| |
