|
Name |
Accession |
Description |
Interval |
E-value |
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
45-698 |
0e+00 |
|
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: 1189.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 45 QRYRELHRRSVEEPREFWGDIAKEFYWKTPCPGPFlrynfDVTKGKIFIEWMKGATTNICYNVLDRNVHekKLGDKVAFY 124
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVL-----DWSKGPPFIKWFEGGKLNISYNCLDRHLK--ERGDKVAII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 125 WEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERIL 204
Cdd:cd05966 74 WEGDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRIN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 205 DSSCSLLITTDAFYRGEKLVNLKELADEALQKCqekgFPVRCCIVVKHLGRAelgmgdstsqsppikrscpdvqgklkek 284
Cdd:cd05966 154 DAQCKLVITADGGYRGGKVIPLKEIVDEALEKC----PSVEKVLVVKRTGGE---------------------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 285 skrvqpqISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAED 364
Cdd:cd05966 202 -------VPMTEGRDLWWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 365 VFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRAS 444
Cdd:cd05966 275 IYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSS 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 445 LQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGE 524
Cdd:cd05966 355 LRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGE 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 525 AEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEH 604
Cdd:cd05966 435 VEGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAH 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 605 EAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 684
Cdd:cd05966 515 PAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIA 594
|
650
....*....|....
gi 253970489 685 QNDHDLGDMSTVAD 698
Cdd:cd05966 595 AGEEELGDTSTLAD 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
31-705 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1113.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 31 PPPEVSRSAHVpSLQRYRELHRRSVEEPREFWGDIAKEFYWKTPcpgpflrYNFDVTKGKIFIEWMKGATTNICYNVLDR 110
Cdd:PRK00174 4 PPAEFAANALI-DMEQYKALYQESVEDPEGFWAEQAKRLDWFKP-------FDTVLDWNAPFIKWFEDGELNVSYNCLDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 111 NVHEKklGDKVAFYWEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIV 190
Cdd:PRK00174 76 HLKTR--GDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 191 FAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQekgfPVRCCIVVKHLGraelgmGDstsqsppi 270
Cdd:PRK00174 154 FGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP----SVEKVIVVRRTG------GD-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 271 krscpdvqgklkekskrvqpqISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYV 350
Cdd:PRK00174 216 ---------------------VDWVEGRDLWWHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 351 ATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLM 430
Cdd:PRK00174 275 AMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALM 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 431 KFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVA 510
Cdd:PRK00174 355 KEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQ 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 511 PAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGH 590
Cdd:PRK00174 435 PAVVDEEGNPLEGGEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGH 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 591 LLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKT 670
Cdd:PRK00174 515 RLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKT 594
|
650 660 670
....*....|....*....|....*....|....*
gi 253970489 671 RSGKIMRRVLRKIAQNDHDLGDMSTVADPSVISHL 705
Cdd:PRK00174 595 RSGKIMRRILRKIAEGEEILGDTSTLADPSVVEKL 629
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
43-705 |
0e+00 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 1032.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 43 SLQRYRELHRRSVEEPREFWGDIAKE-FYWKTPcpgpflrynFDVTK---GKIFIEWMKGATTNICYNVLDRnvHEKKLG 118
Cdd:TIGR02188 3 NLEQYKELYEESIEDPDKFWAKLARElLDWFKP---------FTKVLdwsFPPFYKWFVGGELNVSYNCVDR--HLEARP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 119 DKVAFYWEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 198
Cdd:TIGR02188 72 DKVAIIWEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 199 LCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKgfpVRCCIVVKHLGraelgmgdstsqsppikrscpdvq 278
Cdd:TIGR02188 152 LADRINDAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPVS---VEHVLVVRRTG------------------------ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 279 gklkekskrvQPQISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVF 358
Cdd:TIGR02188 205 ----------NPVVPWVEGRDVWWHDLMAKASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 359 DFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVT 438
Cdd:TIGR02188 275 DIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVK 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 439 KHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNES- 517
Cdd:TIGR02188 355 KHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEg 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 518 GEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEV 597
Cdd:TIGR02188 435 NPVEGPGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEI 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 598 ESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 677
Cdd:TIGR02188 515 ESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMR 594
|
650 660
....*....|....*....|....*....
gi 253970489 678 RVLRKIAQNDHD-LGDMSTVADPSVISHL 705
Cdd:TIGR02188 595 RLLRKIAAGEAEiLGDTSTLEDPSVVEEL 623
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
31-705 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 896.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 31 PPPEVSRSAHVPSLQRYRELHRRSVEEPREFWGDIAKEFYWKTP-CPGPFLRYNFDVTKGKIFIEWMKGATTNICYNVLD 109
Cdd:PLN02654 16 PSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKwEGDEVCSENLDVRKGPISIEWFKGGKTNICYNCLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 110 RNVhEKKLGDKVAFYWEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSI 189
Cdd:PLN02654 96 RNV-EAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 190 VFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKGFPVRCCIVVkhlgraelgmgdstsqspp 269
Cdd:PLN02654 175 VFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSVGICLTY------------------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 270 ikrscpDVQGKLKEKSKRvqpqisWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLY 349
Cdd:PLN02654 236 ------ENQLAMKREDTK------WQEGRDVWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 350 VATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLL 429
Cdd:PLN02654 304 TATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 430 MKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGV 509
Cdd:PLN02654 384 MRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 510 APAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSG 589
Cdd:PLN02654 464 QPVIVDEKGKEIEGECSGYLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 590 HLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPK 669
Cdd:PLN02654 544 HRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPK 623
|
650 660 670
....*....|....*....|....*....|....*..
gi 253970489 670 TRSGKIMRRVLRKIAQNDHD-LGDMSTVADPSVISHL 705
Cdd:PLN02654 624 TRSGKIMRRILRKIASRQLDeLGDTSTLADPGVVDQL 660
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
94-705 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 870.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 94 EWMKGATTNICYNVLDRNVHEKklGDKVAFYWEGnEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPEL 173
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGR--GDKVALIWEG-EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 174 VVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEkgfpVRCCIVVKHL 253
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPS----LEHVIVVGRT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 254 GrAELGMGDstsqsppikrscpdvqgklkekskrvqpqiswnqgiDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGST 333
Cdd:COG0365 154 G-ADVPMEG------------------------------------DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 334 GKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDK 413
Cdd:COG0365 197 GKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEK 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 414 YKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPG 493
Cdd:COG0365 277 YGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 494 aTPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDG 573
Cdd:COG0365 354 -LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDG 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 574 YYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIG 653
Cdd:COG0365 433 YFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELG 512
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 253970489 654 PIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDhDLGDMSTVADPSVISHL 705
Cdd:COG0365 513 PYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR-PLGDTSTLEDPEALDEI 563
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
47-676 |
0e+00 |
|
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: 710.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 47 YRELHRRSVEEPREFWGDIAKEFYWKTPCPGpflRYNFDVTKGKIFIEWMKGATTNICYNVLDRNVHEKklGDKVAFYWE 126
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQK---VKNTSFAPGAPSIKWFEDATLNLAANALDRHLREN--GDRTAIIYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 127 GNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDS 206
Cdd:cd17634 76 GDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 207 SCSLLITTDAFYRGEKLVNLKELADEALQKcqeKGFPVRCCIVVKhlgraelgmgdstsqsppikrscpdvqgklkeksk 286
Cdd:cd17634 156 SSRLLITADGGVRAGRSVPLKKNVDDALNP---NVTSVEHVIVLK----------------------------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 287 RVQPQISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVF 366
Cdd:cd17634 198 RTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIY 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 367 WCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQ 446
Cdd:cd17634 278 WCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 447 VLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAE 526
Cdd:cd17634 358 ILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTE 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 527 GYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 606
Cdd:cd17634 438 GNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPK 517
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 607 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM 676
Cdd:cd17634 518 VAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
47-705 |
0e+00 |
|
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: 600.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 47 YRELHRRSVEEPREFWGDIAKEFYWKTP-------CPGPFLRynfdvtkgkifieWMKGATTNICYNVLDRNVhEKKLGD 119
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPpekildnSNPPFTR-------------WFVGGRLNTCYNALDRHV-EAGRGD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 120 KVAFYWEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESL 199
Cdd:cd05967 67 QIALIYDSPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 200 CERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKgfPVRCciVVKHLGRAELGMGDStsqsppikrscpdvqg 279
Cdd:cd05967 147 ASRIDDAKPKLIVTASCGIEPGKVVPYKPLLDKALELSGHK--PHHV--LVLNRPQVPADLTKP---------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 280 klkekskrvqpqiswnqGIDLWWHELMQEAGdECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFD 359
Cdd:cd05967 207 -----------------GRDLDWSELLAKAE-PVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 360 FHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPT-YPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKF--GDEP 436
Cdd:cd05967 269 IKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVgTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKY 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 437 VTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPG--ATPMKPGSATFPFFGVAPAIL 514
Cdd:cd05967 349 IKKYDLSSLRTLFLAGERLDPPTLEWAENTLGV---PVIDHWWQTETGWPITANPVGlePLPIKAGSPGKPVPGYQVQVL 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 515 NESGEELEGEAEGYLVFKQPW-PGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLS 593
Cdd:cd05967 426 DEDGEPVGPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLS 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 594 TAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP-KLTEELKKQIREKIGPIATPDYIQNAPGLPKTRS 672
Cdd:cd05967 506 TGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAeELEKELVALVREQIGPVAAFRLVIFVKRLPKTRS 585
|
650 660 670
....*....|....*....|....*....|...
gi 253970489 673 GKIMRRVLRKIAQNDhDLGDMSTVADPSVISHL 705
Cdd:cd05967 586 GKILRRTLRKIADGE-DYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
45-702 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 569.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 45 QRYRELHRRSVEEPREFWGDIAKEFYWKTPcPGPFLRYNfdvtkGKIFIEWMKGATTNICYNVLDRnvHEKKLGDKVAFY 124
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTP-FTQVLDYS-----NPPFARWFVGGRTNLCHNAVDR--HLAKRPEQLALI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 125 WEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERIL 204
Cdd:PRK10524 74 AVSTETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARID 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 205 DSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKgfPVRCCIVVKHLGRAElgmgdstsqsppikrscpdvqgklkek 284
Cdd:PRK10524 154 DAKPVLIVSADAGSRGGKVVPYKPLLDEAIALAQHK--PRHVLLVDRGLAPMA--------------------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 285 skrvqpqisWNQGIDLWWHELMQEAGDECEP-EWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAE 363
Cdd:PRK10524 205 ---------RVAGRDVDYATLRAQHLGARVPvEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 364 DVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRA 443
Cdd:PRK10524 276 ETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLS 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 444 SLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPG--ATPMKPGSATFPFFGVAPAILNESGEEL 521
Cdd:PRK10524 356 SLRALFLAGEPLDEPTASWISEALGV---PVIDNYWQTETGWPILAIARGveDRPTRLGSPGVPMYGYNVKLLNEVTGEP 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 522 EGEAEG-YLVFKQPW-PGIMRTVYGNHERFETTYFKKF-PGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVE 598
Cdd:PRK10524 433 CGPNEKgVLVIEGPLpPGCMQTVWGDDDRFVKTYWSLFgRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIE 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 599 SALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS-----PKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 673
Cdd:PRK10524 513 ESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLAdrearLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSG 592
|
650 660
....*....|....*....|....*....
gi 253970489 674 KIMRRVLRKIAQnDHDLGDMSTVADPSVI 702
Cdd:PRK10524 593 KLLRRAIQAIAE-GRDPGDLTTIEDPAAL 620
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
44-699 |
7.25e-178 |
|
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: 521.28 E-value: 7.25e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 44 LQRYRELHRRSVEEPREFWGDIAKEF-YWKTPCPGPFLrynfDVTKGKIFIEWMKGATTNICYNVLDRnvHEKKLGDKVA 122
Cdd:cd05968 6 IPDLEAFLERSAEDNAWFWGEFVKDVgIEWYEPPYQTL----DLSGGKPWAAWFVGGRMNIVEQLLDK--WLADTRTRPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 123 FYWEGnEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCER 202
Cdd:cd05968 80 LRWEG-EDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 203 ILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCqekgFPVRCCIVVKHLGRAELgmgdstsqsppikrscpdvqgklk 282
Cdd:cd05968 159 LQDAEAKALITADGFTRRGREVNLKEEADKACAQC----PTVEKVVVVRHLGNDFT------------------------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 283 ekskrvqpqisWNQGIDLWWHELMQEAGDECEPewCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHA 362
Cdd:cd05968 211 -----------PAKGRDLSYDEEKETAGDGAER--TESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 363 ED-VFWCTaDIGWITGhSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHS 441
Cdd:cd05968 278 GDlLTWFT-DLGWMMG-PWLIFGGLILGATMVLYDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 442 RASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPgATPMKPGSATFPFFGVAPAILNESGEEL 521
Cdd:cd05968 356 LSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEISGGILGNVL-IKPIKPSSFNGPVPGMKADVLDESGKPA 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 522 EGEAEGyLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESAL 601
Cdd:cd05968 435 RPEVGE-LVLLAPWPGMTRGFWRDEDRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVL 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 602 VEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:cd05968 514 NAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
650
....*....|....*...
gi 253970489 682 KiAQNDHDLGDMSTVADP 699
Cdd:cd05968 594 A-AYLGKELGDLSSLENP 610
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
93-698 |
1.21e-177 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 519.07 E-value: 1.21e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 93 IEWMKGATTNICYNVLDRNVHEKkLGDKVAFYWEGNEPGETtqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPE 172
Cdd:PRK04319 34 FSWLETGKVNIAYEAIDRHADGG-RKDKVALRYLDASRKEK--YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 173 LVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELadealqkcqekgfpvrccivvKH 252
Cdd:PRK04319 111 LYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKPADDLPSL---------------------KH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 253 LgraeLGMGDSTSQSPPIkrscpdvqgklkekskrvqpqiswnqgIDLWwhELMQEAGDECEPEWCDAEDPLFILYTSGS 332
Cdd:PRK04319 170 V----LLVGEDVEEGPGT---------------------------LDFN--ALMEQASDEFDIEWTDREDGAILHYTSGS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 333 TGKPKGVVHtVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGiptYPDVNRLWSIVD 412
Cdd:PRK04319 217 TGKPKGVLH-VHNAMLQHYQTGKYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGG---RFSPERWYRILE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 413 KYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLP 492
Cdd:PRK04319 293 DYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGL---PIHDNWWMTETGGIMIANYP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 493 gATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETtYFKkfPGYYVTGDGCQRDQD 572
Cdd:PRK04319 370 -AMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMDED 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 573 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKI 652
Cdd:PRK04319 446 GYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGL 525
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 253970489 653 GPIATPDYIQNAPGLPKTRSGKIMRRVLrKIAQNDHDLGDMSTVAD 698
Cdd:PRK04319 526 GAHAAPREIEFKDKLPKTRSGKIMRRVL-KAWELGLPEGDLSTMED 570
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
137-684 |
3.89e-137 |
|
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: 410.74 E-value: 3.89e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 137 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDa 216
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 217 fyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgKLKEKSkrvqpqiswnq 296
Cdd:cd05969 81 ---------------------------------------------------------------ELYERT----------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 297 gidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHtVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWIT 376
Cdd:cd05969 87 ----------------------DPEDPTLLHYTSGTTGTPKGVLH-VHDAMIFYYFTGKYVLDLHPDDIYWCTADPGWVT 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 377 GHSYVTYGPLANGATSVLFEGiptYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPIN 456
Cdd:cd05969 144 GTVYGIWAPWLNGVTNVVYEG---RFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLN 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 457 PEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPGaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWP 536
Cdd:cd05969 221 PEAIRWGMEVFGV---PIHDTWWQTETGSIMIANYPC-MPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWP 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 537 GIMRTVYGNHERFETtYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHP 616
Cdd:cd05969 297 SMFRGIWNDEERYKN-SFID--GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKP 373
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 253970489 617 HPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 684
Cdd:cd05969 374 DPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
108-588 |
2.62e-106 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 330.04 E-value: 2.62e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 108 LDRNVheKKLGDKVAFywegnEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALH 187
Cdd:pfam00501 1 LERQA--ARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 188 SIVFAGFSSESLCERILDSSCSLLITTDAFYrgeklvnlkelaDEALQKCQEKGFPVRCCIVVKHLGRAELGMGDSTSQS 267
Cdd:pfam00501 74 VPLNPRLPAEELAYILEDSGAKVLITDDALK------------LEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 268 PPIkrscpdvqgklkekskrvqpqiswnqgidlwwhelmqeagDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVgGYM 347
Cdd:pfam00501 142 ADV----------------------------------------PPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 348 LYVATTFKYV----FDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDVNRLWSIVDKYKVTKFYTAP 423
Cdd:pfam00501 181 VANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 424 TAIRLLMKFGDEPVTKHSraSLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPGATPM-KPGSA 502
Cdd:pfam00501 260 TLLNMLLEAGAPKRALLS--SLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGSV 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 503 TFPFFGVAPAILNESGEELEGEAEG-YLVFKQpwPGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRI 581
Cdd:pfam00501 335 GRPLPGTEVKIVDDETGEPVPPGEPgELCVRG--PGVMKGYLNDPELTAEAFDED--GWYRTGDLGRRDEDGYLEIVGRK 410
|
....*..
gi 253970489 582 DDMLNVS 588
Cdd:pfam00501 411 KDQIKLG 417
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
137-682 |
1.59e-105 |
|
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: 328.53 E-value: 1.59e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 137 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLIttda 216
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 217 fyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqpqiswnq 296
Cdd:cd05972 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 297 gidlwwhelmqeagdecepewCDAEDPLFILYTSGSTGKPKGVVHTVGgYMLYVATTFKYVFDFHAEDVFWCTADIGWIT 376
Cdd:cd05972 78 ---------------------TDAEDPALIYFTSGTTGLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAK 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 377 GHSYVTYGPLANGATSVLFEGIPTypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEpvtKHSRASLQVLGTVGEPIN 456
Cdd:cd05972 136 GAWSSFFGPWLLGATVFVYEGPRF--DAERILELLERYGVTSFCGPPTAYRMLIKQDLS---SYKFSHLRLVVSAGEPLN 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 457 PEAWLWYHRVVGAqrcPIVDTFWQTETGgHMLTPLPGaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWP 536
Cdd:cd05972 211 PEVIEWWRAATGL---PIRDGYGQTETG-LTVGNFPD-MPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPP 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 537 GIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHP 616
Cdd:cd05972 286 GLFLGYVGDPEKTEASIRG---DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSP 362
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 253970489 617 HPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:cd05972 363 DPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
40-683 |
6.28e-86 |
|
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: 283.39 E-value: 6.28e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 40 HVPSLQRYRELHRRSVEEPREFWGDIAKefYWKTPCPGPflrYNFDVTKGKIF--IEWMKGATTNICYNVLDRNVHEkkl 117
Cdd:cd05943 12 HGLSLADYAALHRWSVDDPGAFWAAVWD--FSGVRGSKP---YDVVVVSGRIMpgARWFPGARLNYAENLLRHADAD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 118 gDKVAFYweGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSE 197
Cdd:cd05943 84 -DPAAIY--AAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 198 SLCERILDSSCSLLITTDAFYRGEKLVNLKEladealqKCQE--KGFPVRCCIVVkhlgraelgmgdstsqsppIKRSCP 275
Cdd:cd05943 161 GVLDRFGQIEPKVLFAVDAYTYNGKRHDVRE-------KVAElvKGLPSLLAVVV-------------------VPYTVA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 276 DVQGKLKEKSKRVqpqiswnqgidLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFK 355
Cdd:cd05943 215 AGQPDLSKIAKAL-----------TLEDFLATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 356 YVFDFHAEDVFWCTADIGWITGHSYVTYgpLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDE 435
Cdd:cd05943 284 LHCDLRPGDRLFYYTTCGWMMWNWLVSG--LAVGATIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 436 PVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcpivDTFWQTETGGhmlTPLPGA-------TPMKPGSATFPFFG 508
Cdd:cd05943 362 PAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP------DVLLASISGG---TDIISCfvggnplLPVYRGEIQCRGLG 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 509 VAPAILNESGEELEGEAEGyLVFKQPWPGiMRTVYGNHE---RFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDML 585
Cdd:cd05943 433 MAVEAFDEEGKPVWGEKGE-LVCTKPFPS-MPVGFWNDPdgsRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTL 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 586 NVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAP 665
Cdd:cd05943 511 NPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVP 590
|
650
....*....|....*...
gi 253970489 666 GLPKTRSGKIMRRVLRKI 683
Cdd:cd05943 591 DIPRTLSGKKVEVAVKKI 608
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
322-676 |
9.81e-85 |
|
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: 271.08 E-value: 9.81e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 322 DPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWItGHSYVTYGPLANGATSVLFEGipty 401
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 402 PDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQT 481
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPESA--GYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 482 ETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPgiMRtVYGNHErfETTYFKKFPGYY 561
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSV--MK-GYWNNP--EATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 562 VTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPklt 641
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDA--- 301
|
330 340 350
....*....|....*....|....*....|....*
gi 253970489 642 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM 676
Cdd:cd04433 302 EELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
57-682 |
1.64e-80 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 269.30 E-value: 1.64e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 57 EPREFWGDIAKEF-YWKTpcpgpflRYNFDVTKGKIFIEWMKGATTNICYNVLDRNVHEKKLGDKVAFYWEGNEPGETTQ 135
Cdd:PTZ00237 20 NPESFWDEVAKKYvHWDK-------MYDKVYSGDEIYPDWFKGGELNTCYNVLDIHVKNPLKRDQDALIYECPYLKKTIK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 215
Cdd:PTZ00237 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTN 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 216 AFYRGEKLVNLKELADEALQKCQEKgfPVRcciVVKHLgraelgMGDSTSQSppikrscpdvQGKLKEKSKRVQPQISWN 295
Cdd:PTZ00237 173 YGILNDEIITFTPNLKEAIELSTFK--PSN---VITLF------RNDITSES----------DLKKIETIPTIPNTLSWY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 296 QGIDLWwHELMQEAGDECEPewCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWI 375
Cdd:PTZ00237 232 DEIKKI-KENNQSPFYEYVP--VESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 376 TGHSYVtYGPLANGATSVLFEGIPTYPDV--NRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSR---ASLQVLGT 450
Cdd:PTZ00237 309 SFHGFL-YGSLSLGNTFVMFEGGIIKNKHieDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSKydlSNLKEIWC 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 451 VGEPINPEAWLWYHRVVGAqRCPIVdtFWQTETGghMLTPLPGATPMKPGSAT-FPFFGVAPAILNESGEELEGEAEGYL 529
Cdd:PTZ00237 388 GGEVIEESIPEYIENKLKI-KSSRG--YGQTEIG--ITYLYCYGHINIPYNATgVPSIFIKPSILSEDGKELNVNEIGEV 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 530 VFKQPWP-GIMRTVYGNHERFETTyFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVA 608
Cdd:PTZ00237 463 AFKLPMPpSFATTFYKNDEKFKQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVL 541
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 253970489 609 EAAVVGHPHPVKGECLYCFVTLCDGHTFSP----KLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:PTZ00237 542 ECCSIGIYDPDCYNVPIGLLVLKQDQSNQSidlnKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
107-688 |
2.24e-80 |
|
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: 263.21 E-value: 2.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 107 VLDRNVheKKLGDKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAL 186
Cdd:COG0318 4 LLRRAA--ARHPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 187 HSIVFAGFSSESLcERIL-DSSCSLLITtdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdsts 265
Cdd:COG0318 76 VVPLNPRLTAEEL-AYILeDSGARALVT---------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 266 qsppikrscpdvqgklkekskrvqpqiswnqgidlwwhelmqeagdecepewcdaedpLFILYTSGSTGKPKGVVHTVGG 345
Cdd:COG0318 103 ----------------------------------------------------------ALILYTSGTTGRPKGVMLTHRN 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 346 yMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegiPTYPDVNRLWSIVDKYKVTKFYTAPTA 425
Cdd:COG0318 125 -LLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVL----LPRFDPERVLELIERERVTVLFGVPTM 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 426 IRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFP 505
Cdd:COG0318 200 LARLLR--HPEFARYDLSSLRLVVSGGAPLPPELLERFEERFG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRP 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 506 FFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTVYGNHERFEttyfKKFP-GYYVTGDGCQRDQDGYYWITGRIDDM 584
Cdd:COG0318 275 LPGVEVRIVDEDGRELPPGEVGEIVVRGPN--VMKGYWNDPEATA----EAFRdGWLRTGDLGRLDEDGYLYIVGRKKDM 348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 585 LNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNA 664
Cdd:COG0318 349 IISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDA---EELRAFLRERLARYKVPRRVEFV 425
|
570 580
....*....|....*....|....
gi 253970489 665 PGLPKTRSGKIMRRVLRKIAQNDH 688
Cdd:COG0318 426 DELPRTASGKIDRRALRERYAAGA 449
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
136-682 |
6.71e-79 |
|
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: 258.99 E-value: 6.71e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERiLDSSCSLLITTD 215
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHR-LRTSGARLVVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 216 AFYRgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqpqiswn 295
Cdd:cd05973 80 AANR---------------------------------------------------------------------------- 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 296 qgidlwwHELmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATtFKYVFDFHAEDVFWCTADIGWI 375
Cdd:cd05973 84 -------HKL--------------DSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAY-LRDAVDLRPEDSFWNAADPGWA 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 376 TGHSYVTYGPLANGATSVLFEGIPTYPDVnrlWSIVDKYKVTKFYTAPTAIRLLMKFGdEPVTKHSRASLQVLGTVGEPI 455
Cdd:cd05973 142 YGLYYAITGPLALGHPTILLEGGFSVEST---WRVIERLGVTNLAGSPTAYRLLMAAG-AEVPARPKGRLRRVSSAGEPL 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 456 NPEAWLWYHRVVGAqrcPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGeelegeaegylvfKQPW 535
Cdd:cd05973 218 TPEVIRWFDAALGV---PIHDHYGQTELGMVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDG-------------DELG 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 536 PGIMRTVYGNHERFETTYFKKFP---------GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 606
Cdd:cd05973 282 PGEPGRLAIDIANSPLMWFRGYQlpdtpaidgGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPA 361
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 253970489 607 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:cd05973 362 VAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
29-680 |
2.74e-76 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 258.19 E-value: 2.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 29 WSPPPEVSRSAHVPSLQR------------YRELHRRSVEEPREFWGDIAkEFY---WKTPCPgpflrynfDVTKGKIFI 93
Cdd:PRK03584 6 WTPSAERIAASRMTAFIRwlaarrglsfddYAALWRWSVEDLEAFWQSVW-DFFgviGSTPYT--------VVLAGRRMP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 94 --EWMKGATTNICYNVLdRNvhekKLGDKVAFYWEGnEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIP 171
Cdd:PRK03584 77 gaRWFPGARLNYAENLL-RH----RRDDRPAIIFRG-EDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 172 ELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVN----LKELADealqkcqekGFP-VRC 246
Cdd:PRK03584 151 ETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDrrakVAELRA---------ALPsLEH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 247 CIVVKHLGRAELGmgdstsqsPPIKRSCPdvqgklkekskrvqpqiswnqgidlwWHELMQEAGD-ECEPEWCDAEDPLF 325
Cdd:PRK03584 222 VVVVPYLGPAAAA--------AALPGALL--------------------------WEDFLAPAEAaELEFEPVPFDHPLW 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 326 ILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAED-VFWCTAdIGWITGHSYVtyGPLANGATSVLFEGIPTYPDV 404
Cdd:PRK03584 268 ILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDrFFWYTT-CGWMMWNWLV--SGLLVGATLVLYDGSPFYPDP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 405 NRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcpivDTFWQTETG 484
Cdd:PRK03584 345 NVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVKA------DVWLASISG 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 485 G-HMLTPLPGATPMKP---GSATFPFFGVAPAILNESGEELEGEAEGyLVFKQPWPGiMrTVY----GNHERFETTYFKK 556
Cdd:PRK03584 419 GtDICSCFVGGNPLLPvyrGEIQCRGLGMAVEAWDEDGRPVVGEVGE-LVCTKPFPS-M-PLGfwndPDGSRYRDAYFDT 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 557 FPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTF 636
Cdd:PRK03584 496 FPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTL 575
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 253970489 637 SPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM----RRVL 680
Cdd:PRK03584 576 DDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLL 623
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
39-685 |
1.18e-65 |
|
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: 229.38 E-value: 1.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 39 AHVPSLQRYRELHRRSVEEPREFWGDIAKEFywKTPCPGPFLRYnFDVTKGkIFIEWMKGATTNICYNVLdrnvhEKKLG 118
Cdd:TIGR01217 29 HHGAAEGGYDALHRWSVDELDTFWKAVWEWF--DVRFSTPCARV-VDDRTM-PGAQWFPGARLNYAENLL-----RAAGT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 119 DKVAFYWegNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 198
Cdd:TIGR01217 100 EPALLYV--DETHEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 199 LCERILDSSCSLLITTDAFYRGEKlvnlKELADEALQKCQeKGFP-VRCCIVVKHLgraelgmGDSTSQSPPIKRScpdv 277
Cdd:TIGR01217 178 VLDRFQQIEPKLLFTVDGYRYNGK----EHDRRDKVAEVR-KELPtLRAVVHIPYL-------GPRETEAPKIDGA---- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 278 qgklkekskrvqpqiswnqgidLWWHELMQEAGD-ECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKY 356
Cdd:TIGR01217 242 ----------------------LDLEDFTAAAQAaELVFEQLPFDHPLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 357 VFDFHAEDVFWCTADIGWITGHSYVTygPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEP 436
Cdd:TIGR01217 300 HCDLGPGDRLFYYTTTGWMMWNWLVS--GLATGATLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 437 VTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcpivDTFWQTETGG-HMLTPLPGATPMKP---GSATFPFFGVAPA 512
Cdd:TIGR01217 378 ARTHDLSALQCVASTGSPLPPDGFRWVYDEIKA------DVWLASISGGtDICSCFAGANPTLPvhiGEIQAPGLGTAVQ 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 513 ILNESGEELEGEAEGyLVFKQPWPGiMRTVYGNHE---RFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSG 589
Cdd:TIGR01217 452 SWDPEGKPVTGEVGE-LVCTNPMPS-MPIRFWNDPdgsKYRDAYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQG 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 590 HLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPK 669
Cdd:TIGR01217 530 VRMGSAEIYNAVERLDEVRESLCIGQEQPDGGYRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPH 609
|
650
....*....|....*.
gi 253970489 670 TRSGKIMRRVLRKIAQ 685
Cdd:TIGR01217 610 TLTGKRVEVAVKRVLQ 625
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
102-682 |
2.72e-64 |
|
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: 222.73 E-value: 2.72e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 102 NICYNVLDRNVHEKKLGDKV---AFYWEgNEPGETTQITYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAM 177
Cdd:cd05928 6 NFASDVLDQWADKEKAGKRPpnpALWWV-NGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 178 LACARIGAlhsivfagfsseslcerILDSSCSLLITTDAFYRgeklvnlkeladeaLQKCQEKgfpvrcCIVVkhlgrae 257
Cdd:cd05928 85 VACIRTGL-----------------VFIPGTIQLTAKDILYR--------------LQASKAK------CIVT------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 258 lgmGDSTSQS-PPIKRSCPDVQGKLkekskRVQPQiSWNQGIDLwwHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKP 336
Cdd:cd05928 121 ---SDELAPEvDSVASECPSLKTKL-----LVSEK-SRDGWLNF--KELLNEASTEHHCVETGSQEPMAIYFTSGTTGSP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 337 KGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPTYpDVNRLWSIVDKYKV 416
Cdd:cd05928 190 KMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGAC-VFVHHLPRF-DPLVILKTLSSYPI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 417 TKFYTAPTAIRLLMKfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGghMLTPLPGATP 496
Cdd:cd05928 268 TTFCGAPTVYRMLVQ---QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLD---IYEGYGQTETG--LICANFKGMK 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 497 MKPGS--ATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVY-GNHERFETTYFKKFpgyYVTGDGCQRDQDG 573
Cdd:cd05928 340 IKPGSmgKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYvDNPEKTAATIRGDF---YLTGDRGIMDEDG 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 574 YYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLC-DGHTFSP-KLTEELKKQIREK 651
Cdd:cd05928 417 YFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLApQFLSHDPeQLTKELQQHVKSV 496
|
570 580 590
....*....|....*....|....*....|.
gi 253970489 652 IGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:cd05928 497 TAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
131-681 |
4.64e-63 |
|
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: 216.91 E-value: 4.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 210
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 211 LITtdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqp 290
Cdd:cd05971 82 LVT----------------------------------------------------------------------------- 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 291 qiswnqgidlwwhelmqeagDEcepewcdAEDPLFILYTSGSTGKPKGVVHT-------VGGYMLYvattfkyvFDF--H 361
Cdd:cd05971 85 --------------------DG-------SDDPALIIYTSGTTGPPKGALHAhrvllghLPGVQFP--------FNLfpR 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 362 AEDVFWCTADIGWItghsyvtyGPLANGATSVLFEGIP------TYPDVNRLWSIVDKYKVTKFYTAPTAIRLlMKFGDE 435
Cdd:cd05971 130 DGDLYWTPADWAWI--------GGLLDVLLPSLYFGVPvlahrmTKFDPKAALDLMSRYGVTTAFLPPTALKM-MRQQGE 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 436 PVtKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTEtGGHMLTPLPGATPMKPGSATFPFFGVAPAILN 515
Cdd:cd05971 201 QL-KHAQVKLRAIATGGESLGEELLGWAREQFGV---EVNEFYGQTE-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVD 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 516 ESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFEttyfKKFPG-YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLST 594
Cdd:cd05971 276 DNGTPLPPGEVGEIAVELPDPVAFLGYWNNPSATE----KKMAGdWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGP 351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 595 AEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 674
Cdd:cd05971 352 AEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGK 431
|
....*..
gi 253970489 675 IMRRVLR 681
Cdd:cd05971 432 IRRRELR 438
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
105-681 |
1.67e-60 |
|
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: 211.84 E-value: 1.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 105 YN---VLDRNVhEKKLGDKVAFYwegnepGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACA 181
Cdd:cd05959 3 YNaatLVDLNL-NEGRGDKTAFI------DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 182 RIGALhSIVFAGFSSESLCERIL-DSSCSLLITTDAFYrgeklvnlkELADEALqkcqEKGFPVRCCIVVkhlgraelgm 260
Cdd:cd05959 76 RAGIV-PVPVNTLLTPDDYAYYLeDSRARVVVVSGELA---------PVLAAAL----TKSEHTLVVLIV---------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 261 gdstsqsppikrscpdVQGKLkekskrvqpqiswNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVV 340
Cdd:cd05959 132 ----------------SGGAG-------------PEAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 341 HTVGGyMLYVATTF-KYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDvnRLWSIVDKYKVTKF 419
Cdd:cd05959 183 HLHAD-IYWTAELYaRNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERPT-PA--AVFKRIRRYRPTVF 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 420 YTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETGGHMLTPLPGAtpMKP 499
Cdd:cd05959 259 FGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEALPAEVGERWKARFG---LDILDGIGSTEMLHIFLSNRPGR--VRY 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 500 GSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMrtVYGNHERFETTyfkkFPGYYV-TGDGCQRDQDGYYWIT 578
Cdd:cd05959 332 GTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATM--YWNNRDKTRDT----FQGEWTrTGDKYVRDDDGFYTYA 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 579 GRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATP 658
Cdd:cd05959 406 GRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYP 485
|
570 580
....*....|....*....|...
gi 253970489 659 DYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:cd05959 486 RWIVFVDELPKTATGKIQRFKLR 508
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
102-687 |
6.73e-57 |
|
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: 202.73 E-value: 6.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 102 NICYNVLDRNVHEKKlgDKVAFYWeGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACA 181
Cdd:cd05970 17 NFAYDVVDAMAKEYP--DKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 182 RIGAlhsivfagfsseslcerILDSSCSLLITTDAFYRgeklvnlkeladealqkCQEKGFPVRCCIvvkhlgrAELGMG 261
Cdd:cd05970 94 KLGA-----------------IAIPATHQLTAKDIVYR-----------------IESADIKMIVAI-------AEDNIP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 262 DSTSQSPPikrSCPDvqgklkeKSKRVQPQISWNQGIDLWWHELMQEAGDECEPEWCDA---EDPLFILYTSGSTGKPKG 338
Cdd:cd05970 133 EEIEKAAP---ECPS-------KPKLVWVGDPVPEGWIDFRKLIKNASPDFERPTANSYpcgEDILLVYFSSGTTGMPKM 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 339 VVHtVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDvnRLWSIVDKYKVTK 418
Cdd:cd05970 203 VEH-DFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDPK--ALLEKLSKYGVTT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 419 FYTAPTAIRLLMKfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGGHMLTpLPGATPmK 498
Cdd:cd05970 280 FCAPPTIYRFLIR---EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIK---LMEGFGQTETTLTIAT-FPWMEP-K 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 499 PGSATFPFFGVAPAILNESGEELEGEAEGYLVF----KQPWpGIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGY 574
Cdd:cd05970 352 PGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtskGKPV-GLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGY 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 575 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGP 654
Cdd:cd05970 428 LWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAP 507
|
570 580 590
....*....|....*....|....*....|...
gi 253970489 655 IATPDYIQNAPGLPKTRSGKImRRVlrKIAQND 687
Cdd:cd05970 508 YKYPRIVEFVDELPKTISGKI-RRV--EIRERD 537
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
136-681 |
1.15e-53 |
|
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: 191.14 E-value: 1.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITtd 215
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 216 afyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqpqiswn 295
Cdd:cd05919 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 296 qgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADI--G 373
Cdd:cd05919 89 -----------------------SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffG 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 374 WITGHSyvTYGPLANGATSVLFegiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQVLGTVGE 453
Cdd:cd05919 146 YGLGNS--LWFPLAVGASAVLN---PGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGS--PDALRSLRLCVSAGE 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 454 PInPEAwLWYhRVVGAQRCPIVDTFWQTETGGHMLTPLPGAtpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQ 533
Cdd:cd05919 219 AL-PRG-LGE-RWMEHFGGPILDGIGATEVGHIFLSNRPGA--WRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRG 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 534 PWPGIMrtvYGNheRFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVV 613
Cdd:cd05919 294 PSAAVG---YWN--NPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVV 368
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 253970489 614 GHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:cd05919 369 AVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
105-681 |
1.58e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 192.71 E-value: 1.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 105 YNVLDRNVheKKLGDKVAFYWEGNEpgettqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIG 184
Cdd:PRK06187 9 GRILRHGA--RKHPDKEAVYFDGRR------TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 185 A-LHSIVFagFSSESLCERIL-DSSCSLLITTDAFyrgEKLV-NLKELADEalqkcqekgfpVRCCIVVKHLGRAELGmg 261
Cdd:PRK06187 81 AvLHPINI--RLKPEEIAYILnDAEDRVVLVDSEF---VPLLaAILPQLPT-----------VRTVIVEGDGPAAPLA-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 262 dstsqsppikrscPDVQGklkekskrvqpqiswnqgidlwWHELMQEAGDEcePEWCDAE--DPLFILYTSGSTGKPKGV 339
Cdd:PRK06187 143 -------------PEVGE----------------------YEELLAAASDT--FDFPDIDenDAAAMLYTSGTTGHPKGV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 340 V--------HTVGGymlyvattfKYVFDFHAEDVF-----------WctadiGWitghsyvTYGPLANGATSVlfegIPT 400
Cdd:PRK06187 186 VlshrnlflHSLAV---------CAWLKLSRDDVYlvivpmfhvhaW-----GL-------PYLALMAGAKQV----IPR 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 401 YPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGtvGEPINPEAWLWYHRVVGaqrCPIVDTFWQ 480
Cdd:PRK06187 241 RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYG--GAALPPALLREFKEKFG---IDLVQGYGM 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 481 TETGG--HMLTPLPGATPM--KPGSATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWpgIMRTVYGNHERFETTYF 554
Cdd:PRK06187 316 TETSPvvSVLPPEDQLPGQwtKRRSAGRPLPGVEARIVDDDGDELPPDGGEVgeIIVRGPW--LMQGYWNRPEATAETID 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 555 KkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGH 634
Cdd:PRK06187 394 G---GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGA 470
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 253970489 635 TFSPKlteELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:PRK06187 471 TLDAK---ELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
118-677 |
1.15e-52 |
|
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: 188.20 E-value: 1.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 118 GDKVAFYWEGNEpgettqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSE 197
Cdd:cd17631 9 PDRTALVFGGRS------LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 198 SLCERILDSSCSLLIttdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdv 277
Cdd:cd17631 83 EVAYILADSGAKVLF----------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 278 qgklkekskrvqpqiswnqgidlwwhelmqeagdecepewcdaEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYV 357
Cdd:cd17631 98 -------------------------------------------DDLALLMYTSGTTGRPKGAMLTHRN-LLWNAVNALAA 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 358 FDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGiptyPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPV 437
Cdd:cd17631 134 LDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFAT 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 438 TKHSraSLQVLGTVGEPInPEAWLwyhRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNES 517
Cdd:cd17631 210 TDLS--SLRAVIYGGAPM-PERLL---RALQARGVKFVQGYGMTETSPGVTFLSPEDHRRKLGSAGRPVFFVEVRIVDPD 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 518 GEELEGEAEGYLVFKQPwpGIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEV 597
Cdd:cd17631 284 GREVPPGEVGEIVVRGP--HVMAGYWNRPEATAAAFRD---GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEV 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 598 ESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 677
Cdd:cd17631 359 EDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDE---DELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
130-682 |
9.01e-50 |
|
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: 181.74 E-value: 9.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 130 PGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILDSSCS 209
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEF-EFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 210 LLITTDAFYRGEKLVNLKELAdealqkcqekgfpvrccivvkhLGRAELGMGDSTSQSPPIKRSCPDVQGKLKEKSKRVQ 289
Cdd:cd05926 88 KLVLTPKGELGPASRAASKLG----------------------LAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 290 PQiswnqgidlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGV--VHT-VGGYMLYVATTFKYVFD------- 359
Cdd:cd05926 146 PL----------------------------PDDLALILHTSGTTGRPKGVplTHRnLAASATNITNTYKLTPDdrtlvvm 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 360 --FHaedvfwctadigwITGHSYVTYGPLANGATSVlfegIPTYPDVNRLWSIVDKYKVTkFYTA-PTAIRLLMKFgDEP 436
Cdd:cd05926 198 plFH-------------VHGLVASLLSTLAAGGSVV----LPPRFSASTFWPDVRDYNAT-WYTAvPTIHQILLNR-PEP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 437 VTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETGGHM-LTPLPgATPMKPGSATFPFfGVAPAILN 515
Cdd:cd05926 259 NPESPPPKLRFIRSCSASLPPAVLEALEATFGA---PVLEAYGMTEAAHQMtSNPLP-PGPRKPGSVGKPV-GVEVRILD 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 516 ESGEELEGEAEGYLVFKQPwpGIMRTVYGNHE-RFEttYFKKFpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLST 594
Cdd:cd05926 334 EDGEILPPGVVGEICLRGP--NVTRGYLNNPEaNAE--AAFKD-GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISP 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 595 AEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHtfsPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 674
Cdd:cd05926 409 LEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGA---SVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGK 485
|
....*...
gi 253970489 675 IMRRVLRK 682
Cdd:cd05926 486 IQRRKVAE 493
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
105-681 |
1.87e-49 |
|
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: 180.07 E-value: 1.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 105 YNVLDRNVheKKLGDKVAFYWegnePGETtqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIG 184
Cdd:cd05936 2 ADLLEEAA--RRFPDKTALIF----MGRK--LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 185 AlhsIVfagfsseslcerildsscsllITTDAFYRGEklvnlkELAdEALQKCQEKGfpvrccIVVkhlgraelgmgdst 264
Cdd:cd05936 74 A---VV---------------------VPLNPLYTPR------ELE-HILNDSGAKA------LIV-------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 265 sqsppikrscpdvqgklkekskrvqpqiswnqgiDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVG 344
Cdd:cd05936 103 ----------------------------------AVSFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHR 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 345 GYMLYVATTFKYVFDFH-AEDVFWCTADIgwitghsYVTYG-------PLANGATSVLfegIPTyPDVNRLWSIVDKYKV 416
Cdd:cd05936 149 NLVANALQIKAWLEDLLeGDDVVLAALPL-------FHVFGltvalllPLALGATIVL---IPR-FRPIGVLKEIRKHRV 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 417 TKFYTAPTAIRLLMKFGDepVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETG--GHmLTPLPGa 494
Cdd:cd05936 218 TIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVEVAERFEELTG---VPIVEGYGLTETSpvVA-VNPLDG- 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 495 tPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFETTyFKKfpGYYVTGDGCQRDQDGY 574
Cdd:cd05936 291 -PRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGP--QVMKGYWNRPEETAEA-FVD--GWLRTGDIGYMDEDGY 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 575 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGP 654
Cdd:cd05936 365 FFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTE---EEIIAFCREQLAG 441
|
570 580
....*....|....*....|....*..
gi 253970489 655 IATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:cd05936 442 YKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
320-681 |
5.42e-48 |
|
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: 175.36 E-value: 5.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 320 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGip 399
Cdd:cd05958 96 SDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEE-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 400 TYPDvnRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEpvTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFW 479
Cdd:cd05958 174 ATPD--LLLSAIARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATGI---PIIDGIG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 480 QTETGGHMLTPLPGAtpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimrTVY-GNHERFETTYFKKfp 558
Cdd:cd05958 247 STEMFHIFISARPGD--ARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP------TGCrYLADKRQRTYVQG-- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 559 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 638
Cdd:cd05958 317 GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGP 396
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 253970489 639 KLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:cd05958 397 VLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
320-684 |
1.45e-46 |
|
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: 171.21 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 320 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFkYVFDFHAEDVFWCTADIGWiTGHSYVT-YGPLANGATSVLFegi 398
Cdd:cd05974 84 ADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTM-YWIGLKPGDVHWNISSPGW-AKHAWSCfFAPWNAGATVFLF--- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 399 pTYP--DVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgdEPVTKHSRASLQVLGTvGEPINPEAwlwYHRVVGAQRCPIVD 476
Cdd:cd05974 159 -NYArfDAKRVLAALVRYGVTTLCAPPTVWRMLIQ---QDLASFDVKLREVVGA-GEPLNPEV---IEQVRRAWGLTIRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 477 TFWQTETgghmlTPLPGATP---MKPGSATFPFFGVAPAILNESGEELEGEAEGyLVFKQPWP-GIMRTVYGNHERfetT 552
Cdd:cd05974 231 GYGQTET-----TALVGNSPgqpVKAGSMGRPLPGYRVALLDPDGAPATEGEVA-LDLGDTRPvGLMKGYAGDPDK---T 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 553 YFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCD 632
Cdd:cd05974 302 AHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRA 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 253970489 633 GHTFSPKLTEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIA 684
Cdd:cd05974 382 GYEPSPETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
311-681 |
1.96e-46 |
|
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: 170.55 E-value: 1.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 311 DECEPEWCDAeDPLFILYTSGSTGKPKGVV--HTvggYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLAN 388
Cdd:cd05934 72 DHSGAQLVVV-DPASILYTSGTTGPPKGVVitHA---NLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 389 GATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLqvlgTVGEPINPEAWLWYHRVVG 468
Cdd:cd05934 148 GATLVL---LPRF-SASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRA----AYGAPNPPELHEEFEERFG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 469 aqrCPIVDTFWQTETGGHMLTPLPGATPmkPGSATFPFFGVAPAILNESGEELEGEAEGYLVFK-QPWPGIMRTVYGNHE 547
Cdd:cd05934 220 ---VRLLEGYGMTETIVGVIGPRDEPRR--PGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRgLRGWGFFKGYYNMPE 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 548 rfETTyfKKFP-GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYC 626
Cdd:cd05934 295 --ATA--EAMRnGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKA 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 253970489 627 FVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:cd05934 371 VVVLRPGETLDP---EELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
119-682 |
4.49e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 168.96 E-value: 4.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 119 DKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 198
Cdd:PRK08316 26 DKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 199 LCeRILDSSCSLLITTDAfyrgeklvNLKELADEALQKCQEKGFPVRCcivVKHLGRAELGMGDstsqsppikrscpdvq 278
Cdd:PRK08316 100 LA-YILDHSGARAFLVDP--------ALAPTAEAALALLPVDTLILSL---VLGGREAPGGWLD---------------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 279 gklkekskrvqpqiswnqgIDLWwhelmQEAGDECEPE-WCDAEDPLFILYTSGSTGKPKGVVHT----VGGYMLYVATT 353
Cdd:PRK08316 152 -------------------FADW-----AEAGSVAEPDvELADDDLAQILYTSGTESLPKGAMLThralIAEYVSCIVAG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 354 fkyvfDFHAEDVFWCTADIGwitgHS---YVTYGP-LANGATSVLFEGiptyPDVNRLWSIVDKYKVTKFYTAPTA-IRL 428
Cdd:PRK08316 208 -----DMSADDIPLHALPLY----HCaqlDVFLGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVwISL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 429 LmkfgdepvtKH---SRASLQVL--GTVGEPINPEAWLwyHRVvgAQRCPIVdTFW----QTETGghmltplPGATPM-- 497
Cdd:PRK08316 275 L---------RHpdfDTRDLSSLrkGYYGASIMPVEVL--KEL--RERLPGL-RFYncygQTEIA-------PLATVLgp 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 498 -----KPGSATFPFFGVAPAILNESGEELEgeaegylvfkqpwPGIMRTVYGNHERFETTYFKKfP---------GYYVT 563
Cdd:PRK08316 334 eehlrRPGSAGRPVLNVETRVVDDDGNDVA-------------PGEVGEIVHRSPQLMLGYWDD-PektaeafrgGWFHS 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 564 GDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEE 643
Cdd:PRK08316 400 GDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTE---DE 476
|
570 580 590
....*....|....*....|....*....|....*....
gi 253970489 644 LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:PRK08316 477 LIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
102-682 |
5.67e-44 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 165.78 E-value: 5.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 102 NICYNVLDRNVHEKKlGDKVAFYwegnepGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACA 181
Cdd:TIGR02262 4 NAAEDLLDRNVVEGR-GGKTAFI------DDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 182 RIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmg 261
Cdd:TIGR02262 77 RAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALL------------------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 262 dstsqsPPIKrscpDVQGKLKEKSKRVQPQISWNQGIDLwwHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVH 341
Cdd:TIGR02262 114 ------PVIK----AALGKSPHLEHRVVVGRPEAGEVQL--AELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVH 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 342 TVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTyPDvnRLWSIVDKYKVTKFYT 421
Cdd:TIGR02262 182 THSNPYWTAELYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERPT-PD--AVFDRLRRHQPTIFYG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 422 APTAIRLLMkfGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGGHMLTPLPGAtpMKPGS 501
Cdd:TIGR02262 259 VPTLYAAML--ADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVD---IVDGIGSTEMLHIFLSNLPGD--VRYGT 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 502 ATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMrtVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRI 581
Cdd:TIGR02262 332 SGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATM--YWNNRAKSRDTFQG---EWTRSGDKYVRNDDGSYTYAGRT 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 582 DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP---VKGEclyCFVTLCDGHTfspKLTEELKKQIREKIGPIATP 658
Cdd:TIGR02262 407 DDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEdglIKPK---AFVVLRPGQT---ALETELKEHVKDRLAPYKYP 480
|
570 580
....*....|....*....|....
gi 253970489 659 DYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:TIGR02262 481 RWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
132-676 |
1.57e-42 |
|
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: 161.23 E-value: 1.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 211
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 212 ITTDAFYrgeklvnlkeladEALQKCQEKGFPVRCCIVVKHLGRAELGMGDSTSqsppikrscpdvqgklkekskrvqpq 291
Cdd:cd05911 87 FTDPDGL-------------EKVKEAAKELGPKDKIIVLDDKPDGVLSIEDLLS-------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 292 isWNQGIDLWWHELMQEAGDEcepewcdaeDPLFILYTSGSTGKPKGVV--HTVGGYMLYVATTFKYVfDFHAEDVFWCT 369
Cdd:cd05911 128 --PTLGEEDEDLPPPLKDGKD---------DTAAILYSSGTTGLPKGVClsHRNLIANLSQVQTFLYG-NDGSNDVILGF 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 370 ADIGWITG-HSYVTYgpLANGATSVLFEGiptyPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVL 448
Cdd:cd05911 196 LPLYHIYGlFTTLAS--LLNGATVIIMPK----FDSELFLDLIEKYKITFLYLVPPIAAALAK--SPLLDKYDLSSLRVI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 449 GTVGEPINPEAwlwYHRV-VGAQRCPIVDTFWQTETGGhMLTPLPGaTPMKPGSATFPFFGVAPAILNESGEELEGEaeg 527
Cdd:cd05911 268 LSGGAPLSKEL---QELLaKRFPNATIKQGYGMTETGG-ILTVNPD-GDDKPGSVGRLLPNVEAKIVDDDGKDSLGP--- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 528 ylvfKQP---W---PGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESAL 601
Cdd:cd05911 340 ----NEPgeiCvrgPQVMKGYYNNPEATKETFDED--GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVL 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 602 VEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfsPKLTE-ELKKQIREKIgpiatPDY------IQNAPGLPKTRSGK 674
Cdd:cd05911 414 LEHPGVADAAVIGIPDEVSGELPRAYVVRKPG----EKLTEkEVKDYVAKKV-----ASYkqlrggVVFVDEIPKSASGK 484
|
..
gi 253970489 675 IM 676
Cdd:cd05911 485 IL 486
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
29-682 |
2.36e-38 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 152.16 E-value: 2.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 29 WSPPPEVSRSAHVPSLQRYR-----------------ELHRRSVEEPREFWGDIAKEF--YWKTPcPGPFLRYNFDVTKG 89
Cdd:PLN03052 87 WFPSPEIAKLTNLGRLLEARgkellgskykdpissfsEFQRFSVENPEVYWSIVLDELslVFSVP-PRCILDTSDESNPG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 90 KifiEWMKGATTNICYNVLDRNVHEKklGDKVAFYW--EGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYM 167
Cdd:PLN03052 166 G---QWLPGAVLNVAECCLTPKPSKT--DDSIAIIWrdEGSDDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDM 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 168 PMIPELVVAMLAcarigalhsIVFAG---------FSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEAlqkcq 238
Cdd:PLN03052 241 PMNVHAVIIYLA---------IILAGcvvvsiadsFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYSRVVEA----- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 239 ekgfpvrccivvkhlgraelgmgdstsQSP-----PIKRSCPDVQgkLKEKskrvqpqiswnqgiDLWWHELMQEA---- 309
Cdd:PLN03052 307 ---------------------------KAPkaivlPADGKSVRVK--LREG--------------DMSWDDFLARAnglr 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 310 -GDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVfDFHAEDVF-WCTaDIGWITGHsYVTYGPLA 387
Cdd:PLN03052 344 rPDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHL-DIRKGDIVcWPT-NLGWMMGP-WLVYASLL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 388 NGATSVLFEGIPTYPDVNRLwsiVDKYKVTKFYTAPTAIRLLMKFGdePVTKHSRASLQVLGTVGEPINPEAWLWYhrVV 467
Cdd:PLN03052 421 NGATLALYNGSPLGRGFAKF---VQDAKVTMLGTVPSIVKTWKNTN--CMAGLDWSSIRCFGSTGEASSVDDYLWL--MS 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 468 GAQRCPIVDTFWQTETGGHMLTplpgATPMKPGS-ATF--PFFGVAPAILNESGeelegeaegylvfkQPWP-------- 536
Cdd:PLN03052 494 RAGYKPIIEYCGGTELGGGFVT----GSLLQPQAfAAFstPAMGCKLFILDDSG--------------NPYPddapctge 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 537 --------GIMRTVY-GNHERfetTYFKKFPGYYVT-----GDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVE---- 598
Cdd:PLN03052 556 lalfplmfGASSTLLnADHYK---VYFKGMPVFNGKilrrhGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIErvcn 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 599 SAlveHEAVAEAAVVGHPHPVKG-ECLYCFVTLCDGHTFSPKLtEELKK----QIREKIGPIATPDYIQNAPGLPKTRSG 673
Cdd:PLN03052 633 AA---DESVLETAAIGVPPPGGGpEQLVIAAVLKDPPGSNPDL-NELKKifnsAIQKKLNPLFKVSAVVIVPSFPRTASN 708
|
....*....
gi 253970489 674 KIMRRVLRK 682
Cdd:PLN03052 709 KVMRRVLRQ 717
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
132-680 |
9.92e-38 |
|
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: 146.52 E-value: 9.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGFSSESLCERIL----DSS 207
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGA----AYVPLDPSYPAERLAyileDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 208 CSLLITtdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskr 287
Cdd:cd05930 85 AKLVLT-------------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 288 vqpqiswnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATtFKYVFDFHAEDVFW 367
Cdd:cd05930 91 -------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW-MQEAYPLTPGDRVL 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 368 CTADIGWItGHSYVTYGPLANGATSVLfegIP--TYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVtkhsRASL 445
Cdd:cd05930 139 QFTSFSFD-VSVWEIFGALLAGATLVV---LPeeVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA----LPSL 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 446 QVLGTVGEPINPEAW-LWYHRVVGAQ--------RCPIVDTFWQTETGGHMLTPLPGATPMkPGSATFpffgvapaILNE 516
Cdd:cd05930 211 RLVLVGGEALPPDLVrRWRELLPGARlvnlygptEATVDATYYRVPPDDEEDGRVPIGRPI-PNTRVY--------VLDE 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 517 SGeelegeaegylvfkQPWP------------GIMRTVYGNHE----RFETTYFkkFPG--YYVTGD-GCQRDqDG--YY 575
Cdd:cd05930 282 NL--------------RPVPpgvpgelyiggaGLARGYLNRPEltaeRFVPNPF--GPGerMYRTGDlVRWLP-DGnlEF 344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 576 wiTGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPI 655
Cdd:cd05930 345 --LGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELD---EEELRAHLAERLPDY 419
|
570 580
....*....|....*....|....*
gi 253970489 656 ATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:cd05930 420 MVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
115-682 |
1.39e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 147.36 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 115 KKLGDKVAfYWEGNEpgettQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALhsivfagf 194
Cdd:PRK07656 16 RRFGDKEA-YVFGDQ-----RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAV-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 195 sseslcerildsscslLITtdafyrgeklVNLKELADEALQKCQEKGfpVRCCIVVKHLgraeLGMGDSTSQSPP---IK 271
Cdd:PRK07656 82 ----------------VVP----------LNTRYTADEAAYILARGD--AKALFVLGLF----LGVDYSATTRLPaleHV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 272 RSCPDVQGK-LKEKSKRvqpqiswnqgidlwWHELMQEA-GDECEPEwCDAEDPLFILYTSGSTGKPKGVVHTVGG-YML 348
Cdd:PRK07656 130 VICETEEDDpHTEKMKT--------------FTDFLAAGdPAERAPE-VDPDDVADILFTSGTTGRPKGAMLTHRQlLSN 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 349 Y--VATTFKYVFD---------FHaedVFWCTAdiGWITghsyvtygPLANGATSVLfegIPTYpDVNRLWSIVDKYKVT 417
Cdd:PRK07656 195 AadWAEYLGLTEGdrylaanpfFH---VFGYKA--GVNA--------PLMRGATILP---LPVF-DPDEVFRLIETERIT 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 418 KFYTAPTAIRLLMKFGDEpvTKHSRASLQVLGTVGEPInPEAWLwyHRVVGAQRCPIVDT-FWQTETGGHM-LTPLPGAT 495
Cdd:PRK07656 258 VLPGPPTMYNSLLQHPDR--SAEDLSSLRLAVTGAASM-PVALL--ERFESELGVDIVLTgYGLSEASGVTtFNRLDDDR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 496 PMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYY 575
Cdd:PRK07656 333 KTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGP--NVMKGYYDDPE--ATAAAIDADGWLHTGDLGRLDEEGYL 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 576 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfspkLTEE-LKKQIREKIGP 654
Cdd:PRK07656 409 YIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAE----LTEEeLIAYCREHLAK 484
|
570 580
....*....|....*....|....*...
gi 253970489 655 IATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:PRK07656 485 YKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
136-700 |
7.08e-37 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 147.02 E-value: 7.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLAcariGALHSIVFA---GFSSESLCErildsscsLLI 212
Cdd:PRK07529 59 WTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANPinpLLEPEQIAE--------LLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 213 TTDAfyrgEKLVNLKELAD-EALQKCQEKgfpVRCCIVVKHLGRAELGMGDSTSQSPPIKRSCPDVQGKLkekskrvqpq 291
Cdd:PRK07529 127 AAGA----KVLVTLGPFPGtDIWQKVAEV---LAALPELRTVVEVDLARYLPGPKRLAVPLIRRKAHARI---------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 292 ISWNQgidlwwhELMQEAGDECE-PEWCDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTA 370
Cdd:PRK07529 190 LDFDA-------ELARQPGDRLFsGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCGL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 371 DIGWITGhSYVT-YGPLANGAtSVLFEGIPTYPD---VNRLWSIVDKYKVTKFYTAPTAIRLLMkfgDEPVTKHSRASLQ 446
Cdd:PRK07529 262 PLFHVNA-LLVTgLAPLARGA-HVVLATPQGYRGpgvIANFWKIVERYRINFLSGVPTVYAALL---QVPVDGHDISSLR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 447 VLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTE-TGGHMLTPLPGatPMKPGSA--TFPFFGVAPAILNESGEELEG 523
Cdd:PRK07529 337 YALCGAAPLPVEVFRRFEAATGV---RIVEGYGLTEaTCVSSVNPPDG--ERRIGSVglRLPYQRVRVVILDDAGRYLRD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 524 EAEG---YLVFKQP--WPGIMRTVYGNHERFEttyfkkfPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVE 598
Cdd:PRK07529 412 CAVDevgVLCIAGPnvFSGYLEAAHNKGLWLE-------DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 599 SALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP-KLTEELKKQIREkigPIATPDYIQNAPGLPKTRSGKI-- 675
Cdd:PRK07529 485 EALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEaELLAFARDHIAE---RAAVPKHVRILDALPKTAVGKIfk 561
|
570 580 590
....*....|....*....|....*....|...
gi 253970489 676 -------MRRVLRK-IAQNDHDLGDMSTVADPS 700
Cdd:PRK07529 562 palrrdaIRRVLRAaLRDAGVEAEVVDVVEDGR 594
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
135-685 |
3.16e-36 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 143.75 E-value: 3.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 135 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHsiVFAGFS---SE--SLCERildSSCS 209
Cdd:COG1021 50 RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP--VFALPAhrrAEisHFAEQ---SEAV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 210 LLITTDAfYRGeklVNLKELADEALQKCQEkgfpVRCCIVVkhlgraelgmGDStsqsppikrscpdvqgklkekskrvQ 289
Cdd:COG1021 125 AYIIPDR-HRG---FDYRALARELQAEVPS----LRHVLVV----------GDA-------------------------G 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 290 PQISWNqgidlwwhELMQEAGDECEPEwCDAEDPLFILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWCT 369
Cdd:COG1021 162 EFTSLD--------ALLAAPADLSEPR-PDPDDVAFFQLSGGTTGLPKLIPRTHDDY-LYSVRASAEICGLDADTVYLAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 370 ADIGwitgHSY-----VTYGPLANGATSVLfegIPTyPDVNRLWSIVDKYKVTkfYTA--PTAIRLLMKFGDEpvTKHSR 442
Cdd:COG1021 232 LPAA----HNFplsspGVLGVLYAGGTVVL---APD-PSPDTAFPLIERERVT--VTAlvPPLALLWLDAAER--SRYDL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 443 ASLQVLGTVGEPINPEA----------WLW-----------Y-------HRVVGAQRCP--------IVDtfwqtETGgh 486
Cdd:COG1021 300 SSLRVLQVGGAKLSPELarrvrpalgcTLQqvfgmaeglvnYtrlddpeEVILTTQGRPispddevrIVD-----EDG-- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 487 mlTPLPgatpmkPGSAtfpffGVapailnesgeelegeaegyLVFKQPWpgimrTVYGnherfettYFKKfP-------- 558
Cdd:COG1021 373 --NPVP------PGEV-----GE-------------------LLTRGPY-----TIRG--------YYRA-Pehnaraft 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 559 --GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLycFVTLcDGH 634
Cdd:COG1021 407 pdGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGErsCA--FVVP-RGE 483
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 253970489 635 TFSPKlteELKKQIREKiGpIAT---PDYIQNAPGLPKTRSGKIMRRVLRKIAQ 685
Cdd:COG1021 484 PLTLA---ELRRFLRER-G-LAAfklPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
167-681 |
1.83e-34 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 138.02 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 167 MPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALqkcqekgfPVRC 246
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAA--------PAKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 247 cIVVKHLGRaelgmgdstsqsppikrscpDVQGKLKEKskrvqpqiswnqgiDLWWHELMQEA-------GDECEPEWCD 319
Cdd:PLN03051 73 -IVLPAAGE--------------------PVAVPLREQ--------------DLSWCDFLGVAaaqgsvgGNEYSPVYAP 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 320 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVfDFHAEDVFWCTADIGWITGhSYVTYGPLANGATSVLFEGIP 399
Cdd:PLN03051 118 VESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWAHM-DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 400 TYPDVNRLwsiVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRcPIVDTFW 479
Cdd:PLN03051 196 LGRGFGKF---VQDAGVTVLGLVPSIVKAWRHTGAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 480 QTETGGHML--TPLpgaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWPGIM-RTVYGNHERfetTYF 554
Cdd:PLN03051 272 GTELASGYIssTLL---QPQAPGAFSTASLGTRFVLLNDNGVPYPDDQPCVgeVALAPPMLGASdRLLNADHDK---VYY 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 555 KKFPGYYVTGDGCQRDQD-------GYYWITGRIDDMLNVSGHLLSTAEVESALVE-HEAVAEAAVVGHPHPVKG-ECLY 625
Cdd:PLN03051 346 KGMPMYGSKGMPLRRHGDimkrtpgGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGpELLV 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 253970489 626 CFVTLCD-GHTFSPKLTEELKKQ----IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:PLN03051 426 IFLVLGEeKKGFDQARPEALQKKfqeaIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
101-680 |
7.76e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 136.63 E-value: 7.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 101 TNICYNVldrNVHEKKLGDKVAFYWEGNEpgettqITYHQLLVQVCQFSNVL-RKQGIQKGDRVAIYMPMIPELVVAMLA 179
Cdd:PRK08314 10 TSLFHNL---EVSARRYPDKTAIVFYGRA------ISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 180 CARIGALHSIVFAGFSSESLCERILDSSCSLLITTDafyrgeklvnlkELADEALQKCQEKGfpVRCCIVVKhlgraelg 259
Cdd:PRK08314 81 ILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGS------------ELAPKVAPAVGNLR--LRHVIVAQ-------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 260 MGDSTSQSPPIK-----RSCPDVQGKLKEKSkrvqpqISWNQGIDlwwhelmqeAGDECEPEWCDAEDPLFILYTSGSTG 334
Cdd:PRK08314 139 YSDYLPAEPEIAvpawlRAEPPLQALAPGGV------VAWKEALA---------AGLAPPPHTAGPDDLAVLPYTSGTTG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 335 KPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLfegIPTYpDVNRLWSIVDKY 414
Cdd:PRK08314 204 VPKGCMHTHRTVMANAVGSVLW-SNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL---MPRW-DREAAARLIERY 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 415 KVTKFYTAPT-AIRLLMKFGdepVTKHSRASLQVLGTVGEPInPEAWlwyhrvvgAQR------CPIVDTFWQTETGGHM 487
Cdd:PRK08314 279 RVTHWTNIPTmVVDFLASPG---LAERDLSSLRYIGGGGAAM-PEAV--------AERlkeltgLDYVEGYGLTETMAQT 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 488 LTPLPGATpmKPGSATFPFFGVAPAILNESGEELEGEAEG--YLVFKqpwPGIMRTVYGNHERFETTyFKKFPG--YYVT 563
Cdd:PRK08314 347 HSNPPDRP--KLQCLGIPTFGVDARVIDPETLEELPPGEVgeIVVHG---PQVFKGYWNRPEATAEA-FIEIDGkrFFRT 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 564 GDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKlTEE 643
Cdd:PRK08314 421 GDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTT-EEE 499
|
570 580 590
....*....|....*....|....*....|....*..
gi 253970489 644 LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:PRK08314 500 IIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
319-680 |
9.51e-34 |
|
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: 134.74 E-value: 9.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 319 DAEDPLFILYTSGSTGKPKGVVHTVGGYM-LYVATTfkYVFDFHAEDVfwctadigWITGHSYV-------TYGPLANGA 390
Cdd:cd17643 91 DPDDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQ--RWFGFNEDDV--------WTLFHSYAfdfsvweIWGALLHGG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 391 TSVlfegIPTYpDVNR----LWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGtvGEPINPeAWL--WYH 464
Cdd:cd17643 161 RLV----VVPY-EVARspedFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFG--GEALEA-AMLrpWAG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 465 RVvGAQRCPIVDTFWQTETGGHM----LTP--LPGATpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGI 538
Cdd:cd17643 233 RF-GLDRPQLVNMYGITETTVHVtfrpLDAadLPAAA-ASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGY 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 539 MRTVYGNHERFETTYFKKfPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHP 616
Cdd:cd17643 311 LGRPELTAERFVANPFGG-PGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVRE 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 253970489 617 HPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIgpiatPDYIQNA-----PGLPKTRSGKIMRRVL 680
Cdd:cd17643 390 DEPGDTRLVAYVVADDGAAADI---AELRALLKELL-----PDYMVPAryvplDALPLTVNGKLDRAAL 450
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
328-684 |
2.40e-31 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 126.06 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 328 YTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGhSYVTYG-PLANGAtSVLFEGIPTYPD--- 403
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNG-SVVTLLtPLASGA-HVVLAGPAGYRNpgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 404 VNRLWSIVDKYKVTKFYTAPTAIRLLMKfgdEPVTKhSRASLQVLGTVGEPINPEAwlwYHRVVGAQRCPIVDTFWQTE- 482
Cdd:cd05944 86 FDNFWKLVERYRITSLSTVPTVYAALLQ---VPVNA-DISSLRFAMSGAAPLPVEL---RARFEDATGLPVVEGYGLTEa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 483 TGGHMLTPlPGaTPMKPGSA--TFPFFGVAPAILNESGEELEGEAEGYLvfkqpWPGIM--RTVYGNH---ERFETTYFK 555
Cdd:cd05944 159 TCLVAVNP-PD-GPKRPGSVglRLPYARVRIKVLDGVGRLLRDCAPDEV-----GEICVagPGVFGGYlytEGNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 556 kfPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHT 635
Cdd:cd05944 232 --DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAV 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 253970489 636 FSP-KLTEELKKQIREKigpIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 684
Cdd:cd05944 310 VEEeELLAWARDHVPER---AAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
136-680 |
2.86e-31 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 128.51 E-value: 2.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 215
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 216 AfyrgeklvNLKELADEALQkcqekgfpvrccIVVkhLGRAElgmGDSTSQSPPIKRSCPDvqgklkeksKRVQPQISwn 295
Cdd:cd05904 113 E--------LAEKLASLALP------------VVL--LDSAE---FDSLSFSDLLFEADEA---------EPPVVVIK-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 296 qgidlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGYmlyVATTFKYVFDF----HAEDVFWCTAD 371
Cdd:cd05904 157 ------------------------QDDVAALLYSSGTTGRSKGVMLTHRNL---IAMVAQFVAGEgsnsDSEDVFLCVLP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 372 IGWITGHSYVTYGPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTV 451
Cdd:cd05904 210 MFHIYGLSSFALGLLRLGATVVV---MPRF-DLEELLAAIERYKVTHLPVVPPIVLALVK--SPIVDKYDLSSLRQIMSG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 452 GEPINPEAwlwYHRVvgAQRCPIVDtFWQ----TETGG--HMlTPLPGATPMKPGSATFPFFGVAPAILNESGEELegea 525
Cdd:cd05904 284 AAPLGKEL---IEAF--RAKFPNVD-LGQgygmTESTGvvAM-CFAPEKDRAKYGSVGRLVPNVEAKIVDPETGES---- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 526 egyLVFKQP---W---PGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVES 599
Cdd:cd05904 353 ---LPPNQTgelWirgPSIMKGYLNNPEATAATIDKE--GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEA 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 600 ALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKlteELKKQIREKIGP------IATPDYIqnapglPKTRSG 673
Cdd:cd05904 428 LLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTED---EIMDFVAKQVAPykkvrkVAFVDAI------PKSPSG 498
|
....*..
gi 253970489 674 KIMRRVL 680
Cdd:cd05904 499 KILRKEL 505
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
115-682 |
4.76e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 125.15 E-value: 4.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 115 KKLGDKVAFYWegnepGETTqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGf 194
Cdd:PRK07470 18 RRFPDRIALVW-----GDRS-WTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGA----VWVP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 195 sseslcerildsscsllittdafyrgeklVNLKELADEALQKCQEKGfpvrccivvkhlGRAELGMGDSTSQSPPIKRSC 274
Cdd:PRK07470 87 -----------------------------TNFRQTPDEVAYLAEASG------------ARAMICHADFPEHAAAVRAAS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 275 PDVQGKLKEKSKRVQPQISwnqgidlwwHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTvGGYMLYVATTf 354
Cdd:PRK07470 126 PDLTHVVAIGGARAGLDYE---------ALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLT-HGQMAFVITN- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 355 kyvfdfHAEDVFWCTadigwiTGH--SYVTyGPL------------ANGATSVLfegIPTYP-DVNRLWSIVDKYKVTKF 419
Cdd:PRK07470 195 ------HLADLMPGT------TEQdaSLVV-APLshgagihqlcqvARGAATVL---LPSERfDPAEVWALVERHRVTNL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 420 YTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGGHMlTPLPGA----- 494
Cdd:PRK07470 259 FTVPTILKMLVE--HPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKV---LVQYFGLGEVTGNI-TVLPPAlhdae 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 495 -TPM-KPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFEttyfKKF-PGYYVTGDGCQRDQ 571
Cdd:PRK07470 333 dGPDaRIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGP--AVFAGYYNNPEANA----KAFrDGWFRTGDLGHLDA 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 572 DGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREK 651
Cdd:PRK07470 407 RGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDE---AELLAWLDGK 483
|
570 580 590
....*....|....*....|....*....|.
gi 253970489 652 IGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:PRK07470 484 VARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
119-685 |
1.35e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 124.00 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 119 DKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 198
Cdd:PRK06178 48 QRPAIIFYG------HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 199 LCERILDSSCSLLITTDAFYrgeklvnlkELADEALQKCqekgfPVRCCIVVkhlgraelGMGDSTSQSPPIkrSCPD-V 277
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLA---------PVVEQVRAET-----SLRHVIVT--------SLADVLPAEPTL--PLPDsL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 278 QGklkekskrvqPQISWNQGIDLWwhELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTvGGYMLYVATTFKYV 357
Cdd:PRK06178 178 RA----------PRLAAAGAIDLL--PALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHT-QRDMVYTAAAAYAV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 358 FDFHAED-VFWCTADIGWITGHSYVTYGPLANGATSVLFegipTYPDVNRLWSIVDKYKVTK-FYTAPTAIRLLmkfgDE 435
Cdd:PRK06178 245 AVVGGEDsVFLSFLPEFWIAGENFGLLFPLFSGATLVLL----ARWDAVAFMAAVERYRVTRtVMLVDNAVELM----DH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 436 P-VTKHSRASLQVLGTVG--EPINPEAWLWYHRVVGaqrCPIVDTFW-QTET------------GGHMLT--------PL 491
Cdd:PRK06178 317 PrFAEYDLSSLRQVRVVSfvKKLNPDYRQRWRALTG---SVLAEAAWgMTEThtcdtftagfqdDDFDLLsqpvfvglPV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 492 PGA----TPMKPGsATFPFfGV-------APAILnesgeelegeaegylvfkqpwpgimrTVYGNHERFETTYFKKfpGY 560
Cdd:PRK06178 394 PGTefkiCDFETG-ELLPL-GAegeivvrTPSLL--------------------------KGYWNKPEATAEALRD--GW 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 561 YVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkl 640
Cdd:PRK06178 444 LHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA-- 521
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 253970489 641 tEELKKQIREKIGPIATPD-YIQNApgLPKTRSGKIMRRVLRKIAQ 685
Cdd:PRK06178 522 -AALQAWCRENMAVYKVPEiRIVDA--LPMTATGKVRKQDLQALAE 564
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
118-682 |
4.10e-29 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 121.97 E-value: 4.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 118 GDKVAFYWEGnePGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGA-LHSI---VFAg 193
Cdd:cd12119 10 GDREIVSRTH--EGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAvLHTInprLFP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 194 fsseslcERILdsscslLITTDAfyrGEKLVnlkeLADEALQKCQEkgfpvrccivvkhlgraelgmgdstsqspPIKRS 273
Cdd:cd12119 87 -------EQIA------YIINHA---EDRVV----FVDRDFLPLLE-----------------------------AIAPR 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 274 CPDVQGKLKEKSKRVQPQISWNQGIDlWWHELMQEAGDECEPEWcDAEDPLFILYTSGSTGKPKGVV--------HTVGG 345
Cdd:cd12119 118 LPTVEHVVVMTDDAAMPEPAGVGVLA-YEELLAAESPEYDWPDF-DENTAAAICYTSGTTGNPKGVVyshrslvlHAMAA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 346 YMlyvattfKYVFDFHAEDVF-----------WCTADIGWITGHSYVTYGPLANGATsvlfegiptypdvnrLWSIVDKY 414
Cdd:cd12119 196 LL-------TDGLGLSESDVVlpvvpmfhvnaWGLPYAAAMVGAKLVLPGPYLDPAS---------------LAELIERE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 415 KVTKFYTAPTAIRLLMKFGDEpvTKHSRASLQVLgtvgepinpeawlwyhrVVGAQRCP----------IVDTF--W-QT 481
Cdd:cd12119 254 GVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRRV-----------------VIGGSAVPrslieafeerGVRVIhaWgMT 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 482 ETG--GHMLTPLPGATPMKPG-------SATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPWpgIMRTVYGNHErfe 550
Cdd:cd12119 315 ETSplGTVARPPSEHSNLSEDeqlalraKQGRPVPGVELRIVDDDGRELPWDGKAVgeLQVRGPW--VTKSYYKNDE--- 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 551 TTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTL 630
Cdd:cd12119 390 ESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVL 469
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 253970489 631 CDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:cd12119 470 KEGATVTA---EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
119-681 |
4.68e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 122.02 E-value: 4.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 119 DKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAM----LACARIGALHSIVfagf 194
Cdd:PRK06188 27 DRPALVLGD------TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIgaaqLAGLRRTALHPLG---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 195 SSESLCERILDSSCSLLITTDAFYRgeklvnlkELADEALQKCQEkgfpvrccivVKHLgraeLGMGDStsqsppikrsc 274
Cdd:PRK06188 97 SLDDHAYVLEDAGISTLIVDPAPFV--------ERALALLARVPS----------LKHV----LTLGPV----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 275 pdvqgklkekskrvqpqiswNQGIDLWwhelmqEAGDECEPE----WCDAEDPLFILYTSGSTGKPKGVVHTVGGYmlyv 350
Cdd:PRK06188 144 --------------------PDGVDLL------AAAAKFGPAplvaAALPPDIAGLAYTGGTTGKPKGVMGTHRSI---- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 351 aTTFkyvfdfhaedVFWCTADIGWITGHSYVTYGPLANGATS----VLFEGIPTYP----DVNRLWSIVDKYKVTKFYTA 422
Cdd:PRK06188 194 -ATM----------AQIQLAEWEWPADPRFLMCTPLSHAGGAfflpTLLRGGTVIVlakfDPAEVLRAIEEQRITATFLV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 423 PTAIRLLMKFGDEPVTKHSraSLQVLGTVGEPINP----EAwlwyHRVVGaqrcPI-VDTFWQTETGgHMLTPLP----- 492
Cdd:PRK06188 263 PTMIYALLDHPDLRTRDLS--SLETVYYGASPMSPvrlaEA----IERFG----PIfAQYYGQTEAP-MVITYLRkrdhd 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 493 GATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHERFETT--YFKKfpGYYVTGDGCQRD 570
Cdd:PRK06188 332 PDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGP--LVMD---GYWNRPEETaeAFRD--GWLHTGDVARED 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 571 QDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIRE 650
Cdd:PRK06188 405 EDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA---AELQAHVKE 481
|
570 580 590
....*....|....*....|....*....|.
gi 253970489 651 KIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:PRK06188 482 RKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
136-682 |
1.41e-28 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 120.66 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 215
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 216 AFYRgeklvnlkeLADEALQKCqekgfpvrccivvkHLGRAELGMGDSTSQSPPIKRSCPdvqgklkekskrvqpqISWN 295
Cdd:TIGR03098 106 ERLD---------LLHPALPGC--------------HDLRTLIIVGDPAHASEGHPGEEP----------------ASWP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 296 QgidlwwhelMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT----VGGymlyvATTFKYVFDFHAEDVFWCTAD 371
Cdd:TIGR03098 147 K---------LLALGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLShrnlVAG-----AQSVATYLENRPDDRLLAVLP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 372 IGWITGHSYVTYGpLANGATSVLFEgiptYPDVNRLWSIVDKYKVTKFYTAPTairLLMKFGDEPVTKHSRASLQVLGTV 451
Cdd:TIGR03098 213 LSFDYGFNQLTTA-FYVGATVVLHD----YLLPRDVLKALEKHGITGLAAVPP---LWAQLAQLDWPESAAPSLRYLTNS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 452 GEPInPEAWLWYHRvvgaQRCPIVDTFWQ---TETGGHMLTPlPGATPMKPGS--ATFPFFGVapAILNESGEELEGEAE 526
Cdd:TIGR03098 285 GGAM-PRATLSRLR----SFLPNARLFLMyglTEAFRSTYLP-PEEVDRRPDSigKAIPNAEV--LVLREDGSECAPGEE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 527 GYLVFKQP------WPGIMRTVygnhERFE-TTYFK---KFPGYYV-TGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTA 595
Cdd:TIGR03098 357 GELVHRGAlvamgyWNDPEKTA----ERFRpLPPFPgelHLPELAVwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPT 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 596 EVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKlteELKKQIREKIGPIATPDYIQNAPGLPKTRSGKI 675
Cdd:TIGR03098 433 EVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDRA---ALLAECRARLPNYMVPALIHVRQALPRNANGKI 509
|
....*..
gi 253970489 676 MRRVLRK 682
Cdd:TIGR03098 510 DRKALAK 516
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
596-674 |
1.46e-28 |
|
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: 108.79 E-value: 1.46e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 253970489 596 EVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 674
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPG---VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
136-680 |
1.48e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 120.91 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 215
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 216 AFYrgEKLVNLkeladEALQKCQEkgfpvrccIVVKHLgraelgmgdstSQSPPIKRSC--PDVQgklkEKSKRVQPQIS 293
Cdd:PRK06710 130 LVF--PRVTNV-----QSATKIEH--------VIVTRI-----------ADFLPFPKNLlyPFVQ----KKQSNLVVKVS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 294 WNQGIDLWwhELMQEAGDECEPEWCDAEDPLFIL-YTSGSTGKPKGVVHTVGGYMLYVATTFKYVFD-FHAEDVFWCTAD 371
Cdd:PRK06710 180 ESETIHLW--NSVEKEVNTGVEVPCDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNcKEGEEVVLGVLP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 372 IGWITGHSYVTYGPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfgDEPVTK-HSRASLQVLGT 450
Cdd:PRK06710 258 FFHVYGMTAVMNLSIMQGYKMVL---IPKF-DMKMVFEAIKKHKVTLFPGAPTIYIALL---NSPLLKeYDISSIRACIS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 451 VGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETgghmlTPLPGATPM----KPGSATFPFFGVAPAILNESGEELEGEAE 526
Cdd:PRK06710 331 GSAPLPVEVQEKFETVTGGK---LVEGYGLTES-----SPVTHSNFLwekrVPGSIGVPWPDTEAMIMSLETGEALPPGE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 527 G-YLVFKQPwpGIMRTVYGNHErfETTYFKKfPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHE 605
Cdd:PRK06710 403 IgEIVVKGP--QIMKGYWNKPE--ETAAVLQ-DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHE 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 253970489 606 AVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:PRK06710 478 KVQEVVTIGVPDPYRGETVKAFVVLKEGTECS---EEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
131-681 |
1.65e-28 |
|
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: 119.76 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILDSSCSL 210
Cdd:cd17651 16 AEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERL-AFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 211 LITTDAFYRGEklvnlkeLADEAlqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqp 290
Cdd:cd17651 95 LVLTHPALAGE-------LAVEL--------------------------------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 291 qiswnqGIDLWWHELMQEAGDECEPEW-CDAEDPLFILYTSGSTGKPKGVV------------HTVGGYMLYVATTFKYV 357
Cdd:cd17651 111 ------VAVTLLDQPGAAAGADAEPDPaLDADDLAYVIYTSGSTGRPKGVVmphrslanlvawQARASSLGPGARTLQFA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 358 ---FDFHAEDVFwctadigwitghsyvtyGPLANGATSVLfegIPTY--PDVNRLWSIVDKYKVTKFYTAPTAIRLLMKF 432
Cdd:cd17651 185 glgFDVSVQEIF-----------------STLCAGATLVL---PPEEvrTDPPALAAWLDEQRISRVFLPTVALRALAEH 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 433 GDEPVTKHsrASLQVLGTVGEPINPEAWL--WYHRVVGAQrcpIVDTFWQTET---GGHMLTPLPGATPMKPGSATfPFF 507
Cdd:cd17651 245 GRPLGVRL--AALRYLLTGGEQLVLTEDLreFCAGLPGLR---LHNHYGPTEThvvTALSLPGDPAAWPAPPPIGR-PID 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 508 GVAPAILNEsgeelegeaegylvFKQPWP------------GIMRTVYGN----HERFETTYFKKFPGYYVTGDGCQRDQ 571
Cdd:cd17651 319 NTRVYVLDA--------------ALRPVPpgvpgelyiggaGLARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLP 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 572 DGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdGHTFSPKLTEELKKQIREK 651
Cdd:cd17651 385 DGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV---GDPEAPVDAAELRAALATH 461
|
570 580 590
....*....|....*....|....*....|
gi 253970489 652 IGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:cd17651 462 LPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
137-612 |
2.64e-28 |
|
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: 118.14 E-value: 2.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 137 TYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSLLITT 214
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERL-AFILeDAGARLLLTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 215 DAFyrgeklvnlkeladealqkCQEKGFPVRCCIVVkhLGRAELGMGDSTSQSPPIKRSCPDvqgklkekskrvqpqisw 294
Cdd:TIGR01733 80 SAL-------------------ASRLAGLVLPVILL--DPLELAALDDAPAPPPPDAPSGPD------------------ 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 295 nqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVfwctadigW 374
Cdd:TIGR01733 121 ---------------------------DLAYVIYTSGSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------V 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 375 ITGHSYV-------TYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfgDEPVTkhSRASLQV 447
Cdd:TIGR01733 165 LQFASLSfdasveeIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLA---AALPP--ALASLRL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 448 LGTVGEPINPEAWLWYHRVVGAQRcpIVDTFWQTETG---GHMLTPLPGATPMKPGSATFPFFGVAPAILNESGeelege 524
Cdd:TIGR01733 240 VILGGEALTPALVDRWRARGPGAR--LINLYGPTETTvwsTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDL------ 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 525 aegylvfkQPWP------------GIMRtvyGNHERFETT--YFKKFPGY-------YVTGDGCQRDQDGYYWITGRIDD 583
Cdd:TIGR01733 312 --------RPVPvgvvgelyiggpGVAR---GYLNRPELTaeRFVPDPFAggdgarlYRTGDLVRYLPDGNLEFLGRIDD 380
|
490 500
....*....|....*....|....*....
gi 253970489 584 MLNVSGHLLSTAEVESALVEHEAVAEAAV 612
Cdd:TIGR01733 381 QVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
119-687 |
4.03e-28 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 119.39 E-value: 4.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 119 DKVAFYWEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 198
Cdd:PRK13295 39 DKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 199 LCERILDSSCSLLITTDAFyRG---EKLVNlkELADE--ALQKcqekgfpvrccIVVkhlgraeLGMGDSTS----QSPP 269
Cdd:PRK13295 119 LSFMLKHAESKVLVVPKTF-RGfdhAAMAR--RLRPElpALRH-----------VVV-------VGGDGADSfealLITP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 270 IKRSCPDVQGKLKekskRVQPqiswnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHT----VGG 345
Cdd:PRK13295 178 AWEQEPDAPAILA----RLRP----------------------------GPDDVTQLIYTSGTTGEPKGVMHTantlMAN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 346 YMLYVATtfkyvFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEgiptYPDVNRLWSIVDKYKVTkFYTAPTA 425
Cdd:PRK13295 226 IVPYAER-----LGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD----IWDPARAAELIRTEGVT-FTMASTP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 426 irLLMKFGDepVTKHSR---ASLQVLGTVGEPINP----EAWlwyhRVVGAQrcpIVDTFWQTETGGHMLTpLPGATPMK 498
Cdd:PRK13295 296 --FLTDLTR--AVKESGrpvSSLRTFLCAGAPIPGalveRAR----AALGAK---IVSAWGMTENGAVTLT-KLDDPDER 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 499 pGSAT--FPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimrTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYW 576
Cdd:PRK13295 364 -ASTTdgCPLPGVEVRVVDADGAPLPAGQIGRLQVRGC------SNFGGYLKRPQLNGTDADGWFDTGDLARIDADGYIR 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 577 ITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS-PKLTEELKKQireKIGPI 655
Cdd:PRK13295 437 ISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDfEEMVEFLKAQ---KVAKQ 513
|
570 580 590
....*....|....*....|....*....|..
gi 253970489 656 ATPDYIQNAPGLPKTRSGKIMRRVLRKIAQND 687
Cdd:PRK13295 514 YIPERLVVRDALPRTPSGKIQKFRLREMLRGE 545
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
119-683 |
4.11e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 118.53 E-value: 4.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 119 DKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhSIVFAG--FSS 196
Cdd:PRK03640 17 DRTAIEFEE------KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGA--VAVLLNtrLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 197 ESLCERILDSSCSLLITTDAFyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpd 276
Cdd:PRK03640 89 EELLWQLDDAEVKCLITDDDF----------------------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 277 vQGKLKEkskrvqpqiswnqGIDLWWHELMQEAGDECEP-EWCDAEDPLFILYTSGSTGKPKGVVHTVGGYmLYVATTFK 355
Cdd:PRK03640 110 -EAKLIP-------------GISVKFAELMNGPKEEAEIqEEFDLDEVATIMYTSGTTGKPKGVIQTYGNH-WWSAVGSA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 356 YVFDFHAEDVFWCTADIGWITGHSYVTygplangaTSVLFeGIPTY-------PDVNRLwsIVDKyKVTKFYTAPTAI-R 427
Cdd:PRK03640 175 LNLGLTEDDCWLAAVPIFHISGLSILM--------RSVIY-GMRVVlvekfdaEKINKL--LQTG-GVTIISVVSTMLqR 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 428 LLMKFGDEPVTKHSRASLqvLGtvGEPInPEAWLwyhrvvgaQRC-----PIVDTFWQTETGGHMLTPLPGATPMKPGSA 502
Cdd:PRK03640 243 LLERLGEGTYPSSFRCML--LG--GGPA-PKPLL--------EQCkekgiPVYQSYGMTETASQIVTLSPEDALTKLGSA 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 503 TFPFFGVAPAILNESGEELEGEAEGYLVfKQP--WPGIMRTVYGNHERFETTYFKkfpgyyvTGDGCQRDQDGYYWITGR 580
Cdd:PRK03640 310 GKPLFPCELKIEKDGVVVPPFEEGEIVV-KGPnvTKGYLNREDATRETFQDGWFK-------TGDIGYLDEEGFLYVLDR 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 581 IDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdGHTFSpklTEELKKQIREKIGPIATPDY 660
Cdd:PRK03640 382 RSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVT---EEELRHFCEEKLAKYKVPKR 456
|
570 580
....*....|....*....|...
gi 253970489 661 IQNAPGLPKTRSGKIMRRVLRKI 683
Cdd:PRK03640 457 FYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
137-681 |
2.16e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 116.44 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 137 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDA 216
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGDDA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 217 FYRGE-KLVNLKELADEAlqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqpqiswn 295
Cdd:PRK09088 104 VAAGRtDVEDLAAFIASA-------------------------------------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 296 qgidlwwhelmqEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTAD---- 371
Cdd:PRK09088 122 ------------DALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERN-LQQTAHNFGVLGRVDAHSSFLCDAPmfhi 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 372 IGWITGHSYVtygpLANGATSVLFEGIPTYPDVNRLWSIvdKYKVTKFYTAPtaiRLLMKFGDEPVTKHSR-ASLQVLGT 450
Cdd:PRK09088 189 IGLITSVRPV----LAVGGSILVSNGFEPKRTLGRLGDP--ALGITHYFCVP---QMAQAFRAQPGFDAAAlRHLTALFT 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 451 VGEPiNPE----AWLwyhrvvgAQRCPIVDTFWQTETGGHMLTPL-PGATPMKPGSATFPFFGVAPAILNESGEELEGEA 525
Cdd:PRK09088 260 GGAP-HAAedilGWL-------DDGIPMVDGFGMSEAGTVFGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGV 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 526 EGYLVFKQP--WPGIMRTVYGNHERFETTyfkkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 603
Cdd:PRK09088 332 PGELLLRGPnlSPGYWRRPQATARAFTGD------GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLAD 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 253970489 604 HEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:PRK09088 406 HPGIRECAVVGMADAQWGEVGYLAIVPADG---APLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
119-680 |
3.54e-27 |
|
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: 115.42 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 119 DKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 198
Cdd:cd05945 6 DRPAVVEGG------RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 199 LcERILD-SSCSLLITTDAfyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdv 277
Cdd:cd05945 80 I-REILDaAKPALLIADGD------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 278 qgklkekskrvqpqiswnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYv 357
Cdd:cd05945 98 --------------------------------------------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 358 FDFHAEDVFWCTA---------DIgwitghsyvtYGPLANGATSV------------LFEGIPTYPdvnrlwsivdkykV 416
Cdd:cd05945 133 FPLGPGDVFLNQApfsfdlsvmDL----------YPALASGATLVpvprdatadpkqLFRFLAEHG-------------I 189
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 417 TKFYTAPTAIRLLMkfGDEPVTKHSRASL-QVLgTVGEPI-NPEAWLWYHRvvgAQRCPIVDTFWQTET----GGHMLTP 490
Cdd:cd05945 190 TVWVSTPSFAAMCL--LSPTFTPESLPSLrHFL-FCGEVLpHKTARALQQR---FPDARIYNTYGPTEAtvavTYIEVTP 263
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 491 LPGATpMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQP--WPGIMRtVYGNHERFettyFKKFPGY--YVTGDG 566
Cdd:cd05945 264 EVLDG-YDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPsvSKGYLN-NPEKTAAA----FFPDEGQraYRTGDL 337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 567 CQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFspKLTEELKK 646
Cdd:cd05945 338 VRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEA--GLTKAIKA 415
|
570 580 590
....*....|....*....|....*....|....
gi 253970489 647 QIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:cd05945 416 ELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
321-681 |
4.16e-27 |
|
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: 115.23 E-value: 4.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 321 EDPLFILYTSGSTGKPKGVV--HTvggYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGpLANGATSVLFEGi 398
Cdd:cd05922 117 EDLALLLYTSGSTGSPKLVRlsHQ---NLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH-LLRGATLVLTND- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 399 pTYPDVNrLWSIVDKYKVTKFYTAPTAIRLL--MKFGDEPVtkhsrASLQVLGTVGEPInPEAWLWYHR--VVGAQrcpI 474
Cdd:cd05922 192 -GVLDDA-FWEDLREHGATGLAGVPSTYAMLtrLGFDPAKL-----PSLRYLTQAGGRL-PQETIARLRelLPGAQ---V 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 475 VDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTvYGNHERFETTYf 554
Cdd:cd05922 261 YVMYGQTEATRRMTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPN--VMKG-YWNDPPYRRKE- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 555 KKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVkGECLYCFVTLCDGH 634
Cdd:cd05922 337 GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKI 415
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 253970489 635 TFSPklteeLKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:cd05922 416 DPKD-----VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
322-682 |
5.08e-27 |
|
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: 114.79 E-value: 5.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 322 DPLFILYTSGSTGKPKGVVHTVGGYMlyvATTFKYV--FDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIp 399
Cdd:cd05903 94 AVALLLFTSGTTGEPKGVMHSHNTLS---ASIRQYAerLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 400 typDVNRLWSIVDKYKVTKFYTAPTAIRLLMK---FGDEPVtkhsrASLQVLGTVGEPINP----EAWlwyhRVVGAQRC 472
Cdd:cd05903 170 ---DPDKALALMREHGVTFMMGATPFLTDLLNaveEAGEPL-----SRLRTFVCGGATVPRslarRAA----ELLGAKVC 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 473 PIvdtFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpgimRTVYGNHERFETT 552
Cdd:cd05903 238 SA---YGSTECPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGP-----SVFLGYLDRPDLT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 553 YFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCD 632
Cdd:cd05903 310 ADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKS 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 253970489 633 GHTFS-PKLTEELKKQ--IREKIgpiatPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:cd05903 390 GALLTfDELVAYLDRQgvAKQYW-----PERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
135-680 |
6.84e-27 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 114.11 E-value: 6.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 135 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITT 214
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 215 dafyrgeklvnlKELADEALqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqpqisw 294
Cdd:cd05935 81 ------------SELDDLAL------------------------------------------------------------ 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 295 nqgidlwwhelmqeagdecepewcdaedplfILYTSGSTGKPKGVVHTvGGYMLYVATTFKYVFDFHAEDVFWCTADIGW 374
Cdd:cd05935 89 -------------------------------IPYTSGTTGLPKGCMHT-HFSAAANALQSAVWTGLTPSDVILACLPLFH 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 375 ITGHSYVTYGPLANGATSVLFegipTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfGDEPVTKHSRASLQVLGTVGEP 454
Cdd:cd05935 137 VTGFVGSLNTAVYVGGTYVLM----ARWDRETALELIEKYKVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAP 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 455 InPEAWLwyHRVVGAQRCPIVDTFWQTETgghmLTPLPGATPMKPGSATF--PFFGVAPAILNESGEELEGEAEG-YLVF 531
Cdd:cd05935 211 M-PPAVA--EKLLKLTGLRFVEGYGLTET----MSQTHTNPPLRPKLQCLgiP*FGVDARVIDIETGRELPPNEVgEIVV 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 532 KQPwpGIMRTvYGNHERFETTYFKKFPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAE 609
Cdd:cd05935 284 RGP--QIFKG-YWNRPEETEESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*E 360
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 253970489 610 AAVVGHPHPVKGECLYCFVTLCDGhtFSPKLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:cd05935 361 VCVISVPDERVGEEVKAFIVLRPE--YRGKVTEEdIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
326-682 |
7.10e-27 |
|
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: 113.60 E-value: 7.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 326 ILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGpLANGATSVLFEGIptypDVN 405
Cdd:cd05912 82 IMYTSGTTGKPKGVQQTFGNH-WWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDKF----DAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 406 RLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLqvLGtvGEPInPEAWLwyhrvvgaQRC-----PIVDTFWQ 480
Cdd:cd05912 156 QVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNLRCIL--LG--GGPA-PKPLL--------EQCkekgiPVYQSYGM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 481 TETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAegyLVFKQPwpGIMRTVYGNHER----FETTYFKk 556
Cdd:cd05912 223 TETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEVGE---ILLKGP--NVTKGYLNRPDAteesFENGWFK- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 557 fpgyyvTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdghtf 636
Cdd:cd05912 297 ------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVS------ 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 253970489 637 SPKLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:cd05912 365 ERPISeEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
107-682 |
8.02e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 115.48 E-value: 8.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 107 VLDRNVHEkkLGDKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGA- 185
Cdd:PRK05605 37 LYDNAVAR--FGDRPALDFFG------ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 186 --LHSIVFAGFSSESLCErilDSSCSLLITTDafyrgeKLVN-LKELADEAlqkcqekgfPVRCCIVVkhlgraelgmgD 262
Cdd:PRK05605 109 vvEHNPLYTAHELEHPFE---DHGARVAIVWD------KVAPtVERLRRTT---------PLETIVSV-----------N 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 263 STSQSPPIKRscpdVQGKL---KEKSKRVQPQISWNQGIDlwWHELMQEA----GDECEPEWCDAEDPLFILYTSGSTGK 335
Cdd:PRK05605 160 MIAAMPLLQR----LALRLpipALRKARAALTGPAPGTVP--WETLVDAAiggdGSDVSHPRPTPDDVALILYTSGTTGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 336 PKGVVHTVGGYMLYVATTFKYVFD--------------FHAEDVFWCtadigwitghsyVTYGPLAnGATSVLFegiPTy 401
Cdd:PRK05605 234 PKGAQLTHRNLFANAAQGKAWVPGlgdgpervlaalpmFHAYGLTLC------------LTLAVSI-GGELVLL---PA- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 402 PDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEP-VTKHS-RASLQvlgtvgepinpeawlwyhrvvGAQRCPiVDTF- 478
Cdd:PRK05605 297 PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERgVDLSGvRNAFS---------------------GAMALP-VSTVe 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 479 -WQTETGGHM-----LT---PLPGATPM----KPGSATFPFFGVAPAILNESGEELEGEAEGY--LVFKQPwpgimRTVY 543
Cdd:PRK05605 355 lWEKLTGGLLvegygLTetsPIIVGNPMsddrRPGYVGVPFPDTEVRIVDPEDPDETMPDGEEgeLLVRGP-----QVFK 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 544 GNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEC 623
Cdd:PRK05605 430 GYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEE 509
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 253970489 624 LYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:PRK05605 510 VVAAVVLEPGAALDP---EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
135-680 |
2.32e-26 |
|
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: 113.16 E-value: 2.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 135 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSLLIT 213
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRL-RYILeDAEPALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 214 TDAfyrgeklvnlkeLADealqkcqekgfPVRCCIVVKHLGRAELGMGDSTSQSPPikrscpdvqgklkekskrvqpqis 293
Cdd:cd12116 91 DDA------------LPD-----------RLPAGLPVLLLALAAAAAAPAAPRTPV------------------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 294 wnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGY------------------MLYVATtfk 355
Cdd:cd12116 124 -------------------------SPDDLAYVIYTSGSTGRPKGVVVSHRNLvnflhsmrerlglgpgdrLLAVTT--- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 356 YVFDFHAEDVFWctadigwitghsyvtygPLANGATSVLFEGIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDE 435
Cdd:cd12116 176 YAFDISLLELLL-----------------PLLAGARVVIAPRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAGWQ 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 436 PvtkhsRASLQVL-GtvGEPINPEawlwyhrvVGAQRCPIVDTFWQ----TETgghmlTPLPGATPMKPGSATFPffgVA 510
Cdd:cd12116 238 G-----RAGLTALcG--GEALPPD--------LAARLLSRVGSLWNlygpTET-----TIWSTAARVTAAAGPIP---IG 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 511 PAILNESGeelegeaegYLV--FKQPWP-GIMRTVY--------GNHERFETTyFKKF-------PG--YYVTGDGCQRD 570
Cdd:cd12116 295 RPLANTQV---------YVLdaALRPVPpGVPGELYiggdgvaqGYLGRPALT-AERFvpdpfagPGsrLYRTGDLVRRR 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 571 QDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEcLYCFVTLCDGHTFSpklTEELKKQIRE 650
Cdd:cd12116 365 ADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRR-LVAYVVLKAGAAPD---AAALRAHLRA 440
|
570 580 590
....*....|....*....|....*....|
gi 253970489 651 KIGPIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:cd12116 441 TLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
116-681 |
3.81e-26 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 112.85 E-value: 3.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 116 KLGDKVAFYWEgNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFS 195
Cdd:PRK08008 19 VYGHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 196 SESlCERILDSS-CSLLITTDAFYRgeklvnlkelADEALQkcQEKGFPVRCCIVvkhlgraelgmgdstsqsppikrsc 274
Cdd:PRK08008 98 REE-SAWILQNSqASLLVTSAQFYP----------MYRQIQ--QEDATPLRHICL------------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 275 pdvqgkLKEKSKRVQPQISWNQgidlwwhELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT-----VGGYmlY 349
Cdd:PRK08008 140 ------TRVALPADDGVSSFTQ-------LKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVIThynlrFAGY--Y 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 350 ----VATTFKYVF-----DFHAEdvFWCTADIGWITGhsyvtygplanGATSVLFEgipTYpDVNRLWSIVDKYKVTKFY 420
Cdd:PRK08008 205 sawqCALRDDDVYltvmpAFHID--CQCTAAMAAFSA-----------GATFVLLE---KY-SARAFWGQVCKYRATITE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 421 TAPTAIRLLMKfgdEPVTKHSRASL--QVLGTVgePINPEAWLWYHRVVGAQrcpIVDTFWQTETGGHMLTPLPGATPMK 498
Cdd:PRK08008 268 CIPMMIRTLMV---QPPSANDRQHClrEVMFYL--NLSDQEKDAFEERFGVR---LLTSYGMTETIVGIIGDRPGDKRRW 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 499 PgSATFPFFGVAPAILNESGEELEGEAEGYLVFK-QPWPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWI 577
Cdd:PRK08008 340 P-SIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKgVPGKTIFKEYYLDPK--ATAKVLEADGWLHTGDTGYVDEEGFFYF 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 578 TGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIAT 657
Cdd:PRK08008 417 VDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSE---EEFFAFCEQNMAKFKV 493
|
570 580
....*....|....*....|....
gi 253970489 658 PDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:PRK08008 494 PSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
322-682 |
3.22e-25 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 109.30 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 322 DPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFegipTY 401
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDA-WRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFL----PK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 402 PDVNRLWSIVDKYKVTKFYTAPTA-IRLL--MKFGDEPVTKHSRAS-----LQVLGTVGEPInP--EAWlwyhRVVGAQR 471
Cdd:cd05941 165 FDPKEVAISRLMPSITVFMGVPTIyTRLLqyYEAHFTDPQFARAAAaerlrLMVSGSAALPV-PtlEEW----EAITGHT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 472 cpIVDTFWQTETGGHMLTPLPGatPMKPGSATFPFFGVAPAIL-NESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFE 550
Cdd:cd05941 240 --LLERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVdEETGEPLPRGEVGEIQVRGP--SVFKEYWNKPEATK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 551 ttyfKKFP--GYYVTGDGCQRDQDGYYWITGRI-DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCF 627
Cdd:cd05941 314 ----EEFTddGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAV 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 253970489 628 VTLCDGHTfsPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:cd05941 390 VVLRAGAA--ALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
321-681 |
3.48e-25 |
|
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: 109.38 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 321 EDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHSYVtYGPLANGAtSVLFEGIPT 400
Cdd:cd17649 94 RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNFDGAHEQL-LPPLICGA-CVVLRPDEL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 401 YPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEpVTKHSRASLQVLGTVGEPINPE-AWLWyhrvvGAQRCPIVDTFW 479
Cdd:cd17649 171 WASADELAEMVRELGVTVLDLPPAYLQQLAEEADR-TGDGRPPSLRLYIFGGEALSPElLRRW-----LKAPVRLFNAYG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 480 QTETgghMLTPL--PGATPMKPGSATFP----FFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHERFETTY 553
Cdd:cd17649 245 PTEA---TVTPLvwKCEAGAARAGASMPigrpLGGRSAYILDADLNPVPVGVTGELYIGGE--GLAR---GYLGRPELTA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 554 fKKF-------PG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVkGECL 624
Cdd:cd17649 317 -ERFvpdpfgaPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQL 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 253970489 625 YCFVTLCDGHTfSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:cd17649 395 VAYVVLRAAAA-QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
302-681 |
5.92e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 109.73 E-value: 5.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 302 WHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGgyMLYV---ATTFKYvfDFHAEDVFWCTADIGwitgH 378
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHG--RLAFagrALTERF--GLTRDDVCYVSMPLF----H 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 379 S---YVTYGP-LANGATSVL---FEGIPTYPDVNRlwsivdkYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQV-LGT 450
Cdd:PRK13388 203 SnavMAGWAPaVASGAAVALpakFSASGFLDDVRR-------YGATYFNYVGKPLAYILATPERP--DDADNPLRVaFGN 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 451 VGEPINPEAWlwyhrvvgAQR--CPIVDTFWQTETGGhMLTPLPGaTPmkPGSATFPFFGVApaILNESGEelegeaegy 528
Cdd:PRK13388 274 EASPRDIAEF--------SRRfgCQVEDGYGSSEGAV-IVVREPG-TP--PGSIGRGAPGVA--IYNPETL--------- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 529 lvfkQPWPgimRTVYGNH-----------ERFETTYFKKFPGYYV---------------TGDGCQRDQDGYYWITGRID 582
Cdd:PRK13388 331 ----TECA---VARFDAHgallnadeaigELVNTAGAGFFEGYYNnpeataermrhgmywSGDLAYRDADGWIYFAGRTA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 583 DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP-KLTEELKKQirEKIGPIATPDYI 661
Cdd:PRK13388 404 DWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPdAFAAFLAAQ--PDLGTKAWPRYV 481
|
410 420
....*....|....*....|
gi 253970489 662 QNAPGLPKTRSGKIMRRVLR 681
Cdd:PRK13388 482 RIAADLPSTATNKVLKRELI 501
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
301-682 |
2.35e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 107.46 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 301 WWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVG-----GYMLyvATTFkyvfDFHAEDVFWCTADI--- 372
Cdd:PRK07867 132 WADELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRkvasaGVML--AQRF----GLGPDDVCYVSMPLfhs 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 373 -----GWITGhsyvtygpLANGATSVL---FEGIPTYPDVNRlwsivdkYKVTKF--------YTAPTAIR-------LL 429
Cdd:PRK07867 206 navmaGWAVA--------LAAGASIALrrkFSASGFLPDVRR-------YGATYAnyvgkplsYVLATPERpddadnpLR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 430 MKFGDEpvtkhsraslqvlgtvGEPINPEAWlwyhrvvgAQR--CPIVDTFWQTEtGGHMLTPLPGaTPmkPGSATFPFF 507
Cdd:PRK07867 271 IVYGNE----------------GAPGDIARF--------ARRfgCVVVDGFGSTE-GGVAITRTPD-TP--PGALGPLPP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 508 GVA-----------PAILNESGEELEGEAEGYLVFKQPwPGIMRTVYGNHErfeTTYFKKFPGYYVTGDGCQRDQDGYYW 576
Cdd:PRK07867 323 GVAivdpdtgtecpPAEDADGRLLNADEAIGELVNTAG-PGGFEGYYNDPE---ADAERMRGGVYWSGDLAYRDADGYAY 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 577 ITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP-KLTEELKKQirEKIGPI 655
Cdd:PRK07867 399 FAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPdAFAEFLAAQ--PDLGPK 476
|
410 420
....*....|....*....|....*..
gi 253970489 656 ATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:PRK07867 477 QWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
118-680 |
4.84e-24 |
|
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: 106.21 E-value: 4.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 118 GDKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSE 197
Cdd:cd17646 12 PDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 198 SLCERILDSSCSLLITT-DAFYRGEKLVNLKELADEALqkcqeKGFPVrccivvkhlgraelgmgdstsqSPPIKRSCPD 276
Cdd:cd17646 86 RLAYMLADAGPAVVLTTaDLAARLPAGGDVALLGDEAL-----AAPPA----------------------TPPLVPPRPD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 277 vqgklkekskrvqpqiswnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGG---YMLYVATT 353
Cdd:cd17646 139 ---------------------------------------------NLAYVIYTSGSTGRPKGVMVTHAGivnRLLWMQDE 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 354 FK------------YVFDFHAEDVFWctadigwitghsyvtygPLANGATSVLFE----GIPTYpdvnrLWSIVDKYKVT 417
Cdd:cd17646 174 YPlgpgdrvlqktpLSFDVSVWELFW-----------------PLVAGARLVVARpgghRDPAY-----LAALIREHGVT 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 418 KFYTAPTAIRLlmkFGDEPvTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTET----------GGHM 487
Cdd:cd17646 232 TCHFVPSMLRV---FLAEP-AAGSCASLRRVFCSGEALPPELAARFLALPGA---ELHNLYGPTEAaidvthwpvrGPAE 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 488 LTPLPGATPMkPGSATFpffgVAPAILNEsgeelegeaegylvfkQPwPGIMRTVY--------GNH-------ERFETT 552
Cdd:cd17646 305 TPSVPIGRPV-PNTRLY----VLDDALRP----------------VP-VGVPGELYlggvqlarGYLgrpaltaERFVPD 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 553 YFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCD 632
Cdd:cd17646 363 PFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAA 442
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 253970489 633 GHTfsPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:cd17646 443 GAA--GPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
115-680 |
4.93e-24 |
|
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: 106.13 E-value: 4.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 115 KKLGDKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGF 194
Cdd:cd12117 8 ARTPDAVAVVYGD------RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGA----AYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 195 SSESLCERIL----DSSCSLLITtdafyrgeklvnLKELADEAlqkcqekgfPVRCCIVVkhlgraeLGMGDSTSQSPPI 270
Cdd:cd12117 78 DPELPAERLAfmlaDAGAKVLLT------------DRSLAGRA---------GGLEVAVV-------IDEALDAGPAGNP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 271 KRSCpdvqgklkekskrvqpqiswnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYV 350
Cdd:cd12117 130 AVPV--------------------------------------------SPDDLAYVMYTSGSTGRPKGVAVTHRG-VVRL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 351 ATTFKYVfDFHAEDVFWCTADIGWiTGHSYVTYGPLANGATSVLFEGiPTYPDVNRLWSIVDKYKVTK-FYTAPTaIRLL 429
Cdd:cd12117 165 VKNTNYV-TLGPDDRVLQTSPLAF-DASTFEIWGALLNGARLVLAPK-GTLLDPDALGALIAEEGVTVlWLTAAL-FNQL 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 430 MKFGDEpvtkhSRASLQVLGTVGEPINPEawlWYHRVVgaQRCP---IVDTFWQTETGG----HMLTPL-PGATPMKPGS 501
Cdd:cd12117 241 ADEDPE-----CFAGLRELLTGGEVVSPP---HVRRVL--AACPglrLVNGYGPTENTTfttsHVVTELdEVAGSIPIGR 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 502 atfPFFGVAPAILNesgeelegeaegylVFKQPWP------------GIMRTvYGNH-----ERFETTYFkkFPG--YYV 562
Cdd:cd12117 311 ---PIANTRVYVLD--------------EDGRPVPpgvpgelyvggdGLALG-YLNRpaltaERFVADPF--GPGerLYR 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 563 TGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdGHTFSPkltE 642
Cdd:cd12117 371 TGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVA--EGALDA---A 445
|
570 580 590
....*....|....*....|....*....|....*...
gi 253970489 643 ELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:cd12117 446 ELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
112-681 |
5.91e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 106.31 E-value: 5.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 112 VHEKKLGDKVAFYWegnePGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVF 191
Cdd:PRK13391 5 IHAQTTPDKPAVIM----ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 192 AGFSSESLCERILDSSCSLLITTDAFYrgeklvnlkELADEALQKCQEkgfpVRCCIVVkhlgraelgmgDSTSQSPPIK 271
Cdd:PRK13391 81 SHLTPAEAAYIVDDSGARALITSAAKL---------DVARALLKQCPG----VRHRLVL-----------DGDGELEGFV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 272 RscpdvqgklkekskrvqpqiswnqgidlwwhelMQEAGDECePEWCDAEDPL--FILYTSGSTGKPKGVV----HTVGG 345
Cdd:PRK13391 137 G---------------------------------YAEAVAGL-PATPIADESLgtDMLYSSGTTGRPKGIKrplpEQPPD 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 346 YMLYVATTFKYVFDFHAEDVFWCTADIGwitgHSyvtyGPLA-------NGATSVLFEGIptypDVNRLWSIVDKYKVTK 418
Cdd:PRK13391 183 TPLPLTAFLQRLWGFRSDMVYLSPAPLY----HS----APQRavmlvirLGGTVIVMEHF----DAEQYLALIEEYGVTH 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 419 FYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPE------AWlWyhrvvgaqrCPIVDTFWQTETGGhmltplp 492
Cdd:PRK13391 251 TQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQvkeqmiDW-W---------GPIIHEYYAATEGL------- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 493 GATPM-------KPGSATFPFFGVaPAILNESGeelegeaegylvfkQPWP-GIMRTVYGNHER-FEttYFK-------- 555
Cdd:PRK13391 314 GFTACdseewlaHPGTVGRAMFGD-LHILDDDG--------------AELPpGEPGTIWFEGGRpFE--YLNdpaktaea 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 556 --KFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDG 633
Cdd:PRK13391 377 rhPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDG 456
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 253970489 634 HTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:PRK13391 457 VDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
119-682 |
6.63e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 106.40 E-value: 6.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 119 DKVAFYWEGNEpgettqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 198
Cdd:PRK07786 32 DAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 199 LCERILDSSCSLLITTDAfyrgekLVNLKELADEALqkcqekgfPVRCCIVVkhlgraelgMGDSTsqsppikrscpdvq 278
Cdd:PRK07786 106 IAFLVSDCGAHVVVTEAA------LAPVATAVRDIV--------PLLSTVVV---------AGGSS-------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 279 gklkekskrvqpqiswnQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTvggYMLYVATTFKYVF 358
Cdd:PRK07786 149 -----------------DDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLT---HANLTGQAMTCLR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 359 DFHA---EDVFWCTADIGWITGhsyvtygpLANGATSVLFeGIPT--YP----DVNRLWSIVDKYKVTKFYTAPTAIRLL 429
Cdd:PRK07786 209 TNGAdinSDVGFVGVPLFHIAG--------IGSMLPGLLL-GAPTviYPlgafDPGQLLDVLEAEKVTGIFLVPAQWQAV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 430 MkfgDEPVTKHSRASLQVLGTVGEPiNPEAWL--WYHRVVGAQrcpIVDTFWQTEtgghmLTPLpgaTPM--------KP 499
Cdd:PRK07786 280 C---AEQQARPRDLALRVLSWGAAP-ASDTLLrqMAATFPEAQ---ILAAFGQTE-----MSPV---TCMllgedairKL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 500 GSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGN----HERFETtyfkkfpGYYVTGDGCQRDQDGYY 575
Cdd:PRK07786 345 GSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAP--TLMSGYWNNpeatAEAFAG-------GWFHSGDLVRQDEEGYV 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 576 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLT-EELKKQIREKIGP 654
Cdd:PRK07786 416 WVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND---DAALTlEDLAEFLTDRLAR 492
|
570 580
....*....|....*....|....*...
gi 253970489 655 IATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:PRK07786 493 YKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
131-614 |
8.07e-24 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 104.98 E-value: 8.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESlCERIL-DSSCS 209
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQ-IAYILnDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 210 LLITTDAfyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvq 289
Cdd:cd05907 80 ALFVEDP------------------------------------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 290 pqiswnqgidlwwhelmqeagdecepewcdaEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVfDFHAEDVFWCT 369
Cdd:cd05907 87 -------------------------------DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERL-PATEGDRHLSF 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 370 ADIGWITGHSYVTYGPLANGATSVLFEGI-----------PTY-PDVNRLWSIVdkYKVTKFYTAPTAIRLLMKFgdepv 437
Cdd:cd05907 135 LPLAHVFERRAGLYVPLLAGARIYFASSAetllddlsevrPTVfLAVPRVWEKV--YAAIKVKAVPGLKRKLFDL----- 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 438 tkHSRASLQVLGTVGEPINPEAWLWYHrvvgAQRCPIVDTFWQTETGG-HMLTPLPGATPMKPGSATFPF-FGVAPA--I 513
Cdd:cd05907 208 --AVGGRLRFAASGGAPLPAELLHFFR----ALGIPVYEGYGLTETSAvVTLNPPGDNRIGTVGKPLPGVeVRIADDgeI 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 514 LnesgeelegeaegylvFKQpwPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDML-NVSGHLL 592
Cdd:cd05907 282 L----------------VRG--PNVMLGYYKNPE--ATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNI 341
|
490 500
....*....|....*....|..
gi 253970489 593 STAEVESALVEHEAVAEAAVVG 614
Cdd:cd05907 342 SPEPIENALKASPLISQAVVIG 363
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
130-680 |
1.04e-23 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 105.28 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 130 PGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERI-LDSSC 208
Cdd:cd05923 23 PARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIeRGEMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 209 SLLITTDAF-YRGEKLVNLKELAdealqkcqekgfpvrccivvkhLGrAELGMGDSTSQSPPIkrscpdvqgklkekskr 287
Cdd:cd05923 103 AAVIAVDAQvMDAIFQSGVRVLA----------------------LS-DLVGLGEPESAGPLI----------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 288 vqpqiswnqgidlwwhelmqeagdecEPEWCDAEDPLFILYTSGSTGKPKGVV---HTVGGYMLYVATTFKYVFDFHaeD 364
Cdd:cd05923 143 --------------------------EDPPREPEQPAFVFYTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRHGRH--N 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 365 VFWCTADIGWITGHSYVTYGPLANGATSVLfegiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfGDEPVTKHSRAS 444
Cdd:cd05923 195 VVLGLMPLYHVIGFFAVLVAALALDGTYVV----VEEFDPADALKLIEQERVTSLFATPTHLDALA--AAAEFAGLKLSS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 445 LQVLGTVGEPInPEAWLwyHRVVGAQRCPIVDTFWQTETGGHMLTPLPGA-TPMKPGsatfpFFG---VAPaILNESGEE 520
Cdd:cd05923 269 LRHVTFAGATM-PDAVL--ERVNQHLPGEKVNIYGTTEAMNSLYMRDARTgTEMRPG-----FFSevrIVR-IGGSPDEA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 521 LEGEAEGYLVFKQP----WPGIMRtvygnheRFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAE 596
Cdd:cd05923 340 LANGEEGELIVAAAadaaFTGYLN-------QPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSE 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 597 VESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfspKLTEELKKQ--IREKIGPIATPDYIQNAPGLPKTRSGK 674
Cdd:cd05923 413 IERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-----TLSADELDQfcRASELADFKRPRRYFFLDELPKNAMNK 487
|
....*.
gi 253970489 675 IMRRVL 680
Cdd:cd05923 488 VLRRQL 493
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
137-684 |
1.84e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 105.24 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 137 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDA 216
Cdd:PRK12583 47 TWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 217 FYRGEKLVNLKELADEalqkcqekgfpvrccivVKHLGRAELgmgdstsqsppikrSCPdvqgKLKEKSKRVQPQISWNQ 296
Cdd:PRK12583 127 FKTSDYHAMLQELLPG-----------------LAEGQPGAL--------------ACE----RLPELRGVVSLAPAPPP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 297 GIdLWWHELmQEAGDECEPE-------WCDAEDPLFILYTSGSTGKPKGVV---HTV--GGYMLYVAttfkyvFDFHAED 364
Cdd:PRK12583 172 GF-LAWHEL-QARGETVSREalaerqaSLDRDDPINIQYTSGTTGFPKGATlshHNIlnNGYFVAES------LGLTEHD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 365 VFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPTYPDVNrlWSIVDKYKVTKFYTAPTairLLMKFGDEPvtKHSRAS 444
Cdd:PRK12583 244 RLCVPVPLYHCFGMVLANLGCMTVGAC-LVYPNEAFDPLAT--LQAVEEERCTALYGVPT---MFIAELDHP--QRGNFD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 445 LQVLGT---VGEPINPEAwlwYHRVVGAQRCP-IVDTFWQTETGGhmLTPLPGAT-PMKPGSATF----PFFGVApaILN 515
Cdd:PRK12583 316 LSSLRTgimAGAPCPIEV---MRRVMDEMHMAeVQIAYGMTETSP--VSLQTTAAdDLERRVETVgrtqPHLEVK--VVD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 516 ESGEELEGEAEGYLVFKqpwpG--IMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLS 593
Cdd:PRK12583 389 PDGATVPRGEIGELCTR----GysVMKGYWNNPEATAESIDED--GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIY 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 594 TAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 673
Cdd:PRK12583 463 PREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAAS---EEELREFCKARIAHFKVPRYFRFVDEFPMTVTG 539
|
570
....*....|.
gi 253970489 674 KIMRRVLRKIA 684
Cdd:PRK12583 540 KVQKFRMREIS 550
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
304-682 |
3.98e-23 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 103.53 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 304 ELMQEAGDECEPEWCDAE-DPLFILYTSGSTGKPKGVVHTVGGYMLyVATTFKYVFDFHAEDVFWCTADI----GWItgh 378
Cdd:cd12118 115 DLLAEGDPDFEWIPPADEwDPIALNYTSGTTGRPKGVVYHHRGAYL-NALANILEWEMKQHPVYLWTLPMfhcnGWC--- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 379 syVTYGPLANGATSVLFEGIpTYPDVnrlWSIVDKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLgTVGEPiNPE 458
Cdd:cd12118 191 --FPWTVAAVGGTNVCLRKV-DAKAI---YDLIEKHKVTHFCGAPTVLNMLAN-APPSDARPLPHRVHVM-TAGAP-PPA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 459 AWLWYHRVVGAQrcpIVDTFWQTETGGhmltplPGAT-PMKPGSATFPffGVAPAILNESGEELEGEAEGYLVFKQ---- 533
Cdd:cd12118 262 AVLAKMEELGFD---VTHVYGLTETYG------PATVcAWKPEWDELP--TEERARLKARQGVRYVGLEEVDVLDPetmk 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 534 --PWPG------------IMRTVYGNHERFETTyFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVES 599
Cdd:cd12118 331 pvPRDGktigeivfrgniVMKGYLKNPEATAEA-FRG--GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEG 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 600 ALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRV 679
Cdd:cd12118 408 VLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTE---EEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFV 483
|
...
gi 253970489 680 LRK 682
Cdd:cd12118 484 LRD 486
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
131-681 |
7.20e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 102.67 E-value: 7.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 210
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 211 LITTDAfyrgeklvnLKELADEALQKCQekgfpvrccivvkhLGRAELGMGDSTsqsPPIKRSCPDvqgklkekskrvqp 290
Cdd:PRK08276 87 LIVSAA---------LADTAAELAAELP--------------AGVPLLLVVAGP---VPGFRSYEE-------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 291 qiswnqgidlwwhELMQEAGDECEPEWCDAEdplfILYTSGSTGKPKGV--------VHTVGGYMLYVATTFkyvFDFHA 362
Cdd:PRK08276 127 -------------ALAAQPDTPIADETAGAD----MLYSSGTTGRPKGIkrplpgldPDEAPGMMLALLGFG---MYGGP 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 363 EDVFWCTADIGwitgHSYVT-YG--PLANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTK 439
Cdd:PRK08276 187 DSVYLSPAPLY----HTAPLrFGmsALALGGTVVVMEKF----DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRAR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 440 HSRASLQVLGTVGEPINPE------AWlWyhrvvGaqrcPIVD-TFWQTETGGHMLtplpgATP----MKPGSATFPFFG 508
Cdd:PRK08276 259 YDVSSLRVAIHAAAPCPVEvkramiDW-W-----G----PIIHeYYASSEGGGVTV-----ITSedwlAHPGSVGKAVLG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 509 VApAILNESGEELEGEAEGYLVFKQPWPGImrTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLnVS 588
Cdd:PRK08276 324 EV-RILDEDGNELPPGEIGTVYFEMDGYPF--EYHNDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI-IS 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 589 GHL-LSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGL 667
Cdd:PRK08276 398 GGVnIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDEL 477
|
570
....*....|....
gi 253970489 668 PKTRSGKIMRRVLR 681
Cdd:PRK08276 478 PRTPTGKLYKRRLR 491
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
132-680 |
1.07e-22 |
|
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: 101.63 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 211
Cdd:cd12115 21 GDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 212 ITtdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqpq 291
Cdd:cd12115 101 LT------------------------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 292 iswnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVV---HTVGGYMLYVATTF------------KY 356
Cdd:cd12115 103 ---------------------------DPDDLAYVIYTSGSTGRPKGVAiehRNAAAFLQWAAAAFsaeelagvlastSI 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 357 VFDFHAEDVFwctadigwitghsyvtyGPLANGATSVLFEGIPTYPDVNRLwsivdkYKVTKFYTAPTAIRLLMKFGDEP 436
Cdd:cd12115 156 CFDLSVFELF-----------------GPLATGGKVVLADNVLALPDLPAA------AEVTLINTVPSAAAELLRHDALP 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 437 vtkhsrASLQVLGTVGEPINPEAWLWYHRVVGAQRC-----PIVDTFWQTetgGHMLTPLPGATPmkpgSATFPFFGVAP 511
Cdd:cd12115 213 ------ASVRVVNLAGEPLPRDLVQRLYARLQVERVvnlygPSEDTTYST---VAPVPPGASGEV----SIGRPLANTQA 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 512 AILNEsgeelegeaegylvFKQPWP------------GIMRTVYGN----HERFETTYFkkFPG--YYVTGDGCQRDQDG 573
Cdd:cd12115 280 YVLDR--------------ALQPVPlgvpgelyiggaGVARGYLGRpgltAERFLPDPF--GPGarLYRTGDLVRWRPDG 343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 574 YYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIG 653
Cdd:cd12115 344 LLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPG---AAGLVEDLRRHLGTRLP 420
|
570 580
....*....|....*....|....*..
gi 253970489 654 PIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:cd12115 421 AYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
107-615 |
1.86e-22 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 102.10 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 107 VLDRNVheKKLGDKVAFYWEGNepGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAL 186
Cdd:COG1022 16 LLRRRA--ARFPDRVALREKED--GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 187 HSIVFAGfSSESLCERIL-DSSCSLLITTDAfyrgEKLVNLKELADE--ALQKcqekgfpvrccIVVkhlgraelgmgds 263
Cdd:COG1022 92 TVPIYPT-SSAEEVAYILnDSGAKVLFVEDQ----EQLDKLLEVRDElpSLRH-----------IVV------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 264 tsqsppikrscpdvqgkLKEKSKRVQPQIswnqgidLWWHELMQEAGDECEPEW-------CDAEDPLFILYTSGSTGKP 336
Cdd:COG1022 143 -----------------LDPRGLRDDPRL-------LSLDELLALGREVADPAElearraaVKPDDLATIIYTSGTTGRP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 337 KGVVHTVGGyMLYVATTFKYVFDFHAEDVF-----WCtadigWITGHSyVTYGPLANGATSVLFEGIPTYPD-------- 403
Cdd:COG1022 199 KGVMLTHRN-LLSNARALLERLPLGPGDRTlsflpLA-----HVFERT-VSYYALAAGATVAFAESPDTLAEdlrevkpt 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 404 ----VNRLW-SIVDKYkVTKFYTAPTAIRLL----MKFGdepvTKHSRASLQvlgtvGEPINPEAWLWY---HRVVGAQr 471
Cdd:COG1022 272 fmlaVPRVWeKVYAGI-QAKAEEAGGLKRKLfrwaLAVG----RRYARARLA-----GKSPSLLLRLKHalaDKLVFSK- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 472 cpivdtfWQTETGGHMLTPLPGATPMKPgsATFPFF---GV------------APAILNESGEelegeaegylvFK---- 532
Cdd:COG1022 341 -------LREALGGRLRFAVSGGAALGP--ELARFFralGIpvlegygltetsPVITVNRPGD-----------NRigtv 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 533 -QPWPG-----------------IMRTVYGNHErfETTyfKKFP--GYYVTGD-GcQRDQDGYYWITGRIDDMLNVS-GH 590
Cdd:COG1022 401 gPPLPGvevkiaedgeilvrgpnVMKGYYKNPE--ATA--EAFDadGWLHTGDiG-ELDEDGFLRITGRKKDLIVTSgGK 475
|
570 580
....*....|....*....|....*
gi 253970489 591 LLSTAEVESALVEHEAVAEAAVVGH 615
Cdd:COG1022 476 NVAPQPIENALKASPLIEQAVVVGD 500
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
132-618 |
2.46e-22 |
|
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: 103.01 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsivfA------GFSSESLcERIL- 204
Cdd:COG1020 498 GDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGA------AyvpldpAYPAERL-AYMLe 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 205 DSSCSLLITTDAFyrgeklvnLKELADEALQkcqekgfpvrcCIVVKHLGRAElgmgdsTSQSPPIKRSCPDvqgklkek 284
Cdd:COG1020 571 DAGARLVLTQSAL--------AARLPELGVP-----------VLALDALALAA------EPATNPPVPVTPD-------- 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 285 skrvqpqiswnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGG---YMLYVATTFK------ 355
Cdd:COG1020 618 -------------------------------------DLAYVIYTSGSTGRPKGVMVEHRAlvnLLAWMQRRYGlgpgdr 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 356 ------YVFDFHAEDVFWctadigwitghsyvtygPLANGATSVLF--EGIptyPDVNRLWSIVDKYKVTKFYTAPTAIR 427
Cdd:COG1020 661 vlqfasLSFDASVWEIFG-----------------ALLSGATLVLAppEAR---RDPAALAELLARHRVTVLNLTPSLLR 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 428 LLMKFGDEPVtkhsrASLQVLGTVGEPINPEAWLWYHRVVGAQR---------CPIVDTFWQTETGGHMLTPLP-GaTPM 497
Cdd:COG1020 721 ALLDAAPEAL-----PSLRLVLVGGEALPPELVRRWRARLPGARlvnlygpteTTVDSTYYEVTPPDADGGSVPiG-RPI 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 498 kPGSATFpffgvapaILNEsgeelegeaegylvFKQPWP-GIM-------------------RTVygnhERFETTYFkKF 557
Cdd:COG1020 795 -ANTRVY--------VLDA--------------HLQPVPvGVPgelyiggaglargylnrpeLTA----ERFVADPF-GF 846
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 253970489 558 PG--YYVTGDGCQRDQDG---YywiTGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP 618
Cdd:COG1020 847 PGarLYRTGDLARWLPDGnleF---LGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDA 909
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
131-685 |
3.61e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 100.97 E-value: 3.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 210
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 211 LITTDAFyRGEKLVN-LKELADEALQkcqekgfPVRCCIVVkhlgraelgmgDSTSQSPPIKRSCpdvqgklkekskrvq 289
Cdd:PRK06164 111 LVVWPGF-KGIDFAAiLAAVPPDALP-------PLRAIAVV-----------DDAADATPAPAPG--------------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 290 pqiSWNQGIDLWWHELMQEAGDECEPEwcdaeDPLFILYT-SGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWC 368
Cdd:PRK06164 157 ---ARVQLFALPDPAPPAAAGERAADP-----DAGALLFTtSGTTSGPKLVLHRQAT-LLRHARAIARAYGYDPGAVLLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 369 TADIGWITGHSYVTyGPLANGATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtkHSRASLQVL 448
Cdd:PRK06164 228 ALPFCGVFGFSTLL-GALAGGAPLVC---EPVF-DAARTARALRRHRVTHTFGNDEMLRRILDTAGER---ADFPSARLF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 449 GTVGepINPeAWLWYHRVVGAQRCPIVDTFWQTE-----TGGHMLTP-----LPGATPMKPGSATFPFFGVAPAILNESG 518
Cdd:PRK06164 300 GFAS--FAP-ALGELAALARARGVPLTGLYGSSEvqalvALQPATDPvsvriEGGGRPASPEARVRARDPQDGALLPDGE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 519 EELEGEAEgylvfkqpwPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVE 598
Cdd:PRK06164 377 SGEIEIRA---------PSLMRGYLDNPD--ATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 599 SALVEHEAVAEAAVVGHPHPVKGEClYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSG---KI 675
Cdd:PRK06164 446 HALEALPGVAAAQVVGATRDGKTVP-VAFVIPTDGASPDE---AGLMAACREALAGFKVPARVQVVEAFPVTESAngaKI 521
|
570
....*....|
gi 253970489 676 MRRVLRKIAQ 685
Cdd:PRK06164 522 QKHRLREMAQ 531
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
134-680 |
1.88e-21 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 98.17 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 134 TQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALhsIVFAGFSseslcerildsscsllit 213
Cdd:cd05920 39 RRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLALPS------------------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 214 tdafYRGEKLVNLKELADEALqkcqekgfpvrcCIVvkhlgraelgmgdstsqsppikrscPDVQGklkekskRVQPQis 293
Cdd:cd05920 99 ----HRRSELSAFCAHAEAVA------------YIV-------------------------PDRHA-------GFDHR-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 294 wnqgidlwwhELMQEAGDECEpewcdaeDPLFILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWCTADIG 373
Cdd:cd05920 129 ----------ALARELAESIP-------EVALFLLSGGTTGTPKLIPRTHNDY-AYNVRASAEVCGLDQDTVYLAVLPAA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 374 witgHSYVTYGP-----LANGATSVLfegiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPvtKHSRASLQVL 448
Cdd:cd05920 191 ----HNFPLACPgvlgtLLAGGRVVL----APDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASR--RADLSSLRLL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 449 GTVGEPINPEAwlwYHRVVGAQRCPIVDTFWQTE-----------------TGGHMLTPL-------PGATPMKPGSAtf 504
Cdd:cd05920 261 QVGGARLSPAL---ARRVPPVLGCTLQQVFGMAEgllnytrlddpdeviihTQGRPMSPDdeirvvdEEGNPVPPGEE-- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 505 pffgvapailnesgeelegeaeGYLVFKQPWP--GIMRTVYGNHERFETTyfkkfpGYYVTGDGCQRDQDGYYWITGRID 582
Cdd:cd05920 336 ----------------------GELLTRGPYTirGYYRAPEHNARAFTPD------GFYRTGDLVRRTPDGYLVVEGRIK 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 583 DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfSPKLTEELKKQIREKigPIAT---PD 659
Cdd:cd05920 388 DQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD----PPPSAAQLRRFLRER--GLAAyklPD 461
|
570 580
....*....|....*....|.
gi 253970489 660 YIQNAPGLPKTRSGKIMRRVL 680
Cdd:cd05920 462 RIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
131-683 |
4.70e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 97.24 E-value: 4.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 131 GETTQITYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALhSIVFagfsseslcerildsscs 209
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECI-AVPL------------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 210 llittdafyrgeklvNLKELADEALQKCQEKGFPVRCCivvkhlgraelgmgdstsqSPPIKRSCPDVQGKLKekskrVQ 289
Cdd:PRK06839 84 ---------------NIRLTENELIFQLKDSGTTVLFV-------------------EKTFQNMALSMQKVSY-----VQ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 290 PQIsWNQGIDlwwhELMQEAGDECEPEwcDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCT 369
Cdd:PRK06839 125 RVI-SITSLK----EIEDRKIDNFVEK--NESASFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 370 ADIGWITGHSYVTYGPLANGATSVlfegIPTYPDVNRLWSIVDKYKVTKFYTAPT---AIRLLMKFgdepvTKHSRASLQ 446
Cdd:PRK06839 197 LPLFHIGGIGLFAFPTLFAGGVII----VPRKFEPTKALSMIEKHKVTVVMGVPTihqALINCSKF-----ETTNLQSVR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 447 VLGTVGEPInPEAWLwyhRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAE 526
Cdd:PRK06839 268 WFYNGGAPC-PEELM---REFIDRGFLFGQGFGMTETSPTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 527 GYLVFKQPwpGIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEA 606
Cdd:PRK06839 344 GELLIRGP--NVMKEYWNRPDATEETIQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSD 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 253970489 607 VAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 683
Cdd:PRK06839 419 VYEVAVVGRQHVKWGEIPIAFIVKKSSSVLI---EKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
117-683 |
6.76e-21 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 97.14 E-value: 6.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 117 LGDKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSS 196
Cdd:PRK06155 34 YPDRPLLVFGG------TRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 197 ESLcERILDSSCSLLITTDAFYRgeklvnlkeladEALQKCQEKGFPVRCCIVVKHLGRAELGMGDSTSQSPPIKRSCPD 276
Cdd:PRK06155 108 PQL-EHILRNSGARLLVVEAALL------------AALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPLPPLDAPAPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 277 VQgklkekskrVQPQiswnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTvggymlyvattfky 356
Cdd:PRK06155 175 AA---------VQPG------------------------------DTAAILYTSGTTGPSKGVCCP-------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 357 vfdfHAEDVFW---CTADIGWITGHSYVTYGPL-------------ANGATSVLFEGIptypDVNRLWSIVDKYKVTKFY 420
Cdd:PRK06155 202 ----HAQFYWWgrnSAEDLEIGADDVLYTTLPLfhtnalnaffqalLAGATYVLEPRF----SASGFWPAVRRHGATVTY 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 421 TAPTAIRLLMKfgdEPVTKHSRAS-LQVLGTVGEPINpeawlwYHRVVGAqRC--PIVDTFWQTETGGHMLTPLPGAtpm 497
Cdd:PRK06155 274 LLGAMVSILLS---QPARESDRAHrVRVALGPGVPAA------LHAAFRE-RFgvDLLDGYGSTETNFVIAVTHGSQ--- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 498 KPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNH-----ERFETTYFKkfpgyyvTGDGCQRDQD 572
Cdd:PRK06155 341 RPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEPFAFATGYFGMpektvEAWRNLWFH-------TGDRVVRDAD 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 573 GYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKI 652
Cdd:PRK06155 414 GWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEP---VALVRHCEPRL 490
|
570 580 590
....*....|....*....|....*....|.
gi 253970489 653 GPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 683
Cdd:PRK06155 491 AYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
322-684 |
3.36e-20 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 92.39 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 322 DPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTY 401
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAN-LLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 402 PDVNRlwsivdkYKVTKFYTAPTAIRLLMkfgDEPVTKHSRASLQVLGTVGEPINPEAwlwyHRVVGAQRCPIVDTFWQT 481
Cdd:cd17630 80 EDLAP-------PGVTHVSLVPTQLQRLL---DSGQGPAALKSLRAVLLGGAPIPPEL----LERAADRGIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 482 ETGGHMLTPLPGATpmKPGSATFPFFGVAPAILNESGEelegeaegylvfkqpWPGIMRTVYGNHERFETTYFKKfPGYY 561
Cdd:cd17630 146 ETASQVATKRPDGF--GRGGVGVLLPGRELRIVEDGEI---------------WVGGASLAMGYLRGQLVPEFNE-DGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 562 VTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfspklT 641
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPAD-----P 282
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 253970489 642 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 684
Cdd:cd17630 283 AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
322-677 |
3.67e-20 |
|
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: 92.08 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 322 DPLFILYTSGSTGKPKGVVHTVGGYM-LYVATtfKYVFDFHAEDvfwctadigwitghSYVTYGPLA-----NGATSVLF 395
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIeSFVCN--EDLFNISGED--------------AILAPGPLShslflYGAISALY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 396 EG----IPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFgDEPVTKhsrasLQVLGTVGEPINPEAwlwyHRVVGAQ- 470
Cdd:cd17633 65 LGgtfiGQRKFNPKSWIRKINQYNATVIYLVPTMLQALART-LEPESK-----IKSIFSSGQKLFEST----KKKLKNIf 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 471 -RCPIVDTFWQTETGghMLTPLPGATPMKPGSATFPFFGVAPAILNESGeelegeaegylvfkqpwpGIMRTVYGNHERF 549
Cdd:cd17633 135 pKANLIEFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADG------------------GEIGKIFVKSEMV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 550 ETTY----FKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEcLY 625
Cdd:cd17633 195 FSGYvrggFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE-IA 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 253970489 626 CFVTLCDGHTFsPKLTEELKKQI-REKIgpiatPDYIQNAPGLPKTRSGKIMR 677
Cdd:cd17633 274 VALYSGDKLTY-KQLKRFLKQKLsRYEI-----PKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
132-683 |
5.67e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 94.22 E-value: 5.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 211
Cdd:PRK07788 71 ERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKAL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 212 ITTDAFyrgeklvnlkelaDEALQKCQEKgfpvrccivvkhLGRAeLGMGDSTSQSPPIKRSCPDVQGKLKEKSKRVQPQ 291
Cdd:PRK07788 151 VYDDEF-------------TDLLSALPPD------------LGRL-RAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLPK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 292 ISWNQGIdlwwhelmqeagdecepewcdaedplfILYTSGSTGKPKGVVH-------TVGGYMLYVAttfkyvfdFHAED 364
Cdd:PRK07788 205 PPKPGGI---------------------------VILTSGTTGTPKGAPRpepsplaPLAGLLSRVP--------FRAGE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 365 VFWCTADIGWITGHSYVTYGpLANGATSVL---FEGIPTYPDVnrlwsivDKYKVTKFYTAPTAIRLLMKFGDEPVTKHS 441
Cdd:PRK07788 250 TTLLPAPMFHATGWAHLTLA-MALGSTVVLrrrFDPEATLEDI-------AKHKATALVVVPVMLSRILDLGPEVLAKYD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 442 RASLQVLGTVGEPINPEAWLWYHRVVGaqrcPIVDTFW-QTETGGHMLtplpgATP----MKPGSATFPFFGVAPAILNE 516
Cdd:PRK07788 322 TSSLKIIFVSGSALSPELATRALEAFG----PVLYNLYgSTEVAFATI-----ATPedlaEAPGTVGRPPKGVTVKILDE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 517 SGeelegeaegylvfkQPWPG--IMRTVYGNHERFETtYF-----KKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSG 589
Cdd:PRK07788 393 NG--------------NEVPRgvVGRIFVGNGFPFEG-YTdgrdkQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 590 HLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPK 669
Cdd:PRK07788 458 ENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDE---DAIKDYVRDNLARYKVPRDVVFLDELPR 534
|
570
....*....|....
gi 253970489 670 TRSGKIMRRVLRKI 683
Cdd:PRK07788 535 NPTGKVLKRELREM 548
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
326-681 |
9.18e-20 |
|
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: 92.83 E-value: 9.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 326 ILYTSGSTGKPKGVVHTVGGYMLYVAT--TFKYVFDFHAEDVFWCTADIGWITGHSyVTYGPLANGATSVLFEGIptypD 403
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTlmAAALGFGPGADSVYLSPAPLYHAAPFR-WSMTALFMGGTLVLMEKF----D 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 404 VNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINP---EAWL-WYHrvvgaqrcPIVDTFW 479
Cdd:cd05929 205 PEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPPwvkEQWIdWGG--------PIIWEYY 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 480 Q-TETGGhmLTPLPGATPMK-PGSATFPFFGVApAILNESGEelegeaegylvfKQPwPGIMRTVY--GN-----HERFE 550
Cdd:cd05929 277 GgTEGQG--LTIINGEEWLThPGSVGRAVLGKV-HILDEDGN------------EVP-PGEIGEVYfaNGpgfeyTNDPE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 551 TTYFKKFPGYYVT-GDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVT 629
Cdd:cd05929 341 KTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQ 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 253970489 630 LCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:cd05929 421 PAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
537-681 |
1.67e-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.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 90.41 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 537 GIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHP 616
Cdd:cd05917 210 SVMKGYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVP 287
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 253970489 617 HPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:cd05917 288 DERYGEEVCAWIRLKEGAELTE---EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
137-682 |
2.68e-19 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 92.12 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 137 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALhsivfagfsseslcerildsSCSLLITtda 216
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAV--------------------SVPLLPS--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 217 fYRGEKLVnlkeladEALQKCQEKGFpvrCCIVVKHLGRAElgmgdstSQSPPIKRSCPDVQG-KLKEKSKRVQPQISWN 295
Cdd:PRK06087 108 -WREAELV-------WVLNKCQAKMF---FAPTLFKQTRPV-------DLILPLQNQLPQLQQiVGVDKLAPATSSLSLS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 296 QGIDLwwHELMQEagdecePEWCDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWI 375
Cdd:PRK06087 170 QIIAD--YEPLTT------AITTHGDELAAVLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 376 TGHSYVTYGPLANGATSVLFEGIPtyPDvnRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSraSLQVLGTVGEPI 455
Cdd:PRK06087 241 TGFLHGVTAPFLIGARSVLLDIFT--PD--ACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLS--ALRFFLCGGTTI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 456 nPEawlwyhRVVgaQRC-----PIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLV 530
Cdd:PRK06087 315 -PK------KVA--RECqqrgiKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 531 FKQPwpGIMRTVYGNHERfeTTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEA 610
Cdd:PRK06087 386 SRGP--NVFMGYLDEPEL--TARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDA 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 253970489 611 AVVGHPHPVKGECLYCFVTLcDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:PRK06087 462 CVVAMPDERLGERSCAYVVL-KAPHHSLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
131-680 |
2.80e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.48 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 131 GETTqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 210
Cdd:PRK12316 533 GEET-LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 211 LITTDAFyrGEKLvnlkeladealqkcqekgfPVRCCIVVKHLGRAELGMgDSTSQSPPIKRSCPdvqgklkekskrvqp 290
Cdd:PRK12316 612 LLSQSHL--GRKL-------------------PLAAGVQVLDLDRPAAWL-EGYSEENPGTELNP--------------- 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 291 qiswnqgidlwwhelmqeagdecepewcdaEDPLFILYTSGSTGKPKGVVHT------------------VGGYMLYVaT 352
Cdd:PRK12316 655 ------------------------------ENLAYVIYTSGSTGKPKGAGNRhralsnrlcwmqqayglgVGDTVLQK-T 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 353 TFKyvFDFHAEDVFWctadigwitghsyvtygPLANGATSVLF-EGIPTYPDvnRLWSIVDKYKVTKFYTAPTAIRLLMK 431
Cdd:PRK12316 704 PFS--FDVSVWEFFW-----------------PLMSGARLVVAaPGDHRDPA--KLVELINREGVDTLHFVPSMLQAFLQ 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 432 FGDEPvtkhSRASLQVLGTVGEPINPEAWLwyhRVVG-AQRCPIVDTFWQTETGghmlTPLPGATPMKPGSATF----PF 506
Cdd:PRK12316 763 DEDVA----SCTSLRRIVCSGEALPADAQE---QVFAkLPQAGLYNLYGPTEAA----IDVTHWTCVEEGGDSVpigrPI 831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 507 FGVAPAILNESGeelegeaegylvfkQPWP------------GIMRTVYG----NHERFETTYFKKFPGYYVTGDGCQRD 570
Cdd:PRK12316 832 ANLACYILDANL--------------EPVPvgvlgelylagrGLARGYHGrpglTAERFVPSPFVAGERMYRTGDLARYR 897
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 571 QDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGhphpVKGECLYCFVTLCDGhtfSPKLTEELKKQIRE 650
Cdd:PRK12316 898 ADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESE---GGDWREALKAHLAA 970
|
570 580 590
....*....|....*....|....*....|
gi 253970489 651 KIGPIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:PRK12316 971 SLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
136-681 |
6.07e-19 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 90.97 E-value: 6.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 215
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 216 AFyrgeklvnlKELADEALQKCqekgfpvrccivvkhlgraelgmgdstsqsPPIKRScpdvqgklkekskrvqpqISWN 295
Cdd:PRK13382 149 EF---------SATVDRALADC------------------------------PQATRI------------------VAWT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 296 QGIDLWWHELMQEAGDECEPEWCDAEDPLfILYTSGSTGKPKGVVHT-VGGYMlyvatTFKYVFDfhaedvfwctaDIGW 374
Cdd:PRK13382 172 DEDHDLTVEVLIAAHAGQRPEPTGRKGRV-ILLTSGTTGTPKGARRSgPGGIG-----TLKAILD-----------RTPW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 375 ITGHSYVTYGPL--ANGATSVLFEGIPTYPDVNR-------LWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASL 445
Cdd:PRK13382 235 RAEEPTVIVAPMfhAWGFSQLVLAASLACTIVTRrrfdpeaTLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 446 QVLGTVGEPINPEAWLWYHRVVGAQrcpIVDTFWQTETGghMLTPlpgATP----MKPGSATFPFFGVAPAILNESgeel 521
Cdd:PRK13382 315 RFAAASGSRMRPDVVIAFMDQFGDV---IYNNYNATEAG--MIAT---ATPadlrAAPDTAGRPAEGTEIRILDQD---- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 522 egeaegylvFKQPWPGIMRTVY-GNHERFE-----TTyfKKF-PGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLST 594
Cdd:PRK13382 383 ---------FREVPTGEVGTIFvRNDTQFDgytsgST--KDFhDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYP 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 595 AEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 674
Cdd:PRK13382 452 IEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG---ASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGK 528
|
....*..
gi 253970489 675 IMRRVLR 681
Cdd:PRK13382 529 ILRRELQ 535
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
181-681 |
1.53e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 89.30 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 181 ARIGALHSIVFAGFSSESLCERILDSSCSLL--ITTDAFYR-GEKLVNLKELADEAL---QKCQEKGFPVRCciVVKHLG 254
Cdd:PRK13390 7 AQIAPDRPAVIVAETGEQVSYRQLDDDSAALarVLYDAGLRtGDVVALLSDNSPEALvvlWAALRSGLYITA--INHHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 255 RAELG--MGDSTSQsppIKRSCPDVQGKLKEKSKRVQPQISWNQGIDLW--WHELMQEAGDECEPEWCDAedplFILYTS 330
Cdd:PRK13390 85 APEADyiVGDSGAR---VLVASAALDGLAAKVGADLPLRLSFGGEIDGFgsFEAALAGAGPRLTEQPCGA----VMLYSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 331 GSTGKPKGV--------VHTVGGYMLYVATTFkyvFDFHAEDVFWCTADIGwitgHSyvtyGPL-------ANGATSVLF 395
Cdd:PRK13390 158 GTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPIY----HA----APLrwcsmvhALGGTVVLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 396 EGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEA------WLWyhrvvga 469
Cdd:PRK13390 227 KRF----DAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVkhamidWLG------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 470 qrcPIVDTFWQTeTGGHMLTPL-PGATPMKPGSATFPFFGVA----------PAilnesgeelegeaegylvfkqpwpGI 538
Cdd:PRK13390 296 ---PIVYEYYSS-TEAHGMTFIdSPDWLAHPGSVGRSVLGDLhicdddgnelPA------------------------GR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 539 MRTVYGNHERFETTYFKK-----------FPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV 607
Cdd:PRK13390 348 IGTVYFERDRLPFRYLNDpektaaaqhpaHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAV 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 253970489 608 AEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:PRK13390 428 HDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
319-680 |
3.33e-18 |
|
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: 87.91 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 319 DAEDPLFILYTSGSTGKPKGVV-------HTVGGY------------MLYVATtfkYVFDFHAEDvfWCTAdigwitghs 379
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMvehrnvaHAAHAWrreyeldsfpvrLLQMAS---FSFDVFAGD--FARS--------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 380 yvtygpLANGATSVLfegIP--TYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINP 457
Cdd:cd17650 157 ------LLNGGTLVI---CPdeVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSDGCKAQD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 458 EAWLwYHRVvgAQRCPIVDTFWQTET--------GGhmLTPLPGATPMKPGSatfPFFGVAPAILNESGeelegeaegyl 529
Cdd:cd17650 228 FKTL-AARF--GQGMRIINSYGVTEAtidstyyeEG--RDPLGDSANVPIGR---PLPNTAMYVLDERL----------- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 530 vfkQPWP------------GIMRTVYGN----HERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLS 593
Cdd:cd17650 289 ---QPQPvgvagelyiggaGVARGYLNRpeltAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 594 TAEVESALVEHEAVAEAAVVGHpHPVKGE---CLYCFVTlcdgHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKT 670
Cdd:cd17650 366 LGEIESQLARHPAIDEAVVAVR-EDKGGEarlCAYVVAA----ATLN---TAELRAFLAKELPSYMIPSYYVQLDALPLT 437
|
410
....*....|
gi 253970489 671 RSGKIMRRVL 680
Cdd:cd17650 438 PNGKVDRRAL 447
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
132-678 |
4.21e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 88.02 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsIVFAgfsseslceriLDSScslL 211
Cdd:PRK05852 40 DRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADL---VVVP-----------LDPA---L 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 212 ITTDAFYRGEKLVNLKELADeALQKCQEKGFPVRCCIVVKHLGRaelgmgdSTSQSPPIKRSCPDVQGKLkekskrvQPQ 291
Cdd:PRK05852 103 PIAEQRVRSQAAGARVVLID-ADGPHDRAEPTTRWWPLTVNVGG-------DSGPSGGTLSVHLDAATEP-------TPA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 292 ISWNQGIdlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGymlyVATTFKYV---FDFHAEDVfwC 368
Cdd:PRK05852 168 TSTPEGL---------------------RPDDAMIMFTGGTTGLPKMVPWTHAN----IASSVRAIitgYRLSPRDA--T 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 369 TADIGWITGHSYVT--YGPLANGATSVLfegiptyPDVNRL-----WSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHS 441
Cdd:PRK05852 221 VAVMPLYHGHGLIAalLATLASGGAVLL-------PARGRFsahtfWDDIKAVGATWYTAVPTIHQILLERAATEPSGRK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 442 RASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTET---------GGHMLTPLPGATPMKPGSATFPFFGVA-- 510
Cdd:PRK05852 294 PAALRFIRSCSAPLTAETAQALQTEFAA---PVVCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRSTGAQIRIVgs 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 511 ------PAILNesgeelegeaegylvfkQPW---PGIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRI 581
Cdd:PRK05852 371 dglplpAGAVG-----------------EVWlrgTTVVRGYLGDPTITAANFTD---GWLRTGDLGSLSAAGDLSIRGRI 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 582 DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYI 661
Cdd:PRK05852 431 KELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTA---EELVQFCRERLAAFEIPASF 507
|
570
....*....|....*..
gi 253970489 662 QNAPGLPKTRSGKIMRR 678
Cdd:PRK05852 508 QEASGLPHTAKGSLDRR 524
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
152-686 |
5.35e-18 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 87.73 E-value: 5.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 152 LRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYrgEKLVNLKelad 231
Cdd:PLN02246 67 LHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYV--DKLKGLA---- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 232 ealqkcQEKGFPVRCCivvkhlgraelgmgdstsQSPPikRSCpdvqgklkekskrvqpqiswnqgidLWWHELMQEAGD 311
Cdd:PLN02246 141 ------EDDGVTVVTI------------------DDPP--EGC-------------------------LHFSELTQADEN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 312 ECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVAttfKYV------FDFHAEDVFWCTADIGWITGHSYVTYGP 385
Cdd:PLN02246 170 ELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVA---QQVdgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 386 LANGATSVLfegIPTYpDVNRLWSIVDKYKVTkfyTAPTAIRLLMKFGDEP-VTKHSRASLQVLGTVGEPINPEawlwYH 464
Cdd:PLN02246 247 LRVGAAILI---MPKF-EIGALLELIQRHKVT---IAPFVPPIVLAIAKSPvVEKYDLSSIRMVLSGAAPLGKE----LE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 465 RVVGAqRCP---IVDTFWQTETGGHMLTPLPGA---TPMKPGSAtfpffgvAPAILNESGEELEGEAEGYLVFKQPW--- 535
Cdd:PLN02246 316 DAFRA-KLPnavLGQGYGMTEAGPVLAMCLAFAkepFPVKSGSC-------GTVVRNAELKIVDPETGASLPRNQPGeic 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 536 ---PGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAV 612
Cdd:PLN02246 388 irgPQIMKGYLNDPEATANTIDKD--GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 613 VGHPHPVKGECLYCFVTLCDGHTFSpklTEELK----KQI--REKIGPIATPDYIqnapglPKTRSGKIMRRVLR-KIAQ 685
Cdd:PLN02246 466 VPMKDEVAGEVPVAFVVRSNGSEIT---EDEIKqfvaKQVvfYKRIHKVFFVDSI------PKAPSGKILRKDLRaKLAA 536
|
.
gi 253970489 686 N 686
Cdd:PLN02246 537 G 537
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
113-681 |
6.07e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 87.63 E-value: 6.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 113 HEKKLGDKVAFYWEGNEpgettqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFA 192
Cdd:PRK06145 11 HARRTPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGA----VFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 193 GfsseslcerildsscsllittdafyrgeklVNLKELADEALQKCQEKGfpvrccivvkhlgrAELGMGDSTSQSPPIKR 272
Cdd:PRK06145 81 P------------------------------INYRLAADEVAYILGDAG--------------AKLLLVDEEFDAIVALE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 273 SCPDVQGKLKEKSKRVqpqiswnqgidlwwhelMQEAGDECEPEWCDAEDPLF-ILYTSGSTGKPKGVVHTVGgymlyva 351
Cdd:PRK06145 117 TPKIVIDAAAQADSRR-----------------LAQGGLEIPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSYG------- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 352 ttfkyvfdfhaeDVFWCTAD----IGWITGHSYVTYGPLAN-GA-----TSVLFEG----IPTYPDVNRLWSIVDKYKVT 417
Cdd:PRK06145 173 ------------NLHWKSIDhviaLGLTASERLLVVGPLYHvGAfdlpgIAVLWVGgtlrIHREFDPEAVLAAIERHRLT 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 418 KFYTAPTAIRLLMKFGDEpvTKHSRASLQVLGTVGEPiNPEAWLW-YHRVVGAQRcpIVDTFWQTET-GGHMLTPlPGAT 495
Cdd:PRK06145 241 CAWMAPVMLSRVLTVPDR--DRFDLDSLAWCIGGGEK-TPESRIRdFTRVFTRAR--YIDAYGLTETcSGDTLME-AGRE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 496 PMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYY 575
Cdd:PRK06145 315 IEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGP--KVTKGYWKDPEKTAEAFYG---DWFRSGDVGYLDEEGFL 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 576 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPI 655
Cdd:PRK06145 390 YLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLT---LEALDRHCRQRLASF 466
|
570 580
....*....|....*....|....*.
gi 253970489 656 ATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:PRK06145 467 KVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
319-684 |
7.02e-18 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 87.39 E-value: 7.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 319 DAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKyVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGAtSVLFEGI 398
Cdd:cd05909 145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITA-IFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGI-KVVFHPN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 399 PTYPdvNRLWSIVDKYKVTKFYTAPTAIRLLMKFgdepVTKHSRASLQVLGTVGEPINPEAW-LWYHRvvgaQRCPIVDT 477
Cdd:cd05909 223 PLDY--KKIPELIYDKKATILLGTPTFLRGYARA----AHPEDFSSLRLVVAGAEKLKDTLRqEFQEK----FGIRILEG 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 478 FWQTETGGHMLTPLPgATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwPGIMRTVYGNHERFETTYFKkf 557
Cdd:cd05909 293 YGTTECSPVISVNTP-QSPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRG-PNVMLGYLNEPELTSFAFGD-- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 558 pGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAV-AEAAVVGHPHPVKGECLYCFVTlcdGHTF 636
Cdd:cd05909 369 -GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSVPDGRKGEKIVLLTT---TTDT 444
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 253970489 637 SPkltEELKKQIRE-KIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 684
Cdd:cd05909 445 DP---SSLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
559-681 |
2.05e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 86.26 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 559 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsP 638
Cdd:PRK08974 432 GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKD-----P 506
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 253970489 639 KLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:PRK08974 507 SLTeEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
290-686 |
2.99e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 85.22 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 290 PQISWNQgidlwWHELMQEAGDECEPEwCDAE-DPLFILYTSGSTGKPKGVVHTVGGYMlyvattfkYVFDFHAEDVFWC 368
Cdd:PRK07638 117 RVIEIDE-----WKRMIEKYLPTYAPI-ENVQnAPFYMGFTSGSTGKPKAFLRAQQSWL--------HSFDCNVHDFHMK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 369 TADIGWITG---HSYVTYGplangATSVLFEG-----IPTYPDVNRLWSIvDKYKVTKFYTAPTAIRLLMK---FGDEPV 437
Cdd:PRK07638 183 REDSVLIAGtlvHSLFLYG-----AISTLYVGqtvhlMRKFIPNQVLDKL-ETENISVMYTVPTMLESLYKenrVIENKM 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 438 T------KHSRASLQVLGTvgepINPEAWLWyhrvvgaqrcpivdTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAP 511
Cdd:PRK07638 257 KiissgaKWEAEAKEKIKN----IFPYAKLY--------------EFYGASELSFVTALVDEESERRPNSVGRPFHNVQV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 512 AILNESGeelegeaegylvfKQPWPGIMRTVYGNHERFETTY------FKKFP--GYYVTGD-GCQrDQDGYYWITGRID 582
Cdd:PRK07638 319 RICNEAG-------------EEVQKGEIGTVYVKSPQFFMGYiiggvlARELNadGWMTVRDvGYE-DEEGFIYIVGREK 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 583 DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLycfVTLCDGHTFSpkltEELKKQIREKIGPIATPDYIQ 662
Cdd:PRK07638 385 NMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKP---VAIIKGSATK----QQLKSFCLQRLSSFKIPKEWH 457
|
410 420
....*....|....*....|....
gi 253970489 663 NAPGLPKTRSGKIMRRVLRKIAQN 686
Cdd:PRK07638 458 FVDEIPYTNSGKIARMEAKSWIEN 481
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
115-680 |
5.80e-17 |
|
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: 84.30 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 115 KKLGDKVAFYWEGNepgettQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGF 194
Cdd:cd17655 8 EKTPDHTAVVFEDQ------TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 195 SSESLcERIL-DSSCSLLITTdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrs 273
Cdd:cd17655 82 PEERI-QYILeDSGADILLTQ----------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 274 cpdvqgklkeksKRVQPQISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGV----------VHTV 343
Cdd:cd17655 102 ------------SHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVmiehrgvvnlVEWA 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 344 GGYM-----LYVATTFKYVFDFHAEDVFwctadigwitghsyvtyGPLANGATSVLFEGiPTYPDVNRLWSIVDKYKVTK 418
Cdd:cd17655 170 NKVIyqgehLRVALFASISFDASVTEIF-----------------ASLLSGNTLYIVRK-ETVLDGQALTQYIRQNRITI 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 419 FYTAPTAIRLLMKFGDEPvtkhsRASLQVLGTVGEPINPE-AWLWYHRVVGAqrCPIVDTFWQTETG-GHMLTPLpgaTP 496
Cdd:cd17655 232 IDLTPAHLKLLDAADDSE-----GLSLKHLIVGGEALSTElAKKIIELFGTN--PTITNAYGPTETTvDASIYQY---EP 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 497 MKPGSATFPffgVAPAILNESGeelegeaegYLVFK--QPWP------------GIMRTvYGNHErfETTYfKKF----- 557
Cdd:cd17655 302 ETDQQVSVP---IGKPLGNTRI---------YILDQygRPQPvgvagelyiggeGVARG-YLNRP--ELTA-EKFvddpf 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 558 -PG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtlcdgh 634
Cdd:cd17655 366 vPGerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYI------ 439
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 253970489 635 TFSPKLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:cd17655 440 VSEKELPvAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
47-107 |
6.45e-17 |
|
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: 75.20 E-value: 6.45e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 253970489 47 YRELHRRSVEEPREFWGDIAKEFYWKTPCpgpflRYNFDVTKGkIFIEWMKGATTNICYNV 107
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPF-----DKVLDGSNG-PFAKWFVGGKLNVCYNC 55
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
319-685 |
7.91e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 84.30 E-value: 7.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 319 DAEDPLFILYTSGSTGKPKGVV--HTvGGYMLYVATTFKY---VFDFH--AEDVFWCTadiGWItghsyVTYGPLANGAT 391
Cdd:PLN03102 184 DEHDPISLNYTSGTTADPKGVVisHR-GAYLSTLSAIIGWemgTCPVYlwTLPMFHCN---GWT-----FTWGTAARGGT 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 392 SVLFEGIpTYPDVnrlWSIVDKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLgTVGEPiNPEAWLWYHRVVGAQr 471
Cdd:PLN03102 255 SVCMRHV-TAPEI---YKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVL-TGGSP-PPAALVKKVQRLGFQ- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 472 cpIVDTFWQTETGGHML--------TPLPGATPMK-PGSATFPFFGVAPAILNESGEELEG----EAEGYLVFKQPwpGI 538
Cdd:PLN03102 327 --VMHAYGLTEATGPVLfcewqdewNRLPENQQMElKARQGVSILGLADVDVKNKETQESVprdgKTMGEIVIKGS--SI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 539 MRTvYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHP 618
Cdd:PLN03102 403 MKG-YLKNPKATSEAFKH--GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHP 479
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 253970489 619 VKGECLYCFVTLCDGHTFSPKLTEELK-------KQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQ 685
Cdd:PLN03102 480 TWGETPCAFVVLEKGETTKEDRVDKLVtrerdliEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAK 553
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
132-687 |
8.89e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 84.23 E-value: 8.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGA-LH---------SIVFagfsseslce 201
Cdd:PRK08162 40 GDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAvLNtlntrldaaSIAF---------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 202 rILDSSCS-LLITTDAFyrgeklvnlKELADEALQKCqekgfPVRCCIVVkhlgraelgmgdstsqsppikrscpDVQGK 280
Cdd:PRK08162 110 -MLRHGEAkVLIVDTEF---------AEVAREALALL-----PGPKPLVI-------------------------DVDDP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 281 LKEKSKRVQpqiswnqgiDLWWHELMQEAGDECEPEWCDAE-DPLFILYTSGSTGKPKGVV-HTVGGYMLYVATTFKYVF 358
Cdd:PRK08162 150 EYPGGRFIG---------ALDYEAFLASGDPDFAWTLPADEwDAIALNYTSGTTGNPKGVVyHHRGAYLNALSNILAWGM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 359 DFHAE-----DVFWCTadiGWitGHSY-VTygplANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMkf 432
Cdd:PRK08162 221 PKHPVylwtlPMFHCN---GW--CFPWtVA----ARAGTNVCLRKV----DPKLIFDLIREHGVTHYCGAPIVLSALI-- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 433 gdepvtkHSRASLQvlgtvgEPINpeawlwyHRVVG--AQRCPIVDTFWQTETGGHMLTPLPGATPM---------KPGS 501
Cdd:PRK08162 286 -------NAPAEWR------AGID-------HPVHAmvAGAAPPAAVIAKMEEIGFDLTHVYGLTETygpatvcawQPEW 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 502 ATFPFF---------GV------APAILNESGEELEgeaegylvfkqPWPG-----IMrtVYGN-------------HER 548
Cdd:PRK08162 346 DALPLDeraqlkarqGVryplqeGVTVLDPDTMQPV-----------PADGetigeIM--FRGNivmkgylknpkatEEA 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 549 FETtyfkkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFV 628
Cdd:PRK08162 413 FAG-------GWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFV 485
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 253970489 629 TLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIAQND 687
Cdd:PRK08162 486 ELKDGASATE---EEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVLREQAKSL 540
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
303-683 |
9.33e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 85.21 E-value: 9.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 303 HELMQEAGDEC-EPEWC-----DAEDPLFILYTSGSTGKPKGVVHTVGG-----------YMLYVATT----FKYVFDFH 361
Cdd:PRK12467 3213 TALTLDRLDLNgYSENNpstrvMGENLAYVIYTSGSTGKPKGVGVRHGAlanhlcwiaeaYELDANDRvllfMSFSFDGA 3292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 362 AEDVFWctadigwitghsyvtygPLANGATSVLFEGIPTYPDvnRLWSIVDKYKVTKFYTAPTAIRLLMKFGDepvtKHS 441
Cdd:PRK12467 3293 QERFLW-----------------TLICGGCLVVRDNDLWDPE--ELWQAIHAHRISIACFPPAYLQQFAEDAG----GAD 3349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 442 RASLQVLGTVGEPINPEAWLWYHRVV---------GAQRCPIVDTFWQTETGGhmlTPLPGATPMKPGSAtfpffGVAPA 512
Cdd:PRK12467 3350 CASLDIYVFGGEAVPPAAFEQVKRKLkprgltngyGPTEAVVTVTLWKCGGDA---VCEAPYAPIGRPVA-----GRSIY 3421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 513 ILNESGeelegeaegylvfkQPWP-GIMRTVY--------GNH-------ERFETTYFKKFPG-YYVTGDGCQRDQDGYY 575
Cdd:PRK12467 3422 VLDGQL--------------NPVPvGVAGELYiggvglarGYHqrpsltaERFVADPFSGSGGrLYRTGDLARYRADGVI 3487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 576 WITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPhPVKGECLYCFVTLcdgHTFSPKLTEELKKQIREKIgpi 655
Cdd:PRK12467 3488 EYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARD-GAGGKQLVAYVVP---ADPQGDWRETLRDHLAASL--- 3560
|
410 420 430
....*....|....*....|....*....|...
gi 253970489 656 atPDYIQNA-----PGLPKTRSGKIMRRVLRKI 683
Cdd:PRK12467 3561 --PDYMVPAqllvlAAMPLGPNGKVDRKALPDP 3591
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
321-677 |
1.64e-16 |
|
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: 81.54 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 321 EDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATsVLFEGIPT 400
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLC-VTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 401 YpdvNRLWSIVDKYKVTKFYTAPTAIRLLMKfgdepVTKHSRA---SLQVLGTVGE-PINPEA--WLWYHRVvgaqrcPI 474
Cdd:cd17635 80 Y---KSLFKILTTNAVTTTCLVPTLLSKLVS-----ELKSANAtvpSLRLIGYGGSrAIAADVrfIEATGLT------NT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 475 VDTFWQTETGGHMLTPLpGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWpgIMRTVYGNHERFETTYF 554
Cdd:cd17635 146 AQVYGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA--NMLGYWNNPERTAEVLI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 555 KkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdgh 634
Cdd:cd17635 223 D---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA---- 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 253970489 635 tfSPKLTEE----LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 677
Cdd:cd17635 296 --SAELDENairaLKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
321-683 |
2.29e-16 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 82.57 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 321 EDPLFILYTSGSTGKPKGVVHT--------------VGGYMLYVATTFKYVFDFHaeDVFWCTADIGWITGhsyvtygpl 386
Cdd:cd17642 184 EQVALIMNSSGSTGLPKGVQLThknivarfshardpIFGNQIIPDTAILTVIPFH--HGFGMFTTLGYLIC--------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 387 anGATSVLfegIPTYPDVNRLWSIVDkYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEawlwyhrv 466
Cdd:cd17642 253 --GFRVVL---MYKFEEELFLRSLQD-YKVQSALLVPTLFAFFAK--STLVDKYDLSNLHEIASGGAPLSKE-------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 467 VGAQ-----RCPIV-DTFWQTETGGHML-TPlpgATPMKPGSA--TFPFFGvAPAILNESGEELEGEAEGYLVFKQpwPG 537
Cdd:cd17642 317 VGEAvakrfKLPGIrQGYGLTETTSAILiTP---EGDDKPGAVgkVVPFFY-AKVVDLDTGKTLGPNERGELCVKG--PM 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 538 IMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPH 617
Cdd:cd17642 391 IMKGYVNNPEATKALIDKD--GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPD 468
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 253970489 618 PVKGECLYCFVTLCDGHTFSPKLTEEL-------KKQIRekiGPIATPDYIqnapglPKTRSGKIMRRVLRKI 683
Cdd:cd17642 469 EDAGELPAAVVVLEAGKTMTEKEVMDYvasqvstAKRLR---GGVKFVDEV------PKGLTGKIDRRKIREI 532
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
305-688 |
2.47e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.85 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 305 LMQEAGDECEPEW-----CDAEDPLFILYTSGSTGKPKGVV--------HTVGGYMLYVATTFKYV-------FDFHAED 364
Cdd:PRK12316 3175 LDLDRGDENYAEAnpairTMPENLAYVIYTSGSTGKPKGVGirhsalsnHLCWMQQAYGLGVGDRVlqfttfsFDVFVEE 3254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 365 VFWctadigwitghsyvtygPLANGATSVLfEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMkfgdEPVTKHSRAS 444
Cdd:PRK12316 3255 LFW-----------------PLMSGARVVL-AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFL----EEEDAHRCTS 3312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 445 LQVLGTVGEPINPEAwlwYHRVVGAQrcPIVDTFWQTETgghmlTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGE 524
Cdd:PRK12316 3313 LKRIVCGGEALPADL---QQQVFAGL--PLYNLYGPTEA-----TITVTHWQCVEEGKDAVPIGRPIANRACYILDGSLE 3382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 525 AEGYLVFKQPWPGIMRTVYGNH-------ERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEV 597
Cdd:PRK12316 3383 PVPVGALGELYLGGEGLARGYHnrpgltaERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEI 3462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 598 ESALVEHEAVAEAAVVGhphpVKGECLYCFVTLCDGhtfSPKLTEELKKQIREKIgpiatPDYIQNA-----PGLPKTRS 672
Cdd:PRK12316 3463 EARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE---AGDLREALKAHLKASL-----PEYMVPAhllflERMPLTPN 3530
|
410 420
....*....|....*....|
gi 253970489 673 GKIMRRVLRK----IAQNDH 688
Cdd:PRK12316 3531 GKLDRKALPRpdaaLLQQDY 3550
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
135-682 |
2.54e-16 |
|
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: 82.48 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 135 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCErildsscsllitt 214
Cdd:cd05915 24 RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAY------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 215 dafyrgeklvnlkeladeALQKCQEKGFPVRCCIVvkHLGRAELGMGDSTSQSPPIKRSCPDVQGKLKEKSKRVQPQisw 294
Cdd:cd05915 91 ------------------ILNHAEDKVLLFDPNLL--PLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADP--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 295 nqgidlwwhelmqEAGDECepewcdaeDPLFILYTSGSTGKPKGVVHT-VGGYMLYVATTFKYVFDFHAEDVFWCTADIG 373
Cdd:cd05915 148 -------------VRVPER--------AACGMAYTTGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMF 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 374 WITGHSYVtYGPLANGATSVLFEGIPTypDVNRLWSIVdKYKVTKFYTAPTAIRLLMKFGDEpVTKHSRASLQVLGTVGE 453
Cdd:cd05915 207 HVNAWCLP-YAATLVGAKQVLPGPRLD--PASLVELFD-GEGVTFTAGVPTVWLALADYLES-TGHRLKTLRRLVVGGSA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 454 PinPEAWL-----WYHRVVGAQRCPIV-----DTFWQTEtgghmLTPLPGATPMK-PGSATFPFFGVAPAILNESGEELE 522
Cdd:cd05915 282 A--PRSLIarferMGVEVRQGYGLTETspvvvQNFVKSH-----LESLSEEEKLTlKAKTGLPIPLVRLRVADEEGRPVP 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 523 GEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALV 602
Cdd:cd05915 355 KDGKALGEVQLKGPWITGGYYGNEEATRSALTPD--GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALM 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 603 EHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKqireKIGPIAT-PDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:cd05915 433 GHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELNEHLLK----AGFAKWQlPDAYVFAEEIPRTSAGKFLKRALR 508
|
.
gi 253970489 682 K 682
Cdd:cd05915 509 E 509
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
132-685 |
3.16e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 82.58 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 211
Cdd:PLN02479 42 GSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 212 ITTDAFYrgeklvnlkELADEALQ---KCQEKGFPVRCCIVVkhlgraelgmGDSTSQSPPIKRSCPDVQGKLKEKSKRV 288
Cdd:PLN02479 122 MVDQEFF---------TLAEEALKilaEKKKSSFKPPLLIVI----------GDPTCDPKSLQYALGKGAIEYEKFLETG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 289 QPQISWNQGIDLWwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVV-HTVGGYMLyvATTFKYVFDFHAEDVFW 367
Cdd:PLN02479 183 DPEFAWKPPADEW--------------------QSIALGYTSGTTASPKGVVlHHRGAYLM--ALSNALIWGMNEGAVYL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 368 CTADIGWITGHSYvTYGPLANGATSVLFEGIPTypdvNRLWSIVDKYKVTKFYTAPTAIRLL------------------ 429
Cdd:PLN02479 241 WTLPMFHCNGWCF-TWTLAALCGTNICLRQVTA----KAIYSAIANYGVTHFCAAPVVLNTIvnapksetilplprvvhv 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 430 MKFGDEP----VTKHSRASLQVLGTVG--EPINPE---AWL--WYH---------------RVVGAQRCPIVDTfwqtet 483
Cdd:PLN02479 316 MTAGAAPppsvLFAMSEKGFRVTHTYGlsETYGPStvcAWKpeWDSlppeeqarlnarqgvRYIGLEGLDVVDT------ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 484 gghmltplpgaTPMKPGSATFPFFGVAPAILNesgeelegeaegyLVFKqpwpGIMRTVYGNHERFETtyfkkfpGYYVT 563
Cdd:PLN02479 390 -----------KTMKPVPADGKTMGEIVMRGN-------------MVMK----GYLKNPKANEEAFAN-------GWFHS 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 564 GDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFS--PKLT 641
Cdd:PLN02479 435 GDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSdeAALA 514
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 253970489 642 EELKKQIREKIGPIATPDYIQNAPgLPKTRSGKIMRRVLRKIAQ 685
Cdd:PLN02479 515 EDIMKFCRERLPAYWVPKSVVFGP-LPKTATGKIQKHVLRAKAK 557
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
107-681 |
1.10e-15 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 80.85 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 107 VLDRNVHEKKLGDKVAFYwegnepgETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAL 186
Cdd:PRK06060 9 LLAEQASEAGWYDRPAFY-------AADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 187 HSIVFAGFSSESLCERILDSSCSLLITTDAF---YRGEKLVNLKELADEAlqkcqekgfpvrccivvkhlgraelgmgds 263
Cdd:PRK06060 82 AFLANPELHRDDHALAARNTEPALVVTSDALrdrFQPSRVAEAAELMSEA------------------------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 264 tsqsppikrscpdvqgklkeksKRVQPQiswnqgidlwwhelmqeagdECEPEWCDAEdpLFILYTSGSTGKPKGVVHTV 343
Cdd:PRK06060 132 ----------------------ARVAPG--------------------GYEPMGGDAL--AYATYTSGTTGPPKAAIHRH 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 344 ggymlyvATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYG-------PLANGATSVLfEGIPTYPDVNRLWSIvdKYKV 416
Cdd:PRK06060 168 -------ADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGlgnsvwfPLATGGSAVI-NSAPVTPEAAAILSA--RFGP 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 417 TKFYTAPTAIRLLMkfgdEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrCPIVDTFWQTETGGHMLTPlpGATP 496
Cdd:PRK06060 238 SVLYGVPNFFARVI----DSCSPDSFRSLRCVVSAGEALELGLAERLMEFFGG--IPILDGIGSTEVGQTFVSN--RVDE 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 497 MKPGS--ATFPFFGVAPAILNESGEELEGEAEGYLvfkqPWPGIMRTVYGNHERFETTyfkkfPGYYVTGDGCQRDQDGY 574
Cdd:PRK06060 310 WRLGTlgRVLPPYEIRVVAPDGTTAGPGVEGDLWV----RGPAIAKGYWNRPDSPVAN-----EGWLDTRDRVCIDSDGW 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 575 YWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGP 654
Cdd:PRK06060 381 VTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSA 460
|
570 580
....*....|....*....|....*..
gi 253970489 655 IATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:PRK06060 461 FKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
135-680 |
1.33e-15 |
|
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: 80.01 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 135 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSLLIT 213
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARR-EAILaDAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 214 TDafyrgeklvnlkeladEALQKCQekgfPVRCCIVVkhlgraeLGMGDSTSQSPPikrscpdvqgklkekSKRVQPQis 293
Cdd:cd12114 91 DG----------------PDAQLDV----AVFDVLIL-------DLDALAAPAPPP---------------PVDVAPD-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 294 wnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVVHTVGGYMLYVA-TTFKYV--------------F 358
Cdd:cd12114 127 ----------------------------DLAYVIFTSGSTGTPKGVMISHRAALNTILdINRRFAvgpddrvlalsslsF 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 359 DFHAEDVFwctadigwitghsyvtyGPLANGATSVLfegiPTY---PDVNRLWSIVDKYKVTKFYTAPTAIRLLMKF-GD 434
Cdd:cd12114 179 DLSVYDIF-----------------GALSAGATLVL----PDEarrRDPAHWAELIERHGVTLWNSVPALLEMLLDVlEA 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 435 EPVTKHS-R--------------ASLQVLGTVGEPIN----PEAWLW--YHRVVGA---------------QRCPIVDTf 478
Cdd:cd12114 238 AQALLPSlRlvllsgdwipldlpARLRALAPDARLISlggaTEASIWsiYHPIDEVppdwrsipygrplanQRYRVLDP- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 479 wqtetgghMLTPLPGatpmkpgsatfpffGVAPAIlnesgeelegeaegylvfkqpW---PGIMRTVYGNHERFETTYFK 555
Cdd:cd12114 317 --------RGRDCPD--------------WVPGEL---------------------WiggRGVALGYLGDPELTAARFVT 353
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 556 KFPG--YYVTGD-GCQRDqDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPvKGECLYCFVTLCD 632
Cdd:cd12114 354 HPDGerLYRTGDlGRYRP-DGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDN 431
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 253970489 633 GHTfsPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:cd12114 432 DGT--PIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
107-682 |
1.80e-15 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 79.92 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 107 VLDRNVHekKLGDKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAL 186
Cdd:PRK08279 42 VFEEAAA--RHPDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 187 HSIVFAGFSSESL--CERILDSscSLLITtdafyrGEKLVNLKELADEALQKcqekgfPVRCCIVVKHLGRAELGMGD-- 262
Cdd:PRK08279 114 VALLNTQQRGAVLahSLNLVDA--KHLIV------GEELVEAFEEARADLAR------PPRLWVAGGDTLDDPEGYEDla 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 263 --STSQSPPIKRSCPDVQgklkekskrvqpqiswnqgidlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGVV 340
Cdd:PRK08279 180 aaAAGAPTTNPASRSGVT-----------------------------------------AKDTAFYIYTSGTTGLPKAAV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 341 HTVGGYMLYVAtTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVL---FEgiptypdVNRLWSIVDKYKVT 417
Cdd:PRK08279 219 MSHMRWLKAMG-GFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALrrkFS-------ASRFWDDVRRYRAT 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 418 KFYtaptAI----RLLMkfgDEPVTKHSRA-SLQVLgtVGEPINPEAW--------------LW--------------YH 464
Cdd:PRK08279 291 AFQ----YIgelcRYLL---NQPPKPTDRDhRLRLM--IGNGLRPDIWdefqqrfgiprileFYaasegnvgfinvfnFD 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 465 RVVGaqRCP--------IVDtfWQTETGghmlTPLPGA----TPMKPGSAtfpffGVAPAILNEsgeelegeaegylvfK 532
Cdd:PRK08279 362 GTVG--RVPlwlahpyaIVK--YDVDTG----EPVRDAdgrcIKVKPGEV-----GLLIGRITD---------------R 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 533 QPWPG----------IMRTVygnherfettyFKKFPGYYVTGDGCQRDQDGYYWITGRIDDML-----NVsghllSTAEV 597
Cdd:PRK08279 414 GPFDGytdpeasekkILRDV-----------FKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFrwkgeNV-----ATTEV 477
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 598 ESALVEHEAVAEAAVVGHPHP-VKGECLYCFVTLCDGHTFSPKlteELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIM 676
Cdd:PRK08279 478 ENALSGFPGVEEAVVYGVEVPgTDGRAGMAAIVLADGAEFDLA---ALAAHLYERLPAYAVPLFVRLVPELETTGTFKYR 554
|
....*.
gi 253970489 677 RRVLRK 682
Cdd:PRK08279 555 KVDLRK 560
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
559-686 |
1.87e-15 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 79.65 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 559 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLYCFVTlcdghtf 636
Cdd:PRK10946 409 GFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEksCAFLVVK------- 481
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 253970489 637 SPKLTEELKKQIREK-IGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 686
Cdd:PRK10946 482 EPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLAS 532
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
136-683 |
2.20e-15 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 79.89 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 136 ITYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITt 214
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 215 dafyrgeklvnlkelADEALQKCQEKGFPVrccivvkhlgraeLGMGDStsqsppikrscpdvqGKLKEKSKRVQPqisw 294
Cdd:PLN02574 146 ---------------SPENVEKLSPLGVPV-------------IGVPEN---------------YDFDSKRIEFPK---- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 295 nqgidlwWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHA----EDVFWCTA 370
Cdd:PLN02574 179 -------FYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEypgsDNVYLAAL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 371 DIGWITGHSYVTYGPLANGATSVLFEGIptypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLGT 450
Cdd:PLN02574 252 PMFHIYGLSLFVVGLLSLGSTIVVMRRF----DASDMVKVIDRFKVTHFPVVPPILMALTK-KAKGVCGEVLKSLKQVSC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 451 VGEPINPEAWLWYhrvvgAQRCPIVDtFWQtetgGHMLTPLPGATPMKPGSATFPFFG----VAPAILNESGEELEGEAE 526
Cdd:PLN02574 327 GAAPLSGKFIQDF-----VQTLPHVD-FIQ----GYGMTESTAVGTRGFNTEKLSKYSsvglLAPNMQAKVVDWSTGCLL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 527 GYLVFKQPW---PGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVE 603
Cdd:PLN02574 397 PPGNCGELWiqgPGVMKGYLNNPKATQSTIDKD--GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLIS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 604 HEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKI 683
Cdd:PLN02574 475 HPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLS---QEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
115-681 |
3.67e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 79.04 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 115 KKLGDKVAFywegNEPGETtqITYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAG 193
Cdd:PRK05677 35 QRFADKPAF----SNLGKT--LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 194 FSSESLCERILDSSCSLLITtdafyrgekLVNLKELADEALQKCQekgfpvrccivVKHLGRAELGmgdstSQSPPIKRS 273
Cdd:PRK05677 109 YTAREMEHQFNDSGAKALVC---------LANMAHLAEKVLPKTG-----------VKHVIVTEVA-----DMLPPLKRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 274 CpdVQGKLKEKSKRVqPQISWNQGIDLWwHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT---VGGYMLYV 350
Cdd:PRK05677 164 L--INAVVKHVKKMV-PAYHLPQAVKFN-DALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLThrnLVANMLQC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 351 ATTFK-------------------YVFDFHaedvfwCTAdigwitghsyvtygPLANGATSVLfegIPTYPDVNRLWSIV 411
Cdd:PRK05677 240 RALMGsnlnegceiliaplplyhiYAFTFH------CMA--------------MMLIGNHNIL---ISNPRDLPAMVKEL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 412 DKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGaqrCPIVDTFWQTETgghmlTPL 491
Cdd:PRK05677 297 GKWKFSGFVGLNTLFVALCN--NEAFRKLDFSALKLTLSGGMALQLATAERWKEVTG---CAICEGYGMTET-----SPV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 492 PGATPMK---PGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQ 568
Cdd:PRK05677 367 VSVNPSQaiqVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGP--QVMKGYWQRPE--ATDEILDSDGWLKTGDIAL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 569 RDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQI 648
Cdd:PRK05677 443 IQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLT---KEQVMEHM 519
|
570 580 590
....*....|....*....|....*....|...
gi 253970489 649 REKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:PRK05677 520 RANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
322-677 |
7.63e-15 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 76.15 E-value: 7.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 322 DPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSyVTYGPLANGATSVLFEGIpty 401
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 402 pDVNRLWSIVDKYKVTKFYT-APTAIRLLMKFGDEPVtkhSRASLQVLGTVGEPINPEAWlwyHRVVGAqrcpivdTFW- 479
Cdd:cd17637 76 -DPAEALELIEEEKVTLMGSfPPILSNLLDAAEKSGV---DLSSLRHVLGLDAPETIQRF---EETTGA-------TFWs 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 480 ---QTETGGhMLTPLPGATpmKPGSATFPFFGVAPAILNESGEELEGEAEGY------LVFKQPWpgimrtvyGNHERFE 550
Cdd:cd17637 142 lygQTETSG-LVTLSPYRE--RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEivvrgpLVFQGYW--------NLPELTA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 551 TTyFKKfpGYYVTGDGCQRDQDGYYWITGRI--DDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFV 628
Cdd:cd17637 211 YT-FRN--GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVC 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 253970489 629 TLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 677
Cdd:cd17637 288 VLKPGATLTA---DELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
117-674 |
8.36e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 77.62 E-value: 8.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 117 LGDKVAFYWeGNEpgettQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSS 196
Cdd:PRK07798 16 VPDRVALVC-GDR-----RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 197 ESLCERILDSSCSLLITTDAFyrGEKLVNLKEladeALQKcqekgfpVRCCIVVkhlgraelgmGDSTSQSPPikrscpd 276
Cdd:PRK07798 90 DELRYLLDDSDAVALVYEREF--APRVAEVLP----RLPK-------LRTLVVV----------EDGSGNDLL------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 277 vqgklkekskrvqpqiswNQGIDlwWHELMQEAGDECEPEWCDAEDpLFILYTSGSTGKPKGVVHT--------VGGYML 348
Cdd:PRK07798 140 ------------------PGAVD--YEDALAAGSPERDFGERSPDD-LYLLYTGGTTGMPKGVMWRqedifrvlLGGRDF 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 349 YVATTFKYVFDfHAEDVFWCTADIGWITG---H---SYVTYGPLANGATSVLfegiptYP----DVNRLWSIVDKYKVTk 418
Cdd:PRK07798 199 ATGEPIEDEEE-LAKRAAAGPGMRRFPAPplmHgagQWAAFAALFSGQTVVL------LPdvrfDADEVWRTIEREKVN- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 419 fytaptairLLMKFGD---EPVTKHSRA-------SLQVLGTVGEPINP---EAWLWY--HRVvgaqrcpIVDTFWQTET 483
Cdd:PRK07798 271 ---------VITIVGDamaRPLLDALEArgpydlsSLFAIASGGALFSPsvkEALLELlpNVV-------LTDSIGSSET 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 484 G-GHMLTPLPGATPmkPGSATF---PFFGVAPAILNEsgeelegeaegyLVFKQPWPG-IMRT------VYGNHERFETT 552
Cdd:PRK07798 335 GfGGSGTVAKGAVH--TGGPRFtigPRTVVLDEDGNP------------VEPGSGEIGwIARRghiplgYYKDPEKTAET 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 553 yFKKFPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTL 630
Cdd:PRK07798 401 -FPTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQL 479
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 253970489 631 CDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 674
Cdd:PRK07798 480 REGARPDL---AELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
302-619 |
9.59e-15 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 77.51 E-value: 9.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 302 WHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMlYVATTFKYVFDFHAEDVFWCTADIGWITGHSYV 381
Cdd:cd05932 118 WDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFA-WAAQAGIEHIGTEENDRMLSYLPLAHVTERVFV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 382 TYGPLANGATSVLFEGIPTYPD------------VNRLWS-----IVDKYKVTKfytaptaIRLLMK--FGDEPVTKHSR 442
Cdd:cd05932 197 EGGSLYGGVLVAFAESLDTFVEdvqrarptlffsVPRLWTkfqqgVQDKIPQQK-------LNLLLKipVVNSLVKRKVL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 443 ASL-----QVLGTVGEPINPEAWLWYHRVvgaqRCPIVDTFWQTETGGHMLTPLPGATpmKPGSATFPFFGVAPAIlnes 517
Cdd:cd05932 270 KGLgldqcRLAGCGSAPVPPALLEWYRSL----GLNILEAYGMTENFAYSHLNYPGRD--KIGTVGNAGPGVEVRI---- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 518 geelegEAEGYLVFKQPwpGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDMLNVS-GHLLSTAE 596
Cdd:cd05932 340 ------SEDGEILVRSP--ALMMGYYKDPEATAEAFTAD--GFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAP 409
|
330 340
....*....|....*....|....*
gi 253970489 597 VESALVEHEAVAEAAVVGH--PHPV 619
Cdd:cd05932 410 IENKLAEHDRVEMVCVIGSglPAPL 434
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
559-682 |
9.60e-15 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 77.48 E-value: 9.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 559 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 638
Cdd:PRK06018 410 GFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATR 489
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 253970489 639 kltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:PRK06018 490 ---EEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
559-681 |
1.45e-14 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 76.98 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 559 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsP 638
Cdd:PRK07059 435 GFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKD-----P 509
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 253970489 639 KLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:PRK07059 510 ALTEEdVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
320-680 |
3.13e-14 |
|
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: 75.37 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 320 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHSYVTYGPLAnGATSVLFEGIP 399
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA-FDVGPGSRVLQFASPSFDASVWELLMALLA-GATLVLAPAEE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 400 TYPDvNRLWSIVDKYKVTkFYTAPTAIRLLMKFGDEPvtkhsraSLQVLGTVGEPINPE-AWLWyhrvvgAQRCPIVDTF 478
Cdd:cd17652 170 LLPG-EPLADLLREHRIT-HVTLPPAALAALPPDDLP-------DLRTLVVAGEACPAElVDRW------APGRRMINAY 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 479 WQTET--GGHMLTPLPGATPMKPGSatfPFFGVAPAILNESGeelegeaegylvfkQPWP------------GIMRTvYG 544
Cdd:cd17652 235 GPTETtvCATMAGPLPGGGVPPIGR---PVPGTRVYVLDARL--------------RPVPpgvpgelyiagaGLARG-YL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 545 NH-----ERFETTYFKKfPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPH 617
Cdd:cd17652 297 NRpgltaERFVADPFGA-PGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDD 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 253970489 618 PVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:cd17652 376 RPGDKRLVAYVVPAPGAAPTA---AELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
559-677 |
3.89e-14 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 74.07 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 559 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfsp 638
Cdd:cd17638 215 GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVT--- 291
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 253970489 639 kLTEE-LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMR 677
Cdd:cd17638 292 -LTEEdVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
136-682 |
5.36e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.15 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 136 ITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTD 215
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 216 AFYrgEKLVNLKELADEALQKcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqpqiswn 295
Cdd:PRK12316 2109 HLL--ERLPLPAGVARLPLDR----------------------------------------------------------- 2127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 296 qgiDLWWHELMQEAgdecePEWCDAEDPL-FILYTSGSTGKPKGVVHTVGGYMLYVATTFKY---------------VFD 359
Cdd:PRK12316 2128 ---DAEWADYPDTA-----PAVQLAGENLaYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERyelspadcelqfmsfSFD 2199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 360 FHAEDVFWctadigwitghsyvtygPLANGATSVLFEGipTYPDVNRLWSIVDKYKVTKFYTAPTairLLMKFGDEPVTK 439
Cdd:PRK12316 2200 GAHEQWFH-----------------PLLNGARVLIRDD--ELWDPEQLYDEMERHGVTILDFPPV---YLQQLAEHAERD 2257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 440 HSRASLQVLGTVGEPINPEAWLWYHRVVGAQRcpIVDTFWQTETgghMLTPLP-GATPMKPGSATFPFFGVAPA-----I 513
Cdd:PRK12316 2258 GRPPAVRVYCFGGEAVPAASLRLAWEALRPVY--LFNGYGPTEA---VVTPLLwKCRPQDPCGAAYVPIGRALGnrrayI 2332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 514 LNESGEELEGEAEGYLVFKQPwpGIMRTVYG----NHERFETTYFKKFPG-YYVTGDGCQRDQDGYYWITGRIDDMLNVS 588
Cdd:PRK12316 2333 LDADLNLLAPGMAGELYLGGE--GLARGYLNrpglTAERFVPDPFSASGErLYRTGDLARYRADGVVEYLGRIDHQVKIR 2410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 589 GHLLSTAEVESALVEHEAVAEAAVVGHPHPvKGECLYCFVTLCDGHTFSPkltEELKKQIREKIGPIATPDYIQNAPGLP 668
Cdd:PRK12316 2411 GFRIELGEIEARLQAHPAVREAVVVAQDGA-SGKQLVAYVVPDDAAEDLL---AELRAWLAARLPAYMVPAHWVVLERLP 2486
|
570
....*....|....
gi 253970489 669 KTRSGKIMRRVLRK 682
Cdd:PRK12316 2487 LNPNGKLDRKALPK 2500
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
319-682 |
7.80e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 75.76 E-value: 7.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 319 DAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTfkyvfdfhaEDVFWCTADIGWITGHSYV-------TYGPLANGAt 391
Cdd:PRK12316 4692 HPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHAT---------GERYELTPDDRVLQFMSFSfdgshegLYHPLINGA- 4761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 392 SVLFEGiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfGDEPVTKHSRASLQVLGtvGEPINPEAW-LWY------- 463
Cdd:PRK12316 4762 SVVIRD-DSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAE-HAERDGEPPSLRVYCFG--GEAVAQASYdLAWralkpvy 4837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 464 -HRVVGAQRCPIVDTFWQTETGghmltPLPGATPMKPGSatfPFFGVAPAILNESGEELEGEAEGYLVFKQpwPGIMRtv 542
Cdd:PRK12316 4838 lFNGYGPTETTVTVLLWKARDG-----DACGAAYMPIGT---PLGNRSGYVLDGQLNPLPVGVAGELYLGG--EGVAR-- 4905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 543 yGNH-------ERFETTYFKKfPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVV 613
Cdd:PRK12316 4906 -GYLerpaltaERFVPDPFGA-PGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVI 4983
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 253970489 614 GHPHPVkGECLYCFVT-----LCDGHTFSPKLTEELKKQIREKIgpiatPDYIQNA-----PGLPKTRSGKIMRRVLRK 682
Cdd:PRK12316 4984 AQEGAV-GKQLVGYVVpqdpaLADADEAQAELRDELKAALRERL-----PEYMVPAhlvflARMPLTPNGKLDRKALPQ 5056
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
321-680 |
8.83e-14 |
|
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: 74.39 E-value: 8.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 321 EDPLFILYTSGSTGKPKGVV--------HTVGGYMLYVATTFKYV-------FDFHAEDVF--WCTadigwitghsyvty 383
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSSDRVlqfasiaFDVAAEEIYvtLLS-------------- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 384 gplanGATSVLFEGiPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGdEPVTKHSRASLQVLGTVGEPINPEAWLWY 463
Cdd:cd17644 172 -----GATLVLRPE-EMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLEL-LLSTIDLPSSLRLVIVGGEAVQPELVRQW 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 464 HRVVGaQRCPIVDTFWQTE----TGGHMLTPLPGATPMKPGSATfPFFGVAPAILNEsgeelegeaegylvFKQPWP-GI 538
Cdd:cd17644 245 QKNVG-NFIQLINVYGPTEatiaATVCRLTQLTERNITSVPIGR-PIANTQVYILDE--------------NLQPVPvGV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 539 MRTVY--------G-------NHERFETTYFKKFPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESAL 601
Cdd:cd17644 309 PGELHiggvglarGylnrpelTAEKFISHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVL 388
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 253970489 602 VEHEAVAEAAVVGHPHPVKGECLYCFVTlcdGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:cd17644 389 SQHNDVKTAVVIVREDQPGNKRLVAYIV---PHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
133-680 |
1.02e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 74.27 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 133 TTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVfagfsSESLCERILDSSCslli 212
Cdd:PRK05857 39 TSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMA-----DGNLPIAAIERFC---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 213 ttdafyrgeklvnlkELADEAlqkcqekgfpvrCCIVVKHLGRAELGMGDSTSQSPPIKRSCPDVQGKLKEKSKRVQPQI 292
Cdd:PRK05857 110 ---------------QITDPA------------AALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 293 SWNQGidlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGVvhtvggymLYVATTFKYVFD-FHAEDVFWctad 371
Cdd:PRK05857 163 NADQG----------------------SEDPLAMIFTSGTTGEPKAV--------LLANRTFFAVPDiLQKEGLNW---- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 372 IGWITGHSyvTYGPLAngATSV---------LFEG---IPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLL---MKFGDEP 436
Cdd:PRK05857 209 VTWVVGET--TYSPLP--ATHIgglwwiltcLMHGglcVTGGENTTSLLEILTTNAVATTCLVPTLLSKLvseLKSANAT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 437 VtkhsrASLQVLGTVG-EPINPEAwlwyhRVVGAQRCPIVDTFWQTETGGHMLTpLP----GATPMKPGSATFPFFGV-- 509
Cdd:PRK05857 285 V-----PSLRLVGYGGsRAIAADV-----RFIEATGVRTAQVYGLSETGCTALC-LPtddgSIVKIEAGAVGRPYPGVdv 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 510 --APAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKkfpGYYVTGDGCQRDQDGYYWITGRIDDMLNV 587
Cdd:PRK05857 354 ylAATDGIGPTAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMIIC 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 588 SGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFV---TLCDGHTfspklTEELKKQI----REKIGPIATPDY 660
Cdd:PRK05857 431 GGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVvasAELDESA-----ARALKHTIaarfRRESEPMARPST 505
|
570 580
....*....|....*....|
gi 253970489 661 IQNAPGLPKTRSGKIMRRVL 680
Cdd:PRK05857 506 IVIVTDIPRTQSGKVMRASL 525
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
115-684 |
1.17e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 74.09 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 115 KKLGDKVAFywegNEPGETtqITYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAG 193
Cdd:PRK12492 35 KKFADRPAF----SNLGVT--LSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 194 FSSESLCERILDSSCSLLITTDAFyrgEKLVNlKELADEALQkcqekgfpvrccivvkHLgrAELGMGDSTsqsppikrs 273
Cdd:PRK12492 109 YTAREMRHQFKDSGARALVYLNMF---GKLVQ-EVLPDTGIE----------------YL--IEAKMGDLL--------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 274 cPDVQGKL----KEKSKRVQPQISWNQGIDlWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYmly 349
Cdd:PRK12492 158 -PAAKGWLvntvVDKVKKMVPAYHLPQAVP-FKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNL--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 350 VAttfkyvfdfHAEDVFWCTADIGwITGHS---------------YVTYGPLAN-------GATSVLFegipTYP-DVNR 406
Cdd:PRK12492 233 VA---------NMLQVRACLSQLG-PDGQPlmkegqevmiaplplYHIYAFTANcmcmmvsGNHNVLI----TNPrDIPG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 407 LWSIVDKYKVTKFYTAPTAIRLLMkfgDEPVTKHSRAS-LQVLGTVGEPI---NPEAWlwyHRVVGaqrCPIVDTFWQTE 482
Cdd:PRK12492 299 FIKELGKWRFSALLGLNTLFVALM---DHPGFKDLDFSaLKLTNSGGTALvkaTAERW---EQLTG---CTIVEGYGLTE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 483 TgghmlTPLPGATPM----KPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHErfETTYFKKFP 558
Cdd:PRK12492 370 T-----SPVASTNPYgelaRLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGP--QVMKGYWQQPE--ATAEALDAE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 559 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsP 638
Cdd:PRK12492 441 GWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARD-----P 515
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 253970489 639 KLT-EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 684
Cdd:PRK12492 516 GLSvEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
290-681 |
1.17e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 73.96 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 290 PQISWNQGIDLwwHELMQEAGDECEPEWCDAEDPL---------FILYTSGSTGKPKGVVHTVG------GYMLYVATTF 354
Cdd:PRK12406 114 PEIAAAYRISP--ALLTPPAGAIDWEGWLAQQEPYdgppvpqpqSMIYTSGTTGHPKGVRRAAPtpeqaaAAEQMRALIY 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 355 kyvfdfhaedvfwctadiGWITGHSYVTYGPLANGATSV-------LFEGIPTYP--DVNRLWSIVDKYKVTKFYTAPTA 425
Cdd:PRK12406 192 ------------------GLKPGIRALLTGPLYHSAPNAyglragrLGGVLVLQPrfDPEELLQLIERHRITHMHMVPTM 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 426 IRLLMKFGDEPVTKHSRASLQvlgtvgepinpeawlwyHRVVGAQRCP--------------IVDTFWQTETGGhmltpL 491
Cdd:PRK12406 254 FIRLLKLPEEVRAKYDVSSLR-----------------HVIHAAAPCPadvkramiewwgpvIYEYYGSTESGA-----V 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 492 PGATP----MKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHERFETTYFKKfpGYYVTGDGC 567
Cdd:PRK12406 312 TFATSedalSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIA--GNPDFTYHNKPEKRAEIDRG--GFITSGDVG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 568 QRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELKKQ 647
Cdd:PRK12406 388 YLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDE---ADIRAQ 464
|
410 420 430
....*....|....*....|....*....|....
gi 253970489 648 IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:PRK12406 465 LKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
311-682 |
1.34e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 75.20 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 311 DECEPEWCD--------AEDP---LFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYvFDFHAEDVFWCTADIGWITGHs 379
Cdd:PRK12467 635 DEPADLLCGysghnpevALDPdnlAYVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLGV- 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 380 YVTYGPLANGATsVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLGtvGEpINPEA 459
Cdd:PRK12467 713 TELFGALASGAT-LHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQ--ASRVALPRPQRALVCG--GE-ALQVD 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 460 WLWYHRVVGAQrCPIVDTFWQTETGGHMLTPLPGATPMKPGSATF--PFFGVAPAILNEsgeelegeaegYLvfkQPWP- 536
Cdd:PRK12467 787 LLARVRALGPG-ARLINHYGPTETTVGVSTYELSDEERDFGNVPIgqPLANLGLYILDH-----------YL---NPVPv 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 537 -----------GIMRTVYG----NHERFETTYFKKfPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVES 599
Cdd:PRK12467 852 gvvgelyiggaGLARGYHRrpalTAERFVPDPFGA-DGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEA 930
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 600 ALVEHEAVAEAAVVGHPHPVKGECL-YCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRR 678
Cdd:PRK12467 931 RLLAQPGVREAVVLAQPGDAGLQLVaYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRK 1010
|
....
gi 253970489 679 VLRK 682
Cdd:PRK12467 1011 ALPK 1014
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
115-684 |
2.06e-13 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 73.37 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 115 KKLGDKVAFYWEGnepgetTQITYHQLLVQVCQF-SNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAG 193
Cdd:PRK08751 36 AKFADRPAYHSFG------KTITYREADQLVEQFaAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 194 FSSESLCERILDSSCSLLITTDAFYRGEKLVnlkeLADEALQKCQEK------GFPVRCCI--VVKHlgraelgmgdsts 265
Cdd:PRK08751 110 YTPRELKHQLIDSGASVLVVIDNFGTTVQQV----IADTPVKQVITTglgdmlGFPKAALVnfVVKY------------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 266 qsppIKRSCPDVqgklkekskRVQPQISWNQGIDLWWHELMqeagdecEPEWCDAEDPLFILYTSGSTGKPKGVvhtvgg 345
Cdd:PRK08751 173 ----VKKLVPEY---------RINGAIRFREALALGRKHSM-------PTLQIEPDDIAFLQYTGGTTGVAKGA------ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 346 yMLYVATTFKYVFDFHAedvfWCTADIGWITGHSYV-TYGPL-------ANGATSVLFEGiptypdVNRLWS-------I 410
Cdd:PRK08751 227 -MLTHRNLVANMQQAHQ----WLAGTGKLEEGCEVViTALPLyhifaltANGLVFMKIGG------CNHLISnprdmpgF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 411 VDKYKVTKFyTAPTAIRLLM-KFGDEP-VTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAqrcPIVDTFWQTETgghml 488
Cdd:PRK08751 296 VKELKKTRF-TAFTGVNTLFnGLLNTPgFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGL---TLVEAYGLTET----- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 489 TPLPGATPMK----PGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPwpGIMRTVYGNHErfETTYFKKFPGYYVTG 564
Cdd:PRK08751 367 SPAACINPLTlkeyNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGP--QVMKGYWKRPE--ETAKVMDADGWLHTG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 565 DGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDghtfsPKLT-EE 643
Cdd:PRK08751 443 DIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKD-----PALTaED 517
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 253970489 644 LKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 684
Cdd:PRK08751 518 VKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAA 558
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
129-681 |
9.36e-13 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 71.06 E-value: 9.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 129 EPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVF----AGFSSESLCERIL 204
Cdd:PRK07514 22 ETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGA----VFlplnTAYTLAELDYFIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 205 DSSCSLLITTDAfyrgeklvnlkelADEALQKcqekgfpvrccIVVKHLGRAELGMGDstsqsppikrscpDVQGKLKEk 284
Cdd:PRK07514 98 DAEPALVVCDPA-------------NFAWLSK-----------IAAAAGAPHVETLDA-------------DGTGSLLE- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 285 skrvqpqiswnqgidlwwheLMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAED 364
Cdd:PRK07514 140 --------------------AAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGN-LLSNALTLVDYWRFTPDD 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 365 VFWCTADIGWITGHSYVTYGPLANGA------------------TSVLFEGIPTypdvnrlwsivdkykvtkFYTaptai 426
Cdd:PRK07514 199 VLIHALPIFHTHGLFVATNVALLAGAsmiflpkfdpdavlalmpRATVMMGVPT------------------FYT----- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 427 RLLmkfgDEP-----VTKHSRasLQVLGTVgePINPE---AWlwyhrvvgAQRC--PIVDTFWQTETGghMLTPLPGATP 496
Cdd:PRK07514 256 RLL----QEPrltreAAAHMR--LFISGSA--PLLAEthrEF--------QERTghAILERYGMTETN--MNTSNPYDGE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 497 MKPGSATFPFFGVAPAILNESGEELEGEAEGYL-------VFKQPW--PgimrtvygnherfETTY--FKKfPGYYVTGD 565
Cdd:PRK07514 318 RRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMievkgpnVFKGYWrmP-------------EKTAeeFRA-DGFFITGD 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 566 GCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltEELK 645
Cdd:PRK07514 384 LGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDE---AAIL 460
|
570 580 590
....*....|....*....|....*....|....*.
gi 253970489 646 KQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:PRK07514 461 AALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
559-681 |
2.54e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 69.63 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 559 GYYVTGDGCQRDQDGYYWITGRID-DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTfs 637
Cdd:PRK07787 350 GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVA-- 427
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 253970489 638 pklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLR 681
Cdd:PRK07787 428 ---ADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
563-684 |
3.04e-12 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 69.84 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 563 TGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPkltE 642
Cdd:PRK08315 431 TGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTE---E 507
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 253970489 643 ELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIA 684
Cdd:PRK08315 508 DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM 549
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
319-686 |
4.88e-12 |
|
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: 68.72 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 319 DAEDPLFILYTSGSTGKPKGVV---HTVGGYMLYVATTFKY-----VFDF--HAEDVfwCTADIgwitghsyvtYGPLAN 388
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVViehRALSTSALAHGRALGLtsesrVLQFasYTFDV--SILEI----------FTTLAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 389 GATSVlfegIPTYPD-VNRLWSIVDKYKVTkfyTA---PTAIRLLmkfgdEPVTKhsrASLQVLGTVGEPINPEAW-LWY 463
Cdd:cd05918 172 GGCLC----IPSEEDrLNDLAGFINRLRVT---WAfltPSVARLL-----DPEDV---PSLRTLVLGGEALTQSDVdTWA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 464 HRV------------VGAQRCPIVD-------------TFWQTETGGH-MLTPLpGAT-------PMkpgsatfpffgVA 510
Cdd:cd05918 237 DRVrlinaygpaectIAATVSPVVPstdprnigrplgaTCWVVDPDNHdRLVPI-GAVgelliegPI-----------LA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 511 PAILNESGEELEgeaegylVFKQPWPGIMRTVYGNHERFettyfkkfpgyYVTGDGCQRDQDG--YYwiTGRIDDMLNVS 588
Cdd:cd05918 305 RGYLNDPEKTAA-------AFIEDPAWLKQEGSGRGRRL-----------YRTGDLVRYNPDGslEY--VGRKDTQVKIR 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 589 GHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGEC---LYCFVTLcDGHTFSPKLTEELKKQIREKIGPIAT-------- 657
Cdd:cd05918 365 GQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSspqLVAFVVL-DGSSSGSGDGDSLFLEPSDEFRALVAelrsklrq 443
|
410 420 430
....*....|....*....|....*....|....*.
gi 253970489 658 --PDY-IQNA----PGLPKTRSGKIMRRVLRKIAQN 686
Cdd:cd05918 444 rlPSYmVPSVflplSHLPLTASGKIDRRALRELAES 479
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
131-682 |
6.56e-12 |
|
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: 68.10 E-value: 6.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILDSS-CS 209
Cdd:cd17653 18 SLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARI-QAILRTSgAT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 210 LLITTDAfyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvq 289
Cdd:cd17653 97 LLLTTDS------------------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 290 pqiswnqgidlwwhelmqeagdecepewcdAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATT---------------F 354
Cdd:cd17653 104 ------------------------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPparldvgpgsrvaqvL 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 355 KYVFDFHAEDVFWCtadigwitghsyvtygpLANGATSVLFEGIPTYPDVNRlwsivdkyKVTKFYTAPTAIRLLmkfgd 434
Cdd:cd17653 154 SIAFDACIGEIFST-----------------LCNGGTLVLADPSDPFAHVAR--------TVDALMSTPSILSTL----- 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 435 epvtkhSRASLQVLGTV---GEPINP---EAWlWYHRVV----GAQRCPIVDTFWQTETGghmlTPLPGATPMkPGSATF 504
Cdd:cd17653 204 ------SPQDFPNLKTIflgGEAVPPsllDRW-SPGRRLynayGPTECTISSTMTELLPG----QPVTIGKPI-PNSTCY 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 505 pffgvapaILNESgeelegeaegylvfKQPWP------------GIMRTVYGNHERfETTYFKKFPGY-----YVTGDGC 567
Cdd:cd17653 272 --------ILDAD--------------LQPVPegvvgeicisgvQVARGYLGNPAL-TASKFVPDPFWpgsrmYRTGDYG 328
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 568 QRDQDGYYWITGRIDDMLNVSGHLLSTAEVES-ALVEHEAVAEAAVVGHphpvkGECLYCFVTlcdghtfsPKL--TEEL 644
Cdd:cd17653 329 RWTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAIVV-----NGRLVAFVT--------PETvdVDGL 395
|
570 580 590
....*....|....*....|....*....|....*...
gi 253970489 645 KKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:cd17653 396 RSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
119-682 |
8.25e-12 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 68.47 E-value: 8.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 119 DKVAFYwegnEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGFSS-- 196
Cdd:PLN02330 43 DKVAFV----EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG----VFSGANPta 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 197 -ESLCERILDSSCSLLITTDAFYRGEklvnlkeladealqkcqekgfpvrccivVKHLGRAELGMGDStsqsppikrscp 275
Cdd:PLN02330 115 lESEIKKQAEAAGAKLIVTNDTNYGK----------------------------VKGLGLPVIVLGEE------------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 276 dvqgklkekskRVQPQISWNQGIDLwwhelMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHT------------- 342
Cdd:PLN02330 155 -----------KIEGAVNWKELLEA-----ADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLThrnlvanlcsslf 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 343 -VGGYMLYVATTFKYVFDFHaedvfwctadIGWITGHSYVTygpLANGATSVLfegiptypdVNR--LWSIVDKYKVTKF 419
Cdd:PLN02330 219 sVGPEMIGQVVTLGLIPFFH----------IYGITGICCAT---LRNKGKVVV---------MSRfeLRTFLNALITQEV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 420 YTAPTAIRLLMKFGDEPVTKH---SRASLQVLGTVGEPINPEAWLWYH-RVVGAQrcpIVDTFWQTETGGHMLT---PLP 492
Cdd:PLN02330 277 SFAPIVPPIILNLVKNPIVEEfdlSKLKLQAIMTAAAPLAPELLTAFEaKFPGVQ---VQEAYGLTEHSCITLThgdPEK 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 493 GATPMKPGSATFPFFGVAPAILNESGEelegeaegyLVFKQPWPG--------IMRTVYGNHERFETTYFKKfpGYYVTG 564
Cdd:PLN02330 354 GHGIAKKNSVGFILPNLEVKFIDPDTG---------RSLPKNTPGelcvrsqcVMQGYYNNKEETDRTIDED--GWLHTG 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 565 DGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLcdghtfSPKLT--- 641
Cdd:PLN02330 423 DIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVI------NPKAKese 496
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 253970489 642 EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:PLN02330 497 EDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
304-682 |
9.15e-12 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 68.29 E-value: 9.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 304 ELMQEAGDECEPEWCDA-EDPLFILYTSGSTGKPKGVvhTVGGYMLYVATTFKYVFDFHAE-DVFWCTADIGWITGHSYV 381
Cdd:PLN02860 154 MLKQRALGTTELDYAWApDDAVLICFTSGTTGRPKGV--TISHSALIVQSLAKIAIVGYGEdDVYLHTAPLCHIGGLSSA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 382 tygpLAN---GATSVLfegIPTYpDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVL----GTVGEP 454
Cdd:PLN02860 232 ----LAMlmvGACHVL---LPKF-DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKIlnggGSLSSR 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 455 INPEAWLWYhrvvgaQRCPIVDTFWQTETGGHMltplpgaTPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQP 534
Cdd:PLN02860 304 LLPDAKKLF------PNAKLFSAYGMTEACSSL-------TFMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVGKPA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 535 ---------------------WPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLS 593
Cdd:PLN02860 371 phvelkigldessrvgriltrGPHVMLGYWGQNS--ETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVY 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 594 TAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLT-----------EELKKQIREK-IGPIATPD-Y 660
Cdd:PLN02860 449 PEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKenakknltlssETLRHHCREKnLSRFKIPKlF 528
|
410 420
....*....|....*....|..
gi 253970489 661 IQNAPGLPKTRSGKIMRRVLRK 682
Cdd:PLN02860 529 VQWRKPFPLTTTGKIRRDEVRR 550
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
558-688 |
3.75e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 65.79 E-value: 3.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 558 PGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFs 637
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSIS- 401
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 253970489 638 pklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDH 688
Cdd:PRK07445 402 ---LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRL 449
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
308-680 |
5.75e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 66.34 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 308 EAGDECEPEWCDAEDPL-FILYTSGSTGKPKGVVHTVGGYM-LYVATtfKYVFDFHAEDVfwctadigWITGHSYV---- 381
Cdd:PRK12467 1704 EGYSDSNPAVNLAPQNLaYVIYTSGSTGRPKGAGNRHGALVnRLCAT--QEAYQLSAADV--------VLQFTSFAfdvs 1773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 382 ---TYGPLANGAtSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFgDEPVTKHSraSLQVLGTVGEPINPE 458
Cdd:PRK12467 1774 vweLFWPLINGA-RLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQM-DEQVEHPL--SLRRVVCGGEALEVE 1849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 459 AW-LWYHRVVGAQrcpIVDTFWQTETGGHML------------TPLPGATPMkPGSATFpffgVAPAILNEsgeelegea 525
Cdd:PRK12467 1850 ALrPWLERLPDTG---LFNLYGPTETAVDVThwtcrrkdlegrDSVPIGQPI-ANLSTY----ILDASLNP--------- 1912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 526 egylvfkQPwPGIMRTVY--------GNH-------ERFETTYFKKFPG-YYVTGDGCQRDQDGYYWITGRIDDMLNVSG 589
Cdd:PRK12467 1913 -------VP-IGVAGELYlggvglarGYLnrpaltaERFVADPFGTVGSrLYRTGDLARYRADGVIEYLGRIDHQVKIRG 1984
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 590 HLLSTAEVESALVEHEAVAEAAVVGHPHPvKGECLYCFVT-----LCDGHTFSPKLTEELKKQIREKIgpiatPDYIQNA 664
Cdd:PRK12467 1985 FRIELGEIEARLREQGGVREAVVIAQDGA-NGKQLVAYVVptdpgLVDDDEAQVALRAILKNHLKASL-----PEYMVPA 2058
|
410 420
....*....|....*....|.
gi 253970489 665 -----PGLPKTRSGKIMRRVL 680
Cdd:PRK12467 2059 hlvflARMPLTPNGKLDRKAL 2079
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
321-674 |
7.96e-11 |
|
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: 64.33 E-value: 7.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 321 EDPLFILYTSGSTGKPKGVV---HTVGGYMLYVA--TTFKYVFDFHAEDVFWCTADIGW------ITGHSYVTYGPLANG 389
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMwrqEDIFRMLMGGAdfGTGEFTPSEDAHKAAAAAAGTVMfpapplMHGTGSWTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 390 ATSVLFEGIPTYPDvnRLWSIVDKYKVTKF------YTAPTaIRLLMKFGDEPVTkhsraSLQVLGTVGEPINPEawlwy 463
Cdd:cd05924 83 GQTVVLPDDRFDPE--EVWRTIEKHKVTSMtivgdaMARPL-IDALRDAGPYDLS-----SLFAISSGGALLSPE----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 464 hrvVGAQRCP------IVDTFWQTETGGHMLTPlpgATPMKPGSATFPFFGVAPAILNESgeelegeaegyLVFKQPWPG 537
Cdd:cd05924 150 ---VKQGLLElvpnitLVDAFGSSETGFTGSGH---SAGSGPETGPFTRANPDTVVLDDD-----------GRVVPPGSG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 538 IMRTV----------YGNHERFETTyFKKFPG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHE 605
Cdd:cd05924 213 GVGWIarrghiplgyYGDEAKTAET-FPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHP 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 253970489 606 AVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGK 674
Cdd:cd05924 292 AVYDVLVVGRPDERWGQEVVAVVQLREGAGVD---LEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
134-680 |
1.27e-10 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 65.07 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 134 TQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERIL-DSSCSLLI 212
Cdd:PRK10252 482 YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRL-KMMLeDARPSLLI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 213 TTDAFyrgeklvnlkeladealqkcQEKgFPvrccivvkhlgraelGMGDSTSQSPPIKRSCPDVQGKLkekskRVQPQi 292
Cdd:PRK10252 561 TTADQ--------------------LPR-FA---------------DVPDLTSLCYNAPLAPQGAAPLQ-----LSQPH- 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 293 swnqgidlwwhelmqeagdecepewcdaeDPLFILYTSGSTGKPKGVV--HT-VGGYMLYVATTFKyvfdFHAEDVFW-- 367
Cdd:PRK10252 599 -----------------------------HTAYIIFTSGSTGRPKGVMvgQTaIVNRLLWMQNHYP----LTADDVVLqk 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 368 --CTADIG-----WitghsyvtygPLANGATSVLFEgiptyPDVNR----LWSIVDKYKVTKFYTAPTairLLMKFGDEP 436
Cdd:PRK10252 646 tpCSFDVSvweffW----------PFIAGAKLVMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPS---MLAAFVASL 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 437 VTKHSRASLQVLGTV---GEPINPEAWLWYHRVVGAqrcPIVDTFWQTE---------TGGHMLTPLPGAtPMKPGsatF 504
Cdd:PRK10252 708 TPEGARQSCASLRQVfcsGEALPADLCREWQQLTGA---PLHNLYGPTEaavdvswypAFGEELAAVRGS-SVPIG---Y 780
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 505 PFFGVAPAILNESGeelegeaegylvfkQPWP-GIMRTVY--------GNH-------ERFETTYFKkfPG--YYVTGDG 566
Cdd:PRK10252 781 PVWNTGLRILDARM--------------RPVPpGVAGDLYltgiqlaqGYLgrpdltaSRFIADPFA--PGerMYRTGDV 844
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 567 CQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEH----EAVAEAAVVGHPHPVKGEC--LYCFVTLCDGhtfSPKL 640
Cdd:PRK10252 845 ARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALpdveQAVTHACVINQAAATGGDArqLVGYLVSQSG---LPLD 921
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 253970489 641 TEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:PRK10252 922 TSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
132-395 |
2.38e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 63.84 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLL 211
Cdd:PTZ00216 118 ETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 212 ITTdafyrGEKLVNLkeladeaLQKCQEKGFPvRCCIVvkHLGraelgmgdstsqsppikrSCPDvqgKLKEKSKRVqpq 291
Cdd:PTZ00216 198 VCN-----GKNVPNL-------LRLMKSGGMP-NTTII--YLD------------------SLPA---SVDTEGCRL--- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 292 ISWNQGIDLWWHELMQEAGDECEpewcDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFdfhaeDVFWCTAD 371
Cdd:PTZ00216 239 VAWTDVVAKGHSAGSHHPLNIPE----NNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLN-----DLIGPPEE 309
|
250 260
....*....|....*....|....*...
gi 253970489 372 igwitGHSYVTYGPLAN----GATSVLF 395
Cdd:PTZ00216 310 -----DETYCSYLPLAHimefGVTNIFL 332
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
563-680 |
2.50e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 63.13 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 563 TGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGE--CLycfvTLCDGHTFSPkl 640
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErvKA----KVISHEEIDP-- 368
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 253970489 641 tEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:PRK08308 369 -VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
319-677 |
2.77e-10 |
|
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: 63.23 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 319 DAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFdFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGI 398
Cdd:cd05914 87 DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVL-LGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 399 PT-------------YPDVNRLWSIVDKYKVTKFYTAPTAI---RLLMKFGDEPVTKHSRASLQ----------VLGtvG 452
Cdd:cd05914 166 PSakiialafaqvtpTLGVPVPLVIEKIFKMDIIPKLTLKKfkfKLAKKINNRKIRKLAFKKVHeafggnikefVIG--G 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 453 EPINPEAwLWYHRVVGAqrcPIVDTFWQTETGghmltPLPGATP---MKPGSATFPFFGVAPAILNESGEELEGEaegyL 529
Cdd:cd05914 244 AKINPDV-EEFLRTIGF---PYTIGYGMTETA-----PIISYSPpnrIRLGSAGKVIDGVEVRIDSPDPATGEGE----I 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 530 VFKQPwpGIMRTVYGNHERFETTYFKKfpGYYVTGDGCQRDQDGYYWITGRIDDM-LNVSGHLLSTAEVESALVEHEAVA 608
Cdd:cd05914 311 IVRGP--NVMKGYYKNPEATAEAFDKD--GWFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 609 EAAVV---------GHPHP----VKGECLycfvtlcdghtfsPKLTEELKKQIREKIGpIATPDY-------IQNAPgLP 668
Cdd:cd05914 387 ESLVVvqekklvalAYIDPdfldVKALKQ-------------RNIIDAIKWEVRDKVN-QKVPNYkkiskvkIVKEE-FE 451
|
....*....
gi 253970489 669 KTRSGKIMR 677
Cdd:cd05914 452 KTPKGKIKR 460
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
553-690 |
4.55e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 62.80 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 553 YFKK-----FPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCF 627
Cdd:PRK07008 398 YFRGdasplVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLV 477
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 253970489 628 VTLCDGHTFSpklTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQnDHDL 690
Cdd:PRK07008 478 VVKRPGAEVT---REELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFR-DYVL 536
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
558-682 |
6.63e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 61.60 E-value: 6.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 558 PGYYVTGDGCQRDqDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtLCDGHTfS 637
Cdd:PRK07824 233 PGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAV-VGDGGP-A 309
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 253970489 638 PKLtEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:PRK07824 310 PTL-EALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
131-680 |
7.23e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.88 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 131 GETtqITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 210
Cdd:PRK05691 2211 GQT--LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGL 2288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 211 LITTDAFYRGeklvnLKELADEALQKCQEKGFPVRccivvkhlgraelgmgDSTSQSPPIKRSCPDVQGklkekskrvqp 290
Cdd:PRK05691 2289 LLSDRALFEA-----LGELPAGVARWCLEDDAAAL----------------AAYSDAPLPFLSLPQHQA----------- 2336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 291 qiswnqgidlwwhelmqeagdecepewcdaedplFILYTSGSTGKPKGVVHTVGGYMLYVATTFKyVFDFHAEDvfwCTA 370
Cdd:PRK05691 2337 ----------------------------------YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADD---CEL 2378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 371 DIGWIT--GHSYVTYGPLANGATSVL-FEGiptYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFgdePVTKHSRASLQV 447
Cdd:PRK05691 2379 HFYSINfdAASERLLVPLLCGARVVLrAQG---QWGAEEICQLIREQQVSILGFTPSYGSQLAQW---LAGQGEQLPVRM 2452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 448 LGTVGEPINPEAWLWYHRVVGAQRcpIVDTFWQTETgghMLTPLPGATP--MKPGSATFPFFGVAPA----ILNESGEEL 521
Cdd:PRK05691 2453 CITGGEALTGEHLQRIRQAFAPQL--FFNAYGPTET---VVMPLACLAPeqLEEGAASVPIGRVVGArvayILDADLALV 2527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 522 EGEAEGYLvfkqpWPGIMRTVYGNH-------ERFETTYFKKFPG-YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLS 593
Cdd:PRK05691 2528 PQGATGEL-----YVGGAGLAQGYHdrpgltaERFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIE 2602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 594 TAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPK--LTEELKKQIREKIgpiatPDYIQNA-----PG 666
Cdd:PRK05691 2603 LGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDEAQaaLREALKAHLKQQL-----PDYMVPAhlillDS 2677
|
570
....*....|....
gi 253970489 667 LPKTRSGKIMRRVL 680
Cdd:PRK05691 2678 LPLTANGKLDRRAL 2691
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
319-680 |
9.11e-10 |
|
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: 61.65 E-value: 9.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 319 DAEDPLFILYTSGSTGKPKGVVHTVGGYM--------LY---------VATTFKYVFDFHAEDVFwctadIGWITGHSYV 381
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSVVnlrtslseRYfgrdngdeaVLFFSNYVFDFFVEQMT-----LALLNGQKLV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 382 tygplangatsVLFEGIPTYPDvnRLWSIVDKYKVTKFYTAPTAIRLLmKFGdepvtkhSRASLQVLGTVGEPINPEAwl 461
Cdd:cd17648 167 -----------VPPDEMRFDPD--RFYAYINREKVTYLSGTPSVLQQY-DLA-------RLPHLKRVDAAGEEFTAPV-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 462 wYHRVVGAQRCPIVDTFWQTETGGHML-TPLPGATPmKPGSATFPFFGVAPAILNESGeelegeaegylvfkQPWP---- 536
Cdd:cd17648 224 -FEKLRSRFAGLIINAYGPTETTVTNHkRFFPGDQR-FDKSLGRPVRNTKCYVLNDAM--------------KRVPvgav 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 537 --------GIMRTvYGNH-----ERFETTYFK--------KFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTA 595
Cdd:cd17648 288 gelylggdGVARG-YLNRpeltaERFLPNPFQteqerargRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 596 EVESALVEHEAVAEAAVVGHPHPVKGEC-----LYCFVTLCDGHtfspkLTE-ELKKQIREKIGPIATPDYIQNAPGLPK 669
Cdd:cd17648 367 EVEAALASYPGVRECAVVAKEDASQAQSriqkyLVGYYLPEPGH-----VPEsDLLSFLRAKLPRYMVPARLVRLEGIPV 441
|
410
....*....|.
gi 253970489 670 TRSGKIMRRVL 680
Cdd:cd17648 442 TINGKLDVRAL 452
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
132-680 |
1.20e-09 |
|
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: 61.34 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 132 ETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGAlhsiVFAGFSSESLCERI----LDSS 207
Cdd:cd17656 10 ENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGG----AFVPIDPEYPEERRiyimLDSG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 208 CSLLITtdafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppiKRSCPDVQGKLKEKSKR 287
Cdd:cd17656 86 VRVVLT---------------------------------------------------------QRHLKSKLSFNKSTILL 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 288 VQPQISwnqgidlwwHELMQEAGDECEpewcdAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFW 367
Cdd:cd17656 109 EDPSIS---------QEDTSNIDYINN-----SDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQ 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 368 ---CTADIGWITGHSYVTYGplanGATSVLFEgiPTYPDVNRLWSIVDKYKVTKFYTaPTAIrLLMKFGDEPVTKHSRAS 444
Cdd:cd17656 175 fatCSFDVCYQEIFSTLLSG----GTLYIIRE--ETKRDVEQLFDLVKRHNIEVVFL-PVAF-LKFIFSEREFINRFPTC 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 445 LQVLGTVGEPI---NPeawlwYHRVVGAQRCPIVDTFWQTETggHMLT--------PLPGATPM-KPGSATFPFfgvapa 512
Cdd:cd17656 247 VKHIITAGEQLvitNE-----FKEMLHEHNVHLHNHYGPSET--HVVTtytinpeaEIPELPPIgKPISNTWIY------ 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 513 ILNESgeelegeaegylvfKQPWP-GIMRTVY--------GNHERFETTYFKKFPG-------YYVTGDGCQRDQDGYYW 576
Cdd:cd17656 314 ILDQE--------------QQLQPqGIVGELYisgasvarGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIE 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 577 ITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVtlCDGHTFSpklTEELKKQIREKIGPIA 656
Cdd:cd17656 380 FLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYF--VMEQELN---ISQLREYLAKQLPEYM 454
|
570 580
....*....|....*....|....
gi 253970489 657 TPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:cd17656 455 IPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
131-387 |
1.22e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 61.67 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 210
Cdd:PLN02387 102 GEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 211 LITtdafyrGEKlvNLKELAD--EALQkcqekgfpvrcciVVKHLgraeLGMGDSTSQSPPikrSCPDVQGKLKEKSKRV 288
Cdd:PLN02387 182 VIC------DSK--QLKKLIDisSQLE-------------TVKRV----IYMDDEGVDSDS---SLSGSSNWTVSSFSEV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 289 QpqiswnqgidlwwhELMQEAgdECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVfwc 368
Cdd:PLN02387 234 E--------------KLGKEN--PVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--- 294
|
250
....*....|....*....
gi 253970489 369 tadigwitghsYVTYGPLA 387
Cdd:PLN02387 295 -----------YLAYLPLA 302
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
559-680 |
1.25e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 61.17 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 559 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSp 638
Cdd:PRK13383 396 GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVD- 474
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 253970489 639 klTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:PRK13383 475 --AAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
119-680 |
2.56e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 60.95 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 119 DKVAFYWEGNepgettQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSES 198
Cdd:PRK05691 1146 ERIALVWDGG------SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAER 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 199 LCERILDSSCSLLITTDAFYrgEKLVNLKELADEALQKCQEKGFPVrccivvkhlgraelgmgdstsqSPPikrscpdvq 278
Cdd:PRK05691 1220 LAYMLADSGVELLLTQSHLL--ERLPQAEGVSAIALDSLHLDSWPS----------------------QAP--------- 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 279 gklkekskrvqpqiswnqGIDLWWHELMqeagdecepewcdaedplFILYTSGSTGKPKGVVHTVGGYMLYVA-TTFKYV 357
Cdd:PRK05691 1267 ------------------GLHLHGDNLA------------------YVIYTSGSTGQPKGVGNTHAALAERLQwMQATYA 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 358 FDfhAEDVFWCTADIGWITGhSYVTYGPLANGATSVLfEGIPTYPDVNRLWSIVDKYKVTKFYTAPTairLLMKFGDEPV 437
Cdd:PRK05691 1311 LD--DSDVLMQKAPISFDVS-VWECFWPLITGCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPP---LLQLFIDEPL 1383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 438 TKHSRaSLQVLGTVGEPINPE---------AWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLpgatpmkpGSatfPFFG 508
Cdd:PRK05691 1384 AAACT-SLRRLFSGGEALPAElrnrvlqrlPQVQLHNRYGPTETAINVTHWQCQAEDGERSPI--------GR---PLGN 1451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 509 VAPAILNESGEELEGEAEGYLVFKQpwPGIMRTVYG----NHERFETTYFKKfPG--YYVTGDGCQRDQDGYYWITGRID 582
Cdd:PRK05691 1452 VLCRVLDAELNLLPPGVAGELCIGG--AGLARGYLGrpalTAERFVPDPLGE-DGarLYRTGDRARWNADGALEYLGRLD 1528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 583 DMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHpHPVKGECLYCFVTLCDGHTFSPkltEELKKQIREKIgpiatPDYIQ 662
Cdd:PRK05691 1529 QQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVR-EGAAGAQLVGYYTGEAGQEAEA---ERLKAALAAEL-----PEYMV 1599
|
570 580
....*....|....*....|...
gi 253970489 663 NA-----PGLPKTRSGKIMRRVL 680
Cdd:PRK05691 1600 PAqlirlDQMPLGPSGKLDRRAL 1622
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
559-682 |
2.66e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 60.18 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 559 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 638
Cdd:PRK05620 430 GWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTR 509
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 253970489 639 KLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:PRK05620 510 ETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
133-682 |
3.19e-09 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 59.75 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 133 TTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLI 212
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 213 TtdafyrgeklvNLKELADEAlqkcqekgfpvrccivvkhlgraelgmgdsTSQSPPikrSCPDVqgklkekskrvqpqi 292
Cdd:cd05939 81 F-----------NLLDPLLTQ------------------------------SSTEPP---SQDDV--------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 293 swnqgidlwwhelmqeagdecepewcDAEDPLFILYTSGSTGKPKGVVHTVGGYmLYVATTFKYVFDFHAEDVFWCTADI 372
Cdd:cd05939 102 --------------------------NFRDKLFYIYTSGTTGLPKAAVIVHSRY-YRIAAGAYYAFGMRPEDVVYDCLPL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 373 gWITGHSYVTYGP-LANGATSVLFEGIptypDVNRLWSIVDKYKVTKF-YTAPTAIRLLMKFGDEPVTKHsraslQVLGT 450
Cdd:cd05939 155 -YHSAGGIMGVGQaLLHGSTVVIRKKF----SASNFWDDCVKYNCTIVqYIGEICRYLLAQPPSEEEQKH-----NVRLA 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 451 VGEPINPEAWlwyHRVVGAQRCPIVDTFWQTETGGHMLTPLPGatpmKPGSATF-PFFG--VAPAIL---NESGEELEGE 524
Cdd:cd05939 225 VGNGLRPQIW---EQFVRRFGIPQIGEFYGATEGNSSLVNIDN----HVGACGFnSRILpsVYPIRLikvDEDTGELIRD 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 525 AEGYLVFKQPW-PGIM----------RTVYG------NHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNV 587
Cdd:cd05939 298 SDGLCIPCQPGePGLLvgkiiqndplRRFDGyvnegaTNKKIARDVFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRW 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 588 SGHLLSTAEVESALVEHEAVAEAAVVGHPHP-VKGEC----LYCFVTLCDGHTFSPKLTEELKkqirekigPIATPDYIQ 662
Cdd:cd05939 378 KGENVSTTEVEGILSNVLGLEDVVVYGVEVPgVEGRAgmaaIVDPERKVDLDRFSAVLAKSLP--------PYARPQFIR 449
|
570 580
....*....|....*....|
gi 253970489 663 NAPGLPKTRSGKIMRRVLRK 682
Cdd:cd05939 450 LLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
319-685 |
3.36e-09 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 60.32 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 319 DAEDPLFILYTSGSTGKPKGVV---HTVGGYMLYVATtfkyVFDFHAEDVfwctadigwITG-----HSY----VTYGPL 386
Cdd:PRK08633 780 KPDDTATIIFSSGSEGEPKGVMlshHNILSNIEQISD----VFNLRNDDV---------ILSslpffHSFgltvTLWLPL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 387 ANGATSVlFEGIPTypDVNRLWSIVDKYKVTKFYTAPTAIRLLMKfgDEPVTKHSRASLQVLgtvgepinpeawlwyhrV 466
Cdd:PRK08633 847 LEGIKVV-YHPDPT--DALGIAKLVAKHRATILLGTPTFLRLYLR--NKKLHPLMFASLRLV-----------------V 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 467 VGAQRCP--IVDTFWQ------------TETgghmlTP-----LPGA--------TPMKPGSATFPFFGVAPAILNESGE 519
Cdd:PRK08633 905 AGAEKLKpeVADAFEEkfgirilegygaTET-----SPvasvnLPDVlaadfkrqTGSKEGSVGMPLPGVAVRIVDPETF 979
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 520 ELEGEAEGYLVFKQPwPGIMRTVYGNHERF-ETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVE 598
Cdd:PRK08633 980 EELPPGEDGLILIGG-PQVMKGYLGDPEKTaEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVE 1058
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 599 SALveHEAVAEA----AVVGHPHPVKGECLycfVTLcdgHTFSPKLTEELKKQIRE-KIGPIATPDYIQNAPGLPKTRSG 673
Cdd:PRK08633 1059 EEL--AKALGGEevvfAVTAVPDEKKGEKL---VVL---HTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSG 1130
|
410
....*....|..
gi 253970489 674 KIMRRVLRKIAQ 685
Cdd:PRK08633 1131 KLDLKGLKELAL 1142
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
137-682 |
3.45e-09 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 59.75 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 137 TYHQLLVQVCQFSNVLRKQ-GIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESL--CERIldSSCSLLIT 213
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLihCLKL--SGSRFVIV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 214 TDafyrgeklvnlkeladealqkcqekgfpvrccivvkhlgraelgmgdstsqsppikrscpdvqgklkekskrvqpqis 293
Cdd:cd05937 85 DP------------------------------------------------------------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 294 wnqgidlwwhelmqeagdecepewcdaEDPLFILYTSGSTGKPKGVVHTVGgyMLYV-ATTFKYVFDFHAEDVFWCTADI 372
Cdd:cd05937 87 ---------------------------DDPAILIYTSGTTGLPKAAAISWR--RTLVtSNLLSHDLNLKNGDRTYTCMPL 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 373 GWITGHSYVTYGPLANGATSVL---FEgiptypdVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRaslqVLG 449
Cdd:cd05937 138 YHGTAAFLGACNCLMSGGTLALsrkFS-------ASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHK----VRV 206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 450 TVGEPINPEAWLWYHRVVGAqrcPIVDTFWQ-TETGGHMLTPLPGAtpmkpgsatfpfFGvAPAILNESGEELEGEAEGY 528
Cdd:cd05937 207 AWGNGLRPDIWERFRERFNV---PEIGEFYAaTEGVFALTNHNVGD------------FG-AGAIGHHGLIRRWKFENQV 270
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 529 LVFK------QPW---------------PG--IMRTVYGNHERFETTY--------------FKKFPGYYVTGDGCQRDQ 571
Cdd:cd05937 271 VLVKmdpetdDPIrdpktgfcvrapvgePGemLGRVPFKNREAFQGYLhnedatesklvrdvFRKGDIYFRTGDLLRQDA 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 572 DGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVG---HPHPVKGECLYCfvTLCDGHTF-SPKLTEELKKQ 647
Cdd:cd05937 351 DGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGvkvPGHDGRAGCAAI--TLEESSAVpTEFTKSLLASL 428
|
570 580 590
....*....|....*....|....*....|....*
gi 253970489 648 IREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRK 682
Cdd:cd05937 429 ARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
115-682 |
3.94e-09 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 59.56 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 115 KKLGDKVAFYWEGNEPGETTQITYHQLLVQVCQFSNVLRKQGiQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGF 194
Cdd:cd05931 4 AARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 195 SSESLcERIL----DSSCSLLITTDAFyrgeklvnLKELADEALQKCQEKGFPVRCCivvkhlgraelgmgdstsqsppi 270
Cdd:cd05931 83 PGRHA-ERLAailaDAGPRVVLTTAAA--------LAAVRAFAASRPAAGTPRLLVV----------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 271 krscpdvqgklkekskrvqpqiswnqgiDLwwheLMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYV 350
Cdd:cd05931 131 ----------------------------DL----LPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 351 ATTFKyVFDFHAED--VFW--CTADIGWITGhsyvTYGPLANGATSVLFEgiPTY----PdvnRLW-SIVDKYKVTkFYT 421
Cdd:cd05931 179 RQIRR-AYGLDPGDvvVSWlpLYHDMGLIGG----LLTPLYSGGPSVLMS--PAAflrrP---LRWlRLISRYRAT-ISA 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 422 APTairllmkFG-DEPVTKHSRA--------SLQVLGTVGEPINPEAwlwyhrvvgaqrcpiVDTFwQTETGGHMLTP-- 490
Cdd:cd05931 248 APN-------FAyDLCVRRVRDEdlegldlsSWRVALNGAEPVRPAT---------------LRRF-AEAFAPFGFRPea 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 491 -LPG-----AT---PMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVF-------------------KQP-------- 534
Cdd:cd05931 305 fRPSyglaeATlfvSGGPPGTGPVVLRVDRDALAGRAVAVAADDPAARELvscgrplpdqevrivdpetGRElpdgevge 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 535 -W---PGIMRTVYGNHERFETTYFKKFP----GYYVTGD-GcqRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHE 605
Cdd:cd05931 385 iWvrgPSVASGYWGRPEATAETFGALAAtdegGWLRTGDlG--FLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAH 462
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 606 AV---AEAAVVGHPHPVkGECLycFVTLCDGHTFSPKLTEELKKQIREKIGP---IATPDYIQNAPG-LPKTRSGKIMRR 678
Cdd:cd05931 463 PAlrpGCVAAFSVPDDG-EERL--VVVAEVERGADPADLAAIAAAIRAAVARehgVAPADVVLVRPGsIPRTSSGKIQRR 539
|
....
gi 253970489 679 VLRK 682
Cdd:cd05931 540 ACRA 543
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
135-218 |
3.90e-08 |
|
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: 56.21 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 135 QITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESL--CERIldSSCSLLI 212
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLahCLNV--SSAKHLV 80
|
....*.
gi 253970489 213 TTDAFY 218
Cdd:cd05940 81 VDAALY 86
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
561-680 |
8.30e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.94 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 561 YVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAvVGHPHPVKGECLYCFVTLCDGHTFSPKL 640
Cdd:PRK05691 4104 YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGAL 4182
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 253970489 641 TEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:PRK05691 4183 LERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
318-686 |
3.66e-07 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 53.44 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 318 CDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKyVFDFHAEDVF--WCTADigWITGHSYVTYGPLANGATSVlf 395
Cdd:cd05906 164 SRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQ-HNGLTPQDVFlnWVPLD--HVGGLVELHLRAVYLGCQQV-- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 396 eGIPT---YPDVNRLWSIVDKYKVTkfYT-APT-AIRLLMKFGDEPVTKH-SRASLQVLGTVGEPINP---EAWLWYHRV 466
Cdd:cd05906 239 -HVPTeeiLADPLRWLDLIDRYRVT--ITwAPNfAFALLNDLLEEIEDGTwDLSSLRYLVNAGEAVVAktiRRLLRLLEP 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 467 VGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGvapailnesgeelegeaegylvfkQPWPGI-MRTVYGN 545
Cdd:cd05906 316 YGLPPDAIRPAFGMTETCSGVIYSRSFPTYDHSQALEFVSLG------------------------RPIPGVsMRIVDDE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 546 HE--------RFETTYFKKFPGYY---------VTGDGCQRDQD------GYYWITGRIDDMLNVSGHLLSTAEVESALV 602
Cdd:cd05906 372 GQllpegevgRLQVRGPVVTKGYYnnpeanaeaFTEDGWFRTGDlgfldnGNLTITGRTKDTIIVNGVNYYSHEIEAAVE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 603 EHEAVAE--AAVVGHPHPVKGECLYCFVtlcdghtFSPKLTE-----ELKKQIR----EKIGpiATPDYI----QNApgL 667
Cdd:cd05906 452 EVPGVEPsfTAAFAVRDPGAETEELAIF-------FVPEYDLqdalsETLRAIRsvvsREVG--VSPAYLiplpKEE--I 520
|
410
....*....|....*....
gi 253970489 668 PKTRSGKIMRRVLRKIAQN 686
Cdd:cd05906 521 PKTSLGKIQRSKLKAAFEA 539
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
559-673 |
8.52e-07 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 51.53 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 559 GYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSP 638
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTE 296
|
90 100 110
....*....|....*....|....*....|....*
gi 253970489 639 kltEELKKQIREKIGPIATPDYIQNAPGLPKTRSG 673
Cdd:cd17636 297 ---AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
314-460 |
8.87e-07 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 52.21 E-value: 8.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 314 EPEWCDAEDPLFILYTSGSTGKPKGVVHTVGgymlyvattfkyvfDFHA------EDVFWCTADIGWITGHSYVTYGPlA 387
Cdd:PRK09274 167 PMADLAPDDMAAILFTSGSTGTPKGVVYTHG--------------MFEAqiealrEDYGIEPGEIDLPTFPLFALFGP-A 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 388 NGATSVLFEGIPTYP-DVN--RLWSIVDKYKVTKFYTAPTAIrllmkfgdEPVTKHSRASLQVLGTV------GEPINPE 458
Cdd:PRK09274 232 LGMTSVIPDMDPTRPaTVDpaKLFAAIERYGVTNLFGSPALL--------ERLGRYGEANGIKLPSLrrvisaGAPVPIA 303
|
..
gi 253970489 459 AW 460
Cdd:PRK09274 304 VI 305
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
131-388 |
1.31e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 51.77 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLcERILD-SSCS 209
Cdd:PLN02861 73 GPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAV-EFIINhAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 210 LlittdAFYRGEKLvnlkeladEALQKCQEKgfpvrcCivVKHLgRAELGMGDSTSQsppikrscpdvqgkLKEKSKrvq 289
Cdd:PLN02861 152 I-----AFVQESKI--------SSILSCLPK------C--SSNL-KTIVSFGDVSSE--------------QKEEAE--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 290 pqiswNQGIDLW-WHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFdfhaedvfwc 368
Cdd:PLN02861 193 -----ELGVSCFsWEEFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLK---------- 257
|
250 260
....*....|....*....|
gi 253970489 369 TADIGWITGHSYVTYGPLAN 388
Cdd:PLN02861 258 VTDRVATEEDSYFSYLPLAH 277
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
320-645 |
3.37e-06 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 50.15 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 320 AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVAtTFKYVFDFHAEDVFWCTADIgwitghsYVTYGPlANGATSVLFEGIP 399
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTFAAQID-ALRQLYGIRPGEVDLATFPL-------FALFGP-ALGLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 400 TYP---DVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEpvTKHSRASLQVLGTVGEPINPEAWLWYHRVV--------- 467
Cdd:cd05910 155 TRParaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQ--HGITLPSLRRVLSAGAPVPIALAARLRKMLsdeaeiltp 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 468 -GAQRC-PIvdtfwqTETGGHMLTPLPGATPmKPGSAT---FPFFGVAPAILNESGEELEGEAEGYLVfkQPW------- 535
Cdd:cd05910 233 yGATEAlPV------SSIGSRELLATTTAAT-SGGAGTcvgRPIPGVRVRIIEIDDEPIAEWDDTLEL--PRGeigeitv 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 536 --PGIMRTVYGnheRFETTYFKKFPG-----YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVA 608
Cdd:cd05910 304 tgPTVTPTYVN---RPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVR 380
|
330 340 350
....*....|....*....|....*....|....*..
gi 253970489 609 EAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELK 645
Cdd:cd05910 381 RSALVGVGKPGCQLPVLCVEPLPGTITPRARLEQELR 417
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
600-709 |
3.71e-06 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 49.76 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 600 ALVEHEAVAEAAVVGHPHPVKGECLYCFVtlcdgHTFSPKLTEELKKQIREKIGPIAtPDYIQNAPGLPKTRSGKIMRRV 679
Cdd:PRK09188 248 ALKSDPAVSDVAIALFSLPAKGVGLYAFV-----EAELPADEKSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVRDDI 321
|
90 100 110
....*....|....*....|....*....|..
gi 253970489 680 LRKIAQNDHDLGD--MSTVADPSVISHLFSHR 709
Cdd:PRK09188 322 LRLIAMNQIDELDdlLREPEIRGLVEAIAAHR 353
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
312-395 |
5.09e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 49.52 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 312 ECEPEWCD--AEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDvfwctadigwitgHSYVTYGPLAN- 388
Cdd:cd17639 77 ECSAIFTDgkPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPD-------------DRYLAYLPLAHi 143
|
90
....*....|
gi 253970489 389 ---GATSVLF 395
Cdd:cd17639 144 felAAENVCL 153
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
319-680 |
1.58e-05 |
|
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: 47.93 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 319 DAEDPLFILYTSGSTGKPKGVV---HTvggyMLYVATTFKYVFDFHAEDVFWCTADIGWiTGHSYVTYGPLANGAT-SVL 394
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMiehHN----LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAGAAlHVV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 395 FEGIPTypDVNRLWSIVDKYKVTKFYTaPTAIRllmkfgdEPVTKHSRASLQVLGTVGEPINpeawlwyhrVVGAQRCPI 474
Cdd:cd17645 177 PSERRL--DLDALNDYFNQEGITISFL-PTGAA-------EQFMQLDNQSLRVLLTGGDKLK---------KIERKGYKL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 475 VDTFWQTETgghmlTPLPGATPMKPGSATFPFfGVAPA-----ILNESGEELEGEAEGYLVFKQPwpGIMRtvyGNHERF 549
Cdd:cd17645 238 VNNYGPTEN-----TVVATSFEIDKPYANIPI-GKPIDntrvyILDEALQLQPIGVAGELCIAGE--GLAR---GYLNRP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 550 ETTYfKKF------PG--YYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKG 621
Cdd:cd17645 307 ELTA-EKFivhpfvPGerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGR 385
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 253970489 622 ECLYCFVTlcdghtfSPKLT--EELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVL 680
Cdd:cd17645 386 KYLVAYVT-------APEEIphEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
131-213 |
3.90e-05 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 46.82 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 131 GETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSL 210
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
...
gi 253970489 211 LIT 213
Cdd:cd17639 81 IFT 83
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
314-682 |
4.68e-05 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 46.71 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 314 EPEWCDAEDPL-FILYTSGSTGKPKGVV---HTVGGYMLYVATTfkyvFDFHAEDVF--W--CTADIGWITGHsyvtYGP 385
Cdd:cd05908 98 EEVLCELADELaFIQFSSGSTGDPKGVMlthENLVHNMFAILNS----TEWKTKDRIlsWmpLTHDMGLIAFH----LAP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 386 LANGATSVLfegIPTYPDVNR--LW-SIVDKYKVTKFYTAPTAIRLLMK-FGDEPVTKHSRASLQVLGTVGEPINPE--- 458
Cdd:cd05908 170 LIAGMNQYL---MPTRLFIRRpiLWlKKASEHKATIVSSPNFGYKYFLKtLKPEKANDWDLSSIRMILNGAEPIDYElch 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 459 AWLWYHRVVGAQRCPIVDTFWQTETGghmltplPGATPMKPGSATFPFF--------GV-APAILNESGEELEGEAEGY- 528
Cdd:cd05908 247 EFLDHMSKYGLKRNAILPVYGLAEAS-------VGASLPKAQSPFKTITlgrrhvthGEpEPEVDKKDSECLTFVEVGKp 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 529 LVFKQpwpgiMRTVYGNHERFETTYFKKF--------PGYY---------VTGDGCQR--DQ----DGYYWITGRIDDML 585
Cdd:cd05908 320 IDETD-----IRICDEDNKILPDGYIGHIqirgknvtPGYYnnpeatakvFTDDGWLKtgDLgfirNGRLVITGREKDII 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 586 NVSGHLLSTAEVESALVEHEAVAEAAVVG---HPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIG-------PI 655
Cdd:cd05908 395 FVNGQNVYPHDIERIAEELEGVELGRVVAcgvNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKRGGwqinevlPI 474
|
410 420
....*....|....*....|....*..
gi 253970489 656 ATpdyiqnapgLPKTRSGKIMRRVLRK 682
Cdd:cd05908 475 RR---------IPKTTSGKVKRYELAQ 492
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
558-686 |
5.45e-05 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 46.63 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 558 PGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTlcdghtfS 637
Cdd:PRK08043 590 RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTT-------D 662
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 253970489 638 PKLT-EELKKQIREKIGP-IATPDYIQNAPGLPKTRSGKIMRRVLRKIAQN 686
Cdd:PRK08043 663 SELTrEKLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGKPDFVTLKSMVDE 713
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
108-216 |
7.04e-05 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 46.27 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 108 LDRNVHEkkLGDKVAFYW---EGNEPGETTQITYHQLLVQVCQFSNVLrKQGIQKGDRVAIYMPMIPELVVAMLACARIG 184
Cdd:PRK12476 40 IERNIAN--VGDTVAYRYldhSHSAAGCAVELTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVAGFFAAIKAG 116
|
90 100 110
....*....|....*....|....*....|....*.
gi 253970489 185 ALHSIVFA----GfSSESLCERILDSSCSLLITTDA 216
Cdd:PRK12476 117 TIAVPLFApelpG-HAERLDTALRDAEPTVVLTTTA 151
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
297-387 |
1.59e-04 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 44.90 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 297 GIDLW-WHELMQE-AGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFwctaDIgw 374
Cdd:cd05927 88 GVKVYsLEEFEKLgKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPT----DV-- 161
|
90
....*....|...
gi 253970489 375 itghsYVTYGPLA 387
Cdd:cd05927 162 -----YISYLPLA 169
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
319-401 |
3.55e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 44.19 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 319 DAEDPLFILYTSGSTGKPKGVV--HTvggYMLYVATTFKYVFDFHAEDVFWCTADIgwitGHSyvtYGpLANGATSVLFE 396
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVlsHR---NLLANRAQVAARIDFSPEDKVFNALPV----FHS---FG-LTGGLVLPLLS 859
|
....*
gi 253970489 397 GIPTY 401
Cdd:PRK06814 860 GVKVF 864
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
137-350 |
5.66e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 43.27 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 137 TYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARigalHSIVfagfsseslcerildssCSLLITTDA 216
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAA----HSLI-----------------CVPLYDTLG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 217 FYRGEKLVNLKELADEALQKCQEKGFPVRCCIVVKHLGraelGMGDSTSQSPPIKRSCPDVQGKLkekskrvqpqISWNQ 296
Cdd:PLN02430 137 PGAVDYIVDHAEIDFVFVQDKKIKELLEPDCKSAKRLK----AIVSFTSVTEEESDKASQIGVKT----------YSWID 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 253970489 297 gidlWWHELMQEAGDECEPEwcdAEDPLFILYTSGSTGKPKGVVHTVGGYMLYV 350
Cdd:PLN02430 203 ----FLHMGKENPSETNPPK---PLDICTIMYTSGTSGDPKGVVLTHEAVATFV 249
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
119-339 |
1.16e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 42.19 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 119 DKVAFYWEGnepgetTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGalHSIVFAGFSSES 198
Cdd:PRK04813 17 DFPAYDYLG------EKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG--HAYIPVDVSSPA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 199 lcERILD----SSCSLLITTDAFyrGEKLVNLKELADEALQKCQEKGFPVrccivvkhlgraelgmgDSTSQsppikrsc 274
Cdd:PRK04813 89 --ERIEMiievAKPSLIIATEEL--PLEILGIPVITLDELKDIFATGNPY-----------------DFDHA-------- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 253970489 275 pdVQGklkekskrvqpqiswnqgidlwwhelmqeagdecepewcdaEDPLFILYTSGSTGKPKGV 339
Cdd:PRK04813 140 --VKG-----------------------------------------DDNYYIIFTSGTTGKPKGV 161
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
319-615 |
1.37e-03 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 41.96 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 319 DAEDPLFILYTSGSTGKPKGVVHTVGGyMLYVATTFKYVFDFHAEDVFWCTADIgWitgHSY---VTYGPLANGAtSVLF 395
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLSILPI-W---HSYersAEYFIFACGC-SQAY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 396 EGIPTYPD------------VNRLWSIVDKYKVTKFYTAPTAIRLLMKFgdepvtkhsrasLQVLGTVGEPINpeawlwy 463
Cdd:cd17640 160 TSIRTLKDdlkrvkphyivsVPRLWESLYSGIQKQVSKSSPIKQFLFLF------------FLSGGIFKFGIS------- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 464 hrvvGAQRCPI-VDTFWQ------------TETGghmltplPGATPMKP-----GSATFPFFGVAPAILNESGEELEGEA 525
Cdd:cd17640 221 ----GGGALPPhVDTFFEaigievlngyglTETS-------PVVSARRLkcnvrGSVGRPLPGTEIKIVDPEGNVVLPPG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 526 EGYLVFKQPwPGIMRTVYGNHErfETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVS-GHLLSTAEVESALVEH 604
Cdd:cd17640 290 EKGIVWVRG-PQVMKGYYKNPE--ATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRS 366
|
330
....*....|.
gi 253970489 605 EAVAEAAVVGH 615
Cdd:cd17640 367 PFIEQIMVVGQ 377
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
115-213 |
2.38e-03 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 41.00 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 253970489 115 KKLGDKVAFYWEGNepgettQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGF 194
Cdd:cd17645 9 ERTPDHVAVVDRGQ------SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82
|
90
....*....|....*....
gi 253970489 195 SSESLCERILDSSCSLLIT 213
Cdd:cd17645 83 PGERIAYMLADSSAKILLT 101
|
|
| |
