|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
30-664 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1172.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 30 IDAYFKFHRQTVENLESFWESVAKELEWFKPWDKVLDAsNPPFYKWFVGGRLNLSYLAVDRHVKTWrKNKLAIEWEGEPv 109
Cdd:PRK00174 16 MEQYKALYQESVEDPEGFWAEQAKRLDWFKPFDTVLDW-NAPFIKWFEDGELNVSYNCLDRHLKTR-GDKVAIIWEGDD- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 110 dengyPTDRRKLTYYDLYREVNRVAYMLKqNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERI 189
Cdd:PRK00174 93 -----PGDSRKITYRELHREVCRFANALK-SLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 190 NDSQSRIVITADGFWRRGRVVRLKEVVDAALEKATGVESVIVLPRLGlKDVPMTEGRDYWWNKLMQGipPNAYIEPEPVE 269
Cdd:PRK00174 167 IDAGAKLVITADEGVRGGKPIPLKANVDEALANCPSVEKVIVVRRTG-GDVDWVEGRDLWWHELVAG--ASDECEPEPMD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 270 SEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAP 349
Cdd:PRK00174 244 AEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 350 DYPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKVAFGSTWW 429
Cdd:PRK00174 324 NYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVGGERCPIVDTWW 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 430 MTETGGIVISHAPGlyLVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPWPGMLHGIWGDPERYIKTYWSRF 509
Cdd:PRK00174 404 QTETGGIMITPLPG--ATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPWPGMMRTIYGDHERFVKTYFSTF 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 510 PGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPS 589
Cdd:PRK00174 482 KGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPS 561
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20137268 590 DELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVATG-APLGDVTTLEDETSVEEAKRAYEEIK 664
Cdd:PRK00174 562 DELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGeEILGDTSTLADPSVVEKLIEARQNRK 637
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
27-659 |
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: 1115.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 27 YTPIDAYFKFHRQTVENLESFWESVAKE-LEWFKPWDKVLDASNPPFYKWFVGGRLNLSYLAVDRHVKTwRKNKLAIEWE 105
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLARElLDWFKPFTKVLDWSFPPFYKWFVGGELNVSYNCVDRHLEA-RPDKVAIIWE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 106 GEPvdengyPTDRRKLTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADAL 185
Cdd:TIGR02188 80 GDE------PGEVRKITYRELHREVCRFANVLKS-LGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 186 AERINDSQSRIVITADGFWRRGRVVRLKEVVDAALEKATG-VESVIVLPRLGLKDVPMTEGRDYWWNKLMQGIPPnaYIE 264
Cdd:TIGR02188 153 ADRINDAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPVsVEHVLVVRRTGNPVVPWVEGRDVWWHDLMAKASA--YCE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 265 PEPVESEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVI 344
Cdd:TIGR02188 231 PEPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 345 YEGAPDYPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKVAF 424
Cdd:TIGR02188 311 FEGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 425 GSTWWMTETGGIVISHAPGlyLVPMKPGTNGPPLPGFEVDVVDENGNPAP-PGVKGYLVIKKPWPGMLHGIWGDPERYIK 503
Cdd:TIGR02188 391 VDTWWQTETGGIMITPLPG--ATPTKPGSATLPFFGIEPAVVDEEGNPVEgPGEGGYLVIKQPWPGMLRTIYGDHERFVD 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 504 TYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLK 583
Cdd:TIGR02188 469 TYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLK 548
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20137268 584 QGVAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVATGAP--LGDVTTLEDETSVEEAKRA 659
Cdd:TIGR02188 549 DGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAeiLGDTSTLEDPSVVEELIEA 626
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
31-649 |
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: 1099.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 31 DAYFKFHRQTVENLESFWESVAKELEWFKPWDKVLDAS-NPPFYKWFVGGRLNLSYLAVDRHVKTwRKNKLAIEWEGEPv 109
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVLDWSkGPPFIKWFEGGKLNISYNCLDRHLKE-RGDKVAIIWEGDE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 110 dengyPTDRRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERI 189
Cdd:cd05966 79 -----PDQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 190 NDSQSRIVITADGFWRRGRVVRLKEVVDAALEKATGVESVIVLPRLGlKDVPMTEGRDYWWNKLMQGIPPnaYIEPEPVE 269
Cdd:cd05966 153 NDAQCKLVITADGGYRGGKVIPLKEIVDEALEKCPSVEKVLVVKRTG-GEVPMTEGRDLWWHDLMAKQSP--ECEPEWMD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 270 SEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAP 349
Cdd:cd05966 230 SEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 350 DYPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKVAFGSTWW 429
Cdd:cd05966 310 TYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWW 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 430 MTETGGIVISHAPGlyLVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPWPGMLHGIWGDPERYIKTYWSRF 509
Cdd:cd05966 390 QTETGGIMITPLPG--ATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFSKF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 510 PGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPS 589
Cdd:cd05966 468 PGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPS 547
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20137268 590 DELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVATG-APLGDVTTLED 649
Cdd:cd05966 548 DELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGeEELGDTSTLAD 608
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
74-658 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 916.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 74 KWFVGGRLNLSYLAVDRHVKtWRKNKLAIEWEGEPVDengyptdRRKLTYYDLYREVNRVAYMLKqNFGVKKGDKITLYL 153
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAE-GRGDKVALIWEGEDGE-------ERTLTYAELRREVNRFANALR-ALGVKKGDRVAIYL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 154 PMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITADGFWRRGRVVRLKEVVDAALEKATGVESVIVLP 233
Cdd:COG0365 72 PNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSLEHVIVVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 234 RLGlKDVPMTEgrDYWWNKLMQGIPPNAyiEPEPVESEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDD 313
Cdd:COG0365 152 RTG-ADVPMEG--DLDWDELLAAASAEF--EPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 314 DIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAPDYPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLS 393
Cdd:COG0365 227 DVFWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 394 TLRIIHSVGEPINPEAWRWAYRVLGnekVAFGSTWWMTETGGIVISHAPGLylvPMKPGTNGPPLPGFEVDVVDENGNPA 473
Cdd:COG0365 307 SLRLLGSAGEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPGL---PVKPGSMGKPVPGYDVAVVDEDGNPV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 474 PPGVKGYLVIKKPWPGMLHGIWGDPERYIKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESAL 553
Cdd:COG0365 381 PPGEEGELVIKGPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESAL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 554 ISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:COG0365 461 VSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLR 540
|
570 580
....*....|....*....|....*
gi 20137268 634 AVATGAPLGDVTTLEDETSVEEAKR 658
Cdd:COG0365 541 KIAEGRPLGDTSTLEDPEALDEIKE 565
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
33-655 |
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: 720.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 33 YFKFHRQTVENLESFWESVAKELEWFKPWDKVLDASNPPFYKWFVGGRLNLSYLAVDRHVKTWRKNKLAIEWEgEPVDEN 112
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPPEKILDNSNPPFTRWFVGGRLNTCYNALDRHVEAGRGDQIALIYD-SPVTGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 113 gyptdRRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDS 192
Cdd:cd05967 80 -----ERTYTYAELLDEVSRLAGVL-RKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 193 QSRIVITADGFWRRGRVVRLKEVVDAALEKA-TGVESVIVLPRLGLKDVPMTEGRDYWWNKLMQGIppnAYIEPEPVESE 271
Cdd:cd05967 154 KPKLIVTASCGIEPGKVVPYKPLLDKALELSgHKPHHVLVLNRPQVPADLTKPGRDLDWSELLAKA---EPVDCVPVAAT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 272 HPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAPD- 350
Cdd:cd05967 231 DPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVg 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 351 YPQPDRWWSIIERYGVTIFYTSPTAIRMFMRY--GEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGnekVAFGSTW 428
Cdd:cd05967 311 TPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHW 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 429 WMTETGGIVISHAPGLYLVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPW-PGMLHGIWGDPERYIKTYWS 507
Cdd:cd05967 388 WQTETGWPITANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLpPGCLLTLWKNDERFKKLYLS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 508 RFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVA 587
Cdd:cd05967 468 KFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVK 547
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20137268 588 PS-DELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVATGAPLGDVTTLEDETSVEE 655
Cdd:cd05967 548 ITaEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDYTIPSTIEDPSVLDE 616
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
31-662 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 681.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 31 DAYFKFHRQTVENLESFWESVAKELEWFKPWDKVLDASNPPFYKWFVGGRLNLSYLAVDRHVKTwRKNKLAIEWEGEPVD 110
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTPFTQVLDYSNPPFARWFVGGRTNLCHNAVDRHLAK-RPEQLALIAVSTETD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 111 EngyptdRRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERIN 190
Cdd:PRK10524 81 E------ERTYTFRQLHDEVNRMAAML-RSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARID 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 191 DSQSRIVITADGFWRRGRVVRLKEVVDAALEKAT-GVESVIVLPRlGLKDVPMTEGRDYWWNKLMQGIPpNAYIEPEPVE 269
Cdd:PRK10524 154 DAKPVLIVSADAGSRGGKVVPYKPLLDEAIALAQhKPRHVLLVDR-GLAPMARVAGRDVDYATLRAQHL-GARVPVEWLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 270 SEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAP 349
Cdd:PRK10524 232 SNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 350 DYPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGnekVAFGSTWW 429
Cdd:PRK10524 312 TRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALG---VPVIDNYW 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 430 MTETGGIVISHAPGLYLVPMKPGTNGPPLPGFEVDVVDEN-GNPAPPGVKGYLVIKKPW-PGMLHGIWGDPERYIKTYWS 507
Cdd:PRK10524 389 QTETGWPILAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEGPLpPGCMQTVWGDDDRFVKTYWS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 508 RFPGMFYAG-DYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGV 586
Cdd:PRK10524 469 LFGRQVYSTfDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSD 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 587 APSDE-----LRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVATGAPLGDVTTLEDETSVEEAKRAYE 661
Cdd:PRK10524 549 SLADRearlaLEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGRDPGDLTTIEDPAALQQIRQALE 628
|
.
gi 20137268 662 E 662
Cdd:PRK10524 629 E 629
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
37-628 |
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: 676.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 37 HRQTVENLESFWESVAKELEWFKPWDKV---LDASNPPFYKWFVGGRLNLSYLAVDRHVKTwRKNKLAIEWEGEPVdeng 113
Cdd:cd17634 5 YRQSINDPDTFWGEAGKILDWITPYQKVkntSFAPGAPSIKWFEDATLNLAANALDRHLRE-NGDRTAIIYEGDDT---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 114 ypTDRRKLTYYDLYREVNRVAYMLKqNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQ 193
Cdd:cd17634 80 --SQSRTISYRELHREVCRFAGTLL-DLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 194 SRIVITADGFWRRGRVVRLKEVVDAALE-KATGVESVIVLPRLGLkDVPMTEGRDYWWNKLMQGIPPNAyiEPEPVESEH 272
Cdd:cd17634 157 SRLLITADGGVRAGRSVPLKKNVDDALNpNVTSVEHVIVLKRTGS-DIDWQEGRDLWWRDLIAKASPEH--QPEAMNAED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 273 PSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAPDYP 352
Cdd:cd17634 234 PLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNWP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 353 QPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKVAFGSTWWMTE 432
Cdd:cd17634 314 TPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 433 TGGIVISHAPGlyLVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPWPGMLHGIWGDPERYIKTYWSRFPGM 512
Cdd:cd17634 394 TGGFMITPLPG--AIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGM 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 513 FYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDEL 592
Cdd:cd17634 472 YFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPEL 551
|
570 580 590
....*....|....*....|....*....|....*.
gi 20137268 593 RKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIM 628
Cdd:cd17634 552 YAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
33-655 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 610.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 33 YFKFHRQTVENLESFWESVAKELEWFKPW--DKV----LDASNPPF-YKWFVGGRLNLSYLAVDRHVKTWRKNKLAIEWE 105
Cdd:PLN02654 32 YMEMYKRSVDDPAGFWSDIASQFYWKQKWegDEVcsenLDVRKGPIsIEWFKGGKTNICYNCLDRNVEAGNGDKIAIYWE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 106 GEPvdengyPTDRRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADAL 185
Cdd:PLN02654 112 GNE------PGFDASLTYSELLDRVCQLANYLKDV-GVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 186 AERINDSQSRIVITADGFWRRGRVVRLKEVVDAALEKAT--GVESVIVLP---RLGLK--DVPMTEGRDYWWNKLMQGIP 258
Cdd:PLN02654 185 AQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAknGVSVGICLTyenQLAMKreDTKWQEGRDVWWQDVVPNYP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 259 PNAyiEPEPVESEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLM 338
Cdd:PLN02654 265 TKC--EVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLN 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 339 GATEVIYEGAPDYPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLG 418
Cdd:PLN02654 343 GATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 419 NEKVAFGSTWWMTETGGIVISHAPGLYlvPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPWPGMLHGIWGDP 498
Cdd:PLN02654 423 DSRCPISDTWWQTETGGFMITPLPGAW--PQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKSWPGAFRTLYGDH 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 499 ERYIKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIA 578
Cdd:PLN02654 501 ERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYA 580
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20137268 579 FVVLKQGVAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVATGA--PLGDVTTLEDETSVEE 655
Cdd:PLN02654 581 FVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQldELGDTSTLADPGVVDQ 659
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
48-649 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 603.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 48 WESVAKELEWFKpwdkvldasnppfykwfvGGRLNLSYLAVDRHVKTWRKNKLAIEWEGepvdengyPTDRRKLTYYDLY 127
Cdd:PRK04319 27 WEEVEKEFSWLE------------------TGKVNIAYEAIDRHADGGRKDKVALRYLD--------ASRKEKYTYKELK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 128 REVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITADGFWRRG 207
Cdd:PRK04319 81 ELSNKFANVLKE-LGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 208 RVVRLKEVvdaalekatgvESVIVLprlglkDVPMTEGRDYW-WNKLMQGIPPNAyiEPEPVESEHPSFILYTSGTTGKP 286
Cdd:PRK04319 160 PADDLPSL-----------KHVLLV------GEDVEEGPGTLdFNALMEQASDEF--DIEWTDREDGAILHYTSGSTGKP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 287 KGIVHDTGGWAVHvYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAPDypqPDRWWSIIERYGV 366
Cdd:PRK04319 221 KGVLHVHNAMLQH-YQTGKYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGGRFS---PERWYRILEDYKV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 367 TIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEkvaFGSTWWMTETGGIVISHAPGLyl 446
Cdd:PRK04319 297 TVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGLP---IHDNWWMTETGGIMIANYPAM-- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 447 vPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPWPGMLHGIWGDPERYIKTYWsrfPGMFYAGDYAIKDKDGY 526
Cdd:PRK04319 372 -DIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMMRGIWNNPEKYESYFA---GDWYVSGDSAYMDEDGY 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 527 IWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDELRKELREHVRRTIGP 606
Cdd:PRK04319 448 FWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGA 527
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 20137268 607 IAEPAQIFFVTKLPKTRSGKIMRRLLKAVATGAPLGDVTTLED 649
Cdd:PRK04319 528 HAAPREIEFKDKLPKTRSGKIMRRVLKAWELGLPEGDLSTMED 570
|
|
| propion_prpE |
TIGR02316 |
propionate--CoA ligase; This family contains one of three readily separable clades of proteins ... |
31-662 |
0e+00 |
|
propionate--CoA ligase; This family contains one of three readily separable clades of proteins in the group of acetate and propionate--CoA ligases. Characterized members of this family act on propionate. From propionyl-CoA, there is a cyclic degradation pathway: it is ligated by PrpC to the TCA cycle intermediate oxaloacetate, acted upon further by PrpD and an aconitase, then cleaved by PrpB to pyruvate and the TCA cycle intermediate succinate.
Pssm-ID: 131369 [Multi-domain] Cd Length: 628 Bit Score: 594.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 31 DAYFKFHRQTVENLESFWESVAKELEWFKPWDKVLDASNPPFYKWFVGGRLNLSYLAVDRHVKTwRKNKLAIEWEGEPVD 110
Cdd:TIGR02316 1 MRYEEFYQRSIEQPEAFWAEQARRIDWQTPPQRILDYSNPPFARWFAGGRTNLCHNALDRHLDE-RGEQLALVTVSSETG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 111 ENgyptdrRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERIN 190
Cdd:TIGR02316 80 QE------RTLTYRQLHREVNVFASAL-RALGVGRGDRVLIYMPMIAEAVFAMLACARIGAIHSVVFGGFASHSLALRID 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 191 DSQSRIVITADGFWRRGRVVRLKEVVDAALEKATGVESVIVLPRLGLKDVPMTEGRDYWWNKL-MQGIppNAYIEPEPVE 269
Cdd:TIGR02316 153 DATPKLIVSADAGMRGGKVIPYKPLLDAAIAEAQHPPPHVLLVDRGLAPMRLIPGRDVDYAALrTQHE--DAQVPVEWLE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 270 SEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAP 349
Cdd:TIGR02316 231 SNEPSYILYTSGTTGKPKGVQRDVGGYAVALALSMWAIFGIRAGQVMFSASDVGWVVGHSYIVYAPLLAGAATVLYEGLP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 350 DYPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKVafgSTWW 429
Cdd:TIGR02316 311 TNPDPGVWWSIVERYGVRTMFSAPTAIRVLKKQDAAWLRKHDLSSLHWLFLAGEPLDEPTAHWITDGLGKPVI---DNYW 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 430 MTETGGIVISHAPGLYLVPMKPGTNGPPLPGFEVDVVDE-NGNPAPPGVKGYLVIKKPW-PGMLHGIWGDPERYIKTYWS 507
Cdd:TIGR02316 388 QTETGWPVLAIMPGLDLKPVKLGSPGLPMYGYHLRVLDEaTGRPCGPNEKGVLTVVPPLpPGCLSTVWGDDARFLKTYWS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 508 RFPGMFYAG-DYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGV 586
Cdd:TIGR02316 468 HFKRPLYSSfDWGIRDEDGYTFILGRTDDVINVAGHRLGTREIEESVSSHPSVAEVAVVGVHDELKGQVAVVFAILKESD 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 587 APSD-----ELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVATGAPLGDVTTLEDETSVEEAKRAYE 661
Cdd:TIGR02316 548 SAGDahdphAVETGMMDCVVRQLGAVARPARVYFVAALPKTRSGKLLRRSIQALAEGRDPGDLTTIDDPGALEQVRRAME 627
|
.
gi 20137268 662 E 662
Cdd:TIGR02316 628 R 628
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
33-649 |
0e+00 |
|
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: 591.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 33 YFKFHRQTVENLESFWESVAKEL--EWFKPWDKVLDASN-PPFYKWFVGGRLNLSYLAVDRHVKTwRKNKLAIEWEGEpv 109
Cdd:cd05968 9 LEAFLERSAEDNAWFWGEFVKDVgiEWYEPPYQTLDLSGgKPWAAWFVGGRMNIVEQLLDKWLAD-TRTRPALRWEGE-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 110 deNGyptDRRKLTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERI 189
Cdd:cd05968 86 --DG---TSRTLTYGELLYEVKRLANGLRA-LGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 190 NDSQSRIVITADGFWRRGRVVRLKEVVDAALEKATGVESVIVLPRLGLkDVPMTEGRDYWWNKLMQGIPPNAyiepEPVE 269
Cdd:cd05968 160 QDAEAKALITADGFTRRGREVNLKEEADKACAQCPTVEKVVVVRHLGN-DFTPAKGRDLSYDEEKETAGDGA----ERTE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 270 SEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDD-IFWCTaDIGWVTGhSYVVLGPLLMGATEVIYEGA 348
Cdd:cd05968 235 SEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGWMMG-PWLIFGGLILGATMVLYDGA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 349 PDYPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKVAFGSTW 428
Cdd:cd05968 313 PDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 429 WMTE-TGGIVishapGLYLV-PMKPGTNGPPLPGFEVDVVDENGNPAPPGVkGYLVIKKPWPGMLHGIWGDPERYIKTYW 506
Cdd:cd05968 393 GGTEiSGGIL-----GNVLIkPIKPSSFNGPVPGMKADVLDESGKPARPEV-GELVLLAPWPGMTRGFWRDEDRYLETYW 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 507 SRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGV 586
Cdd:cd05968 467 SRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGV 546
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20137268 587 APSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVATGAPLGDVTTLED 649
Cdd:cd05968 547 TPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKELGDLSSLEN 609
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
121-636 |
8.32e-172 |
|
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: 497.80 E-value: 8.32e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLKqNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITA 200
Cdd:cd05969 1 YTFAQLKVLSARFANVLK-SLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 201 DGFWRRgrvvrlkevvdaalekatgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepVESEHPSFILYTS 280
Cdd:cd05969 80 EELYER-------------------------------------------------------------TDPEDPTLLHYTS 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 281 GTTGKPKGIVHDTGGWAVHvYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAPDypqPDRWWSI 360
Cdd:cd05969 99 GTTGTPKGVLHVHDAMIFY-YFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFD---AESWYGI 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 361 IERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGnekVAFGSTWWMTETGGIVISH 440
Cdd:cd05969 175 IERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSIMIAN 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 441 APGLylvPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPWPGMLHGIWGDPERYIKTywsrFPGMFY-AGDYA 519
Cdd:cd05969 252 YPCM---PIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERYKNS----FIDGWYlTGDLA 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 520 IKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDELRKELREH 599
Cdd:cd05969 325 YRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINF 404
|
490 500 510
....*....|....*....|....*....|....*..
gi 20137268 600 VRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVA 636
Cdd:cd05969 405 VRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
121-634 |
2.13e-137 |
|
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: 409.03 E-value: 2.13e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITa 200
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 201 dgfwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepvESEHPSFILYTS 280
Cdd:cd05972 79 --------------------------------------------------------------------DAEDPALIYFTS 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 281 GTTGKPKGIVHdTGGWAVHVYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAPDypQPDRWWSI 360
Cdd:cd05972 91 GTTGLPKGVLH-THSYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRF--DAERILEL 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 361 IERYGVTIFYTSPTAIRMFMRYGeewPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGnEKVAFGstWWMTETGgIVISH 440
Cdd:cd05972 168 LERYGVTSFCGPPTAYRMLIKQD---LSSYKFSHLRLVVSAGEPLNPEVIEWWRAATG-LPIRDG--YGQTETG-LTVGN 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 441 APGLylvPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPWPGMLHGIWGDPERYiKTYWSRfpGMFYAGDYAI 520
Cdd:cd05972 241 FPDM---PVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKT-EASIRG--DYYLTGDRAY 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 521 KDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDELRKELREHV 600
Cdd:cd05972 315 RDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHV 394
|
490 500 510
....*....|....*....|....*....|....
gi 20137268 601 RRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:cd05972 395 KKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
29-648 |
6.51e-112 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 351.02 E-value: 6.51e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 29 PIDAYFKFHRQTVENLESFWESVAK--ELEWFKPWDKVLDASNPPFYKWFVGGRLNLSylavdRHVKTWRK-NKLAIEWE 105
Cdd:PRK03584 32 SFDDYAALWRWSVEDLEAFWQSVWDffGVIGSTPYTVVLAGRRMPGARWFPGARLNYA-----ENLLRHRRdDRPAIIFR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 106 GEpvdeNGyptDRRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADAL 185
Cdd:PRK03584 107 GE----DG---PRRELSWAELRRQVAALAAALRAL-GVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 186 AERINDSQSRIVITADGFWRRGRVVRLKEVVDAALEKATGVESVIVLPRLGLKDVPMTEGRDYWWNKLMQGIPPNAyIEP 265
Cdd:PRK03584 179 LDRFGQIEPKVLIAVDGYRYGGKAFDRRAKVAELRAALPSLEHVVVVPYLGPAAAAAALPGALLWEDFLAPAEAAE-LEF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 266 EPVESEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDD-IFWCTAdIGW------VTGhsyvvlgpLLM 338
Cdd:PRK03584 258 EPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDrFFWYTT-CGWmmwnwlVSG--------LLV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 339 GATEVIYEGAPDYPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLG 418
Cdd:PRK03584 329 GATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPLPPEGFDWVYEHVK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 419 NEkvafgsTWWMTETGG--IVISHAPGLYLVPMKPGTNGPPLPGFEVDVVDENGNPApPGVKGYLVIKKPWPGMLHGIWG 496
Cdd:PRK03584 409 AD------VWLASISGGtdICSCFVGGNPLLPVYRGEIQCRGLGMAVEAWDEDGRPV-VGEVGELVCTKPFPSMPLGFWN 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 497 DP--ERYIKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGE 574
Cdd:PRK03584 482 DPdgSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDV 561
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20137268 575 VPIAFVVLKQGVAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIM----RRLLkavaTGAPLGDVTTLE 648
Cdd:PRK03584 562 RMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVelpvKKLL----HGRPVKKAVNRD 635
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
117-540 |
3.82e-110 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 338.52 E-value: 3.82e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRI 196
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGL-RALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VITADGFwrrgrvvrLKEVVDAALEKATGVESVIVLPRLGLkdvpmtegRDYWWNKLMQGIPPNAYIEPEPVESEHPSFI 276
Cdd:pfam00501 97 LITDDAL--------KLEELLEALGKLEVVKLVLVLDRDPV--------LKEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIVHDTGGwAVHVYATMKWV----FDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAPDYP 352
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRN-LVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPALD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 353 qPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRkhDLSTLRIIHSVGEPINPEAWRWAYRVLGNekvAFGSTWWMTE 432
Cdd:pfam00501 240 -PAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRA--LLSSLRLVLSGGAPLPPELARRFRELFGG---ALVNGYGLTE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 433 TGGIVISHAPGLYLVPmKPGTNGPPLPGFEVDVVDEN-GNPAPPGVKGYLVIKKpwPGMLHGIWGDPERYIKTYWSrfPG 511
Cdd:pfam00501 314 TTGVVTTPLPLDEDLR-SLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRG--PGVMKGYLNDPELTAEAFDE--DG 388
|
410 420
....*....|....*....|....*....
gi 20137268 512 MFYAGDYAIKDKDGYIWVLGRADEVIKVA 540
Cdd:pfam00501 389 WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
117-642 |
5.64e-108 |
|
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: 334.09 E-value: 5.64e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRI 196
Cdd:COG0318 21 GGRRLTYAELDARARRLAAAL-RALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VITAdgfwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepvesehpsFI 276
Cdd:COG0318 100 LVTA--------------------------------------------------------------------------LI 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIVHDTGGWAVHVYATMKWvFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIyegaPDYPQPDR 356
Cdd:COG0318 106 LYTSGTTGRPKGVMLTHRNLLANAAAIAAA-LGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVL----LPRFDPER 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 357 WWSIIERYGVTIFYTSPTAIRMFMRYGEEwpRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGnekVAFGSTWWMTETGGI 436
Cdd:COG0318 181 VLELIERERVTVLFGVPTMLARLLRHPEF--ARYDLSSLRLVVSGGAPLPPELLERFEERFG---VRIVEGYGLTETSPV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 437 VISHAPGLYLVpmKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPWpgMLHGIWGDPERYIKTYwsrFPGMFYAG 516
Cdd:COG0318 256 VTVNPEDPGER--RPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPN--VMKGYWNDPEATAEAF---RDGWLRTG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 517 DYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDElrkEL 596
Cdd:COG0318 329 DLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAE---EL 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 20137268 597 REHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVATGAPLG 642
Cdd:COG0318 406 RAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
30-654 |
3.60e-106 |
|
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: 335.40 E-value: 3.60e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 30 IDAYFKFHRQTVENLESFWESVAKELE--WFKPWDKVLDASNP-PFYKWFVGGRLNLSYLAVDRHVKTwrkNKLAIEweg 106
Cdd:cd05943 16 LADYAALHRWSVDDPGAFWAAVWDFSGvrGSKPYDVVVVSGRImPGARWFPGARLNYAENLLRHADAD---DPAAIY--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 107 epVDENGyptDRRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALA 186
Cdd:cd05943 90 --AAEDG---ERTEVTWAELRRRVARLAAALRAL-GVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 187 ERINDSQSRIVITADGFWRRGRVVRLKEVVDAALEKATGVESVIVLPRL---GLKDVPMTeGRDYWWNKLMQGiPPNAYI 263
Cdd:cd05943 164 DRFGQIEPKVLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVVVVPYTvaaGQPDLSKI-AKALTLEDFLAT-GAAGEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 264 EPEPVESEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDD-IFWCTAdIGWVTGHSYVvlGPLLMGATE 342
Cdd:cd05943 242 EFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDrLFYYTT-CGWMMWNWLV--SGLAVGATI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 343 VIYEGAPDYPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNekv 422
Cdd:cd05943 319 VLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKP--- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 423 afgSTWWMTETGG--IVISHAPGLYLVPMKPGTNGPPLPGFEVDVVDENGNPAPpGVKGYLVIKKPWPGMLHGIWGDPE- 499
Cdd:cd05943 396 ---DVLLASISGGtdIISCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPVW-GEKGELVCTKPFPSMPVGFWNDPDg 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 500 -RYIKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIA 578
Cdd:cd05943 472 sRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVIL 551
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20137268 579 FVVLKQGVAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVATGAPLGDVTTLEDETSVE 654
Cdd:cd05943 552 FVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGRPVKNAGALANPESLD 627
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
117-634 |
2.22e-103 |
|
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: 322.07 E-value: 2.22e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRI 196
Cdd:cd05971 3 TPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VITAdgfwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepvESEHPSFI 276
Cdd:cd05971 82 LVTD--------------------------------------------------------------------GSDDPALI 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIVHDTG---GWAVHVYATMKwvFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAPDypQ 353
Cdd:cd05971 94 IYTSGTTGPPKGALHAHRvllGHLPGVQFPFN--LFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKF--D 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 354 PDRWWSIIERYGVTIFYTSPTAIRMFMRYGEewPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLG---NEkvAFGSTwwm 430
Cdd:cd05971 170 PKAALDLMSRYGVTTAFLPPTALKMMRQQGE--QLKHAQVKLRAIATGGESLGEELLGWAREQFGvevNE--FYGQT--- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 431 teTGGIVISHAPGLYlvPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPWPGMLHGIWGDPERYIKTYWSRFp 510
Cdd:cd05971 243 --ECNLVIGNCSALF--PIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAFLGYWNNPSATEKKMAGDW- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 511 gmFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSD 590
Cdd:cd05971 318 --LLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSD 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 20137268 591 ELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:cd05971 396 ALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
272-628 |
1.44e-101 |
|
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: 313.45 E-value: 1.44e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 272 HPSFILYTSGTTGKPKGIVHDTGGWAVHVYAtMKWVFDIRDDDIFWCTADIGWVtGHSYVVLGPLLMGATEVIYEGapdy 351
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAA-LAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 352 PQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEwpRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGnekVAFGSTWWMT 431
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLKAPES--AGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 432 ETGGIVISHAPglYLVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPWPGMlhGIWGDPERyikTYWSRFPG 511
Cdd:cd04433 150 ETGGTVATGPP--DDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMK--GYWNNPEA---TAAVDEDG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 512 MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGvapSDE 591
Cdd:cd04433 223 WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPG---ADL 299
|
330 340 350
....*....|....*....|....*....|....*..
gi 20137268 592 LRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIM 628
Cdd:cd04433 300 DAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
121-633 |
3.76e-101 |
|
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: 316.00 E-value: 3.76e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITa 200
Cdd:cd05973 1 LTFGELRALSARFANAL-QELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 201 dgfwrrgrvvrlkevvDAAlekatgvesvivlprlglkdvpmteGRDywwnKLMQGippnayiepepvesehPSFILYTS 280
Cdd:cd05973 79 ----------------DAA-------------------------NRH----KLDSD----------------PFVMMFTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 281 GTTGKPKGIVHDTGGWAVHVyATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAPdypQPDRWWSI 360
Cdd:cd05973 98 GTTGLPKGVPVPLRALAAFG-AYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGF---SVESTWRV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 361 IERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLStLRIIHSVGEPINPEAWRWAYRVLGnekVAFGSTWWMTETGGIVISH 440
Cdd:cd05973 174 IERLGVTNLAGSPTAYRLLMAAGAEVPARPKGR-LRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTELGMVLANH 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 441 -APGLylvPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVI-KKPWPGM-LHGIWGDPERYIKTYWSRfpgmfyAGD 517
Cdd:cd05973 250 hALEH---PVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIdIANSPLMwFRGYQLPDTPAIDGGYYL------TGD 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 518 YAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDELRKELR 597
Cdd:cd05973 321 TVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQ 400
|
490 500 510
....*....|....*....|....*....|....*.
gi 20137268 598 EHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:cd05973 401 LHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
87-633 |
6.48e-87 |
|
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: 281.18 E-value: 6.48e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 87 AVDRHVKTWRKNKLAiewegepvdengYPTDRRKLTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAA 166
Cdd:cd05959 8 LVDLNLNEGRGDKTA------------FIDDAGSLTYAELEAEARRVAGALRA-LGVKREERVLLIMLDTVDFPTAFLGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 167 WRIGAITSVVFSGFSADALAERINDSQSRIVITADGFWrrgrvvrlkEVVDAALEKATGVESVIVLPRlglkDVPMTEGR 246
Cdd:cd05959 75 IRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELA---------PVLAAALTKSEHTLVVLIVSG----GAGPEAGA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 247 DyWWNKLMQGIPPNAyiEPEPVESEHPSFILYTSGTTGKPKGIVHDTGG--WAVHVYAtmKWVFDIRDDDIFWCTADIGW 324
Cdd:cd05959 142 L-LLAELVAAEAEQL--KPAATHADDPAFWLYSSGSTGRPKGVVHLHADiyWTAELYA--RNVLGIREDDVCFSAAKLFF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 325 VTGHSYVVLGPLLMGATEVIYegaPDYPQPDRWWSIIERYGVTIFYTSPTaIRMFMRYGEEWPrKHDLSTLRIIHSVGEP 404
Cdd:cd05959 217 AYGLGNSLTFPLSVGATTVLM---PERPTPAAVFKRIRRYRPTVFFGVPT-LYAAMLAAPNLP-SRDLSSLRLCVSAGEA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 405 INPEAW-RWAYRvLGNEKV-AFGSTwwmtETGGIVISHAPGlylvPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLV 482
Cdd:cd05959 292 LPAEVGeRWKAR-FGLDILdGIGST----EMLHIFLSNRPG----RVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 483 IKKPwpGMLHGIWGDPERYIKT---YWsrfpgmFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAV 559
Cdd:cd05959 363 VRGP--SSATMYWNNRDKTRDTfqgEW------TRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAV 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20137268 560 AESAVVGVPDAIKGEVPIAFVVLKQGVAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:cd05959 435 LEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
90-634 |
6.57e-84 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 273.60 E-value: 6.57e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 90 RHVKTWRKNKLAIEWEGepvdengyptdrRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRI 169
Cdd:PRK06187 13 RHGARKHPDKEAVYFDG------------RRTTYAELDERVNRLANAL-RALGVKKGDRVAVFDWNSHEYLEAYFAVPKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 170 GAITSVVFSGFSADALAERINDSQSRIVITADGFWrrgrvvrlkEVVDAALEKATGVESVIVLprlglKDVPMTEGRDYW 249
Cdd:PRK06187 80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFV---------PLLAAILPQLPTVRTVIVE-----GDGPAAPLAPEV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 250 WN--KLMQGIPPNaYIEPEPVESEhPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWvFDIRDDDIF----------- 316
Cdd:PRK06187 146 GEyeELLAAASDT-FDFPDIDEND-AAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAW-LKLSRDDVYlvivpmfhvha 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 317 WctadiGWvtghSYVvlgPLLMGATEVIyegaPDYPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEewPRKHDLSTLR 396
Cdd:PRK06187 223 W-----GL----PYL---ALMAGAKQVI----PRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPR--AYFVDFSSLR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 397 IIHSVGEPINPEAWRWAYRVLGnekVAFGSTWWMTETGGIV-ISH-APGLYLVPMKPGTNGPPLPGFEVDVVDENGNPAP 474
Cdd:PRK06187 285 LVIYGGAALPPALLREFKEKFG---IDLVQGYGMTETSPVVsVLPpEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 475 PGVK--GYLVIKKPWpgMLHGIWGDPERYIKTY---WSRfpgmfyAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYEL 549
Cdd:PRK06187 362 PDGGevGEIIVRGPW--LMQGYWNRPEATAETIdggWLH------TGDVGYIDEDGYLYITDRIKDVIISGGENIYPREL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 550 ESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDelrKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMR 629
Cdd:PRK06187 434 EDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDA---KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILK 510
|
....*
gi 20137268 630 RLLKA 634
Cdd:PRK06187 511 RVLRE 515
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
82-629 |
2.03e-83 |
|
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: 272.83 E-value: 2.03e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 82 NLSYLAVDRHVKTwRKNKLAIEWegepVDENGyptDRRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPI 161
Cdd:cd05970 17 NFAYDVVDAMAKE-YPDKLALVW----CDDAG---EERIFTFAELADYSDKTANFFKAM-GIGKGDTVMLTLKRRYEFWY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 162 TMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITADGfwrrgrvVRLKEVVDAALEKATgvesviVLPRLGLKDVP 241
Cdd:cd05970 88 SLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAE-------DNIPEEIEKAAPECP------SKPKLVWVGDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 242 MTEGrdywWNKLMQGI--------PPNAYIEPEpveSEHPSFILYTSGTTGKPKGIVHDtggwavHVY-----ATMKWVF 308
Cdd:cd05970 155 VPEG----WIDFRKLIknaspdfeRPTANSYPC---GEDILLVYFSSGTTGMPKMVEHD------FTYplghiVTAKYWQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 309 DIRDDDIFWCTADIGW---VTGHSYvvlGPLLMGATEVIYegapDYPQ--PDRWWSIIERYGVTIFYTSPTAIRMFMRyg 383
Cdd:cd05970 222 NVREGGLHLTVADTGWgkaVWGKIY---GQWIAGAAVFVY----DYDKfdPKALLEKLSKYGVTTFCAPPTIYRFLIR-- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 384 eEWPRKHDLSTLRIIHSVGEPINPEAW-RWAYRVLGNEKVAFGSTwwmtETGgIVISHAPGLylvPMKPGTNGPPLPGFE 462
Cdd:cd05970 293 -EDLSRYDLSSLRYCTTAGEALNPEVFnTFKEKTGIKLMEGFGQT----ETT-LTIATFPWM---EPKPGSMGKPAPGYE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 463 VDVVDENGNPAPPGVKGYLVI----KKPWpGMLHGIWGDPERYIKTYwsrFPGMFYAGDYAIKDKDGYIWVLGRADEVIK 538
Cdd:cd05970 364 IDLIDREGRSCEAGEEGEIVIrtskGKPV-GLFGGYYKDAEKTAEVW---HDGYYHTGDAAWMDEDGYLWFVGRTDDLIK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 539 VAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDELRKELREHVRRTIGPIAEPAQIFFVTK 618
Cdd:cd05970 440 SSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDE 519
|
570
....*....|.
gi 20137268 619 LPKTRSGKIMR 629
Cdd:cd05970 520 LPKTISGKIRR 530
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
119-633 |
6.42e-81 |
|
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: 263.18 E-value: 6.42e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:cd05958 9 REWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TADgfwrrgrvvrlkevvdaaleKATGVESVIVLPrlglkdvpmtegrdywwnklmqgippnayiepepvesehpsfilY 278
Cdd:cd05958 89 CAH--------------------ALTASDDICILA--------------------------------------------F 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 279 TSGTTGKPKGIVH-------DTGGWAVHVyatmkwvFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGApdy 351
Cdd:cd05958 105 TSGTTGAPKATMHfhrdplaSADRYAVNV-------LRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA--- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 352 pQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEwpRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKV-AFGSTwwm 430
Cdd:cd05958 175 -TPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIdGIGST--- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 431 tETGGIVISHAPGlylvPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpgmlHGIWGDPERYIKTYWSRfp 510
Cdd:cd05958 249 -EMFHIFISARPG----DARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP-----TGCRYLADKRQRTYVQG-- 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 511 GMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSD 590
Cdd:cd05958 317 GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGP 396
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 20137268 591 ELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:cd05958 397 VLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
119-633 |
3.71e-78 |
|
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: 256.72 E-value: 3.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:cd05936 23 RKLTYRELDALAEAFAAGL-QNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TADGFwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmtegrdywwNKLMQgiPPNAYIEPEPVESEHPSFILY 278
Cdd:cd05936 102 VAVSF-----------------------------------------------TDLLA--AGAPLGERVALTPEDVAVLQY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 279 TSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRD-DDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGapdyPQPDRW 357
Cdd:cd05936 133 TSGTTGVPKGAMLTHRNLVANALQIKAWLEDLLEgDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPR----FRPIGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 358 WSIIERYGVTIFYTSPTAIRMFMRYGEewPRKHDLSTLRIIHSVGEPINPE-AWRWAyRVLGNEKV-AFGstwwMTETGG 435
Cdd:cd05936 209 LKEIRKHRVTIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVEvAERFE-ELTGVPIVeGYG----LTETSP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 436 IVISHAPGlylVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPERYIKTYWSrfpGMFYA 515
Cdd:cd05936 282 VVAVNPLD---GPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGP--QVMKGYWNRPEETAEAFVD---GWLRT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 516 GDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSdelRKE 595
Cdd:cd05936 354 GDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLT---EEE 430
|
490 500 510
....*....|....*....|....*....|....*...
gi 20137268 596 LREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:cd05936 431 IIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
132-633 |
9.84e-78 |
|
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: 257.78 E-value: 9.84e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 132 RVAYMLKQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITADgfwrrgrvvr 211
Cdd:cd05928 53 KAANVLSGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD---------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 212 lkevvdaalEKATGVESVIV-LPRLGLKDVPMTEGRDYWWN--KLMQgippNAYIEPEPVE--SEHPSFILYTSGTTGKP 286
Cdd:cd05928 123 ---------ELAPEVDSVASeCPSLKTKLLVSEKSRDGWLNfkELLN----EASTEHHCVEtgSQEPMAIYFTSGTTGSP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 287 KGIVHDTGGWAVHVYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEgapdYPQ--PDRWWSIIERY 364
Cdd:cd05928 190 KMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFVHH----LPRfdPLVILKTLSSY 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 365 GVTIFYTSPTAIRMFMrygEEWPRKHDLSTLRIIHSVGEPINPEawrwayrVLGNEKVAFG----STWWMTETGgIVISH 440
Cdd:cd05928 266 PITTFCGAPTVYRMLV---QQDLSSYKFPSLQHCVTGGEPLNPE-------VLEKWKAQTGldiyEGYGQTETG-LICAN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 441 APGLylvPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIK----KPWpGMLHGIWGDPERYIKTywsrFPGMFY-A 515
Cdd:cd05928 335 FKGM---KIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvkpiRPF-GLFSGYVDNPEKTAAT----IRGDFYlT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 516 GDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSD--ELR 593
Cdd:cd05928 407 GDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDpeQLT 486
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 20137268 594 KELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:cd05928 487 KELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELR 526
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
43-632 |
7.16e-75 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 253.13 E-value: 7.16e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 43 NLESFWESVAKEL-EWFKPWDKVLdASNPPFYKWFVGGRLNLSYLAVDRHVKT-WRKNKLAIEWEGEpvdengYPTDRRK 120
Cdd:PTZ00237 20 NPESFWDEVAKKYvHWDKMYDKVY-SGDEIYPDWFKGGELNTCYNVLDIHVKNpLKRDQDALIYECP------YLKKTIK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITA 200
Cdd:PTZ00237 93 LTYYQLYEKVCEFSRVL-LNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 201 DGFWRRGRVVRLKEVVDAALEKATGVES-VIVLPR------------LGLKDVPMTEGrdywWNKLMQGIPPN---AYIE 264
Cdd:PTZ00237 172 NYGILNDEIITFTPNLKEAIELSTFKPSnVITLFRnditsesdlkkiETIPTIPNTLS----WYDEIKKIKENnqsPFYE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 265 PEPVESEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDDIFWCTADIGWVTGHSYVvLGPLLMGATEVI 344
Cdd:PTZ00237 248 YVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFL-YGSLSLGNTFVM 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 345 YEGAPDYPQ--PDRWWSIIERYGVTIFYTSPTAIRMFMRY---GEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLgn 419
Cdd:PTZ00237 327 FEGGIIKNKhiEDDLWNTIEKHKVTHTLTLPKTIRYLIKTdpeATIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKL-- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 420 eKVAFGSTWWMTETGGIVISHapglYLVPMKP-GTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPWP-GMLHGIWGD 497
Cdd:PTZ00237 405 -KIKSSRGYGQTEIGITYLYC----YGHINIPyNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKLPMPpSFATTFYKN 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 498 PERYiKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPI 577
Cdd:PTZ00237 480 DEKF-KQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPI 558
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 20137268 578 AFVVLKQGVAPS----DELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:PTZ00237 559 GLLVLKQDQSNQsidlNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
116-633 |
1.18e-73 |
|
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: 243.91 E-value: 1.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 116 TDRRKLTYYDLYREVNRVAYMLKqNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSR 195
Cdd:cd05919 6 AADRSVTYGQLHDGANRLGSALR-NLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 196 IVITADgfwrrgrvvrlkevvDAAlekatgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepvesehpSF 275
Cdd:cd05919 85 LVVTSA---------------DDI------------------------------------------------------AY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 276 ILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDDIFWCTADI--GWVTGHSyvVLGPLLMGATEVIYEGAPDypq 353
Cdd:cd05919 96 LLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVLNPGWPT--- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 354 PDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPrkHDLSTLRIIHSVGEPINPEAW-RWAYRVLGNEKVAFGSTwwmtE 432
Cdd:cd05919 171 AERVLATLARFRPTVLYGVPTFYANLLDSCAGSP--DALRSLRLCVSAGEALPRGLGeRWMEHFGGPILDGIGAT----E 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 433 TGGIVISHAPGLYlvpmKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPERYIKTYWSrfpGM 512
Cdd:cd05919 245 VGHIFLSNRPGAW----RLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGP--SAAVGYWNNPEKSRATFNG---GW 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 513 FYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDEL 592
Cdd:cd05919 316 YRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESL 395
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 20137268 593 RKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:cd05919 396 ARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
98-629 |
1.54e-73 |
|
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: 243.67 E-value: 1.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 98 NKLAIEWEGepvdengyptdrRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVF 177
Cdd:cd17631 10 DRTALVFGG------------RSLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 178 SGFSADALAERINDSQSRIVItadgfwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmtegrdywwnklmqgi 257
Cdd:cd17631 77 FRLTPPEVAYILADSGAKVLF----------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 258 ppnayiepepvesEHPSFILYTSGTTGKPKGIVHDTGGWAvhvYATMKWV--FDIRDDDIFWCTADIGWVTGHSYVVLGP 335
Cdd:cd17631 98 -------------DDLALLMYTSGTTGRPKGAMLTHRNLL---WNAVNALaaLDLGPDDVLLVVAPLFHIGGLGVFTLPT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 336 LLMGATEVIYEGapdyPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEewPRKHDLSTLRIIHSVGEPInPEAWRWAYR 415
Cdd:cd17631 162 LLRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQHPR--FATTDLSSLRAVIYGGAPM-PERLLRALQ 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 416 VLGnekVAFGSTWWMTETGGIVishapgLYLVP----MKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGML 491
Cdd:cd17631 235 ARG---VKFVQGYGMTETSPGV------TFLSPedhrRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGP--HVM 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 492 HGIWGDPEryiKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAI 571
Cdd:cd17631 304 AGYWNRPE---ATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEK 380
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 20137268 572 KGEVPIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMR 629
Cdd:cd17631 381 WGEAVVAVVVPRPGAELDED---ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
119-628 |
1.63e-69 |
|
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: 234.41 E-value: 1.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TADGFwrrgrvvrlKEVVDAALEKATGVESVIVLPrlgLKDVPMTEGRDYWWNKLmqGIPPNAYIEPEPVESEHPSFILY 278
Cdd:cd05911 88 TDPDG---------LEKVKEAAKELGPKDKIIVLD---DKPDGVLSIEDLLSPTL--GEEDEDLPPPLKDGKDDTAAILY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 279 TSGTTGKPKG--IVHDtggwavHVYATMKWVFDIRDDDIFWCTADIG-----WVTGHSYVVLGPLLmGATEVIYEGapdy 351
Cdd:cd05911 154 SSGTTGLPKGvcLSHR------NLIANLSQVQTFLYGNDGSNDVILGflplyHIYGLFTTLASLLN-GATVIIMPK---- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 352 PQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEewPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKVAFGstWWMT 431
Cdd:cd05911 223 FDSELFLDLIEKYKITFLYLVPPIAAALAKSPL--LDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQG--YGMT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 432 ETGGIvISHAPGLYLvpmKPGTNGPPLPGFEVDVVDENGNPA-PPGVKGYLVIKKPwpGMLHGIWGDPEryiKTYWSRFP 510
Cdd:cd05911 299 ETGGI-LTVNPDGDD---KPGSVGRLLPNVEAKIVDDDGKDSlGPNEPGEICVRGP--QVMKGYYNNPE---ATKETFDE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 511 GMFY-AGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQG-VAP 588
Cdd:cd05911 370 DGWLhTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGeKLT 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 20137268 589 SDELRKELREHV----RRTIGpiaepaqIFFVTKLPKTRSGKIM 628
Cdd:cd05911 450 EKEVKDYVAKKVasykQLRGG-------VVFVDEIPKSASGKIL 486
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
118-633 |
1.72e-64 |
|
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: 219.09 E-value: 1.72e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 118 RRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIV 197
Cdd:cd05934 1 GRRWTYAELLRESARIAAAL-AALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 198 ITAdgfwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepvesehPSFIL 277
Cdd:cd05934 80 VVD------------------------------------------------------------------------PASIL 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 278 YTSGTTGKPKGIVhDTGGWAVHVYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIyegAPDYpQPDRW 357
Cdd:cd05934 88 YTSGTTGPPKGVV-ITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVL---LPRF-SASRF 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 358 WSIIERYGVTIFYTSPTAIRMFMRYGE-EWPRKHdlsTLRIIHsvGEPINPEAWRWAYRVLGnekVAFGSTWWMTETGGI 436
Cdd:cd05934 163 WSDVRRYGATVTNYLGAMLSYLLAQPPsPDDRAH---RLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTETIVG 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 437 VISHAPGlylvPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIK-KPWPGMLHGIWGDPERYIKtywsRFP-GMFY 514
Cdd:cd05934 235 VIGPRDE----PRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRgLRGWGFFKGYYNMPEATAE----AMRnGWFH 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 515 AGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDElrk 594
Cdd:cd05934 307 TGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE--- 383
|
490 500 510
....*....|....*....|....*....|....*....
gi 20137268 595 ELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:cd05934 384 ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
121-636 |
6.44e-64 |
|
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: 217.82 E-value: 6.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINdsqsrivita 200
Cdd:cd05974 1 VSFAEMSARSSRVANFLRS-IGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVD---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 201 dgfwrRGRVVRlkevvdAALEKATgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepvESEHPSFILYTS 280
Cdd:cd05974 70 -----RGGAVY------AAVDENT--------------------------------------------HADDPMLLYFTS 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 281 GTTGKPKGIVHDTGGWAVHVYATMKWVfDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYegapDYPQ--PDRWW 358
Cdd:cd05974 95 GTTSKPKLVEHTHRSYPVGHLSTMYWI-GLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLF----NYARfdAKRVL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 359 SIIERYGVTIFYTSPTAIRMFMrygeewprKHDLST----LRIIHSVGEPINPEawrwayrVLGNEKVAFGST----WWM 430
Cdd:cd05974 170 AALVRYGVTTLCAPPTVWRMLI--------QQDLASfdvkLREVVGAGEPLNPE-------VIEQVRRAWGLTirdgYGQ 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 431 TETGgIVISHAPGLylvPMKPGTNGPPLPGFEVDVVDENGNPAPPGvKGYLVIKKPWP-GMLHGIWGDPEryiKTYWSRF 509
Cdd:cd05974 235 TETT-ALVGNSPGQ---PVKAGSMGRPLPGYRVALLDPDGAPATEG-EVALDLGDTRPvGLMKGYAGDPD---KTAHAMR 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 510 PGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPS 589
Cdd:cd05974 307 GGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPS 386
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 20137268 590 DELRKELREHVRRTIGPIAEPAQIFFVtKLPKTRSGKIMRRLLKAVA 636
Cdd:cd05974 387 PETALEIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRRRE 432
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
115-633 |
6.28e-62 |
|
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: 214.48 E-value: 6.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 115 PTDRRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQS 194
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQL-AALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 195 RIVITADGFWR---RGRVVRLKEVVDAALEKATGVESVIVLPRLGLKDVPmtegrdywwnklmqgipPNAYIEPEPVESE 271
Cdd:cd05926 88 KLVLTPKGELGpasRAASKLGLAILELALDVGVLIRAPSAESLSNLLADK-----------------KNAKSEGVPLPDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 272 hPSFILYTSGTTGKPKG--IVHDTGGWAVHVYATmkwVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIyegaP 349
Cdd:cd05926 151 -LALILHTSGTTGRPKGvpLTHRNLAASATNITN---TYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVL----P 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 350 DYPQPDRWWSIIERYGVTIFYTSPTAIR-MFMRYGEEWPRKHdlSTLRIIHSVGEPINPEawrwayrVLGNEKVAFGS-- 426
Cdd:cd05926 223 PRFSASTFWPDVRDYNATWYTAVPTIHQiLLNRPEPNPESPP--PKLRFIRSCSASLPPA-------VLEALEATFGApv 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 427 --TWWMTETggiviSHA----PgLYLVPMKPGTNGPPLpGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPEr 500
Cdd:cd05926 294 leAYGMTEA-----AHQmtsnP-LPPGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGP--NVTRGYLNNPE- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 501 yiKTYWSRFP-GMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAF 579
Cdd:cd05926 364 --ANAEAAFKdGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAA 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 20137268 580 VVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:cd05926 442 VVLREGASVTEE---ELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
98-640 |
3.54e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 204.78 E-value: 3.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 98 NKLAIEWEGepvdengyptdrRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVF 177
Cdd:PRK08316 26 DKTALVFGD------------RSWTYAELDAAVNRVAAAL-LDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 178 SGFSADALAERINDSQSRIVITADGfwrrgrvvrLKEVVDAALEKAtGVESVIVLPRLGLKDVPmteGRDYWWNKLMQGI 257
Cdd:PRK08316 93 FMLTGEELAYILDHSGARAFLVDPA---------LAPTAEAALALL-PVDTLILSLVLGGREAP---GGWLDFADWAEAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 258 PPNayiEPEP-VESEHPSFILYTSGTTGKPKGIVHdTGGWAVHVYATMKWVFDIRDDDIFWCTADIGwvtgHS---YVVL 333
Cdd:PRK08316 160 SVA---EPDVeLADDDLAQILYTSGTESLPKGAML-THRALIAEYVSCIVAGDMSADDIPLHALPLY----HCaqlDVFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 334 GP-LLMGATEVIYEGapdyPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYgeewPR--KHDLSTLRIIHsVGEPINPEAw 410
Cdd:PRK08316 232 GPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLRH----PDfdTRDLSSLRKGY-YGASIMPVE- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 411 rwayrVLgNE------KVAFGSTWWMTETGGIVISHAPGLYLvpMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIK 484
Cdd:PRK08316 302 -----VL-KElrerlpGLRFYNCYGQTEIAPLATVLGPEEHL--RRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 485 KPwpGMLHGIWGDPEryiKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAV 564
Cdd:PRK08316 374 SP--QLMLGYWDDPE---KTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAV 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20137268 565 VGVPDAIKGEVPIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVATGAP 640
Cdd:PRK08316 449 IGLPDPKWIEAVTAVVVPKAGATVTED---ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGAF 521
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
114-634 |
1.10e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 203.21 E-value: 1.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 114 YPTDRRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQ 193
Cdd:PRK07656 24 YVFGDQRLTYAELNARVRRAAAAL-AALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 194 SRIVITADGFwrrgrvVRLKEVVDAALEKatgVESVIVLPRLGLKDVPMTEGRdywWNKLMqGIPPNAYIEPEpVESEHP 273
Cdd:PRK07656 103 AKALFVLGLF------LGVDYSATTRLPA---LEHVVICETEEDDPHTEKMKT---FTDFL-AAGDPAERAPE-VDPDDV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 274 SFILYTSGTTGKPKGIV--HDTGGWAVHVYATmkwVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIyegAPDY 351
Cdd:PRK07656 169 ADILFTSGTTGRPKGAMltHRQLLSNAADWAE---YLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILP---LPVF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 352 pQPDRWWSIIERYGVTIFYTSPTaIRMFMrYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKVAFGstWWMT 431
Cdd:PRK07656 243 -DPDEVFRLIETERITVLPGPPT-MYNSL-LQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTG--YGLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 432 ETGGIVISHAPGLYLVPMkPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKpwPGMLHGIWGDPERYIKTYwsRFPG 511
Cdd:PRK07656 318 EASGVTTFNRLDDDRKTV-AGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRG--PNVMKGYYDDPEATAAAI--DADG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 512 MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGvAPSDE 591
Cdd:PRK07656 393 WLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG-AELTE 471
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 20137268 592 lrKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:PRK07656 472 --EELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
119-632 |
2.98e-56 |
|
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: 199.38 E-value: 2.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKqNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:cd05904 31 RALTYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TADGfwrrgrvvRLKEVVDAALEkatgvesVIVLPRLglKDVPMTEGRDYWWNKlmQGIPPNAYIEPEpveseHPSFILY 278
Cdd:cd05904 110 TTAE--------LAEKLASLALP-------VVLLDSA--EFDSLSFSDLLFEAD--EAEPPVVVIKQD-----DVAALLY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 279 TSGTTGKPKGIV--HDTGGWAVHVYaTMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIyegAPDYPQPDr 356
Cdd:cd05904 166 SSGTTGRSKGVMltHRNLIAMVAQF-VAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVV---MPRFDLEE- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 357 WWSIIERYGVTIFYTSPTAIRMFMRYGEEwpRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNekVAFGSTWWMTETGGI 436
Cdd:cd05904 241 LLAAIERYKVTHLPVVPPIVLALVKSPIV--DKYDLSSLRQIMSGAAPLGKELIEAFRAKFPN--VDLGQGYGMTESTGV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 437 VISHAPGLYLvPMKPGTNGPPLPGFEVDVVD-ENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPERYIKTYwsRFPGMFYA 515
Cdd:cd05904 317 VAMCFAPEKD-RAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGP--SIMKGYLNNPEATAATI--DKEGWLHT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 516 GDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGvapSDELRKE 595
Cdd:cd05904 392 GDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPG---SSLTEDE 468
|
490 500 510
....*....|....*....|....*....|....*..
gi 20137268 596 LREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:cd05904 469 IMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
117-632 |
8.88e-56 |
|
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: 196.21 E-value: 8.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAitsvVFSGFSADALAERIN----DS 192
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRER-GVGPGDLVAVLLERSLEMVVAILAVLKAGA----AYVPLDPSYPAERLAyileDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 193 QSRIVITadgfwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepvESEH 272
Cdd:cd05930 84 GAKLVLT---------------------------------------------------------------------DPDD 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 273 PSFILYTSGTTGKPKGIVHDTGGWAVHVYAtMKWVFDIRDDDIFWCTADIGWVtGHSYVVLGPLLMGATEVI--YEGAPD 350
Cdd:cd05930 95 LAYVIYTSGSTGKPKGVMVEHRGLVNLLLW-MQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATLVVlpEEVRKD 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 351 ypqPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWprkhDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKV-------- 422
Cdd:cd05930 173 ---PEALADLLAEEGITVLHLTPSLLRLLLQELELA----ALPSLRLVLVGGEALPPDLVRRWRELLPGARLvnlygpte 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 423 -AFGSTWW-----MTETGGIVIshapglylvpmkpgtnGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWG 496
Cdd:cd05930 246 aTVDATYYrvppdDEEDGRVPI----------------GRPIPNTRVYVLDENLRPVPPGVPGELYIGGA--GLARGYLN 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 497 DPE----RYIKTYWsrFPGM-FYA-GDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDA 570
Cdd:cd05930 308 RPEltaeRFVPNPF--GPGErMYRtGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDG 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20137268 571 IKGEVPIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:cd05930 386 DGEKRLVAYVVPDEGGELDEE---ELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
61-636 |
3.58e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 194.87 E-value: 3.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 61 WDKVLDASNPPFYKWFVGGRLNLSYLavdRHVKTWRKNKLAIEWEGepvdengyptdrRKLTYYDLYREVNRVAYMLKQN 140
Cdd:PRK06178 14 QQAAWPAGIPREPEYPHGERPLTEYL---RAWARERPQRPAIIFYG------------HVITYAELDELSDRFAALLRQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 141 fGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITADGFWRRGRVVR----LKEVV 216
Cdd:PRK06178 79 -GVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRaetsLRHVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 217 DAALEKATGVESVIVLPRLGLKDVPMTEGrdywWNKLMQGIP-PNAYIEPEPVESEHPSFILYTSGTTGKPKGIVHdTGG 295
Cdd:PRK06178 158 VTSLADVLPAEPTLPLPDSLRAPRLAAAG----AIDLLPALRaCTAPVPLPPPALDALAALNYTGGTTGMPKGCEH-TQR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 296 WAVHVYATMKWV-FDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEgapdypqpdRW-----WSIIERYGVTif 369
Cdd:PRK06178 233 DMVYTAAAAYAVaVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLA---------RWdavafMAAVERYRVT-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 370 ytsptaiRMFM---RYGE--EWPR--KHDLSTLRIIHSVG--EPINPEaWRWAYRVLGNEKVAFGStWWMTETggivisH 440
Cdd:PRK06178 302 -------RTVMlvdNAVElmDHPRfaEYDLSSLRQVRVVSfvKKLNPD-YRQRWRALTGSVLAEAA-WGMTET------H 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 441 APGLYLVPMK---------PGTNGPPLPGFEVDVVD-ENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPEryiKTYWSRFP 510
Cdd:PRK06178 367 TCDTFTAGFQdddfdllsqPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTP--SLLKGYWNKPE---ATAEALRD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 511 GMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGvapSD 590
Cdd:PRK06178 442 GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPG---AD 518
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 20137268 591 ELRKELREHVRRTIGPIAEPaQIFFVTKLPKTRSGKIMRRLLKAVA 636
Cdd:PRK06178 519 LTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDLQALA 563
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
121-649 |
3.18e-53 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 193.63 E-value: 3.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAawriGAITSVVFS---GFSADALAERINDSQSRIV 197
Cdd:PRK07529 59 WTYAELLADVTRTANLLHS-LGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANPinpLLEPEQIAELLRAAGAKVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 198 ITADGF-----WR-----RGRVVRLKEVVDAALEKATGVESVIVLPRLGlkdvPMTEGRDYWWNKLMQGIPPNAYIEPEP 267
Cdd:PRK07529 134 VTLGPFpgtdiWQkvaevLAALPELRTVVEVDLARYLPGPKRLAVPLIR----RKAHARILDFDAELARQPGDRLFSGRP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 268 VESEHPSFILYTSGTTGKPKGIVHDTG-----GWAVHVyatmkwVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATe 342
Cdd:PRK07529 210 IGPDDVAAYFHTGGTTGMPKLAQHTHGnevanAWLGAL------LLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAH- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 343 VIYEGAPDYPQP---DRWWSIIERYGVTIFYTSPTAIRMFMRYgeewPR-KHDLSTLRIIHSVGEPINPEAWRWAYRVLG 418
Cdd:PRK07529 283 VVLATPQGYRGPgviANFWKIVERYRINFLSGVPTVYAALLQV----PVdGHDISSLRYALCGAAPLPVEVFRRFEAATG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 419 NEKV-AFGstwwMTETGGIVISHAPGlylVPMKPGTNGPPLPGFEVDVV--DENGN---PAPPGVKGYLVIKKP--WPGM 490
Cdd:PRK07529 359 VRIVeGYG----LTEATCVSSVNPPD---GERRIGSVGLRLPYQRVRVVilDDAGRylrDCAVDEVGVLCIAGPnvFSGY 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 491 L-----HGIWGDpERYIKTywsrfpgmfyaGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVV 565
Cdd:PRK07529 432 LeaahnKGLWLE-DGWLNT-----------GDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAV 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 566 GVPDAIKGEVPIAFVVLKQGVAPSDElrkELREHVRRTIG-PIAEPAQIFFVTKLPKTRSGKI---------MRRLLKAV 635
Cdd:PRK07529 500 GRPDAHAGELPVAYVQLKPGASATEA---ELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIfkpalrrdaIRRVLRAA 576
|
570
....*....|....*.
gi 20137268 636 AT--GAPLGDVTTLED 649
Cdd:PRK07529 577 LRdaGVEAEVVDVVED 592
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
121-634 |
1.13e-52 |
|
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: 187.59 E-value: 1.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITA 200
Cdd:cd05903 2 LTYSELDTRADRLAAGLAA-LGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 201 DGFwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmtEGRDYwwnklmqgippnayiEPEPVEsehPSFILYTS 280
Cdd:cd05903 81 ERF----------------------------------------RQFDP---------------AAMPDA---VALLLFTS 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 281 GTTGKPKGIVH--DTGGWAVHVYATMkwvFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYegapDYPQPDRWW 358
Cdd:cd05903 103 GTTGEPKGVMHshNTLSASIRQYAER---LGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQ----DIWDPDKAL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 359 SIIERYGVTIFYTSPTAIRMFMRYGEEWPRkhDLSTLRIIHSVGEPINPEAWRWAYRVLGnEKVAfgSTWWMTETGGIVI 438
Cdd:cd05903 176 ALMREHGVTFMMGATPFLTDLLNAVEEAGE--PLSRLRTFVCGGATVPRSLARRAAELLG-AKVC--SAYGSTECPGAVT 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 439 SHAPGLYLVPMkpGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPERYIKTYWSrfpGMFYAGDY 518
Cdd:cd05903 251 SITPAPEDRRL--YTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGP--SVFLGYLDRPDLTADAAPE---GWFRTGDL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 519 AIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDElrkELRE 598
Cdd:cd05903 324 ARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFD---ELVA 400
|
490 500 510
....*....|....*....|....*....|....*..
gi 20137268 599 HV-RRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:cd05903 401 YLdRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
117-634 |
8.83e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 187.50 E-value: 8.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIG-AITSVVFSGfSADALAERINDSQSR 195
Cdd:PRK06188 34 GDTRLTYGQLADRISRYIQAF-EALGLGTGDAVALLSLNRPEVLMAIGAAQLAGlRRTALHPLG-SLDDHAYVLEDAGIS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 196 IVITADG-FWRRGRvvrlkevvdAALEKATGVESVivlprLGLKDVPmtEGRDYWwnklmQGIppnAYIEPEPVESEH-- 272
Cdd:PRK06188 112 TLIVDPApFVERAL---------ALLARVPSLKHV-----LTLGPVP--DGVDLL-----AAA---AKFGPAPLVAAAlp 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 273 --PSFILYTSGTTGKPKGIVH---DTGGWAVHVYATMKWVFDIRdddiFWCTADIGWVTGhSYVVlgPLLM-GATEVIYE 346
Cdd:PRK06188 168 pdIAGLAYTGGTTGKPKGVMGthrSIATMAQIQLAEWEWPADPR----FLMCTPLSHAGG-AFFL--PTLLrGGTVIVLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 347 GApdypQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEewPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNekvAFGS 426
Cdd:PRK06188 241 KF----DPAEVLRAIEEQRITATFLVPTMIYALLDHPD--LRTRDLSSLETVYYGASPMSPVRLAEAIERFGP---IFAQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 427 TWWMTETGgIVISHAPGLYLVPMKP---GTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPERYIK 503
Cdd:PRK06188 312 YYGQTEAP-MVITYLRKRDHDPDDPkrlTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGP--LVMDGYWNRPEETAE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 504 TYWSrfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLK 583
Cdd:PRK06188 389 AFRD---GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLR 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 20137268 584 QGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:PRK06188 466 PGAAVDAA---ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRA 513
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
118-641 |
2.27e-51 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 186.80 E-value: 2.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 118 RRKLTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIV 197
Cdd:PRK13295 53 PRRFTYRELAALVDRVAVGLAR-LGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 198 ITADGFwrRG----RVVR--------LKEVVDAALEKATGVESVIVLPRlglkdvpmtegrdywWNKLMQGIPPNAYIEP 265
Cdd:PRK13295 132 VVPKTF--RGfdhaAMARrlrpelpaLRHVVVVGGDGADSFEALLITPA---------------WEQEPDAPAILARLRP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 266 EPVESehpSFILYTSGTTGKPKGIVH--DTGGWAVHVYATMkwvFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEV 343
Cdd:PRK13295 195 GPDDV---TQLIYTSGTTGEPKGVMHtaNTLMANIVPYAER---LGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 344 IYegapDYPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEwpRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKVa 423
Cdd:PRK13295 269 LQ----DIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKE--SGRPVSSLRTFLCAGAPIPGALVERARAALGAKIV- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 424 fgSTWWMTETGgIVISHAPGLYLvPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPERYIk 503
Cdd:PRK13295 342 --SAWGMTENG-AVTLTKLDDPD-ERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGC--SNFGGYLKRPQLNG- 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 504 tywSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLK 583
Cdd:PRK13295 415 ---TDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPR 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 20137268 584 QGVAPSDELRKELREHVRRTIGPIAEPAQIffVTKLPKTRSGKIMRRLLKAVATGAPL 641
Cdd:PRK13295 492 PGQSLDFEEMVEFLKAQKVAKQYIPERLVV--RDALPRTPSGKIQKFRLREMLRGEDA 547
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
116-634 |
3.10e-51 |
|
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: 183.65 E-value: 3.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 116 TDRRKLTYYDLYREVNRVAYMLKQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSR 195
Cdd:cd05941 7 DDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 196 IVItadgfwrrgrvvrlkevvDAALekatgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepvesehpsf 275
Cdd:cd05941 87 LVL------------------DPAL------------------------------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 276 ILYTSGTTGKPKGIVHDTGGWAVHVYA-TMKWVFdiRDDDIFWCTADIGWVTGHSYVVLGPLLMGATeVIYEGAPDypqP 354
Cdd:cd05941 94 ILYTSGTTGRPKGVVLTHANLAANVRAlVDAWRW--TEDDVLLHVLPLHHVHGLVNALLCPLFAGAS-VEFLPKFD---P 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 355 DRWWSIIERYGVTIFYTSPTA-IRM-----FMRYGEEWPRKHDLSTLRIIHSVGEPINPEAW-RWAYRvlgnekvaFGST 427
Cdd:cd05941 168 KEVAISRLMPSITVFMGVPTIyTRLlqyyeAHFTDPQFARAAAAERLRLMVSGSAALPVPTLeEWEAI--------TGHT 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 428 ----WWMTETGGIVISHAPGlylvPMKPGTNGPPLPGFEVDVVDENGN-PAPPGVKGYLVIKKPwpGMLHGIWGDPERYI 502
Cdd:cd05941 240 llerYGMTEIGMALSNPLDG----ERRPGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVRGP--SVFKEYWNKPEATK 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 503 KtyWSRFPGMFYAGDYAIKDKDGYIWVLGR-ADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVV 581
Cdd:cd05941 314 E--EFTDDGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVV 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 20137268 582 LKQGVAPSDELrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:cd05941 392 LRAGAAALSLE--ELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
90-632 |
3.72e-51 |
|
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: 185.53 E-value: 3.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 90 RHVKTWRKNKLAIEWEGEPvdengyptDRRKLTYYDLYREVNRVAYMLKqNFGVKKGDKI-TL------YLpmvpELpit 162
Cdd:cd12119 3 EHAARLHGDREIVSRTHEG--------EVHRYTYAEVAERARRLANALR-RLGVKPGDRVaTLawnthrHL----EL--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 163 MLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITADGFWRrgrvvrlkeVVDAALEKATGVESVIVLPRLGLKDVPM 242
Cdd:cd12119 67 YYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRDFLP---------LLEAIAPRLPTVEHVVVMTDDAAMPEPA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 243 TEG-RDYWwnKLMQGIPPNayiEPEPVESEH-PSFILYTSGTTGKPKGIVHDTGGWAVHVYAT-MKWVFDIRDDDIF--- 316
Cdd:cd12119 138 GVGvLAYE--ELLAAESPE---YDWPDFDENtAAAICYTSGTTGNPKGVVYSHRSLVLHAMAAlLTDGLGLSESDVVlpv 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 317 --------WCTADIGWVTGHSYVVLGPLLMGATevIYEgapdypqpdrwwsIIERYGVTIFYTSPTAIRMFMRYGEEwpR 388
Cdd:cd12119 213 vpmfhvnaWGLPYAAAMVGAKLVLPGPYLDPAS--LAE-------------LIEREGVTFAAGVPTVWQGLLDHLEA--N 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 389 KHDLSTLRIIHSVGEPINP---EAWRWAYrvlgnekVAFGSTWWMTETGGIVISHAPGLYLVPMKPG-------TNGPPL 458
Cdd:cd12119 276 GRDLSSLRRVVIGGSAVPRsliEAFEERG-------VRVIHAWGMTETSPLGTVARPPSEHSNLSEDeqlalraKQGRPV 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 459 PGFEVDVVDENGNPAP--PGVKGYLVIKKPWpgMLHGIWGDPERyIKTYWSRfpGMFYAGDYAIKDKDGYIWVLGRADEV 536
Cdd:cd12119 349 PGVELRIVDDDGRELPwdGKAVGELQVRGPW--VTKSYYKNDEE-SEALTED--GWLRTGDVATIDEDGYLTITDRSKDV 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 537 IKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFV 616
Cdd:cd12119 424 IKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAE---ELLEFLADKVAKWWLPDDVVFV 500
|
570
....*....|....*.
gi 20137268 617 TKLPKTRSGKIMRRLL 632
Cdd:cd12119 501 DEIPKTSTGKIDKKAL 516
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
104-634 |
8.63e-51 |
|
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: 184.58 E-value: 8.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 104 WEGEPVDE------NGYPtDR-------RKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIG 170
Cdd:COG1021 22 WRGETLGDllrrraERHP-DRiavvdgeRRLSYAELDRRADRLAAGL-LALGLRPGDRVVVQLPNVAEFVIVFFALFRAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 171 AItsVVFSGFS-----ADALAERindSQSRIVITADGFwrrgRVVRLKEVVDAALEKATGVESVIVL----PRLGLKDVP 241
Cdd:COG1021 100 AI--PVFALPAhrraeISHFAEQ---SEAVAYIIPDRH----RGFDYRALARELQAEVPSLRHVLVVgdagEFTSLDALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 242 MTegrdywwnklmqgipPNAYIEPEPvESEHPSFILYTSGTTGKPKGI--VHDTGGWAVHVYATMkWVFDirDDDIFWCT 319
Cdd:COG1021 171 AA---------------PADLSEPRP-DPDDVAFFQLSGGTTGLPKLIprTHDDYLYSVRASAEI-CGLD--ADTVYLAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 320 ADIGwvtgHSY-----VVLGPLLMGATEVIyegAPDyPQPDRWWSIIERYGVTIfyTS--PTAIRMFMRYGEEwpRKHDL 392
Cdd:COG1021 232 LPAA----HNFplsspGVLGVLYAGGTVVL---APD-PSPDTAFPLIERERVTV--TAlvPPLALLWLDAAER--SRYDL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 393 STLRIIHSVGEPINPEAwrwAYRV-------LGNekvAFGstwwMTEtggivishapGL--YLVPMKP-----GTNGPPL 458
Cdd:COG1021 300 SSLRVLQVGGAKLSPEL---ARRVrpalgctLQQ---VFG----MAE----------GLvnYTRLDDPeevilTTQGRPI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 459 -PGFEVDVVDENGNPAPPGVKGYLVIKKPWpgmlhgiwgdperYIKTYWsRFP----------GMFYAGDYAIKDKDGYI 527
Cdd:COG1021 360 sPDDEVRIVDEDGNPVPPGEVGELLTRGPY-------------TIRGYY-RAPehnaraftpdGFYRTGDLVRRTPDGYL 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 528 WVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLkQGVAPSdelRKELREHVRRtIGpI 607
Cdd:COG1021 426 VVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVP-RGEPLT---LAELRRFLRE-RG-L 499
|
570 580 590
....*....|....*....|....*....|
gi 20137268 608 AE---PAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:COG1021 500 AAfklPDRLEFVDALPLTAVGKIDKKALRA 529
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
116-632 |
6.25e-50 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 181.60 E-value: 6.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 116 TDRRKLTYYDLYREVNRVAYMLKQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSR 195
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 196 IVITADGFwrrgrvvrlkEVVDAALEKATGVESVIvlprlglkdvpmtegrdywWNKLMQGIPPNAYIEPEPVESEHPSF 275
Cdd:PRK06839 103 VLFVEKTF----------QNMALSMQKVSYVQRVI-------------------SITSLKEIEDRKIDNFVEKNESASFI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 276 ILYTSGTTGKPKGIV--HDTGGW-AVHVYATMkwvfDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIyegaPDYP 352
Cdd:PRK06839 154 ICYTSGTTGKPKGAVltQENMFWnALNNTFAI----DLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIV----PRKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 353 QPDRWWSIIERYGVTIFYTSPT---AIRMFMRYgeewpRKHDLSTLRIIHSVGEPInPEAWRWAYRVLGnekVAFGSTWW 429
Cdd:PRK06839 226 EPTKALSMIEKHKVTVVMGVPTihqALINCSKF-----ETTNLQSVRWFYNGGAPC-PEELMREFIDRG---FLFGQGFG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 430 MTETggivishAPGLYLVP-----MKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPERYIKT 504
Cdd:PRK06839 297 MTET-------SPTVFMLSeedarRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGP--NVMKEYWNRPDATEET 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 505 YWSrfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQ 584
Cdd:PRK06839 368 IQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKS 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 20137268 585 GVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:PRK06839 445 SSVLIEK---DVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
121-632 |
5.66e-49 |
|
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: 177.29 E-value: 5.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITa 200
Cdd:cd05935 2 LTYLELLEVVKKLASFL-SNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 201 dgfwrrgrvvrLKEVVDAALekatgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepvesehpsfILYTS 280
Cdd:cd05935 80 -----------GSELDDLAL-------------------------------------------------------IPYTS 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 281 GTTGKPKGIVHDTGGWAVHVYATMKWvFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIY-----EGAPDypqpd 355
Cdd:cd05935 94 GTTGLPKGCMHTHFSAAANALQSAVW-TGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMarwdrETALE----- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 356 rwwsIIERYGVTIFYTSPTAIRMFMRYGEEwpRKHDLSTLRIIHSVGEPInPEAWrwAYRVLGNEKVAFGSTWWMTETGG 435
Cdd:cd05935 168 ----LIEKYKVTFWTNIPTMLVDLLATPEF--KTRDLSSLKVLTGGGAPM-PPAV--AEKLLKLTGLRFVEGYGLTETMS 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 436 IVISHAPGlylvPMKPGTNGPPLPGFEVDVVD-ENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPERYIKTYWS----RFp 510
Cdd:cd05935 239 QTHTNPPL----RPKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGP--QIFKGYWNRPEETEESFIEikgrRF- 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 511 gmFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLK---QGVA 587
Cdd:cd05935 312 --FRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRpeyRGKV 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 20137268 588 PSDELRKELREHvrrtIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:cd05935 390 TEEDIIEWAREQ----MAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
122-564 |
1.84e-48 |
|
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: 175.15 E-value: 1.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 122 TYYDLYREVNRVAYMLKQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAitsvVFSGFSADALAERIN----DSQSRIV 197
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGA----AYVPLDPAYPAERLAfileDAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 198 ITADGFW-RRGRVVRLKEVVDAALEKATGVESVIVLPrlglkdvpmtegrdywwnklmqgippnayiePEPVESEHPSFI 276
Cdd:TIGR01733 77 LTDSALAsRLAGLVLPVILLDPLELAALDDAPAPPPP-------------------------------DAPSGPDDLAYV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIVHDTGGwAVHVYATMKWVFDIRDDDIfwctadigWVTGHSYV-------VLGPLLMGATEVIYEGAP 349
Cdd:TIGR01733 126 IYTSGSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------VLQFASLSfdasveeIFGALLAGATLVVPPEDE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 350 DYPQPDRWWSIIERYGVTIFYTSPTAIRMFMrygEEWPRkhDLSTLRIIHSVGEPINPEA---WRWAY--RVLGNE---- 420
Cdd:TIGR01733 197 ERDDAALLAALIAEHPVTVLNLTPSLLALLA---AALPP--ALASLRLVILGGEALTPALvdrWRARGpgARLINLygpt 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 421 KVAFGSTWWMTEtggivISHAPGLYLVPMkpgtnGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDP-- 498
Cdd:TIGR01733 272 ETTVWSTATLVD-----PDDAPRESPVPI-----GRPLANTRLYVLDDDLRPVPVGVVGELYIGGP--GVARGYLNRPel 339
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20137268 499 --ERYIK-TYWSRFPGMFYA-GDYAIKDKDGYIWVLGRADEVIKVAGHR--LGtyELESALISHPAVAESAV 564
Cdd:TIGR01733 340 taERFVPdPFAGGDGARLYRtGDLVRYLPDGNLEFLGRIDDQVKIRGYRieLG--EIEAALLRHPGVREAVV 409
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
98-634 |
4.69e-48 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 175.92 E-value: 4.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 98 NKLAIEWEGEpvdengyptdrrKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVF 177
Cdd:PRK03640 17 DRTAIEFEEK------------KVTFMELHEAVVSVAGKL-AALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 178 SGFSADALAERINDSQSRIVITADGFwrrgrvvrlkevvdaaLEKATGVESVIvlprlglkdvpmtegrdywWNKLMQGi 257
Cdd:PRK03640 84 TRLSREELLWQLDDAEVKCLITDDDF----------------EAKLIPGISVK-------------------FAELMNG- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 258 ppnAYIEPEPVESEHPSF---ILYTSGTTGKPKGIVHDTGGwavHVYATMKWVFD--IRDDDIFWCTADIGWVTGHSyvv 332
Cdd:PRK03640 128 ---PKEEAEIQEEFDLDEvatIMYTSGTTGKPKGVIQTYGN---HWWSAVGSALNlgLTEDDCWLAAVPIFHISGLS--- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 333 lgpLLMgaTEVIYeGAPDYPQP----DRWWSIIERYGVTIFYTSPTairMFMRYGEEWPRKHDLSTLRIIHSVGEPINP- 407
Cdd:PRK03640 199 ---ILM--RSVIY-GMRVVLVEkfdaEKINKLLQTGGVTIISVVST---MLQRLLERLGEGTYPSSFRCMLLGGGPAPKp 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 408 ---EAWRWAYRVLgnekvafgSTWWMTETGGIVISHAPGLYLvpMKPGTNGPPLPGFEVDVVDeNGNPAPPGVKGYLVIK 484
Cdd:PRK03640 270 lleQCKEKGIPVY--------QSYGMTETASQIVTLSPEDAL--TKLGSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 485 KP--WPGMLHgiwgDPEryiKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAES 562
Cdd:PRK03640 339 GPnvTKGYLN----RED---ATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEA 411
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20137268 563 AVVGVPDAIKGEVPIAFVVLKQGVaPSDELRKELREHvrrtigpIAE---PAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:PRK03640 412 GVVGVPDDKWGQVPVAFVVKSGEV-TEEELRHFCEEK-------LAKykvPKRFYFVEELPRNASGKLLRHELKQ 478
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
119-656 |
2.37e-47 |
|
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: 180.44 E-value: 2.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAitsvVF----SGFSADALAERINDSQS 194
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRAL-GVGPGDLVGVCLERSLEMVVALLAVLKAGA----AYvpldPAYPAERLAYMLEDAGA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 195 RIVITADGFwrrgrvvrlkevvdAALEKATGVEsVIVLPRLGLKDVPMTegrdywwnklmqgiPPnayiePEPVESEHPS 274
Cdd:COG1020 575 RLVLTQSAL--------------AARLPELGVP-VLALDALALAAEPAT--------------NP-----PVPVTPDDLA 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 275 FILYTSGTTGKPKGIVHDTGGwAVHVYATMKWVFDIRDDDIfwctadIGWVTGHS-----YVVLGPLLMGATEVIY--EG 347
Cdd:COG1020 621 YVIYTSGSTGRPKGVMVEHRA-LVNLLAWMQRRYGLGPGDR------VLQFASLSfdasvWEIFGALLSGATLVLAppEA 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 348 APDypqPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEwprkhDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKV--AFG 425
Cdd:COG1020 694 RRD---PAALAELLARHRVTVLNLTPSLLRALLDAAPE-----ALPSLRLVLVGGEALPPELVRRWRARLPGARLvnLYG 765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 426 stwwMTETGGIVISHAPGLYLVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIkkpwpgmlHGI------WGDP- 498
Cdd:COG1020 766 ----PTETTVDSTYYEVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYI--------GGAglargyLNRPe 833
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 499 ---ERYIKTYWSrFPG--MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHR--LGtyELESALISHPAVAESAVVGVPDAI 571
Cdd:COG1020 834 ltaERFVADPFG-FPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRieLG--EIEAALLQHPGVREAVVVAREDAP 910
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 572 KGEVPIAFVVLKQGVAPSDELRkelREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVATGAPLGDVTTLEDET 651
Cdd:COG1020 911 GDKRLVAYVVPEAGAAAAAALL---RLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEE 987
|
....*
gi 20137268 652 SVEEA 656
Cdd:COG1020 988 EEEAA 992
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
117-633 |
2.85e-47 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 174.49 E-value: 2.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRI 196
Cdd:PRK08008 34 VVRRYSYLELNEEINRTANLFYS-LGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VITADGFWRRGRvvRLKEVVDAALEKatgvesvIVLPRLGLkdvPMTEGR-DYWWNKLMQgipPNAYIEPEPVESEHPSF 275
Cdd:PRK08008 113 LVTSAQFYPMYR--QIQQEDATPLRH-------ICLTRVAL---PADDGVsSFTQLKAQQ---PATLCYAPPLSTDDTAE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 276 ILYTSGTTGKPKGIV--HDTGGWAVHVYAtmkWVFDIRDDDI-----------FWCTAdigwvtghsyvVLGPLLMGATE 342
Cdd:PRK08008 178 ILFTSGTTSRPKGVVitHYNLRFAGYYSA---WQCALRDDDVyltvmpafhidCQCTA-----------AMAAFSAGATF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 343 VIYEgapDYpQPDRWWSIIERYGVTIFYTSPTAIRMFM-RYGEEWPRKHDLSTLRIIHSVGEpinpeawrwayrvlgNEK 421
Cdd:PRK08008 244 VLLE---KY-SARAFWGQVCKYRATITECIPMMIRTLMvQPPSANDRQHCLREVMFYLNLSD---------------QEK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 422 VAFGS--------TWWMTETGGIVISHAPGlylVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKK-PWPGMLH 492
Cdd:PRK08008 305 DAFEErfgvrlltSYGMTETIVGIIGDRPG---DKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGKTIFK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 493 GIWGDPERYIKTYwsRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIK 572
Cdd:PRK08008 382 EYYLDPKATAKVL--EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIR 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20137268 573 GEVPIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:PRK08008 460 DEAIKAFVVLNEGETLSEE---EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
119-632 |
3.52e-47 |
|
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: 173.54 E-value: 3.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:cd12117 21 RSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TadgfwrrgrvvrlkevvDAALEKATGVESVIVLPRLGLKDVPmtegrdywwnklmqgiPPNAyiePEPVESEHPSFILY 278
Cdd:cd12117 100 T-----------------DRSLAGRAGGLEVAVVIDEALDAGP----------------AGNP---AVPVSPDDLAYVMY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 279 TSGTTGKPKGI----------VHDTGgwavhvyatmkWVfDIRDDDIFWCTADIGWvTGHSYVVLGPLLMGATEVIYEga 348
Cdd:cd12117 144 TSGSTGRPKGVavthrgvvrlVKNTN-----------YV-TLGPDDRVLQTSPLAF-DASTFEIWGALLNGARLVLAP-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 349 PDYP-QPDRWWSIIERYGVT-IFYTSPtairMFMRYGEEWPRKhdLSTLRIIHSVGEPINPEAWRWAYR-----VLGN-- 419
Cdd:cd12117 209 KGTLlDPDALGALIAEEGVTvLWLTAA----LFNQLADEDPEC--FAGLRELLTGGEVVSPPHVRRVLAacpglRLVNgy 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 420 ---EKVAFgSTWWMTETGGIVISHapglylVPMkpgtnGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWG 496
Cdd:cd12117 283 gptENTTF-TTSHVVTELDEVAGS------IPI-----GRPIANTRVYVLDEDGRPVPPGVPGELYVGGD--GLALGYLN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 497 DP----ERYIKTywSRFPG--MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDA 570
Cdd:cd12117 349 RPaltaERFVAD--PFGPGerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDA 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20137268 571 IKGEVPIAFVVLKQGVAPSdelrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:cd12117 427 GGDKRLVAYVVAEGALDAA-----ELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
119-632 |
6.41e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 174.38 E-value: 6.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:PRK08314 34 RAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TADGFWRRGR----VVRLKEVVDAALEKATGVESVIVLPRLGLKDVP---MTEGRDYWWNK-LMQGIPPnayiEPEPVES 270
Cdd:PRK08314 114 VGSELAPKVApavgNLRLRHVIVAQYSDYLPAEPEIAVPAWLRAEPPlqaLAPGGVVAWKEaLAAGLAP----PPHTAGP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 271 EHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWvFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIY----- 345
Cdd:PRK08314 190 DDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLW-SNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMprwdr 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 346 EGAPDypqpdrwwsIIERYGVTIFYTSPTAIRMFMRYgeewPR--KHDLSTLRIIHSVGEPInPEAWrwAYRVLGNEKVA 423
Cdd:PRK08314 269 EAAAR---------LIERYRVTHWTNIPTMVVDFLAS----PGlaERDLSSLRYIGGGGAAM-PEAV--AERLKELTGLD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 424 FGSTWWMTETGGIVISHAPGlylvpmKPGTNGPPLPGFEVD--VVD-ENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPER 500
Cdd:PRK08314 333 YVEGYGLTETMAQTHSNPPD------RPKLQCLGIPTFGVDarVIDpETLEELPPGEVGEIVVHGP--QVFKGYWNRPEA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 501 ----YIKTYWSRFpgmFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVP 576
Cdd:PRK08314 405 taeaFIEIDGKRF---FRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETV 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20137268 577 IAFVVLK---QGVAPSDELRKELREHvrrtigpIAE---PAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:PRK08314 482 KAVVVLRpeaRGKTTEEEIIAWAREH-------MAAykyPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
130-633 |
9.52e-47 |
|
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: 171.85 E-value: 9.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 130 VNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADalaerINDSQSRIVITADGfwrrGRV 209
Cdd:cd05922 3 VSAAASALLEA-GGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPT-----LKESVLRYLVADAG----GRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 210 VRLKEVVDAALEKAtgvesVIVLPrlglkDVPMTEGRDYWWNKlmqgippNAYIEPEPVESEHPSFILYTSGTTGKPKGI 289
Cdd:cd05922 73 VLADAGAADRLRDA-----LPASP-----DPGTVLDADGIRAA-------RASAPAHEVSHEDLALLLYTSGSTGSPKLV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 290 V--H---DTGGWAVHVYatmkwvFDIRDDDIFWCTADIGWVTGHSyVVLGPLLMGATEVIyegAPDYPQPDRWWSIIERY 364
Cdd:cd05922 136 RlsHqnlLANARSIAEY------LGITADDRALTVLPLSYDYGLS-VLNTHLLRGATLVL---TNDGVLDDAFWEDLREH 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 365 GVTIFYTSPTAIRMFMRYGeeWPrKHDLSTLRIIHSVGEPINPEAWRwAYRVLGnekvafgSTWWMTETGGIVISHAPGL 444
Cdd:cd05922 206 GATGLAGVPSTYAMLTRLG--FD-PAKLPSLRYLTQAGGRLPQETIA-RLRELL-------PGAQVYVMYGQTEATRRMT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 445 YLVP----MKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPWpGMLHGiWGDPERYIKTywSRFPGMFYAGDYAI 520
Cdd:cd05922 275 YLPPerilEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPN-VMKGY-WNDPPYRRKE--GRGGGVLHTGDLAR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 521 KDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIkGEVPIAFVVLKQGVAPSDELRkelreHV 600
Cdd:cd05922 351 RDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKDVLR-----SL 424
|
490 500 510
....*....|....*....|....*....|...
gi 20137268 601 RRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:cd05922 425 AERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
117-632 |
2.31e-46 |
|
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: 170.57 E-value: 2.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAitsvVFSGFSADALAERI----NDS 192
Cdd:cd17643 9 EDRRLTYGELDARANRLARTLRAE-GVGPGDRVALALPRSAELIVALLAILKAGG----AYVPIDPAYPVERIafilADS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 193 QSRIVITadgfwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepvESEH 272
Cdd:cd17643 84 GPSLLLT---------------------------------------------------------------------DPDD 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 273 PSFILYTSGTTGKPKGIV--HdtgGWAVHVYATMKWVFDIRDDDIfwctadigWVTGHSYV-------VLGPLLMGATEV 343
Cdd:cd17643 95 LAYVIYTSGSTGRPKGVVvsH---ANVLALFAATQRWFGFNEDDV--------WTLFHSYAfdfsvweIWGALLHGGRLV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 344 I--YEGAPDypqPDRWWSIIERYGVTIFYTSPTAIRMFMRygEEWPRKHDLSTLRIIHSVGEPINPEAWR-WAYRVlGNE 420
Cdd:cd17643 164 VvpYEVARS---PEDFARLLRDEGVTVLNQTPSAFYQLVE--AADRDGRDPLALRYVIFGGEALEAAMLRpWAGRF-GLD 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 421 KVAFGSTWWMTETgGIVISHAPGL--YLVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKpwPGMLHGIWGDP 498
Cdd:cd17643 238 RPQLVNMYGITET-TVHVTFRPLDaaDLPAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSG--AGVARGYLGRP 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 499 ----ERYIKTYWSRfPG--MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIK 572
Cdd:cd17643 315 eltaERFVANPFGG-PGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPG 393
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 573 GEVPIAFVVLKQGVAPsdeLRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:cd17643 394 DTRLVAYVVADDGAAA---DIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
110-634 |
1.34e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 170.22 E-value: 1.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 110 DENGYPTDRRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAItsVVFSGF--SADALAE 187
Cdd:PRK07470 22 DRIALVWGDRSWTWREIDARVDALAAAL-AARGVRKGDRILVHSRNCNQMFESMFAAFRLGAV--WVPTNFrqTPDEVAY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 188 RINDSQSRIVITADGFwrrgrvvrlKEVVDAALEKATGVESVIVL--PRLGLkDVPMTEGRDywwnklmqgipPNAYIEP 265
Cdd:PRK07470 99 LAEASGARAMICHADF---------PEHAAAVRAASPDLTHVVAIggARAGL-DYEALVARH-----------LGARVAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 266 EPVESEHPSFILYTSGTTGKPKGivhdtggwAVHVYATMKWVFDIRDDDIFWCTadigwvTGH--SYVVlGPL------- 336
Cdd:PRK07470 158 AAVDHDDPCWFFFTSGTTGRPKA--------AVLTHGQMAFVITNHLADLMPGT------TEQdaSLVV-APLshgagih 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 337 -LM----GATEVIYegAPDYPQPDRWWSIIERYGVTIFYTSPTAIRMFMrygeEWPR--KHDLSTLRIIHSVGEPINPEA 409
Cdd:PRK07470 223 qLCqvarGAATVLL--PSERFDPAEVWALVERHRVTNLFTVPTILKMLV----EHPAvdRYDHSSLRYVIYAGAPMYRAD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 410 WRWAYRVLGNEKVA-FGstwwMTE-TGGIVI----SHAPGLylVPM-KPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLV 482
Cdd:PRK07470 297 QKRALAKLGKVLVQyFG----LGEvTGNITVlppaLHDAED--GPDaRIGTCGFERTGMEVQIQDDEGRELPPGETGEIC 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 483 IKKPwpGMLHGIWGDPERYIKTYWSrfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAES 562
Cdd:PRK07470 371 VIGP--AVFAGYYNNPEANAKAFRD---GWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEV 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20137268 563 AVVGVPDAIKGEVPIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:PRK07470 446 AVLGVPDPVWGEVGVAVCVARDGAPVDEA---ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
115-633 |
2.03e-45 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 169.49 E-value: 2.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 115 PTDRRKLTYYDLYREVNRVAYMLKqNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQS 194
Cdd:PRK13391 19 ASTGEVVTYRELDERSNRLAHLFR-SLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 195 RIVITAdgfwrrgrvVRLKEVVDAALEKATGVESVIVLPRLG-----------LKDVPMTEGRDYWWNKLMqgippnayi 263
Cdd:PRK13391 98 RALITS---------AAKLDVARALLKQCPGVRHRLVLDGDGelegfvgyaeaVAGLPATPIADESLGTDM--------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 264 epepvesehpsfiLYTSGTTGKPKGIV----HDTGGWAVHVYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGpLLMG 339
Cdd:PRK13391 160 -------------LYSSGTTGRPKGIKrplpEQPPDTPLPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLV-IRLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 340 ATEVIYEgapdYPQPDRWWSIIERYGVTIFYTSPTairMFMRY---GEEWPRKHDLSTLRI-IHSVGePINPEAWRWAYR 415
Cdd:PRK13391 226 GTVIVME----HFDAEQYLALIEEYGVTHTQLVPT---MFSRMlklPEEVRDKYDLSSLEVaIHAAA-PCPPQVKEQMID 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 416 vlgnekvafgstWW---------MTETGGI-VISHAPGLylvpMKPGTNGPPLPGfEVDVVDENGNPAPPGVKGYLVIKK 485
Cdd:PRK13391 298 ------------WWgpiiheyyaATEGLGFtACDSEEWL----AHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 486 PWPGMLHGiwgDPEryiKTYWSRFP--GMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESA 563
Cdd:PRK13391 361 GRPFEYLN---DPA---KTAEARHPdgTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAA 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 564 VVGVPDAIKGEVPIAFVVLKQGVAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:PRK13391 435 VFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
117-632 |
2.93e-45 |
|
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: 168.22 E-value: 2.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRI 196
Cdd:cd17646 20 EGRTLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VITadgfwRRGRVVRLKEVVDAAlekatgvesviVLPRLGLKDVPMTegrdywwnklmqgiPPnayiePEPVESEHPSFI 276
Cdd:cd17646 99 VLT-----TADLAARLPAGGDVA-----------LLGDEALAAPPAT--------------PP-----LVPPRPDNLAYV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIVHDTGGWAVHVyATMKWVFDIRDDDIFWCTADIGW-VTGhsYVVLGPLLMGATEVIYE----GAPDY 351
Cdd:cd17646 144 IYTSGSTGRPKGVMVTHAGIVNRL-LWMQDEYPLGPGDRVLQKTPLSFdVSV--WELFWPLVAGARLVVARpgghRDPAY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 352 PQpdrwwSIIERYGVTIFYTSPTAIRMFMrygeEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNE--------KVA 423
Cdd:cd17646 221 LA-----ALIREHGVTTCHFVPSMLRVFL----AEPAAGSCASLRRVFCSGEALPPELAARFLALPGAElhnlygptEAA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 424 FGSTWWMTETGGIVIShapglylVPMkpgtnGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDP----E 499
Cdd:cd17646 292 IDVTHWPVRGPAETPS-------VPI-----GRPVPNTRLYVLDDALRPVPVGVPGELYLGGV--QLARGYLGRPaltaE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 500 RYIKtywSRF-PG--MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVP 576
Cdd:cd17646 358 RFVP---DPFgPGsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARL 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 20137268 577 IAFVVLKQGVAPSDElrKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:cd17646 435 VGYVVPAAGAAGPDT--AALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
95-633 |
5.33e-45 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 168.77 E-value: 5.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 95 WRKNKLAIEW----EGEP-----VDENGYptdrrKLTYYDLYREVNRVA-YMLKQnfGVKKGDKITLYLPMVPELPITML 164
Cdd:PRK06087 20 WGDASLADYWqqtaRAMPdkiavVDNHGA-----SYTYSALDHAASRLAnWLLAK--GIEPGDRVAFQLPGWCEFTIIYL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 165 AAWRIGAITSVVFSGFSADALAERINDSQSRIVITADGFWRRGRVVRLKEVVD--AALEKATGVEsvivlprlglKDVPM 242
Cdd:PRK06087 93 ACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLQNqlPQLQQIVGVD----------KLAPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 243 TEGRDYwwNKLMQGIPPNAYiePEPVESEHPSFILYTSGTTGKPKGIV--HDTGGWAVHVYATmkwVFDIRDDDIFWCTA 320
Cdd:PRK06087 163 TSSLSL--SQIIADYEPLTT--AITTHGDELAAVLFTSGTEGLPKGVMltHNNILASERAYCA---RLNLTWQDVFMMPA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 321 DIGWVTGHSYVVLGPLLMGATEVIYegapDYPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPrkHDLSTLRIIHS 400
Cdd:PRK06087 236 PLGHATGFLHGVTAPFLIGARSVLL----DIFTPDACLALLEQQRCTCMLGATPFIYDLLNLLEKQP--ADLSALRFFLC 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 401 VGEPINPEAWRWAYRvlgnEKVAFGSTWWMTETggivishAPGLYLVPMKP-----GTNGPPLPGFEVDVVDENGNPAPP 475
Cdd:PRK06087 310 GGTTIPKKVARECQQ----RGIKLLSVYGSTES-------SPHAVVNLDDPlsrfmHTDGYAAAGVEIKVVDEARKTLPP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 476 GVKGYLVIKKPwpGMLHGIWGDPERYIKTYWSRfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALIS 555
Cdd:PRK06087 379 GCEGEEASRGP--NVFMGYLDEPELTARALDEE--GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQ 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 556 HPAVAESAVVGVPDAIKGEVPIAFVVLKQGVA-PSDElrkELREHVRRT-IGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:PRK06087 455 HPKIHDACVVAMPDERLGERSCAYVVLKAPHHsLTLE---EVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLLR 531
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
117-632 |
5.43e-45 |
|
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: 167.52 E-value: 5.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRI 196
Cdd:cd17651 17 EGRRLTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VITADgfwrrgrvvrlkevvdaALEKATGVESVIVLPRLglkdvpmtegrdywWNKLMQGIPPNAYIEPEPvesEHPSFI 276
Cdd:cd17651 96 VLTHP-----------------ALAGELAVELVAVTLLD--------------QPGAAAGADAEPDPALDA---DDLAYV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIVHDTGGWAVHVY------------ATMKWV---FDIRDDDIFwctadigwvtghsyvvlGPLLMGAT 341
Cdd:cd17651 142 IYTSGSTGRPKGVVMPHRSLANLVAwqarasslgpgaRTLQFAglgFDVSVQEIF-----------------STLCAGAT 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 342 EVIyegAPDY--PQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGeeWPRKHDLSTLRIIHSVGEP-INPEAWRWAYRVLG 418
Cdd:cd17651 205 LVL---PPEEvrTDPPALAAWLDEQRISRVFLPTVALRALAEHG--RPLGVRLAALRYLLTGGEQlVLTEDLREFCAGLP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 419 NEKV--AFGSTWWMTETGGIVishaPGLYLVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKpwPGMLHGIWG 496
Cdd:cd17651 280 GLRLhnHYGPTETHVVTALSL----PGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGG--AGLARGYLN 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 497 DP----ERYIKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIK 572
Cdd:cd17651 354 RPeltaERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPG 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 573 GEVPIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:cd17651 434 EKRLVAYVVGDPEAPVDAA---ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
117-632 |
2.49e-43 |
|
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: 162.46 E-value: 2.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRI 196
Cdd:cd12116 9 DDRSLSYAELDERANRLAARL-RARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VITadgfwrrgrvvrlkevvDAALEKAtgvesvivLPRLGlkDVPMTEGRDywwnklmqgiPPNAYIEPEP-VESEHPSF 275
Cdd:cd12116 88 VLT-----------------DDALPDR--------LPAGL--PVLLLALAA----------AAAAPAAPRTpVSPDDLAY 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 276 ILYTSGTTGKPKGiVHDTGGWAVHVYATMKWVFDIRDDDIFWCtadigwVTGHSYVV-----LGPLLMGATEVIYEgAPD 350
Cdd:cd12116 131 VIYTSGSTGRPKG-VVVSHRNLVNFLHSMRERLGLGPGDRLLA------VTTYAFDIsllelLLPLLAGARVVIAP-RET 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 351 YPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEwprkhDLSTLRIIHSvGEPINPE-AWRWAYRVlgnekvafGSTWW 429
Cdd:cd12116 203 QRDPEALARLIEAHSITVMQATPATWRMLLDAGWQ-----GRAGLTALCG-GEALPPDlAARLLSRV--------GSLWN 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 430 M---TETggiVISHAPGLYLVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPERYIKtyw 506
Cdd:cd12116 269 LygpTET---TIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGD--GVAQGYLGRPALTAE--- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 507 sRF-------PG--MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVpI 577
Cdd:cd12116 341 -RFvpdpfagPGsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRL-V 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 20137268 578 AFVVLKQGVAPSdelRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:cd12116 419 AYVVLKAGAAPD---AAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
119-639 |
3.40e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 163.52 E-value: 3.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVA-YMLKQnfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIV 197
Cdd:PRK07798 27 RRLTYAELEERANRLAhYLIAQ--GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 198 ITADGFwrRGRVVRLkevvdaaLEKATGVESVIVLPRlGLKDVPMTEGRDYWwNKLMQGIPPNAYIEPepveSEHPSFIL 277
Cdd:PRK07798 105 VYEREF--APRVAEV-------LPRLPKLRTLVVVED-GSGNDLLPGAVDYE-DALAAGSPERDFGER----SPDDLYLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 278 YTSGTTGKPKGIVhdtggwavhvyatmkWvfdiRDDDIFWCTAD-IGWVTG---HSYV---------------------- 331
Cdd:PRK07798 170 YTGGTTGMPKGVM---------------W----RQEDIFRVLLGgRDFATGepiEDEEelakraaagpgmrrfpapplmh 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 332 ------VLGPLLMGATEVIYEGapDYPQPDRWWSIIERYGVTifytsptaiRMFMrYGE----------EWPRKHDLSTL 395
Cdd:PRK07798 231 gagqwaAFAALFSGQTVVLLPD--VRFDADEVWRTIEREKVN---------VITI-VGDamarplldalEARGPYDLSSL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 396 RIIHSVGEPINPEAWRWAYRVLGNEKV--AFGSTwwmtETGGIVISHApglylvpmKPGTNGPPLPGFEVD----VVDEN 469
Cdd:PRK07798 299 FAIASGGALFSPSVKEALLELLPNVVLtdSIGSS----ETGFGGSGTV--------AKGAVHTGGPRFTIGprtvVLDED 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 470 GNPAPPG--VKGYLVIKKPWPgmlHGIWGDPERYIKTYwSRFPGMFYA--GDYAIKDKDGYIWVLGRADEVIKVAGHRLG 545
Cdd:PRK07798 367 GNPVEPGsgEIGWIARRGHIP---LGYYKDPEKTAETF-PTIDGVRYAipGDRARVEADGTITLLGRGSVCINTGGEKVF 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 546 TYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSG 625
Cdd:PRK07798 443 PEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLA---ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAG 519
|
570
....*....|....
gi 20137268 626 KIMRRLLKAVATGA 639
Cdd:PRK07798 520 KADYRWAKEQAAER 533
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
119-634 |
5.70e-43 |
|
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: 162.64 E-value: 5.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:TIGR03098 24 RTLTYAALSERVLALASGL-RGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TADgfwrrgrvVRLKEVVDAALEKATGVESVIV-LPRLGLKDVPMTEGRDywWNKLMQGIPPnayIEPEPVESEHPSFIL 277
Cdd:TIGR03098 103 TSS--------ERLDLLHPALPGCHDLRTLIIVgDPAHASEGHPGEEPAS--WPKLLALGDA---DPPHPVIDSDMAAIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 278 YTSGTTGKPKGIV--HDT---GGWAVHVYatmkwvFDIRDDDIFWCTADIGWVTGHSYvVLGPLLMGATEVIYegapDYP 352
Cdd:TIGR03098 170 YTSGSTGRPKGVVlsHRNlvaGAQSVATY------LENRPDDRLLAVLPLSFDYGFNQ-LTTAFYVGATVVLH----DYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 353 QPDRWWSIIERYGVTIFYTSPTairMFMRYGE-EWPrKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKV--------A 423
Cdd:TIGR03098 239 LPRDVLKALEKHGITGLAAVPP---LWAQLAQlDWP-ESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLflmyglteA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 424 FGSTWWMTEtggivishapglyLVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPWpgMLHGIWGDPERYIK 503
Cdd:TIGR03098 315 FRSTYLPPE-------------EVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGAL--VAMGYWNDPEKTAE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 504 TY--------WSRFPGM-FYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGE 574
Cdd:TIGR03098 380 RFrplppfpgELHLPELaVWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQ 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 575 VpIAFVVLKQGVAPSDelRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:TIGR03098 460 A-IVLVVTPPGGEELD--RAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
120-636 |
2.55e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 161.48 E-value: 2.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 120 KLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVIT 199
Cdd:PRK12583 45 RYTWRQLADAVDRLARGL-LALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVIC 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 200 ADGFWRRGRVVRLKEVVDAALEKATGVESVIVLPRLG---LKDVPMTEGRDYWWN--KLMQGIPPNAYIEPEPVESEH-P 273
Cdd:PRK12583 124 ADAFKTSDYHAMLQELLPGLAEGQPGALACERLPELRgvvSLAPAPPPGFLAWHElqARGETVSREALAERQASLDRDdP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 274 SFILYTSGTTGKPKGIV---HDTGGWAVHVYATMKwvfdIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATeVIYEGapD 350
Cdd:PRK12583 204 INIQYTSGTTGFPKGATlshHNILNNGYFVAESLG----LTEHDRLCVPVPLYHCFGMVLANLGCMTVGAC-LVYPN--E 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 351 YPQPDRWWSIIERYGVTIFYTSPTairMFMRYGEEWPRKH-DLSTLRIIHSVGEPINPEAWRwayRVLGNE-----KVAF 424
Cdd:PRK12583 277 AFDPLATLQAVEEERCTALYGVPT---MFIAELDHPQRGNfDLSSLRTGIMAGAPCPIEVMR---RVMDEMhmaevQIAY 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 425 GstwwMTETGGIVISHAPGLYLvPMKPGTNGPPLPGFEVDVVDENGNPAPPG------VKGYLVIKkpwpgmlhGIWGDP 498
Cdd:PRK12583 351 G----MTETSPVSLQTTAADDL-ERRVETVGRTQPHLEVKVVDPDGATVPRGeigelcTRGYSVMK--------GYWNNP 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 499 ERYIKTYWSRfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIA 578
Cdd:PRK12583 418 EATAESIDED--GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVA 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 20137268 579 FVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVA 636
Cdd:PRK12583 496 WVRLHPGHAASEE---ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
114-633 |
5.24e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 159.30 E-value: 5.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 114 YPTDRRkLTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQ 193
Cdd:PRK08276 6 APSGEV-VTYGELEARSNRLAHGLRA-LGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 194 SRIVITADGFwrrgrvvrlkevVDAALEKATGVESVIVLPRLGLKDVPMTEGrdywWNKLMQGIPPnayiepEPVESEHP 273
Cdd:PRK08276 84 AKVLIVSAAL------------ADTAAELAAELPAGVPLLLVVAGPVPGFRS----YEEALAAQPD------TPIADETA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 274 -SFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWV-----FDIRDDDIFWCTADIGwvtgHSYVVL---GPLLMGATEVI 344
Cdd:PRK08276 142 gADMLYSSGTTGRPKGIKRPLPGLDPDEAPGMMLAllgfgMYGGPDSVYLSPAPLY----HTAPLRfgmSALALGGTVVV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 345 YEGApdypQPDRWWSIIERYGVTIFYTSPTairMFMRY---GEEWPRKHDLSTLRIIHSVGEPINPEAWRwayRVLgnek 421
Cdd:PRK08276 218 MEKF----DAEEALALIERYRVTHSQLVPT---MFVRMlklPEEVRARYDVSSLRVAIHAAAPCPVEVKR---AMI---- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 422 vafgsTWW---------MTETGGI-VISHAPGLylvpMKPGTNGPPLPGfEVDVVDENGNPAPPGVKGYLVIKKPWPGM- 490
Cdd:PRK08276 284 -----DWWgpiiheyyaSSEGGGVtVITSEDWL----AHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFe 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 491 LHGiwgDPEryiKTYWSRFP-GMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPD 569
Cdd:PRK08276 354 YHN---DPE---KTAAARNPhGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPD 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20137268 570 AIKGEVPIAFVVLKQGVAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:PRK08276 428 EEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
117-634 |
1.07e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 159.32 E-value: 1.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRI 196
Cdd:PRK07788 71 ERGTLTYAELDEQSNALARGL-LALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VITADGFwrrgrvvrlKEVVDAALEKATGVESVIVLPRLGLKDVPMTEGRDywwnKLMQGIPPnayiEPEPVESEHPSFI 276
Cdd:PRK07788 150 LVYDDEF---------TDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETLD----DLIAGSST----APLPKPPKPGGIV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIVHDTggwaVHVYATMKWVFD---IRDDDIFWCTADIGWVTGHSYVVLGpLLMGATEVIYEGApdypQ 353
Cdd:PRK07788 213 ILTSGTTGTPKGAPRPE----PSPLAPLAGLLSrvpFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVLRRRF----D 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 354 PDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWA--------YRVLGNEKVAFG 425
Cdd:PRK07788 284 PEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRAleafgpvlYNLYGSTEVAFA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 426 STWWMTEtggivishapglylVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKK--PWPGMLHGiwGDPERyIK 503
Cdd:PRK07788 364 TIATPED--------------LAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNgfPFEGYTDG--RDKQI-ID 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 504 tywsrfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLK 583
Cdd:PRK07788 427 -------GLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKA 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 20137268 584 QGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:PRK07788 500 PGAALDED---AIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
119-632 |
2.77e-41 |
|
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: 156.32 E-value: 2.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:cd12115 23 ESLTYAELNRRANRLAARLRAA-GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TadgfwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepvESEHPSFILY 278
Cdd:cd12115 102 T---------------------------------------------------------------------DPDDLAYVIY 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 279 TSGTTGKPKG--IVHDTGG----WAVHVYATMKW---------VFDIRDDDIFwctadigwvtghsyvvlGPLLMGATEV 343
Cdd:cd12115 113 TSGSTGRPKGvaIEHRNAAaflqWAAAAFSAEELagvlastsiCFDLSVFELF-----------------GPLATGGKVV 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 344 IYEGA---PDYPQPDrwwsiieryGVTIFYTSPTAIRMFMRygeewprkHDL--STLRIIHSVGEPINPEAWRWAYRVLG 418
Cdd:cd12115 176 LADNVlalPDLPAAA---------EVTLINTVPSAAAELLR--------HDAlpASVRVVNLAGEPLPRDLVQRLYARLQ 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 419 NEKVA--FGSTWWMT-ETGGIVISHAPGlylvpmkPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIW 495
Cdd:cd12115 239 VERVVnlYGPSEDTTySTVAPVPPGASG-------EVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGA--GVARGYL 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 496 GDP----ERYIKTywSRFPG--MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPD 569
Cdd:cd12115 310 GRPgltaERFLPD--PFGPGarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGD 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20137268 570 AIKGEVPIAFVVLKQGVAPsdeLRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:cd12115 388 AAGERRLVAYIVAEPGAAG---LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
120-634 |
3.42e-41 |
|
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: 155.20 E-value: 3.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 120 KLTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSqsrivit 199
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAA-LGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDS------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 200 adgfwrrgrvvrlkevvDAALEKATGvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepvesehpsfILYT 279
Cdd:cd05912 73 -----------------DVKLDDIAT--------------------------------------------------IMYT 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 280 SGTTGKPKGIVHDTGGWAVHVYATMKwVFDIRDDDIFWCTADIGWVTGHSyVVLGPLLMGATEVIYegapDYPQPDRWWS 359
Cdd:cd05912 86 SGTTGKPKGVQQTFGNHWWSAIGSAL-NLGLTEDDNWLCALPLFHISGLS-ILMRSVIYGMTVYLV----DKFDAEQVLH 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 360 IIERYGVTIFYTSPTAI-RMFMRYGEEWPrkhdlSTLRIIHSVGEPINPeawrwayrVLGNEKVAFG----STWWMTETG 434
Cdd:cd05912 160 LINSGKVTIISVVPTMLqRLLEILGEGYP-----NNLRCILLGGGPAPK--------PLLEQCKEKGipvyQSYGMTETC 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 435 GIVISHAPgLYLvPMKPGTNGPPLPGFEVDVVDENGNPAPPG---VKGylvikkpwPGMLHGIWGDPERyikTYWSRFPG 511
Cdd:cd05912 227 SQIVTLSP-EDA-LNKIGSAGKPLFPVELKIEDDGQPPYEVGeilLKG--------PNVTKGYLNRPDA---TEESFENG 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 512 MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVApSDE 591
Cdd:cd05912 294 WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPIS-EEE 372
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 20137268 592 LRKELREHVRRtigpIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:cd05912 373 LIAYCSEKLAK----YKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
104-632 |
4.90e-41 |
|
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: 156.33 E-value: 4.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 104 WEGEPVDE------NGYPT------DRRKLTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGA 171
Cdd:cd05920 12 WQDEPLGDllarsaARHPDriavvdGDRRLTYRELDRRADRLAAGLRG-LGIRPGDRVVVQLPNVAEFVVLFFALLRLGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 172 ItsVVFSGFSAdalaerindsqsrivitadgfwrrgrvvRLKEVvdAALEKATGVESVIVLPRLGLKDvpmtegrdywwn 251
Cdd:cd05920 91 V--PVLALPSH----------------------------RRSEL--SAFCAHAEAVAYIVPDRHAGFD------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 252 klmqgiPPNAYIEpepVESEHP--SFILYTSGTTGKPKGI--VHDtgGWAVHVYATMKWV-FDirDDDIFWCTADIGwvt 326
Cdd:cd05920 127 ------HRALARE---LAESIPevALFLLSGGTTGTPKLIprTHN--DYAYNVRASAEVCgLD--QDTVYLAVLPAA--- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 327 gHSYV-----VLGPLLMGATEVIyegAPDyPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEwpRKHDLSTLRIIHSV 401
Cdd:cd05920 191 -HNFPlacpgVLGTLLAGGRVVL---APD-PSPDAAFPLIEREGVTVTALVPALVSLWLDAAAS--RRADLSSLRLLQVG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 402 GEPINPEAWRWAYRVLGN--EKVaFGstwwMTEtggivishapGL--YLVPMKPG-----TNGPPL-PGFEVDVVDENGN 471
Cdd:cd05920 264 GARLSPALARRVPPVLGCtlQQV-FG----MAE----------GLlnYTRLDDPDeviihTQGRPMsPDDEIRVVDEEGN 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 472 PAPPGVKGYLVIKKPWpgMLHGIWGDPERYIKTYWSRfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELES 551
Cdd:cd05920 329 PVPPGEEGELLTRGPY--TIRGYYRAPEHNARAFTPD--GFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVEN 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 552 ALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDELRKELREhvrRTIGPIAEPAQIFFVTKLPKTRSGKIMRRL 631
Cdd:cd05920 405 LLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQLRRFLRE---RGLAAYKLPDRIEFVDSLPLTAVGKIDKKA 481
|
.
gi 20137268 632 L 632
Cdd:cd05920 482 L 482
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
119-630 |
5.15e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 157.85 E-value: 5.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGAItsVVFSG--FSADALAERINDSQSRI 196
Cdd:PRK05605 56 ATTTYAELGKQVRRAAAGLRA-LGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV--VVEHNplYTAHELEHPFEDHGARV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VItadgFWRR--GRVVRLKEvvDAALEKATGVESVIVLP---RLGLK-DVPMT-EGRDYW---------WNKLMQ-GIPP 259
Cdd:PRK05605 133 AI----VWDKvaPTVERLRR--TTPLETIVSVNMIAAMPllqRLALRlPIPALrKARAALtgpapgtvpWETLVDaAIGG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 260 NAYIEPEP-VESEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDD--------IFwctadigwvtgHSY 330
Cdd:PRK05605 207 DGSDVSHPrPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGKAWVPGLGDGPervlaalpMF-----------HAY 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 331 vvlgPLLMGATEVIYEGA-----PDyPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEwpRKHDLSTLRIIHSVGEPI 405
Cdd:PRK05605 276 ----GLTLCLTLAVSIGGelvllPA-PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEE--RGVDLSGVRNAFSGAMAL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 406 NPE-AWRWAYRVLGNEKVAFGstwwMTETGGIVISHapglylvPM----KPGTNGPPLPGFEVDVVDENgNPA---PPGV 477
Cdd:PRK05605 349 PVStVELWEKLTGGLLVEGYG----LTETSPIIVGN-------PMsddrRPGYVGVPFPDTEVRIVDPE-DPDetmPDGE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 478 KGYLVIKKPwpGMLHGIWGDPERYIKTYwsrFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHP 557
Cdd:PRK05605 417 EGELLVRGP--QVFKGYWNRPEETAKSF---LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHP 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20137268 558 AVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDE-LRKELREHVRRtigpIAEPAQIFFVTKLPKTRSGKIMRR 630
Cdd:PRK05605 492 GVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEgLRAYCREHLTR----YKVPRRFYHVDELPRDQLGKVRRR 561
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
271-633 |
5.72e-41 |
|
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: 155.22 E-value: 5.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 271 EHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKwVFDIRDDDIFWCTADIGWVTGHSYVvLGPLLMGATeVIYEGAPD 350
Cdd:cd17649 94 RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAE-RYGLTPGDRELQFASFNFDGAHEQL-LPPLICGAC-VVLRPDEL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 351 YPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLStLRIIHSVGEPINPEAWRwayRVLGNEkVAFGSTWWM 430
Cdd:cd17649 171 WASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPPS-LRLYIFGGEALSPELLR---RWLKAP-VRLFNAYGP 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 431 TETggiVIShaPGLYLVPMKPGTNGP------PLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDP----ER 500
Cdd:cd17649 246 TEA---TVT--PLVWKCEAGAARAGAsmpigrPLGGRSAYILDADLNPVPVGVTGELYIGGE--GLARGYLGRPeltaER 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 501 YIKTYWSRfPG--MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVpIA 578
Cdd:cd17649 319 FVPDPFGA-PGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQL-VA 396
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 20137268 579 FVVLKQGVAPSdELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:cd17649 397 YVVLRAAAAQP-ELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
25-634 |
2.22e-40 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 157.93 E-value: 2.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 25 SKY-TPIDAYFKFHRQTVENLESFWESVAKELE--WFKPWDKVLDASNP--PFYKWFVGGRLNLSY--LAVDRHVktwRK 97
Cdd:PLN03052 113 SKYkDPISSFSEFQRFSVENPEVYWSIVLDELSlvFSVPPRCILDTSDEsnPGGQWLPGAVLNVAEccLTPKPSK---TD 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 98 NKLAIEWEGEpvDENGYPTDRrkLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVF 177
Cdd:PLN03052 190 DSIAIIWRDE--GSDDLPVNR--MTLSELRSQVSRVANAL-DALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 178 SGFSADALAERINDSQSRIVITADGFWRRGRVVRL-KEVVDAALEKAtgvesvIVLPRLG-LKDVPMTEGRDYWWNKLMQ 255
Cdd:PLN03052 265 DSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLySRVVEAKAPKA------IVLPADGkSVRVKLREGDMSWDDFLAR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 256 GIPPNAYIEPEPVESEHPSF--ILYTSGTTGKPKGI--VHDT------GGWAVHvyatmkwvfDIRDDDIF-WCTaDIGW 324
Cdd:PLN03052 339 ANGLRRPDEYKAVEQPVEAFtnILFSSGTTGEPKAIpwTQLTplraaaDAWAHL---------DIRKGDIVcWPT-NLGW 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 325 VTGHsYVVLGPLLMGATEVIYEGAPDypqpDRWWS-IIERYGVTIFYTSPTAIRMfmrygeeWPRKH-----DLSTLRII 398
Cdd:PLN03052 409 MMGP-WLVYASLLNGATLALYNGSPL----GRGFAkFVQDAKVTMLGTVPSIVKT-------WKNTNcmaglDWSSIRCF 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 399 HSVGEPINPEAWRWayrvlgnekvAFGSTWWM--------TETGGIVIShapGLYLVPMKPGTNGPPLPGFEVDVVDENG 470
Cdd:PLN03052 477 GSTGEASSVDDYLW----------LMSRAGYKpiieycggTELGGGFVT---GSLLQPQAFAAFSTPAMGCKLFILDDSG 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 471 NPAPPGVkgylvikkpwPGM----LHG-IWGDPERYI-----KTYwsrFPGM-FYA-------GDYAIKDKDGYIWVLGR 532
Cdd:PLN03052 544 NPYPDDA----------PCTgelaLFPlMFGASSTLLnadhyKVY---FKGMpVFNgkilrrhGDIFERTSGGYYRAHGR 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 533 ADEVIKVAGHRLGTYELESAL-ISHPAVAESAVVGVPDAIKG-EVPIAFVVLKQ--GVAPS-DELRKELREHVRRTIGPI 607
Cdd:PLN03052 611 ADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGpEQLVIAAVLKDppGSNPDlNELKKIFNSAIQKKLNPL 690
|
650 660
....*....|....*....|....*..
gi 20137268 608 AEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:PLN03052 691 FKVSAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
119-640 |
2.89e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 155.32 E-value: 2.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:PRK07786 41 NTTTWRELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TADGfwrrgrvvrLKEVVDAALEKATGVESVIVL------PRLGLKDVPMTEGrdywwnklmqgiPPNAyiePEPVESEH 272
Cdd:PRK07786 120 TEAA---------LAPVATAVRDIVPLLSTVVVAggssddSVLGYEDLLAEAG------------PAHA---PVDIPNDS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 273 PSFILYTSGTTGKPKGIV--HD--TGGWAVHVYAtmkWVFDIrDDDIFWCTADIGWVTGHSYVVLGpLLMGATEVIYE-G 347
Cdd:PRK07786 176 PALIMYTSGTTGRPKGAVltHAnlTGQAMTCLRT---NGADI-NSDVGFVGVPLFHIAGIGSMLPG-LLLGAPTVIYPlG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 348 APDypqPDRWWSIIERYGVTIFYTSPTAIRMFMryGEEWPRKHDLStLRIIHSVGEPINPEAWRWAYRVLGNEKV--AFG 425
Cdd:PRK07786 251 AFD---PGQLLDVLEAEKVTGIFLVPAQWQAVC--AEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQIlaAFG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 426 STWWMTETGGIVISHAPglylvpMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPERYIKTY 505
Cdd:PRK07786 325 QTEMSPVTCMLLGEDAI------RKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAP--TLMSGYWNNPEATAEAF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 506 WSrfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQG 585
Cdd:PRK07786 397 AG---GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 20137268 586 VAP--SDELRKELREHVRRtigpIAEPAQIFFVTKLPKTRSGKIMRRLLKaVATGAP 640
Cdd:PRK07786 474 DAAltLEDLAEFLTDRLAR----YKHPKALEIVDALPRNPAGKVLKTELR-ERYGAC 525
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
119-634 |
1.79e-39 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 152.99 E-value: 1.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSR-IV 197
Cdd:PRK06155 45 TRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARlLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 198 ITADGFwrrgrvvrlkEVVDAALEkatgveSVIVLPRLGLKDVPMTEGRDYWWNKLmqGIPP-NAYIEPEPVESEHPSFI 276
Cdd:PRK06155 124 VEAALL----------AALEAADP------GDLPLPAVWLLDAPASVSVPAGWSTA--PLPPlDAPAPAAAVQPGDTAAI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIVHDTGG---WAVHVYATMkwvfDIRDDDIFWCTADIGWVTGHSYVVLGpLLMGATEVIYEGApdypQ 353
Cdd:PRK06155 186 LYTSGTTGPSKGVCCPHAQfywWGRNSAEDL----EIGADDVLYTTLPLFHTNALNAFFQA-LLAGATYVLEPRF----S 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 354 PDRWWSIIERYGVTIFYTSPTAIRMFMRygeEWPRKHD-LSTLRIIHSVGEPIN-PEAWRWAYRVLGNEkvAFGSTwwmt 431
Cdd:PRK06155 257 ASGFWPAVRRHGATVTYLLGAMVSILLS---QPARESDrAHRVRVALGPGVPAAlHAAFRERFGVDLLD--GYGST---- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 432 ETGGIVishapGLYLVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPWPG-MLHGIWGDPERYIKTY---Ws 507
Cdd:PRK06155 328 ETNFVI-----AVTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEPFaFATGYFGMPEKTVEAWrnlW- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 508 rfpgmFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVA 587
Cdd:PRK06155 402 -----FHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTA 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 20137268 588 PSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:PRK06155 477 LEPV---ALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLRE 520
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
117-632 |
5.91e-39 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 155.50 E-value: 5.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRI 196
Cdd:PRK12316 4573 DEEKLTYAELNRRANRLAHALIAR-GVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAAL 4651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VITADGFWRRgrvvrlkevvdaaLEKATGVESVIVlprlglkdvpmteGRDYWWnklmQGIPPNAyiePE-PVESEHPSF 275
Cdd:PRK12316 4652 LLTQSHLLQR-------------LPIPDGLASLAL-------------DRDEDW----EGFPAHD---PAvRLHPDNLAY 4698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 276 ILYTSGTTGKPKGIVHDTGGWAVHVYAT---------------MKWVFDIRDDDIFWctadigwvtghsyvvlgPLLMGA 340
Cdd:PRK12316 4699 VIYTSGSTGRPKGVAVSHGSLVNHLHATgeryeltpddrvlqfMSFSFDGSHEGLYH-----------------PLINGA 4761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 341 TEVIyeGAPDYPQPDRWWSIIERYGVTIFYTSPTAIRMFMrygEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNe 420
Cdd:PRK12316 4762 SVVI--RDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLA---EHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKP- 4835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 421 kVAFGSTWWMTETGGIVI------SHAPGLYLVPMkpgtnGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGI 494
Cdd:PRK12316 4836 -VYLFNGYGPTETTVTVLlwkardGDACGAAYMPI-----GTPLGNRSGYVLDGQLNPLPVGVAGELYLGGE--GVARGY 4907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 495 WGDP----ERYIKTYWSRFPGMFY-AGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPD 569
Cdd:PRK12316 4908 LERPaltaERFVPDPFGAPGGRLYrTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEG 4987
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20137268 570 AIkGEVPIAFVV-LKQGVAPSD----ELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:PRK12316 4988 AV-GKQLVGYVVpQDPALADADeaqaELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
153-634 |
7.65e-39 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 150.35 E-value: 7.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 153 LPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITADGFWRRGRVVRL-KEVVDAALEKAtgvesvIV 231
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLySKVVEAAPAKA------IV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 232 LPRLGLK-DVPMTEGRDYWWNKLMQGIPPN----AYIEPEPVESEHPSFILYTSGTTGKPKGI----------VHDtgGW 296
Cdd:PLN03051 75 LPAAGEPvAVPLREQDLSWCDFLGVAAAQGsvggNEYSPVYAPVESVTNILFSSGTTGEPKAIpwthlsplrcASD--GW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 297 AvHVyatmkwvfDIRDDDIFWCTADIGWVTGhSYVVLGPLLMGATEVIYEGAPDYPQpdrWWSIIERYGVTIFYTSPTAI 376
Cdd:PLN03051 153 A-HM--------DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGRG---FGKFVQDAGVTVLGLVPSIV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 377 RMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEK----VAFGstwwmTETGGIVISHAPglyLVPMKPG 452
Cdd:PLN03051 220 KAWRHTGAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYKpvieYCGG-----TELASGYISSTL---LQPQAPG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 453 TNGPPLPGFEVDVVDENGNPAPPG--VKGYLVIKKPWPGMLHGIWGDPERyiKTYWSRFPgMFYA--------GDYAIKD 522
Cdd:PLN03051 292 AFSTASLGTRFVLLNDNGVPYPDDqpCVGEVALAPPMLGASDRLLNADHD--KVYYKGMP-MYGSkgmplrrhGDIMKRT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 523 KDGYIWVLGRADEVIKVAGHRLGTYELESALI-SHPAVAESAVVGVPdAIKGEVPIAFVVLKQGV-------APSDELRK 594
Cdd:PLN03051 369 PGGYFCVQGRADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVA-PPDGGPELLVIFLVLGEekkgfdqARPEALQK 447
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 20137268 595 ELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:PLN03051 448 KFQEAIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLRD 487
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
278-637 |
1.43e-38 |
|
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: 146.47 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 278 YTSGTTGKPKGIVHDTGGWAVHVYAtMKWVFDIRDDDIFWCTADIGWVTGhSYVVLGPLLMGATEVIYEGAPDYPQP--- 354
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEVYNAWM-LALNSLFDPDDVLLCGLPLFHVNG-SVVTLLTPLASGAHVVLAGPAGYRNPglf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 355 DRWWSIIERYGVTIFYTSPTAIRMFMRYgeewPRKHDLSTLRIIHSVGEPINPEAWRwayRVLGNEKVAFGSTWWMTETG 434
Cdd:cd05944 87 DNFWKLVERYRITSLSTVPTVYAALLQV----PVNADISSLRFAMSGAAPLPVELRA---RFEDATGLPVVEGYGLTEAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 435 GIVISHAPGlylVPMKPGTNGPPLPGFEVDVVDENGN-----PAPPGVKGYLVIKKP--WPGMLH-----GIWGDPeryi 502
Cdd:cd05944 160 CLVAVNPPD---GPKRPGSVGLRLPYARVRIKVLDGVgrllrDCAPDEVGEICVAGPgvFGGYLYtegnkNAFVAD---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 503 ktywsrfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVL 582
Cdd:cd05944 233 --------GWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQL 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 20137268 583 KQGVAPSDElrkELREHVRRTIGP-IAEPAQIFFVTKLPKTRSGKIMRRLLKAVAT 637
Cdd:cd05944 305 KPGAVVEEE---ELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADAI 357
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
120-632 |
5.88e-38 |
|
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: 147.66 E-value: 5.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 120 KLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVIT 199
Cdd:cd05923 28 RLTYSELRARIEAVAARLHAR-GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 200 ADGfwrrgrvvrlKEVVDAALEKATGVESVIVLPRLGlkdVPMTEGrdywwnklmqgiPPnayIEPEPVESEHPSFILYT 279
Cdd:cd05923 107 AVD----------AQVMDAIFQSGVRVLALSDLVGLG---EPESAG------------PL---IEDPPREPEQPAFVFYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 280 SGTTGKPKGIVHDTGGWAVHVYAtMKWVFDIR--DDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIyegaPDYPQPDRW 357
Cdd:cd05923 159 SGTTGLPKGAVIPQRAAESRVLF-MSTQAGLRhgRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVV----VEEFDPADA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 358 WSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKhdLSTLRIIHSVGEPINPEAWRWAYRVLGNEKV-AFGSTWWMTEtggi 436
Cdd:cd05923 234 LKLIEQERVTSLFATPTHLDALAAAAEFAGLK--LSSLRHVTFAGATMPDAVLERVNQHLPGEKVnIYGTTEAMNS---- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 437 vishapgLYLVPMKPGTNGPPlpGF--EVDVVDENGNP---APPGVKGYLVIKKPWPGMLHGIWGDPEryiKTYWSRFPG 511
Cdd:cd05923 308 -------LYMRDARTGTEMRP--GFfsEVRIVRIGGSPdeaLANGEEGELIVAAAADAAFTGYLNQPE---ATAKKLQDG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 512 MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDE 591
Cdd:cd05923 376 WYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADE 455
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 20137268 592 LrkelrEHVRRT--IGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:cd05923 456 L-----DQFCRAseLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
117-632 |
2.95e-37 |
|
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: 144.70 E-value: 2.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVA-YMLKQnfGVKKGDKITLYLPMVPELPITMLAAWRIGAitsvVFSGFSADALAERINdsqsr 195
Cdd:cd05945 13 GGRTLTYRELKERADALAaALASL--GLDAGDPVVVYGHKSPDAIAAFLAALKAGH----AYVPLDASSPAERIR----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 196 ivitadgfwrrgrvvrlkEVVDAAlekatGVESVIVLPRlglkdvpmtegrdywwnklmqgipPNAYIepepvesehpsf 275
Cdd:cd05945 82 ------------------EILDAA-----KPALLIADGD------------------------DNAYI------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 276 iLYTSGTTGKPKGIVHdTGGWAVHVYATMKWVFDIRDDDIFWCTADI-----------GWVTGHSYVVLGPLLMGatevi 344
Cdd:cd05945 103 -IFTSGSTGRPKGVQI-SHDNLVSFTNWMLSDFPLGPGDVFLNQAPFsfdlsvmdlypALASGATLVPVPRDATA----- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 345 yegapDYPQPDRWwsiIERYGVTIFYTSPTAIRMFMRYGEEWPrkHDLSTLRIIHSVGEPI-NPEAWRWAYRvLGNEKV- 422
Cdd:cd05945 176 -----DPKQLFRF---LAEHGITVWVSTPSFAAMCLLSPTFTP--ESLPSLRHFLFCGEVLpHKTARALQQR-FPDARIy 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 423 -AFGSTWWMTETGGIVISHAPglyLVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPEry 501
Cdd:cd05945 245 nTYGPTEATVAVTYIEVTPEV---LDGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGP--SVSKGYLNNPE-- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 502 iKTYWSRFPGM----FYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPI 577
Cdd:cd05945 318 -KTAAAFFPDEgqraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELI 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 20137268 578 AFVVLKQGVAPsdELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:cd05945 397 AFVVPKPGAEA--GLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
119-633 |
3.17e-37 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 145.61 E-value: 3.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYlpMVPELPI--TMLAAWRIGAITSVVFSGFSADALAERINDSQSRI 196
Cdd:PRK12406 10 RRRSFDELAQRAARAAGGL-AALGVRPGDCVALL--MRNDFAFfeAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VITADGFWR--RGRVVRLKEVVDAA----LEKATGVESVIVLPRLGLKDvpmtegrdywWNKLMQGIPPnayiePEPVES 270
Cdd:PRK12406 87 LIAHADLLHglASALPAGVTVLSVPtppeIAAAYRISPALLTPPAGAID----------WEGWLAQQEP-----YDGPPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 271 EHPSFILYTSGTTGKPKGiVHDTGGWAVHVYATMKWVFDIrdddifwctadIGWVTGHSYVVLGPLlmgateviYEGAPD 350
Cdd:PRK12406 152 PQPQSMIYTSGTTGHPKG-VRRAAPTPEQAAAAEQMRALI-----------YGLKPGIRALLTGPL--------YHSAPN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 351 ---------------YPQ--PDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLR-IIHSvGEPINPEAWR- 411
Cdd:PRK12406 212 ayglragrlggvlvlQPRfdPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRhVIHA-AAPCPADVKRa 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 412 ---WAYRVLgNEkvAFGSTwwmtETGgIVISHAPGLYLvpMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKpwP 488
Cdd:PRK12406 291 mieWWGPVI-YE--YYGST----ESG-AVTFATSEDAL--SHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRI--A 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 489 GM----LHgiwGDPEryiKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAV 564
Cdd:PRK12406 359 GNpdftYH---NKPE---KRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAV 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 565 VGVPDAIKGEVPIAFVVLKQGVAPS-DELRKELREHVrrtiGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:PRK12406 433 FGIPDAEFGEALMAVVEPQPGATLDeADIRAQLKARL----AGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
119-640 |
1.30e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 143.79 E-value: 1.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQsrivi 198
Cdd:PRK09088 21 RRWTYAELDALVGRLAAVL-RRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAE----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 tadgfwrrgrvvrlkevvdaalekatgvesvivlPRLGLKDVPMTEGR--DYWWNKLMQGIPPNAYIEPEPVESEHPSFI 276
Cdd:PRK09088 95 ----------------------------------PRLLLGDDAVAAGRtdVEDLAAFIASADALEPADTPSIPPERVSLI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIV---HDTGGWAVHVYATMKwvfdIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAPdyPQ 353
Cdd:PRK09088 141 LFTSGTSGQPKGVMlseRNLQQTAHNFGVLGR----VDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFE--PK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 354 PDRWWSIIERYGVTIFYTSPTAIRMFmrygeewpRKH---DLSTLR---IIHSVGEPINPEAWRWAYrvlgNEKVAFGST 427
Cdd:PRK09088 215 RTLGRLGDPALGITHYFCVPQMAQAF--------RAQpgfDAAALRhltALFTGGAPHAAEDILGWL----DDGIPMVDG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 428 WWMTEtGGIVISHAPGLYLVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPERYIKTYWS 507
Cdd:PRK09088 283 FGMSE-AGTVFGMSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGP--NLSPGYWRRPQATARAFTG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 508 RfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVA 587
Cdd:PRK09088 360 D--GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAP 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 20137268 588 PSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK-AVATGAP 640
Cdd:PRK09088 438 LDLE---RIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRdALAAGRK 488
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
119-632 |
1.91e-36 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 147.62 E-value: 1.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:PRK12467 3119 QQLSYAELNRRANRLAHRLIAI-GVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLL 3197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TADGFWRRgrvvrlkevvdaaLEKATGVESVivlprlglkdvpmtegrdywwnkLMQGIPPNAYIEPEPVESEHP---SF 275
Cdd:PRK12467 3198 TQAHLLEQ-------------LPAPAGDTAL-----------------------TLDRLDLNGYSENNPSTRVMGenlAY 3241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 276 ILYTSGTTGKPKGIVHDTGGWAVHVYAT---------------MKWVFDIRDDDIFWctadigwvtghsyvvlgPLLMGA 340
Cdd:PRK12467 3242 VIYTSGSTGKPKGVGVRHGALANHLCWIaeayeldandrvllfMSFSFDGAQERFLW-----------------TLICGG 3304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 341 TEVIYEGapDYPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEewprKHDLSTLRIIHSVGEPINPEAWRWAYRVLgnE 420
Cdd:PRK12467 3305 CLVVRDN--DLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAG----GADCASLDIYVFGGEAVPPAAFEQVKRKL--K 3376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 421 KVAFGSTWWMTETGGIVI------SHAPGLYLVPMkpgtnGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGI 494
Cdd:PRK12467 3377 PRGLTNGYGPTEAVVTVTlwkcggDAVCEAPYAPI-----GRPVAGRSIYVLDGQLNPVPVGVAGELYIGGV--GLARGY 3449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 495 WGDP----ERYIKTYWSRFPGMFY-AGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPD 569
Cdd:PRK12467 3450 HQRPsltaERFVADPFSGSGGRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDG 3529
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20137268 570 AiKGEVPIAFVVLKqgvAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:PRK12467 3530 A-GGKQLVAYVVPA---DPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
121-633 |
2.18e-36 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 144.21 E-value: 2.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLKQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITA 200
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 201 DGfwrrgRVVRLKevvdaalekATGVeSVIVLPRLGLKDVPMTEGRDYWWNKLMQGIPPnayiePEPVESEHP-SFILYT 279
Cdd:PLN02574 147 PE-----NVEKLS---------PLGV-PVIGVPENYDFDSKRIEFPKFYELIKEDFDFV-----PKPVIKQDDvAAIMYS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 280 SGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRD----DDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYE--GAPDYPQ 353
Cdd:PLN02574 207 SGTTGASKGVVLTHRNLIAMVELFVRFEASQYEypgsDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRrfDASDMVK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 354 pdrwwsIIERYGVTIFYTSPtAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNekVAFGSTWWMTEt 433
Cdd:PLN02574 287 ------VIDRFKVTHFPVVP-PILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPH--VDFIQGYGMTE- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 434 ggiviSHAPGLYLVPMKPGTN----GPPLPGFEVDVVD-ENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPE----RYIKT 504
Cdd:PLN02574 357 -----STAVGTRGFNTEKLSKyssvGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGP--GVMKGYLNNPKatqsTIDKD 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 505 YWSRfpgmfyAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQ 584
Cdd:PLN02574 430 GWLR------TGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQ 503
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 20137268 585 GVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:PLN02574 504 GSTLSQE---AVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
261-634 |
3.56e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 142.05 E-value: 3.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 261 AYIEPEPvesEHPSFILYTSGTTGKPKGIVHDTGGWAvhvyATMkwvfDIRDDDIFWcTADIGWVTG------HSYV--V 332
Cdd:PRK07787 121 RYPEPDP---DAPALIVYTSGTTGPPKGVVLSRRAIA----ADL----DALAEAWQW-TADDVLVHGlplfhvHGLVlgV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 333 LGPLLMGATeVIYEGAPDypqPDRWWSIIERYGvTIFYTSPTairMFMRYGEEWPRKHDLSTLRIIHSVGEPIN-PEAWR 411
Cdd:PRK07787 189 LGPLRIGNR-FVHTGRPT---PEAYAQALSEGG-TLYFGVPT---VWSRIAADPEAARALRGARLLVSGSAALPvPVFDR 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 412 WAyRVLGNEKVA-FGstwwMTETGGIVISHAPGlylvPMKPGTNGPPLPGFEVDVVDENGNPAPPGVK--GYLVIKKPWp 488
Cdd:PRK07787 261 LA-ALTGHRPVErYG----MTETLITLSTRADG----ERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPT- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 489 gMLHGIWGDPEryiKTYWSRFP-GMFYAGDYAIKDKDGYIWVLGR-ADEVIKVAGHRLGTYELESALISHPAVAESAVVG 566
Cdd:PRK07787 331 -LFDGYLNRPD---ATAAAFTAdGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVG 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20137268 567 VPDAIKGEVPIAFVVLKQGVAPSdelrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:PRK07787 407 VPDDDLGQRIVAYVVGADDVAAD-----ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
264-634 |
3.96e-36 |
|
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: 142.13 E-value: 3.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 264 EPEPVESEhPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDI--RDDDIFWCTADIGWVTGHSYVVLGpLLMGAT 341
Cdd:cd05929 119 TPIEDEAA-GWKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGFgpGADSVYLSPAPLYHAAPFRWSMTA-LFMGGT 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 342 EVIYEGApdypQPDRWWSIIERYGVTIFYTSPTairMFMRY---GEEWPRKHDLSTLRIIHSVGEPINPE------AWrW 412
Cdd:cd05929 197 LVLMEKF----DPEEFLRLIERYRVTFAQFVPT---MFVRLlklPEAVRNAYDLSSLKRVIHAAAPCPPWvkeqwiDW-G 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 413 AYRVL----GNEkvAFGSTW-----WMTetggivisHapglylvpmkPGTNGPPLPGfEVDVVDENGNPAPPGVKGYLVI 483
Cdd:cd05929 269 GPIIWeyygGTE--GQGLTIingeeWLT--------H----------PGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYF 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 484 KKPWPGMLHgiwgdpERYIKTYWSRFP-GMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAES 562
Cdd:cd05929 328 ANGPGFEYT------NDPEKTAAARNEgGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDA 401
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20137268 563 AVVGVPDAIKGEVPIAFVVLKQGVAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:cd05929 402 AVVGVPDEELGQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
119-630 |
4.73e-36 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 143.70 E-value: 4.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:COG1022 39 QSLTWAEFAERVRALAAGL-LALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TADGFwrrgrvvrLKEVVDAALEKATGVESVIVLPRLGLKDVP--------MTEGRDYWwnklmqgiPPNAYIE-PEPVE 269
Cdd:COG1022 118 VEDQE--------QLDKLLEVRDELPSLRHIVVLDPRGLRDDPrllsldelLALGREVA--------DPAELEArRAAVK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 270 SEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKwVFDIRDDDIF-----WCtadigWVTGHSYVVLgpLLMGATEVI 344
Cdd:COG1022 182 PDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLE-RLPLGPGDRTlsflpLA-----HVFERTVSYY--ALAAGATVA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 345 YEGAPDYPQPDrwwsiIERYGVTIFYTSP--------------------------TAIRMFMRYGEEWPRKHDLST-LRI 397
Cdd:COG1022 254 FAESPDTLAED-----LREVKPTFMLAVPrvwekvyagiqakaeeagglkrklfrWALAVGRRYARARLAGKSPSLlLRL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 398 IHSV-----------------------GEPINPEAWRWaYRVLG-NEKVAFGstwwMTETGGIVISHAPGLYlvpmKPGT 453
Cdd:COG1022 329 KHALadklvfsklrealggrlrfavsgGAALGPELARF-FRALGiPVLEGYG----LTETSPVITVNRPGDN----RIGT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 454 NGPPLPGFEVDVvdengnpAPPG---VKGylvikkpwPGMLHGIWGDPERYIKTY----WsrfpgmFYAGDYAIKDKDGY 526
Cdd:COG1022 400 VGPPLPGVEVKI-------AEDGeilVRG--------PNVMKGYYKNPEATAEAFdadgW------LHTGDIGELDEDGF 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 527 IWVLGRADEVIKVAGhrlGTY----ELESALISHPAVAESAVVGvpDAIKgeVPIAFVVL----------KQGVAPSD-- 590
Cdd:COG1022 459 LRITGRKKDLIVTSG---GKNvapqPIENALKASPLIEQAVVVG--DGRP--FLAALIVPdfealgewaeENGLPYTSya 531
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 20137268 591 ------ELRKELREHVRRTIGPIAEPAQI--FFVtkLPK---------TRSGKIMRR 630
Cdd:COG1022 532 elaqdpEVRALIQEEVDRANAGLSRAEQIkrFRL--LPKeftiengelTPTLKLKRK 586
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
119-634 |
5.56e-36 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 142.44 E-value: 5.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIG-AITSVVFS--GFSADALAERIndsQSR 195
Cdd:PRK10946 47 RQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLGNVAEFYITFFALLKLGvAPVNALFShqRSELNAYASQI---EPA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 196 IVItADgfwRRGRVVRLKEVVDAALEKATGVESVIVL---PRLGLKDVPMTEGRDYWwnklmqgippnayiePEPVESEH 272
Cdd:PRK10946 123 LLI-AD---RQHALFSDDDFLNTLVAEHSSLRVVLLLnddGEHSLDDAINHPAEDFT---------------ATPSPADE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 273 PSFILYTSGTTGKPKGI--VHDTGGWAVHvyatmkwvfdiRDDDIFWCTADIGWV----TGHSYVVLGPllmGATEVIYE 346
Cdd:PRK10946 184 VAFFQLSGGSTGTPKLIprTHNDYYYSVR-----------RSVEICGFTPQTRYLcalpAAHNYPMSSP---GALGVFLA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 347 G-----APDyPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNE- 420
Cdd:PRK10946 250 GgtvvlAPD-PSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQl 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 421 KVAFGstwwMTEtgGIV-----------ISHAPGLylvPMKPGTngpplpgfEVDVVDENGNPAPPGVKGYLVIKKPWpg 489
Cdd:PRK10946 329 QQVFG----MAE--GLVnytrlddsderIFTTQGR---PMSPDD--------EVWVADADGNPLPQGEVGRLMTRGPY-- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 490 MLHGIWGDPERYIKTYWSRfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPD 569
Cdd:PRK10946 390 TFRGYYKSPQHNASAFDAN--GFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMED 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20137268 570 AIKGEVPIAFVVLKQGVAPSdELRKELREHvrrtigPIAE---PAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:PRK10946 468 ELMGEKSCAFLVVKEPLKAV-QLRRFLREQ------GIAEfklPDRVECVDSLPLTAVGKVDKKQLRQ 528
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
121-644 |
2.14e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 144.33 E-value: 2.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITA 200
Cdd:PRK12316 537 LDYAELNRRANRLAHALIER-GVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQ 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 201 DgfwrrgrvvRLKEVVDAALEkatgvesvivLPRLGLkDVPMTEGRDYWWNklmqgiPPNAYIEPEpveseHPSFILYTS 280
Cdd:PRK12316 616 S---------HLGRKLPLAAG----------VQVLDL-DRPAAWLEGYSEE------NPGTELNPE-----NLAYVIYTS 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 281 GTTGKPKGIVHDTGGWAVHVYAtMKWVFDIRDDDIFWCTADIGWVTGHsYVVLGPLLMGATEVIyEGAPDYPQPDRWWSI 360
Cdd:PRK12316 665 GSTGKPKGAGNRHRALSNRLCW-MQQAYGLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGARLVV-AAPGDHRDPAKLVEL 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 361 IERYGVTIFYTSPTAIRMFMRYgeewPRKHDLSTLRIIHSVGEPI------NPEAWRWA---YRVLGNEKVAFGSTWW-- 429
Cdd:PRK12316 742 INREGVDTLHFVPSMLQAFLQD----EDVASCTSLRRIVCSGEALpadaqeQVFAKLPQaglYNLYGPTEAAIDVTHWtc 817
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 430 MTETGGIVishapglylvPMkpgtnGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDP----ERYIKTY 505
Cdd:PRK12316 818 VEEGGDSV----------PI-----GRPIANLACYILDANLEPVPVGVLGELYLAGR--GLARGYHGRPgltaERFVPSP 880
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 506 WSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVgvpdAIKGEVPIAFVVLKqg 585
Cdd:PRK12316 881 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AVDGKQLVGYVVLE-- 954
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20137268 586 vAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVATG-------APLGDV 644
Cdd:PRK12316 955 -SEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASvaqqgyvAPRNAL 1019
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
119-638 |
2.17e-35 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 140.89 E-value: 2.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKqNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:PLN02246 49 RVYTYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLII 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TADGFwrrgrVVRLKEvvdaaLEKATGVESVIVlprlglkDVPmTEGRDYWWNKLM--QGIPPNAYIEPEPVESehpsfI 276
Cdd:PLN02246 128 TQSCY-----VDKLKG-----LAEDDGVTVVTI-------DDP-PEGCLHFSELTQadENELPEVEISPDDVVA-----L 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIVHDTGGWavhVYATMKWV------FDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVI---YEG 347
Cdd:PLN02246 185 PYSSGTTGLPKGVMLTHKGL---VTSVAQQVdgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILImpkFEI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 348 ApdypqpdRWWSIIERYGVTI----------FYTSPTAirmfmrygeewpRKHDLSTLRIIHSVGEPINPEAWRwAYRV- 416
Cdd:PLN02246 262 G-------ALLELIQRHKVTIapfvppivlaIAKSPVV------------EKYDLSSIRMVLSGAAPLGKELED-AFRAk 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 417 LGNEKvaFGSTWWMTETGGiVISHAPGLYLVP--MKPGTNGPPLPGFEVDVVD-ENGNPAPPGVKGYLVIKKPwpGMLHG 493
Cdd:PLN02246 322 LPNAV--LGQGYGMTEAGP-VLAMCLAFAKEPfpVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGP--QIMKG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 494 IWGDPERYIKTYWSRfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKG 573
Cdd:PLN02246 397 YLNDPEATANTIDKD--GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAG 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20137268 574 EVPIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA-VATG 638
Cdd:PLN02246 475 EVPVAFVVRSNGSEITED---EIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAkLAAG 537
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
116-632 |
8.30e-35 |
|
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: 138.17 E-value: 8.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 116 TDRRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAitsvVFSGFSADALAERIN----D 191
Cdd:cd12114 8 CGDGTLTYGELAERARRVAGALKAA-GVRPGDLVAVTLPKGPEQVVAVLGILAAGA----AYVPVDIDQPAARREailaD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 192 SQSRIVITaDGFWRRGRVVRLKEVVDAALEKATGvesvivlprlglkdvpmtegrdywwnklmqGIPPnayiePEPVESE 271
Cdd:cd12114 83 AGARLVLT-DGPDAQLDVAVFDVLILDLDALAAP------------------------------APPP-----PVDVAPD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 272 HPSFILYTSGTTGKPKGIVHDTGGwAVHVYATMKWVFDIRDDDIFWCTADIGW---VtghsYVVLGPLLMGATEVIYEGA 348
Cdd:cd12114 127 DLAYVIFTSGSTGTPKGVMISHRA-ALNTILDINRRFAVGPDDRVLALSSLSFdlsV----YDIFGALSAGATLVLPDEA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 349 PDyPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRkhDLSTLR-IIHSvGEPINPE-AWRWAYRVLGNEKVAFGS 426
Cdd:cd12114 202 RR-RDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQA--LLPSLRlVLLS-GDWIPLDlPARLRALAPDARLISLGG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 427 twwMTETGGIVISHA-----PGLYLVPMkpgtnGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPERY 501
Cdd:cd12114 278 ---ATEASIWSIYHPidevpPDWRSIPY-----GRPLANQRYRVLDPRGRDCPDWVPGELWIGGR--GVALGYLGDPELT 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 502 IktywSRF-----PGMFY-AGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAiKGEV 575
Cdd:cd12114 348 A----ARFvthpdGERLYrTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKR 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 20137268 576 PIAFVVLKQGVAP--SDELRKELREHVRRTigpiAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:cd12114 423 LAAFVVPDNDGTPiaPDALRAFLAQTLPAY----MIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
119-634 |
8.56e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 138.48 E-value: 8.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:PRK06145 26 QEISYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TADGFWRRGRVVRLKEVVDAALEKATGvesvivlpRLGLKDVPmtegrdywwnklmqgIPPNAYIEPEPVESehpsfILY 278
Cdd:PRK06145 105 VDEEFDAIVALETPKIVIDAAAQADSR--------RLAQGGLE---------------IPPQAAVAPTDLVR-----LMY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 279 TSGTTGKPKGIVHDTGgwavhvyatmkwvfdirddDIFWCTAD----IGWVTGHSYVVLGPLLmgateviYEGAPDYP-- 352
Cdd:PRK06145 157 TSGTTDRPKGVMHSYG-------------------NLHWKSIDhviaLGLTASERLLVVGPLY-------HVGAFDLPgi 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 353 ---------------QPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEewPRKHDLSTLRIIHSVGEPINPEAWRWAYRVL 417
Cdd:PRK06145 211 avlwvggtlrihrefDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPD--RDRFDLDSLAWCIGGGEKTPESRIRDFTRVF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 418 GNEKV--AFGstwwMTET-GGIVISHApGLYLvpMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGI 494
Cdd:PRK06145 289 TRARYidAYG----LTETcSGDTLMEA-GREI--EKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGP--KVTKGY 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 495 WGDPEryiKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGE 574
Cdd:PRK06145 360 WKDPE---KTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGE 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 575 VPIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:PRK06145 437 RITAVVVLNPGATLTLE---ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
119-632 |
1.47e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 138.63 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYL-QKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TADGFWRRGrvvrlkevvdAALEKATGVESVIV------LPRLGLKDVPMTEGRD-------------YWWNKLMQGIPP 259
Cdd:PRK06710 127 CLDLVFPRV----------TNVQSATKIEHVIVtriadfLPFPKNLLYPFVQKKQsnlvvkvsesetiHLWNSVEKEVNT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 260 NAYIEPEPveSEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRD-DDIFWCTADIGWVTGHSYVVLGPLLM 338
Cdd:PRK06710 197 GVEVPCDP--ENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEgEEVVLGVLPFFHVYGMTAVMNLSIMQ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 339 GATEVIYegapdyPQPDR--WWSIIERYGVTIFYTSPTAIRMFMryGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRV 416
Cdd:PRK06710 275 GYKMVLI------PKFDMkmVFEAIKKHKVTLFPGAPTIYIALL--NSPLLKEYDISSIRACISGSAPLPVEVQEKFETV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 417 LGNEKVafgSTWWMTETGGIviSHAPGLYLVPMkPGTNGPPLPGFEVDVVD-ENGNPAPPGVKGYLVIKKPwpGMLHGIW 495
Cdd:PRK06710 347 TGGKLV---EGYGLTESSPV--THSNFLWEKRV-PGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGP--QIMKGYW 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 496 GDPERYIKTYWSrfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEV 575
Cdd:PRK06710 419 NKPEETAAVLQD---GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGET 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 20137268 576 PIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:PRK06710 496 VKAFVVLKEGTECSEE---ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
116-636 |
2.19e-34 |
|
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: 137.08 E-value: 2.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 116 TDRRKLTYYDLYREVNRVAYMLKQNfgVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSR 195
Cdd:cd05909 3 TLGTSLTYRKLLTGAIALARKLAKM--TKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 196 IVITADGFWRRGRVVRLKEVvdaalekATGVESVIvlprlgLKDVpmtEGRDYWWNKLMQGIppNAYIEPE--------- 266
Cdd:cd05909 81 TVLTSKQFIEKLKLHHLFDV-------EYDARIVY------LEDL---RAKISKADKCKAFL--AGKFPPKwllrifgva 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 267 PVESEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKwVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYE 346
Cdd:cd05909 143 PVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITA-IFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 347 GAPDYPQPDRwwsIIERYGVTIFYTSPTAIRMFMRYGEewprKHDLSTLRIIHSVGEPINP---EAWRWAYRVLGNEkvA 423
Cdd:cd05909 222 NPLDYKKIPE---LIYDKKATILLGTPTFLRGYARAAH----PEDFSSLRLVVAGAEKLKDtlrQEFQEKFGIRILE--G 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 424 FGStwwmTETGGIVISHAPGLylvPMKPGTNGPPLPGFEVDVVD-ENGNPAPPGVKGYLVIKKpwPGMLHGIWGDPEryi 502
Cdd:cd05909 293 YGT----TECSPVISVNTPQS---PNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRG--PNVMLGYLNEPE--- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 503 KTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISH-PAVAESAVVGVPDAIKGEVPIAFVV 581
Cdd:cd05909 361 LTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTT 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 20137268 582 LKqgVAPSDELRKELREHvrrTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVA 636
Cdd:cd05909 441 TT--DTDPSSLNDILKNA---GISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
117-649 |
2.50e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 141.07 E-value: 2.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRI 196
Cdd:PRK12467 534 GEQVLSYAELNRQANRLAHVL-IAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRL 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VITadgfwrRGRVVRLKEVVDaalekatgvesvivlprlGLKDVPMTEGRDYWwnklmQGIPpnAYIEPEPVESEHPSFI 276
Cdd:PRK12467 613 LLT------QSHLLAQLPVPA------------------GLRSLCLDEPADLL-----CGYS--GHNPEVALDPDNLAYV 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIVHDTGGWAVHVYATMKWvFDIRDDDIFWCTADIGWVTGHsYVVLGPLLMGATEVI--YEGAPDypqP 354
Cdd:PRK12467 662 IYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMVSTFAFDLGV-TELFGALASGATLHLlpPDCARD---A 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 355 DRWWSIIERYGVTIFYTSPTAIRMFMrygeEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKVAfgSTWWMTETg 434
Cdd:PRK12467 737 EAFAALMADQGVTVLKIVPSHLQALL----QASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLI--NHYGPTET- 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 435 GIVISHAP-GLYLVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKpwPGMLHGIWGDP----ERYIKTYWSRF 509
Cdd:PRK12467 810 TVGVSTYElSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGG--AGLARGYHRRPaltaERFVPDPFGAD 887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 510 PGMFY-AGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPdAIKGEVPIAFVVLKQGV-- 586
Cdd:PRK12467 888 GGRLYrTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQP-GDAGLQLVAYLVPAAVAdg 966
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20137268 587 APSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLkavatgaPLGDVTTLED 649
Cdd:PRK12467 967 AEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL-------PKPDASAVQA 1022
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
109-633 |
2.95e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 137.06 E-value: 2.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 109 VDENGYPTDRRKLTyyDLYREVNRVAYmlkqNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAER 188
Cdd:PRK13390 18 VAETGEQVSYRQLD--DDSAALARVLY----DAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 189 INDSQSRIVITAdgfwrrgrvvrlkEVVDAALEKATGVESVivlpRLGLKDvpMTEGRDYWWNKLMQGIPPNAyiepepv 268
Cdd:PRK13390 92 VGDSGARVLVAS-------------AALDGLAAKVGADLPL----RLSFGG--EIDGFGSFEAALAGAGPRLT------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 269 esEHP--SFILYTSGTTGKPKGIVHDTGGWAVH-----VYATMKWVFDIRDDDIFWCTADIGwvtgHSyvvlGPL----- 336
Cdd:PRK13390 146 --EQPcgAVMLYSSGTTGFPKGIQPDLPGRDVDapgdpIVAIARAFYDISESDIYYSSAPIY----HA----APLrwcsm 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 337 --LMGATEVIyegAPDYPQPDRWwSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLR-IIHSVGePINPEAWRWA 413
Cdd:PRK13390 216 vhALGGTVVL---AKRFDAQATL-GHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRaVIHAAA-PCPVDVKHAM 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 414 YRVLGNEKVAFGSTwwmTETGGIVISHAPGLYlvpMKPGTNGPPLPGfEVDVVDENGNPAPPGVKGYLVIKK-PWPGMLH 492
Cdd:PRK13390 291 IDWLGPIVYEYYSS---TEAHGMTFIDSPDWL---AHPGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFERdRLPFRYL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 493 GiwgDPERYIKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIK 572
Cdd:PRK13390 364 N---DPEKTAAAQHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEM 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20137268 573 GEVPIAFVVLKQGVAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:PRK13390 441 GEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
273-634 |
4.84e-34 |
|
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: 132.45 E-value: 4.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 273 PSFILYTSGTTGKPKGIVHDtggWAVHVYATM---KWV-FDIRDDdifW-CTADIGWVTGHSYVVLGpLLMGATEVIYEG 347
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHT---AANLLASAAglhSRLgFGGGDS---WlLSLPLYHVGGLAILVRS-LLAGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 348 APDYPQPdrwwsiIERYGVTifYTS--PTAIRMFMRYGEEWPrkhDLSTLRIIHSVGEPINPEAWRWAyrvlGNEKVAFG 425
Cdd:cd17630 75 NQALAED------LAPPGVT--HVSlvPTQLQRLLDSGQGPA---ALKSLRAVLLGGAPIPPELLERA----ADRGIPLY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 426 STWWMTETGGIVISHAPGLYlvpmKPGTNGPPLPGFEVDVVDengnpappgvkgylvikkpwPGMlhgIWGDPERYIKTY 505
Cdd:cd17630 140 TTYGMTETASQVATKRPDGF----GRGGVGVLLPGRELRIVE--------------------DGE---IWVGGASLAMGY 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 506 WSRFP-------GMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIA 578
Cdd:cd17630 193 LRGQLvpefnedGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVA 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 20137268 579 FVVLKQGVAPSdelrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:cd17630 273 VIVGRGPADPA-----ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
276-629 |
9.40e-34 |
|
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: 132.40 E-value: 9.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 276 ILYTSGTTGKPKGIV---HDTGGWAVHVYATMKWvfdiRDDDI-------FWCtadIGWVTGhsyvVLGPLLMGATEVIY 345
Cdd:cd05917 7 IQFTSGTTGSPKGATlthHNIVNNGYFIGERLGL----TEQDRlcipvplFHC---FGSVLG----VLACLTHGATMVFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 346 EGAPDypqPDRWWSIIERYGVTIFYTSPTairMFMR-YGEEWPRKHDLSTLR--IIhsVGEPINPEAWRWAYRVLGNEKV 422
Cdd:cd05917 76 SPSFD---PLAVLEAIEKEKCTALHGVPT---MFIAeLEHPDFDKFDLSSLRtgIM--AGAPCPPELMKRVIEVMNMKDV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 423 --AFGstwwMTETGGIVISHAPGLYlVPMKPGTNGPPLPGFEVDVVDENGNPAPP----G---VKGYLVIKkpwpgmlhG 493
Cdd:cd05917 148 tiAYG----MTETSPVSTQTRTDDS-IEKRVNTVGRIMPHTEAKIVDPEGGIVPPvgvpGelcIRGYSVMK--------G 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 494 IWGDPERYIKT------YWSrfpgmfyaGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGV 567
Cdd:cd05917 215 YWNDPEKTAEAidgdgwLHT--------GDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGV 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20137268 568 PDAIKGEVPIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMR 629
Cdd:cd05917 287 PDERYGEEVCAWIRLKEGAELTEE---DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
548-626 |
5.38e-33 |
|
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: 121.50 E-value: 5.38e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20137268 548 ELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVapsDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGK 626
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGV---ELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
119-636 |
1.08e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 132.94 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNR-VAYMLKQnfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIV 197
Cdd:PRK06164 34 RPLSRAELRALVDRlAAWLAAQ--GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 198 ITADGFWRRGRVVRLKEVVDAALEKATGVESVivlpRLGLKDVPM-TEGRDYWWNKLMQGIPPNAYIEPEPVESehPSFI 276
Cdd:PRK06164 112 VVWPGFKGIDFAAILAAVPPDALPPLRAIAVV----DDAADATPApAPGARVQLFALPDPAPPAAAGERAADPD--AGAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LY-TSGTTGKPKGIVHDTGGWAVHVYATMKwVFDIRDDDIFWCTADIGWVTGHSyVVLGPLLMGATeVIYEGAPDYPQPD 355
Cdd:PRK06164 186 LFtTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFS-TLLGALAGGAP-LVCEPVFDAARTA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 356 RwwsIIERYGVTIFYTSPtaiRMFMRYGEEWPRKHDLSTLRIihsVG----EPINPEAWRWA-------YRVLGNEKV-A 423
Cdd:PRK06164 263 R---ALRRHRVTHTFGND---EMLRRILDTAGERADFPSARL---FGfasfAPALGELAALArargvplTGLYGSSEVqA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 424 FGSTWWMT-------ETGGIVIShapglylvpmkpgtngpplPGFEVDVVD-ENGNPAPPGVKGYLVIKKpwPGMLHGIW 495
Cdd:PRK06164 334 LVALQPATdpvsvriEGGGRPAS-------------------PEARVRARDpQDGALLPDGESGEIEIRA--PSLMRGYL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 496 GDPERYIKTYwsRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVpdAIKGE- 574
Cdd:PRK06164 393 DNPDATARAL--TDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKt 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20137268 575 VPIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSG---KIMRRLLKAVA 636
Cdd:PRK06164 469 VPVAFVIPTDGASPDEA---GLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMA 530
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
119-634 |
1.75e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 135.29 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:PRK12467 1598 QELTYGELNRRANRLAHRLIAL-GVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLL 1676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TadgfwrrgrvvrlKEVVDAALEKATGVESVIVlprlglkdvpmtEGRDYWwnklMQGIPP-NAYIEPEPvesEHPSFIL 277
Cdd:PRK12467 1677 T-------------QSHLQARLPLPDGLRSLVL------------DQEDDW----LEGYSDsNPAVNLAP---QNLAYVI 1724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 278 YTSGTTGKPKGIVHDTGGWAVHVYATMKWvfdirdddiFWCTADIGWVTGHSYV-------VLGPLLMGATEVIyegAPD 350
Cdd:PRK12467 1725 YTSGSTGRPKGAGNRHGALVNRLCATQEA---------YQLSAADVVLQFTSFAfdvsvweLFWPLINGARLVI---APP 1792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 351 --YPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGE--EWPRKhdlstLRIIHSVGEPINPEAWRWAYRVLGNekVAFGS 426
Cdd:PRK12467 1793 gaHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEqvEHPLS-----LRRVVCGGEALEVEALRPWLERLPD--TGLFN 1865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 427 TWWMTETgGIVISHAP-------GLYLVPMkpgtnGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKpwPGMLHGIWGDP- 498
Cdd:PRK12467 1866 LYGPTET-AVDVTHWTcrrkdleGRDSVPI-----GQPIANLSTYILDASLNPVPIGVAGELYLGG--VGLARGYLNRPa 1937
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 499 ---ERYIKTYWSRFPGMFY-AGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVpDAIKGE 574
Cdd:PRK12467 1938 ltaERFVADPFGTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGK 2016
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20137268 575 VPIAFVV------LKQGVAPSdELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:PRK12467 2017 QLVAYVVptdpglVDDDEAQV-ALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPA 2081
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
110-634 |
2.03e-32 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 132.19 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 110 DENGYPTDRRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERI 189
Cdd:PRK13382 58 DRPGLIDELGTLTWRELDERSDALAAAL-QALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 190 NDSQSRIVITADGFwrrgrvvrlKEVVDAALE---KATGVESVIVLPRLGLKDVPMTEgrdywwnklmqgiPPNAYIEPE 266
Cdd:PRK13382 137 TREGVDTVIYDEEF---------SATVDRALAdcpQATRIVAWTDEDHDLTVEVLIAA-------------HAGQRPEPT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 267 PVESEhpsFILYTSGTTGKPKGIVHDTGGwavhVYATMKWVFD---IRDDDIFWCTADIGWVTGHSYVVLGPLLmgATEV 343
Cdd:PRK13382 195 GRKGR---VILLTSGTTGTPKGARRSGPG----GIGTLKAILDrtpWRAEEPTVIVAPMFHAWGFSQLVLAASL--ACTI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 344 IYEGAPDypqPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNekvA 423
Cdd:PRK13382 266 VTRRRFD---PEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD---V 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 424 FGSTWWMTETGGIVISHAPGLYlvpMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKpwpGMLHgiwgdpERYIK 503
Cdd:PRK13382 340 IYNNYNATEAGMIATATPADLR---AAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRN---DTQF------DGYTS 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 504 TYWSRF-PGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVL 582
Cdd:PRK13382 408 GSTKDFhDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVL 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 20137268 583 KQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:PRK13382 488 KPGASATPE---TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
121-635 |
2.27e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 135.08 E-value: 2.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITA 200
Cdd:PRK12316 3083 LSYAELNRRANRLAHRLIER-GVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQ 3161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 201 DGFwrrgrvvrlkevvdaALEKATGVESVIVLPRlglkdvpmtegrdywwnklmqgipPNAYIEPEP---VESEHPSFIL 277
Cdd:PRK12316 3162 SHL---------------RLPLAQGVQVLDLDRG------------------------DENYAEANPairTMPENLAYVI 3202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 278 YTSGTTGKPKGIVHDTGGWAVHVYAtMKWVFDIRDDDIFWCTADIGWvTGHSYVVLGPLLMGATeVIYEGAPDYPQPDRW 357
Cdd:PRK12316 3203 YTSGSTGKPKGVGIRHSALSNHLCW-MQQAYGLGVGDRVLQFTTFSF-DVFVEELFWPLMSGAR-VVLAGPEDWRDPALL 3279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 358 WSIIERYGVTIFYTSPTAIRMFMrygeEWPRKHDLSTLRIIHSVGEPINPEAWRWAyrvlgNEKVAFGSTWWMTETGGIV 437
Cdd:PRK12316 3280 VELINSEGVDVLHAYPSMLQAFL----EEEDAHRCTSLKRIVCGGEALPADLQQQV-----FAGLPLYNLYGPTEATITV 3350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 438 ISHAPGLYLVPMKPgtNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDP----ERYIKTYWSRFPGMF 513
Cdd:PRK12316 3351 THWQCVEEGKDAVP--IGRPIANRACYILDGSLEPVPVGALGELYLGGE--GLARGYHNRPgltaERFVPDPFVPGERLY 3426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 514 YAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVgvpdAIKGEVPIAFVVLKqgvAPSDELR 593
Cdd:PRK12316 3427 RTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPE---DEAGDLR 3499
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 20137268 594 KELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAV 635
Cdd:PRK12316 3500 EALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRP 3541
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
119-632 |
4.35e-32 |
|
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: 129.29 E-value: 4.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:cd17652 11 ETLTYAELNARANRLARLLAA-RGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TadgfwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepvESEHPSFILY 278
Cdd:cd17652 90 T---------------------------------------------------------------------TPDNLAYVIY 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 279 TSGTTGKPKGIVHDTGGWAVHVYATMKwVFDIRDDDIFWCTADIGWvTGHSYVVLGPLLMGATEVIyegAPDYP----QP 354
Cdd:cd17652 101 TSGSTGRPKGVVVTHRGLANLAAAQIA-AFDVGPGSRVLQFASPSF-DASVWELLMALLAGATLVL---APAEEllpgEP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 355 DRwwSIIERYGVTIFYTSPTAIRMFmrygeewpRKHDLSTLRIIHSVGEPINPE-AWRWAY-RVLGNekvAFGSTwwmtE 432
Cdd:cd17652 176 LA--DLLREHRITHVTLPPAALAAL--------PPDDLPDLRTLVVAGEACPAElVDRWAPgRRMIN---AYGPT----E 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 433 TGGIVISHAPglyLVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDP----ERYIKTYWSR 508
Cdd:cd17652 239 TTVCATMAGP---LPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGA--GLARGYLNRPgltaERFVADPFGA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 509 fPG--MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGV 586
Cdd:cd17652 314 -PGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGA 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 20137268 587 APSdelRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:cd17652 393 APT---AAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
117-632 |
7.81e-32 |
|
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: 128.74 E-value: 7.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRI 196
Cdd:cd17650 9 ATRQLTYRELNERANQLARTL-RGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VITadgfwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepvESEHPSFI 276
Cdd:cd17650 88 LLT---------------------------------------------------------------------QPEDLAYV 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIVHDTGGWAvHVYATMKWVFDIrddDIFwcTADIGWVTGHSYVV-----LGPLLMGATEVIyegAPD- 350
Cdd:cd17650 99 IYTSGTTGKPKGVMVEHRNVA-HAAHAWRREYEL---DSF--PVRLLQMASFSFDVfagdfARSLLNGGTLVI---CPDe 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 351 -YPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEwpRKHDLSTLRIIhSVGEPINPEAW-RWAYRVLGNEKV---AFG 425
Cdd:cd17650 170 vKLDPAALYDLILKSRITLMESTPALIRPVMAYVYR--NGLDLSAMRLL-IVGSDGCKAQDfKTLAARFGQGMRiinSYG 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 426 STWWMTETGGIVISHAP--GLYLVPMkpgtnGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPE---- 499
Cdd:cd17650 247 VTEATIDSTYYEEGRDPlgDSANVPI-----GRPLPNTAMYVLDERLQPQPVGVAGELYIGGA--GVARGYLNRPEltae 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 500 RYIKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAiKGEVPI-A 578
Cdd:cd17650 320 RFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGEARLcA 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 20137268 579 FVVlkqgvaPSDELR-KELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:cd17650 399 YVV------AAATLNtAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
119-633 |
2.09e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 129.50 E-value: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSR-IV 197
Cdd:PRK05677 48 KTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKaLV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 198 ITADgfwrrgrvvrLKEVVDAALEKaTGVESVIV---------LPRLGL--------KDVPMTEgrdywwnkLMQGIPPN 260
Cdd:PRK05677 128 CLAN----------MAHLAEKVLPK-TGVKHVIVtevadmlppLKRLLInavvkhvkKMVPAYH--------LPQAVKFN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 261 AYI--------EPEPVESEHPSFILYTSGTTGKPKG--IVHDtggwavHVYATMkwvfdirdddiFWCTADIGWVTGH-S 329
Cdd:PRK05677 189 DALakgagqpvTEANPQADDVAVLQYTGGTTGVAKGamLTHR------NLVANM-----------LQCRALMGSNLNEgC 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 330 YVVLGPL----------------LMGATEVIYEGAPDYP---QPDRWWSIIERYGVTIFYTSPTAIRMFmrygeewpRKH 390
Cdd:PRK05677 252 EILIAPLplyhiyaftfhcmammLIGNHNILISNPRDLPamvKELGKWKFSGFVGLNTLFVALCNNEAF--------RKL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 391 DLSTLRIIHSVGEPINPE-AWRWAyRVLGNEkVAFGstWWMTETGGIVISHAPGlylvPMKPGTNGPPLPGFEVDVVDEN 469
Cdd:PRK05677 324 DFSALKLTLSGGMALQLAtAERWK-EVTGCA-ICEG--YGMTETSPVVSVNPSQ----AIQVGTIGIPVPSTLCKVIDDD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 470 GNPAPPGVKGYLVIKKPwpGMLHGIWGDPERYIKTYWSRfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYEL 549
Cdd:PRK05677 396 GNELPLGEVGELCVKGP--QVMKGYWQRPEATDEILDSD--GWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNEL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 550 ESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMR 629
Cdd:PRK05677 472 EDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKE---QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILR 548
|
....
gi 20137268 630 RLLK 633
Cdd:PRK05677 549 RELR 552
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
276-629 |
2.38e-31 |
|
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: 125.07 E-value: 2.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 276 ILYTSGTTGKPKGIVHDTGGW---AVHVYATMKwvfdIRDDDIFWCTADIGWVTGHSyVVLGPLLMGATEVIYEGApdyp 352
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLiaaNLQLIHAMG----LTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 353 QPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRkhDLSTLRIIHSVGEPINPEAWrwayrvlgnEKVAfGSTWWM-- 430
Cdd:cd17637 76 DPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGV--DLSSLRHVLGLDAPETIQRF---------EETT-GATFWSly 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 431 --TETGGIViSHAPglylVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPERYIKTYWSr 508
Cdd:cd17637 144 gqTETSGLV-TLSP----YRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGP--LVFQGYWNLPELTAYTFRN- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 509 fpGMFYAGDYAIKDKDGYIWVLGR--ADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGV 586
Cdd:cd17637 216 --GWHHTGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGA 293
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 20137268 587 APSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMR 629
Cdd:cd17637 294 TLTAD---ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
122-633 |
2.64e-31 |
|
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: 128.80 E-value: 2.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 122 TYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITAd 201
Cdd:cd17642 46 SYAEYLEMSVRLAEAL-KKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 202 gfwRRGrvvrLKEVVDAAlEKATGVESVIVLPrlGLKDVpmtEGRDYWWNKLMQGIPPN----AYIEPEPVESEHPSFIL 277
Cdd:cd17642 124 ---KKG----LQKVLNVQ-KKLKIIKTIIILD--SKEDY---KGYQCLYTFITQNLPPGfneyDFKPPSFDRDEQVALIM 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 278 YTSGTTGKPKGIVhdtggwAVHVYATMKwvFDIRDDDIFWC-----TADIGWVTGHS----YVVLGPLLMGATEVIYega 348
Cdd:cd17642 191 NSSGSTGLPKGVQ------LTHKNIVAR--FSHARDPIFGNqiipdTAILTVIPFHHgfgmFTTLGYLICGFRVVLM--- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 349 PDYPQpDRWWSIIERYGVTIFYTSPTAIRMFMRygEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKVAFGstW 428
Cdd:cd17642 260 YKFEE-ELFLRSLQDYKVQSALLVPTLFAFFAK--STLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQG--Y 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 429 WMTETGGIVISHAPGLylvpMKPGTNGPPLPGFEVDVVD-ENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPER----YIK 503
Cdd:cd17642 335 GLTETTSAILITPEGD----DKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGP--MIMKGYVNNPEAtkalIDK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 504 TYWsrfpgmFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLK 583
Cdd:cd17642 409 DGW------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLE 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 20137268 584 QGVAPSDelrKELREHVRRTIGPIAE-PAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:cd17642 483 AGKTMTE---KEVMDYVASQVSTAKRlRGGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
275-626 |
3.29e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 125.57 E-value: 3.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 275 FILYTSGTTGKPKGIV---HDTGGWAVHVYATMKWVFDirddDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAPDY 351
Cdd:cd05924 7 YILYTGGTTGMPKGVMwrqEDIFRMLMGGADFGTGEFT----PSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 352 PQ----------PDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEK 421
Cdd:cd05924 83 GQtvvlpddrfdPEEVWRTIEKHKVTSMTIVGDAMARPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 422 V--AFGSTwwmtETGGIVISHAPGlylvpMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpG-MLHGIWGDP 498
Cdd:cd05924 163 LvdAFGSS----ETGFTGSGHSAG-----SGPETGPFTRANPDTVVLDDDGRVVPPGSGGVGWIARR--GhIPLGYYGDE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 499 ERYIKTYwSRFPGMFYA--GDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVP 576
Cdd:cd05924 232 AKTAETF-PEVDGVRYAvpGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 20137268 577 IAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGK 626
Cdd:cd05924 311 VAVVQLREGAGVDLE---ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
121-636 |
6.43e-31 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 128.02 E-value: 6.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLKQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITA 200
Cdd:PRK12492 50 LSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 201 DGFWRRGRVVRLKEVVDAALEKATG----------VESVI----------VLPR-LGLKDVpMTEGRDYwwnklmqgipp 259
Cdd:PRK12492 130 NMFGKLVQEVLPDTGIEYLIEAKMGdllpaakgwlVNTVVdkvkkmvpayHLPQaVPFKQA-LRQGRGL----------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 260 naYIEPEPVESEHPSFILYTSGTTGKPKGIVHDTGgwavHVYATMKWVFDirdddifwCTADIGwVTGHsyvvlgPLLMG 339
Cdd:PRK12492 198 --SLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHG----NLVANMLQVRA--------CLSQLG-PDGQ------PLMKE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 340 ATEVIYEGAPDYpqpdrwwsiiERYGVT-------------IFYTSPTAIRMFMRYGEEWP------------------- 387
Cdd:PRK12492 257 GQEVMIAPLPLY----------HIYAFTancmcmmvsgnhnVLITNPRDIPGFIKELGKWRfsallglntlfvalmdhpg 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 388 -RKHDLSTLRIIHSVGEP-INPEAWRWAyRVLGnekVAFGSTWWMTETGGiVISHAPglYLVPMKPGTNGPPLPGFEVDV 465
Cdd:PRK12492 327 fKDLDFSALKLTNSGGTAlVKATAERWE-QLTG---CTIVEGYGLTETSP-VASTNP--YGELARLGTVGIPVPGTALKV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 466 VDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPERYIKTYWSRfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLG 545
Cdd:PRK12492 400 IDDDGNELPLGERGELCIKGP--QVMKGYWQQPEATAEALDAE--GWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVY 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 546 TYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDELRKELREHvrrtIGPIAEPAQIFFVTKLPKTRSG 625
Cdd:PRK12492 476 PNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKEN----FTGYKVPKHIVLRDSLPMTPVG 551
|
570
....*....|.
gi 20137268 626 KIMRRLLKAVA 636
Cdd:PRK12492 552 KILRRELRDIA 562
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
117-635 |
1.36e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 129.31 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRI 196
Cdd:PRK12316 2025 GDQHLSYAELDSRANRLAHRLRA-RGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAAL 2103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VITADGfwrrgrvvrlkevVDAALEKATGVesvivlPRLGLKdvpmtegRDYWWNKLMQGIPPNAyiepepVESEHPSFI 276
Cdd:PRK12316 2104 LLTQRH-------------LLERLPLPAGV------ARLPLD-------RDAEWADYPDTAPAVQ------LAGENLAYV 2151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIVHDTGGWAVHVYAT---------------MKWVFDIRDDDIFWctadigwvtghsyvvlgPLLMGAT 341
Cdd:PRK12316 2152 IYTSGSTGLPKGVAVSHGALVAHCQAAgeryelspadcelqfMSFSFDGAHEQWFH-----------------PLLNGAR 2214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 342 EVIYEGapDYPQPDRWWSIIERYGVTIFYTSPTairMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGneK 421
Cdd:PRK12316 2215 VLIRDD--ELWDPEQLYDEMERHGVTILDFPPV---YLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALR--P 2287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 422 VAFGSTWWMTETGGIVISH------APGLYLVPMkpgtnGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIW 495
Cdd:PRK12316 2288 VYLFNGYGPTEAVVTPLLWkcrpqdPCGAAYVPI-----GRALGNRRAYILDADLNLLAPGMAGELYLGGE--GLARGYL 2360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 496 GDP----ERYIKTYWSRFPGMFY-AGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVpDA 570
Cdd:PRK12316 2361 NRPgltaERFVPDPFSASGERLYrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DG 2439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20137268 571 IKGEVPIAFVVlkqGVAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAV 635
Cdd:PRK12316 2440 ASGKQLVAYVV---PDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKP 2501
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
139-652 |
4.80e-30 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 126.30 E-value: 4.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 139 QNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITADGFWRRgrvVRLKEVVDA 218
Cdd:PRK06060 48 RNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDR---FQPSRVAEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 219 A--LEKATGVEsvivlprlglkdvpmtegrdywwnklmqgipPNAYiepEPVESEHPSFILYTSGTTGKPKGIVHDTGGW 296
Cdd:PRK06060 125 AelMSEAARVA-------------------------------PGGY---EPMGGDALAYATYTSGTTGPPKAAIHRHADP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 297 AVHVYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIyegAPDYPQPDRWWSIIERYGVTIFYTSPTai 376
Cdd:PRK06060 171 LTFVDAMCRKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVI---NSAPVTPEAAAILSARFGPSVLYGVPN-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 377 rMFMRYGEEWpRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKV--AFGSTwwmtETGGIVISHAPGLYlvpmKPGTN 454
Cdd:PRK06060 246 -FFARVIDSC-SPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPIldGIGST----EVGQTFVSNRVDEW----RLGTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 455 GPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPERYIKTywsrfPGMFYAGDYAIKDKDGYIWVLGRAD 534
Cdd:PRK06060 316 GRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGP--AIAKGYWNRPDSPVAN-----EGWLDTRDRVCIDSDGWVTYRCRAD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 535 EVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDELRKELREHVRRTIGPIAEPAQIF 614
Cdd:PRK06060 389 DTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFA 468
|
490 500 510
....*....|....*....|....*....|....*...
gi 20137268 615 FVTKLPKTRSGKIMRRLLKAVATGAPLGDVTTLEDETS 652
Cdd:PRK06060 469 VVDRLPRTPNGKLVRGALRKQSPTKPIWELSLTEPGSG 506
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
119-599 |
1.40e-29 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 123.47 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:PRK09274 40 DELSFAELDARSDAIAHGLNA-AGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TadgfwrrgrvvrlkevvdaaLEKATGVESVIVLPRLGLKDVpMTEGRDYWWN-----KLMQGIPPNAYiEPEPVESEHP 273
Cdd:PRK09274 119 G--------------------IPKAHLARRLFGWGKPSVRRL-VTVGGRLLWGgttlaTLLRDGAAAPF-PMADLAPDDM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 274 SFILYTSGTTGKPKGIVHDTGGWAVHVYAtMKWVFDIRDDDIFWCTADIgwvtghsyVVLGPLLMGATEVIYEGAPDYP- 352
Cdd:PRK09274 177 AAILFTSGSTGTPKGVVYTHGMFEAQIEA-LREDYGIEPGEIDLPTFPL--------FALFGPALGMTSVIPDMDPTRPa 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 353 --QPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEwpRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNE---------- 420
Cdd:PRK09274 248 tvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEA--NGIKLPSLRRVISAGAPVPIAVIERFRAMLPPDaeiltpygat 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 421 ------KVA----FGSTWWMTETGGivishapGlYLVpmkpgtnGPPLPGFEVDVVDENGNP---------APPG----- 476
Cdd:PRK09274 326 ealpisSIEsreiLFATRAATDNGA-------G-ICV-------GRPVDGVEVRIIAISDAPipewddalrLATGeigei 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 477 -VKGYLV----IKKPWPGMLHGIWgDPERYIktyWSRFpgmfyaGDYAIKDKDGYIWVLGR-ADEVIKVAGhRLGTYELE 550
Cdd:PRK09274 391 vVAGPMVtrsyYNRPEATRLAKIP-DGQGDV---WHRM------GDLGYLDAQGRLWFCGRkAHRVETAGG-TLYTIPCE 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 20137268 551 SALISHPAVAESAVVGVPdaIKGEV-PIAFVVLKQGVAPSDE-LRKELREH 599
Cdd:PRK09274 460 RIFNTHPGVKRSALVGVG--VPGAQrPVLCVELEPGVACSKSaLYQELRAL 508
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
115-634 |
2.00e-29 |
|
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: 123.12 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 115 PTDRRKLTYYDLYREVNRVAYMLkQNFGvKKGDKITLYLPMVPELPITMLAAWRIGAITSVVF---SGFSADALAERIND 191
Cdd:cd05931 19 GGREETLTYAELDRRARAIAARL-QAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPpptPGRHAERLAAILAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 192 SQSRIVITADGFwrrgrvvrlkevvDAALEKATGVESVIVLPRLGLKDVPMTEGRDYWwnklmqgippnayiEPEPVESE 271
Cdd:cd05931 97 AGPRVVLTTAAA-------------LAAVRAFAASRPAAGTPRLLVVDLLPDTSAADW--------------PPPSPDPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 272 HPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKwVFDIRDDDIF--W--CTADIGWVTGhsyvVLGPLLMGATEVIYEg 347
Cdd:cd05931 150 DIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRR-AYGLDPGDVVvsWlpLYHDMGLIGG----LLTPLYSGGPSVLMS- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 348 apdyP-----QPDRWWSIIERYGVTIfytspTAIRMF------MRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRW---A 413
Cdd:cd05931 224 ----PaaflrRPLRWLRLISRYRATI-----SAAPNFaydlcvRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRfaeA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 414 YRVLGNEKVAFGSTWWMTETGGIVISHAPG---------------LYLVPMKPGTN-------GPPLPGFEVDVVDENGN 471
Cdd:cd05931 295 FAPFGFRPEAFRPSYGLAEATLFVSGGPPGtgpvvlrvdrdalagRAVAVAADDPAarelvscGRPLPDQEVRIVDPETG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 472 -PAPPGVKGYLVIKKpwPGMLHGIWGDPERYIKTYWSRFP----GMFYAGDYAIKdKDGYIWVLGRADEVIKVAGHRLGT 546
Cdd:cd05931 375 rELPDGEVGEIWVRG--PSVASGYWGRPEATAETFGALAAtdegGWLRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYP 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 547 YELE-SALISHPAVAES--AVVGVPDAikGEVPIAFVV-LKQGVAPSD--ELRKELREHVRRTIGpiAEPAQIFFVT--K 618
Cdd:cd05931 452 QDIEaTAEEAHPALRPGcvAAFSVPDD--GEERLVVVAeVERGADPADlaAIAAAIRAAVAREHG--VAPADVVLVRpgS 527
|
570
....*....|....*.
gi 20137268 619 LPKTRSGKIMRRLLKA 634
Cdd:cd05931 528 IPRTSSGKIQRRACRA 543
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
119-634 |
2.20e-29 |
|
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: 122.41 E-value: 2.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:cd12118 28 RRYTWRQTYDRCRRLASAL-AALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 tadgfwrrgrvvrlkevVDAALEkatgvesvivlprlglkdvpmtegrdywWNKLMQGIPPNAyiEPEPVESEHPSFIL- 277
Cdd:cd12118 107 -----------------VDREFE----------------------------YEDLLAEGDPDF--EWIPPADEWDPIALn 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 278 YTSGTTGKPKGIVHDTGGWAVHVYATMkWVFDIRDDDIFWCTADI----GWvtGHSYVVLGpllMGATEVIYEGApDYPQ 353
Cdd:cd12118 140 YTSGTTGRPKGVVYHHRGAYLNALANI-LEWEMKQHPVYLWTLPMfhcnGW--CFPWTVAA---VGGTNVCLRKV-DAKA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 354 PdrwWSIIERYGVTIFYTSPTAIRMFMRYGEEW--PRKHDLSTLriihSVGEPinPEAwrwayRVLGN-EKVAFGST--W 428
Cdd:cd12118 213 I---YDLIEKHKVTHFCGAPTVLNMLANAPPSDarPLPHRVHVM----TAGAP--PPA-----AVLAKmEELGFDVThvY 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 429 WMTETGGIVISHApglylvpMKPGTNGPPLP---------------GFEVDVVDENGNPAPPG---------VKGYLVIK 484
Cdd:cd12118 279 GLTETYGPATVCA-------WKPEWDELPTEerarlkarqgvryvgLEEVDVLDPETMKPVPRdgktigeivFRGNIVMK 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 485 kpwpgmlhGIWGDPEryiKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAV 564
Cdd:cd12118 352 --------GYLKNPE---ATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAV 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 565 VGVPDAIKGEVPIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVtKLPKTRSGKIMRRLLKA 634
Cdd:cd12118 421 VARPDEKWGEVPCAFVELKEGAKVTEE---EIIAFCREHLAGFMVPKTVVFG-ELPKTSTGKIQKFVLRD 486
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
272-629 |
2.46e-29 |
|
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: 119.05 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 272 HPSFILYTSGTTGKPKGIVHDTGGWAVHvyatmkwvFDIRDDDIFWCTADIgwvtghsYVVLGPL-----LMGATEVIYE 346
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIES--------FVCNEDLFNISGEDA-------ILAPGPLshslfLYGAISALYL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 347 GAPDYPQ----PDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEwprkhdLSTLRIIHSVGEPINPEAWRWAYRVLGNEKV 422
Cdd:cd17633 66 GGTFIGQrkfnPKSWIRKINQYNATVIYLVPTMLQALARTLEP------ESKIKSIFSSGQKLFESTKKKLKNIFPKANL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 423 A--FGSTwwmtETGGIVishapglYLVP---MKPGTNGPPLPGFEVDVVDENGnpappGVKGYLVIKKPwpgMLHGIWGD 497
Cdd:cd17633 140 IefYGTS----ELSFIT-------YNFNqesRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSE---MVFSGYVR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 498 PERYIKTYWsrfpgmFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPI 577
Cdd:cd17633 201 GGFSNPDGW------MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAV 274
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 20137268 578 AFVVLKQGVapsdelRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMR 629
Cdd:cd17633 275 ALYSGDKLT------YKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
271-629 |
2.90e-29 |
|
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: 119.29 E-value: 2.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 271 EHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDDIFWCTADIGwvtgHSyvvlGPLLMGATEVIYEGA-- 348
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPAT----HI----GGLWWILTCLIHGGLcv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 349 --PDYPQPDRWWSIIERYGVTIFYTSPTA----IRMFMRYGEEWPRkhdlstLRIIHSVGE-PINPEAWRWAYRVLGNEK 421
Cdd:cd17635 73 tgGENTTYKSLFKILTTNAVTTTCLVPTLlsklVSELKSANATVPS------LRLIGYGGSrAIAADVRFIEATGLTNTA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 422 VAFGstwwMTETGGIV-ISHAPGLylvpMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPWpgMLHGIWGDPER 500
Cdd:cd17635 147 QVYG----LSETGTALcLPTDDDS----IEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA--NMLGYWNNPER 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 501 YIKTYwsrFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFV 580
Cdd:cd17635 217 TAEVL---IDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAV 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 20137268 581 VLKqgvAPSDELR-KELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMR 629
Cdd:cd17635 294 VAS---AELDENAiRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
114-629 |
8.14e-29 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 121.46 E-value: 8.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 114 YPTDRRKLTYYDLYREVNRVAY-MLKQnfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDS 192
Cdd:PRK08315 37 YRDQGLRWTYREFNEEVDALAKgLLAL--GIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 193 QSRIVITADGFWRRGRVVRLKEVvdaALEKATGVESVIVLPRL-GLKDV----PMTEGRDYWWNKLM---QGIPPNAYIE 264
Cdd:PRK08315 115 GCKALIAADGFKDSDYVAMLYEL---APELATCEPGQLQSARLpELRRViflgDEKHPGMLNFDELLalgRAVDDAELAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 265 PEPVESEH-PSFILYTSGTTGKPKG-------IVHDtggwAVHVYATMKwvfdIRDDD-------IFWCtadIGWVTGhs 329
Cdd:PRK08315 192 RQATLDPDdPINIQYTSGTTGFPKGatlthrnILNN----GYFIGEAMK----LTEEDrlcipvpLYHC---FGMVLG-- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 330 yvVLGPLLMGATEVIYEGAPDypqPDRWWSIIERYGVTIFYTSPTairMFMryGE-EWPR--KHDLSTLRIIHSVGEPIN 406
Cdd:PRK08315 259 --NLACVTHGATMVYPGEGFD---PLATLAAVEEERCTALYGVPT---MFI--AElDHPDfaRFDLSSLRTGIMAGSPCP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 407 PEAWRwayRVlgNEK-------VAFGstwwMTETG-GIVIS--HAPglylVPMKPGTNGPPLPGFEVDVVD-ENGNPAPP 475
Cdd:PRK08315 329 IEVMK---RV--IDKmhmsevtIAYG----MTETSpVSTQTrtDDP----LEKRVTTVGRALPHLEVKIVDpETGETVPR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 476 GV------KGYLVIKkpwpgmlhGIWGDPEryiKTYWSRFP-GMFYAGDYAIKDKDGYIWVLGRA-DEVIkvaghRLG-- 545
Cdd:PRK08315 396 GEqgelctRGYSVMK--------GYWNDPE---KTAEAIDAdGWMHTGDLAVMDEEGYVNIVGRIkDMII-----RGGen 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 546 TY--ELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDElrkELREHVRrtiGPIAE---PAQIFFVTKLP 620
Cdd:PRK08315 460 IYprEIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEE---DVRDFCR---GKIAHykiPRYIRFVDEFP 533
|
570
....*....|...
gi 20137268 621 KTRSGKI----MR 629
Cdd:PRK08315 534 MTVTGKIqkfkMR 546
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
121-633 |
8.24e-29 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 121.31 E-value: 8.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLKQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITA 200
Cdd:PRK08974 49 MTFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 201 DGFWRRgrvvrLKEVVDAalekaTGVESVIvLPRLG------------------LKDVP-------------MTEGRDyw 249
Cdd:PRK08974 129 SNFAHT-----LEKVVFK-----TPVKHVI-LTRMGdqlstakgtlvnfvvkyiKRLVPkyhlpdaisfrsaLHKGRR-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 250 wnklMQgippnaYIEPEpVESEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATmKWVFdirdddifwctadigwvtghs 329
Cdd:PRK08974 196 ----MQ------YVKPE-LVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQA-KAAY--------------------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 330 yvvlGPLLMGATEVIYEGAPDYpqpdrwwSI----------IERYGVTIFYTSPTAIRMFMRYGEEWP------------ 387
Cdd:PRK08974 243 ----GPLLHPGKELVVTALPLY-------HIfaltvncllfIELGGQNLLITNPRDIPGFVKELKKYPftaitgvntlfn 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 388 --------RKHDLSTLRIIHSVGEPINPE-AWRWAyRVLGNEKV-AFGstwwMTETGGIVishAPGLYLVPMKPGTNGPP 457
Cdd:PRK08974 312 allnneefQELDFSSLKLSVGGGMAVQQAvAERWV-KLTGQYLLeGYG----LTECSPLV---SVNPYDLDYYSGSIGLP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 458 LPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPE---RYIKTYWsrfpgmFYAGDYAIKDKDGYIWVLGRAD 534
Cdd:PRK08974 384 VPSTEIKLVDDDGNEVPPGEPGELWVKGP--QVMLGYWQRPEatdEVIKDGW------LATGDIAVMDEEGFLRIVDRKK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 535 EVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDELRKelreHVRRTIGPIAEPAQIF 614
Cdd:PRK08974 456 DMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELIT----HCRRHLTGYKVPKLVE 531
|
570
....*....|....*....
gi 20137268 615 FVTKLPKTRSGKIMRRLLK 633
Cdd:PRK08974 532 FRDELPKSNVGKILRRELR 550
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
119-634 |
4.79e-28 |
|
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: 118.20 E-value: 4.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:cd17655 21 QTLTYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TadgfwrrgrvvrlkevvdaalekatgvESVIVLPRLGLKDVPMTEGRDywwnklmqgippnAYIEPE-----PVESEHP 273
Cdd:cd17655 100 T---------------------------QSHLQPPIAFIGLIDLLDEDT-------------IYHEESenlepVSKSDDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 274 SFILYTSGTTGKPKGIVHDTGGwaVHVYatmKWVFDIRdddifwctadiGWVTGHSYVVL--------------GPLLMG 339
Cdd:cd17655 140 AYVIYTSGSTGKPKGVMIEHRG--VVNL---VEWANKV-----------IYQGEHLRVALfasisfdasvteifASLLSG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 340 ATEVIYEGAPDYPQPdRWWSIIERYGVTIFYTSPTAIRMF--MRYGEEwprkhdlSTLRIIHSVGEPINPE-AWRWAYRV 416
Cdd:cd17655 204 NTLYIVRKETVLDGQ-ALTQYIRQNRITIIDLTPAHLKLLdaADDSEG-------LSLKHLIVGGEALSTElAKKIIELF 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 417 lgNEKVAFGSTWWMTETggiVISHAPGLYlVPMKPGTN----GPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLH 492
Cdd:cd17655 276 --GTNPTITNAYGPTET---TVDASIYQY-EPETDQQVsvpiGKPLGNTRIYILDQYGRPQPVGVAGELYIGGE--GVAR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 493 GIWGDPERYIKTYWSR--FPG--MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVP 568
Cdd:cd17655 348 GYLNRPELTAEKFVDDpfVPGerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARK 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20137268 569 DAIKGEVPIAFVVLKQGVAPSDelrkeLREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:cd17655 428 DEQGQNYLCAYIVSEKELPVAQ-----LREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPE 488
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
119-633 |
7.48e-28 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 118.54 E-value: 7.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKqNFGVKKGDKITLYLPMVPELPITMLAAWRIGAitsvVFSGFSADALAERIND----SQS 194
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG----VFSGANPTALESEIKKqaeaAGA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 195 RIVITADgfwrrgrvvrlkevvdAALEKATGVEsvivLPRLGLKDVPMTEGRDywWNKLMQ-GIPPNAYIEPEPVESEHP 273
Cdd:PLN02330 129 KLIVTND----------------TNYGKVKGLG----LPVIVLGEEKIEGAVN--WKELLEaADRAGDTSDNEEILQTDL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 274 SFILYTSGTTGKPKGIVHDTGGWAVHVYATMkwvFDIRDDDIFWCTAdIGWVTG-HSYVVLG---PLLMGATEVIyegap 349
Cdd:PLN02330 187 CALPFSSGTTGISKGVMLTHRNLVANLCSSL---FSVGPEMIGQVVT-LGLIPFfHIYGITGiccATLRNKGKVV----- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 350 dypqpdrwwsIIERYGVTIFYTS------------PTAIRMFMR--YGEEWprkhDLSTLRI--IHSVGEPINPEAWRWA 413
Cdd:PLN02330 258 ----------VMSRFELRTFLNAlitqevsfapivPPIILNLVKnpIVEEF----DLSKLKLqaIMTAAAPLAPELLTAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 414 YRVLGNEKV--AFGstwwMTETGGIVISHA-PGLYLVPMKPGTNGPPLPGFEVDVVD-ENGNPAPPGVKGYLVIKKPWpg 489
Cdd:PLN02330 324 EAKFPGVQVqeAYG----LTEHSCITLTHGdPEKGHGIAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQC-- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 490 MLHGIWGDPERYIKTYWSRfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPD 569
Cdd:PLN02330 398 VMQGYYNNKEETDRTIDED--GWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPD 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20137268 570 AIKGEVPIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:PLN02330 476 EEAGEIPAACVVINPKAKESEE---DILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLK 536
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
117-636 |
1.35e-27 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 117.29 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSvvfsgfsadALAERINDSQSRI 196
Cdd:PRK05852 40 DRIAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVVV---------PLDPALPIAEQRV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VITADGfwrrGRVVrlkeVVDAALEKATGVESVIVLPrlglkdVPMTEGRDYWWNKLMQGIPPNAYIEPEPVES------ 270
Cdd:PRK05852 110 RSQAAG----ARVV----LIDADGPHDRAEPTTRWWP------LTVNVGGDSGPSGGTLSVHLDAATEPTPATStpeglr 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 271 EHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKwVFDIRDDDIfwCTADIGWVTGHSYV--VLGPLLMGateviyeGA 348
Cdd:PRK05852 176 PDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIIT-GYRLSPRDA--TVAVMPLYHGHGLIaaLLATLASG-------GA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 349 PDYPQPDRW-----WSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKV- 422
Cdd:PRK05852 246 VLLPARGRFsahtfWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVc 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 423 AFGstwwMTET---------GGIVISHAPGlylvpMKPGTNGPPlPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHG 493
Cdd:PRK05852 326 AFG----MTEAthqvtttqiEGIGQTENPV-----VSTGLVGRS-TGAQIRIVGSDGLPLPAGAVGEVWLRGT--TVVRG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 494 IWGDPERYIKTYWSrfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKG 573
Cdd:PRK05852 394 YLGDPTITAANFTD---GWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYG 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20137268 574 EVPIAFVVLKQGVAPSdelRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRllkAVA 636
Cdd:PRK05852 471 EAVAAVIVPRESAPPT---AEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR---AVA 527
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
117-630 |
1.88e-27 |
|
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: 115.77 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRI 196
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGL-IALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VITADGfwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepvesEHPSFI 276
Cdd:cd05907 81 LFVEDP--------------------------------------------------------------------DDLATI 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIVHDTGGWAVHVYATMKwVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAPDYPqPDr 356
Cdd:cd05907 93 IYTSGTTGRPKGVMLSHRNILSNALALAE-RLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLL-DD- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 357 wwsiIERYGVTIFYTSP---------------TAIRMFMRygeewpRKHDLSTLRIIHSVGEPINPEAWRWaYRVLGnek 421
Cdd:cd05907 170 ----LSEVRPTVFLAVPrvwekvyaaikvkavPGLKRKLF------DLAVGGRLRFAASGGAPLPAELLHF-FRALG--- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 422 VAFGSTWWMTETGGIVISHAPGLYlvpmKPGTNGPPLPGFEVDVVDEngnpappgvkGYLVIKKpwPGMLHGIWGDPEry 501
Cdd:cd05907 236 IPVYEGYGLTETSAVVTLNPPGDN----RIGTVGKPLPGVEVRIADD----------GEILVRG--PNVMLGYYKNPE-- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 502 iKTYWSRFP-GMFYAGDYAIKDKDGYIWVLGRADEVIKVAGhrlGTY----ELESALISHPAVAESAVVGvpDAIKgeVP 576
Cdd:cd05907 298 -ATAEALDAdGWLHTGDLGEIDEDGFLHITGRKKDLIITSG---GKNispePIENALKASPLISQAVVIG--DGRP--FL 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 577 IAFVVLKQGVAPS------------------DELRKELREHVRRTIGPIAEPAQI--FFVTKLP-------KTRSGKIMR 629
Cdd:cd05907 370 VALIVPDPEALEAwaeehgiaytdvaelaanPAVRAEIEAAVEAANARLSRYEQIkkFLLLPEPftiengeLTPTLKLKR 449
|
.
gi 20137268 630 R 630
Cdd:cd05907 450 P 450
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
276-629 |
1.93e-27 |
|
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: 113.75 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 276 ILYTSGTTGKPKGIV--HDTggwAVHVYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATeVIYEGAPDypq 353
Cdd:cd17638 5 IMFTSGTTGRSKGVMcaHRQ---TLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGAT-VVPVAVFD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 354 PDRWWSIIERYGVTIFYTSPTAIRMFMryGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKVAFGstWWMTET 433
Cdd:cd17638 78 VDAILEAIERERITVLPGPPTLFQSLL--DHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTA--YGLTEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 434 GGIVISHaPGLYLVPMKpGTNGPPLPGFEVDVVDengnPAPPGVKGYLVikkpwpgMLhGIWGDPERYIKTYWSRfpGMF 513
Cdd:cd17638 154 GVATMCR-PGDDAETVA-TTCGRACPGFEVRIAD----DGEVLVRGYNV-------MQ-GYLDDPEATAEAIDAD--GWL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 514 YAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDElr 593
Cdd:cd17638 218 HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEE-- 295
|
330 340 350
....*....|....*....|....*....|....*.
gi 20137268 594 kELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMR 629
Cdd:cd17638 296 -DVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
119-633 |
5.46e-27 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 115.89 E-value: 5.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:PRK07059 47 KAITYGELDELSRALAAWL-QSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TADGFWRRGRVV----RLKEVVDAALEKATGVESVIV--LPRLGLKDVPMtegrdywWNkLMQGIPPNAYI--------E 264
Cdd:PRK07059 126 VLENFATTVQQVlaktAVKHVVVASMGDLLGFKGHIVnfVVRRVKKMVPA-------WS-LPGHVRFNDALaegarqtfK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 265 PEPVESEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKW---VFDIRDDD---IFWCTADIGWVTGHSYVVLGPLLM 338
Cdd:PRK07059 198 PVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWlqpAFEKKPRPdqlNFVCALPLYHIFALTVCGLLGMRT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 339 GATEVIYEGAPDYPqpdrwwSII---ERYGVTIFYTSPTAIRMFMRYGEEwpRKHDLSTLRIIHSVGEPIN-PEAWRWaY 414
Cdd:PRK07059 278 GGRNILIPNPRDIP------GFIkelKKYQVHIFPAVNTLYNALLNNPDF--DKLDFSKLIVANGGGMAVQrPVAERW-L 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 415 RVLGnekVAFGSTWWMTETGGIVISHAPGlylVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGI 494
Cdd:PRK07059 349 EMTG---CPITEGYGLSETSPVATCNPVD---ATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGP--QVMAGY 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 495 WGDPERYIKTYWSrfPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGE 574
Cdd:PRK07059 421 WNRPDETAKVMTA--DGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGE 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 20137268 575 VPIAFVVLKQgvapSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:PRK07059 499 AVKLFVVKKD----PALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
99-634 |
8.13e-27 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 117.58 E-value: 8.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 99 KLAIEWEGEpvdengyptdrrKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFS 178
Cdd:PRK05691 1147 RIALVWDGG------------SLDYAELHAQANRLAHYL-RDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDP 1213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 179 GFSADALAERINDSQSRIVITADGFWRRgrvvrlkevvdaaLEKATGVeSVIVLPRLGLKDVPMTegrdywwnklmqgiP 258
Cdd:PRK05691 1214 DYPAERLAYMLADSGVELLLTQSHLLER-------------LPQAEGV-SAIALDSLHLDSWPSQ--------------A 1265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 259 PNAYIEpepveSEHPSFILYTSGTTGKPKGiVHDTGGWAVHVYATMKWVFDIRDDDIFWCTADIGWVTGhSYVVLGPLLM 338
Cdd:PRK05691 1266 PGLHLH-----GDNLAYVIYTSGSTGQPKG-VGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVS-VWECFWPLIT 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 339 GATEVIyEGAPDYPQPDRWWSIIERYGVTIFYTSPTAIRMFMrygeEWPRKHDLSTLRIIHSVGEPINPEAWRwayRVLG 418
Cdd:PRK05691 1339 GCRLVL-AGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFI----DEPLAAACTSLRRLFSGGEALPAELRN---RVLQ 1410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 419 N-EKVAFGSTWWMTETGgIVISH-----APGLYlVPMkpgtnGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLH 492
Cdd:PRK05691 1411 RlPQVQLHNRYGPTETA-INVTHwqcqaEDGER-SPI-----GRPLGNVLCRVLDAELNLLPPGVAGELCIGGA--GLAR 1481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 493 GIWGDP----ERYIKTYWSRFPGMFY-AGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGV 567
Cdd:PRK05691 1482 GYLGRPaltaERFVPDPLGEDGARLYrTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVR 1561
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20137268 568 PDAIKGEVPIAFVVLKQGVAPSDELRKELREHVRRTIgpiaEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:PRK05691 1562 EGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYM----VPAQLIRLDQMPLGPSGKLDRRALPE 1624
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
121-634 |
9.98e-27 |
|
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: 114.69 E-value: 9.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPElpiTMLAAWR--IGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDNED---FIPAFWAcvLAGFVPAPLTVPPTYDEPNARLRKLRHIWQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TADgfwrRGRVVRLKEVVD--AALEKATGVESVIVLPRLGLKDVPmtegrdywwnklmqgIPPNAYiepePVESEHPSFI 276
Cdd:cd05906 116 LLG----SPVVLTDAELVAefAGLETLSGLPGIRVLSIEELLDTA---------------ADHDLP----QSRPDDLALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIVHDTGGWAVHVYATMkWVFDIRDDDIF--WCTADigWVTGHSYVVLGPLLMGATEViyEGAPDY--P 352
Cdd:cd05906 173 MLTSGSTGFPKAVPLTHRNILARSAGKI-QHNGLTPQDVFlnWVPLD--HVGGLVELHLRAVYLGCQQV--HVPTEEilA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 353 QPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKH-DLSTLRIIHSVGEPINPEAWRWAYRVLGNEKV---AFGSTW 428
Cdd:cd05906 248 DPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGTwDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLppdAIRPAF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 429 WMTETG-GIVISHAPGLYLVPMKP--GTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKpwPGMLHGIWGDPERYIKTY 505
Cdd:cd05906 328 GMTETCsGVIYSRSFPTYDHSQALefVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRG--PVVTKGYYNNPEANAEAF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 506 WSrfPGMFYAGDYAIKDkDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAES--AVVGVPDAIKG--EVPIAFVV 581
Cdd:cd05906 406 TE--DGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVRDPGAEteELAIFFVP 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 20137268 582 LKQGVAPSDELRKELREHVRRTIGpIAePAQIFFVTK--LPKTRSGKIMRRLLKA 634
Cdd:cd05906 483 EYDLQDALSETLRAIRSVVSREVG-VS-PAYLIPLPKeeIPKTSLGKIQRSKLKA 535
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
116-636 |
1.50e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 113.72 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 116 TDRRKLTYYDLYREVNRVAYMLKQNfgVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSR 195
Cdd:PRK07638 22 ENDRVLTYKDWFESVCKVANWLNEK--ESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 196 IVITADGFwrrgrvvrlkevvdaaLEKATGVESVIVLPRlglkdvpmtegrdyWWNKLMQgippNAYIEPEPVES-EHPS 274
Cdd:PRK07638 100 MIVTERYK----------------LNDLPDEEGRVIEID--------------EWKRMIE----KYLPTYAPIENvQNAP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 275 FIL-YTSGTTGKPKGIVHDTGGWaVHVYATMKWVFDIRDDDifwctadigwvtghSYVVLGPL-----LMGATEVIYEGA 348
Cdd:PRK07638 146 FYMgFTSGSTGKPKAFLRAQQSW-LHSFDCNVHDFHMKRED--------------SVLIAGTLvhslfLYGAISTLYVGQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 349 PDYPQ----PDRWWSIIERYGVTIFYTSPTAIRMFMRY-------------GEEWPR--KHDLSTlriihsvgepINPEA 409
Cdd:PRK07638 211 TVHLMrkfiPNQVLDKLETENISVMYTVPTMLESLYKEnrvienkmkiissGAKWEAeaKEKIKN----------IFPYA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 410 WRwaYRVLGNEKVAFGStwwmtetggivishapglYLVP----MKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKK 485
Cdd:PRK07638 281 KL--YEFYGASELSFVT------------------ALVDeeseRRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKS 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 486 P--WPGMLHGIWGDPERYIKtywsrfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESA 563
Cdd:PRK07638 341 PqfFMGYIIGGVLARELNAD-------GWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIV 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20137268 564 VVGVPDAIKGEVPIAFVvlkqgvaPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVA 636
Cdd:PRK07638 414 VIGVPDSYWGEKPVAII-------KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWI 479
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
156-640 |
3.13e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 113.24 E-value: 3.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 156 VPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITADGFwrrgrvvrlKEVVDAALekaTGVESVIVlprl 235
Cdd:PRK07867 64 TPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAH---------AELLDGLD---PGVRVINV---- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 236 glkDVPMtegrdywWNKLMQGiPPNAYIEPEPVESEHPSFILYTSGTTGKPKGIV--HDTGGWAVHVYATMkwvFDIRDD 313
Cdd:PRK07867 128 ---DSPA-------WADELAA-HRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRctHRKVASAGVMLAQR---FGLGPD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 314 DIFWCTADIGwvtgHSYVVLG----PLLMGATEVIYE--GAPDYpQPDrwwsiIERYGVTIF--------YTSPTairmf 379
Cdd:PRK07867 194 DVCYVSMPLF----HSNAVMAgwavALAAGASIALRRkfSASGF-LPD-----VRRYGATYAnyvgkplsYVLAT----- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 380 mrygEEWPRKHDlSTLRIIHSvGEPINPEAWRWAYRvLGNEKV-AFGSTwwmteTGGIVISHAPGlylVPmkPGTNGPPL 458
Cdd:PRK07867 259 ----PERPDDAD-NPLRIVYG-NEGAPGDIARFARR-FGCVVVdGFGST-----EGGVAITRTPD---TP--PGALGPLP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 459 PGfeVDVVD-ENGNPAPPGVK------------GYLViKKPWPGMLHGIWGDPEryiKTYWSRFPGMFYAGDYAIKDKDG 525
Cdd:PRK07867 322 PG--VAIVDpDTGTECPPAEDadgrllnadeaiGELV-NTAGPGGFEGYYNDPE---ADAERMRGGVYWSGDLAYRDADG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 526 YIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVA-PSDELRKELREhvRRTI 604
Cdd:PRK07867 396 YAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKfDPDAFAEFLAA--QPDL 473
|
490 500 510
....*....|....*....|....*....|....*.
gi 20137268 605 GPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVATGAP 640
Cdd:PRK07867 474 GPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVDCA 509
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
117-633 |
8.04e-26 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 111.51 E-value: 8.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGAitsvVF----SGFSADALAERINDS 192
Cdd:PRK07514 25 DGLRYTYGDLDAASARLANLLVA-LGVKPGDRVAVQVEKSPEALALYLATLRAGA----VFlplnTAYTLAELDYFIGDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 193 QSRIVITADGfwRRGRVvrlkevvdAALEKATGVESVIVLPRLGlkDVPMTEgrdywwnkLMQGIPPNayIEPEPVESEH 272
Cdd:PRK07514 100 EPALVVCDPA--NFAWL--------SKIAAAAGAPHVETLDADG--TGSLLE--------AAAAAPDD--FETVPRGADD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 273 PSFILYTSGTTGKPKG--IVHD---TGGWAVHVYatmkWVFdiRDDD-------IFwctadigwvtgHS---YVVLGPLL 337
Cdd:PRK07514 158 LAAILYTSGTTGRSKGamLSHGnllSNALTLVDY----WRF--TPDDvlihalpIF-----------HThglFVATNVAL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 338 MGATEVIYEGAPDypqPDRwwsIIERY-------GVTIFYTsptaiRMFmryGEEWPRKHDLSTLRIIHSVGEPINPE-- 408
Cdd:PRK07514 221 LAGASMIFLPKFD---PDA---VLALMpratvmmGVPTFYT-----RLL---QEPRLTREAAAHMRLFISGSAPLLAEth 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 409 -AW--RWAYRVLgnEKvaFGstwwMTETGgiVISHAPglYLVPMKPGTNGPPLPGFEVDVVD-ENGNPAPPGVKGYLVIK 484
Cdd:PRK07514 287 rEFqeRTGHAIL--ER--YG----MTETN--MNTSNP--YDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVK 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 485 KPwpGMLHGIWGDPEryiKTYWS-RFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESA 563
Cdd:PRK07514 355 GP--NVFKGYWRMPE---KTAEEfRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESA 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 564 VVGVPDAIKGEVPIAFVVLKQGVAPsDElrKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:PRK07514 430 VIGVPHPDFGEGVTAVVVPKPGAAL-DE--AAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
87-633 |
2.41e-25 |
|
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: 109.32 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 87 AVDRHVKTWrKNKLAIEWEGEpvdengyptdrrKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAA 166
Cdd:cd17653 2 AFERIAAAH-PDAVAVESLGG------------SLTYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 167 WRIGAITSVVFSGFSADALAERINDSQSRIVITADGfwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmteGR 246
Cdd:cd17653 68 LKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTDS------------------------------------------PD 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 247 DYwwnklmqgippnAYIepepvesehpsfiLYTSGTTGKPKGIVHDTGGwAVHVYATMKWVFDIRDDD--------IFWC 318
Cdd:cd17653 106 DL------------AYI-------------IFTSGSTGIPKGVMVPHRG-VLNYVSQPPARLDVGPGSrvaqvlsiAFDA 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 319 TADigwvtghsyVVLGPLLMGATEVIYEgapdypqPDRWWSIIERyGVTIFYTSPTAIRMFmrygeewpRKHDLSTLRII 398
Cdd:cd17653 160 CIG---------EIFSTLCNGGTLVLAD-------PSDPFAHVAR-TVDALMSTPSILSTL--------SPQDFPNLKTI 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 399 HSVGEPINP---EAWrWAYRVLGNekvAFGSTwwmtETGgIVISHApglYLVPMKPGTNGPPLPGFEVDVVDENGNPAPP 475
Cdd:cd17653 215 FLGGEAVPPsllDRW-SPGRRLYN---AYGPT----ECT-ISSTMT---ELLPGQPVTIGKPIPNSTCYILDADLQPVPE 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 476 GVKGYLVIKKPwpGMLHGIWGDPERYIKTY--WSRFPG--MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELES 551
Cdd:cd17653 283 GVVGEICISGV--QVARGYLGNPALTASKFvpDPFWPGsrMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEE 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 552 ALI-SHPAVAESAVVGVPDAIkgevpIAFvvlkqgVAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRR 630
Cdd:cd17653 361 VVLqSQPEVTQAAAIVVNGRL-----VAF------VTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRK 429
|
...
gi 20137268 631 LLK 633
Cdd:cd17653 430 ALR 432
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
110-636 |
6.54e-25 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 109.58 E-value: 6.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 110 DENGYPTDRRKLTYYDLYREVNRVAYMLKQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERI 189
Cdd:PRK08751 40 DRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 190 NDSQSRIVITADGFwrrGRVVRlKEVVDAALEK--ATGVESVIVLPRLGL---------KDVPmtegrDYWWNK------ 252
Cdd:PRK08751 120 IDSGASVLVVIDNF---GTTVQ-QVIADTPVKQviTTGLGDMLGFPKAALvnfvvkyvkKLVP-----EYRINGairfre 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 253 -LMQGIP---PNAYIEPEPVesehpSFILYTSGTTGKPKG--IVHDtggwavHVYATMKWVFDirdddifwctadigWVT 326
Cdd:PRK08751 191 aLALGRKhsmPTLQIEPDDI-----AFLQYTGGTTGVAKGamLTHR------NLVANMQQAHQ--------------WLA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 327 GHsyvvlGPLLMGaTEVIYEGAPDY---PQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWP---------------- 387
Cdd:PRK08751 246 GT-----GKLEEG-CEVVITALPLYhifALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRftaftgvntlfnglln 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 388 ----RKHDLSTLRIIHSVGEPINPE-AWRWAyRVLGNEKV-AFGstwwMTETggivishAPGLYLVPMK----PGTNGPP 457
Cdd:PRK08751 320 tpgfDQIDFSSLKMTLGGGMAVQRSvAERWK-QVTGLTLVeAYG----LTET-------SPAACINPLTlkeyNGSIGLP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 458 LPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPERYIKTYWSRfpGMFYAGDYAIKDKDGYIWVLGRADEVI 537
Cdd:PRK08751 388 IPSTDACIKDDAGTVLAIGEIGELCIKGP--QVMKGYWKRPEETAKVMDAD--GWLHTGDIARMDEQGFVYIVDRKKDMI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 538 KVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVpIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVT 617
Cdd:PRK08751 464 LVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEI-VKVVIVKKDPALTAE---DVKAHARANLTGYKQPRIIEFRK 539
|
570
....*....|....*....
gi 20137268 618 KLPKTRSGKIMRRLLKAVA 636
Cdd:PRK08751 540 ELPKTNVGKILRRELRDAA 558
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
98-632 |
1.17e-24 |
|
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: 107.91 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 98 NKLAIEWEGEpvdengyptdrrKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVF 177
Cdd:cd17644 15 DAVAVVFEDQ------------QLTYEELNTKANQLAHYL-QSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 178 SGFSADALAERINDSQSRIVITadgfwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmtegrdywwnklmqgi 257
Cdd:cd17644 82 PNYPQERLTYILEDAQISVLLT---------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 258 ppnayiepepvESEHPSFILYTSGTTGKPKGI-------VHDTGGWAVHVYAT--------MKWVFDIRDDDIFwctadI 322
Cdd:cd17644 104 -----------QPENLAYVIYTSGSTGKPKGVmiehqslVNLSHGLIKEYGITssdrvlqfASIAFDVAAEEIY-----V 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 323 GWVTGHSyVVLGPLLMgateviyegapdYPQPDRWWSIIERYGVTIFYTSPTairmfmrYGEEWPRKHDLSTLRIIHSV- 401
Cdd:cd17644 168 TLLSGAT-LVLRPEEM------------RSSLEDFVQYIQQWQLTVLSLPPA-------YWHLLVLELLLSTIDLPSSLr 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 402 -----GEPINPEAWRWAYRVLGNeKVAFGSTWWMTE-TGGIVISHAPGLYLVPMKPGTNGPPLPGFEVDVVDENGNPAPP 475
Cdd:cd17644 228 lvivgGEAVQPELVRQWQKNVGN-FIQLINVYGPTEaTIAATVCRLTQLTERNITSVPIGRPIANTQVYILDENLQPVPV 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 476 GVKGYLVIKKPwpGMLHGIWGDPE----RYIKTYWSRFPG--MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYEL 549
Cdd:cd17644 307 GVPGELHIGGV--GLARGYLNRPEltaeKFISHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEI 384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 550 ESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMR 629
Cdd:cd17644 385 EAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTV---ELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDR 461
|
...
gi 20137268 630 RLL 632
Cdd:cd17644 462 RAL 464
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
122-633 |
1.29e-24 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 108.30 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 122 TYYDLYREVNRVAYMLKQNfGVKKGDKITlylpmvpelpiTM-------LAAWR----IGAITSVVFSGFSADALAERIN 190
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRD-GIKLGDRVA-----------TIawntwrhLEAWYgimgIGAICHTVNPRLFPEQIAWIIN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 191 DSQSRIVITADGFwrrgrvvrlKEVVDAALEKATGVESVIVLprlglkdvpmTEGRDYWWNKLmqgipPNAYIEPEPVES 270
Cdd:PRK06018 109 HAEDRVVITDLTF---------VPILEKIADKLPSVERYVVL----------TDAAHMPQTTL-----KNAVAYEEWIAE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 271 EHPSF------------ILYTSGTTGKPKGIVHDTGGWAVHVYATM-KWVFDIRDDDIF-----------WCTADIGWVT 326
Cdd:PRK06018 165 ADGDFawktfdentaagMCYTSGTTGDPKGVLYSHRSNVLHALMANnGDALGTSAADTMlpvvplfhansWGIAFSAPSM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 327 GHSYVVLGPLLMGATevIYEgapdypqpdrwwsIIERYGVTIFYTSPTAIRMFMRYGEEWPRKhdLSTLRIIhSVGEPIN 406
Cdd:PRK06018 245 GTKLVMPGAKLDGAS--VYE-------------LLDTEKVTFTAGVPTVWLMLLQYMEKEGLK--LPHLKMV-VCGGSAM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 407 PEAWRWAYRVLGNEKVafgSTWWMTETG--GIV------ISHAPGLYLVPMKPGTNGPPLpGFEVDVVDENGNPAPPGVK 478
Cdd:PRK06018 307 PRSMIKAFEDMGVEVR---HAWGMTEMSplGTLaalkppFSKLPGDARLDVLQKQGYPPF-GVEMKITDDAGKELPWDGK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 479 --GYLVIKKPwpgmlhgiwGDPERYIKTYWSRF--PGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALI 554
Cdd:PRK06018 383 tfGRLKVRGP---------AVAAAYYRVDGEILddDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAV 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 555 SHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDElrkelrEHVRRTIGPIAE---PAQIFFVTKLPKTRSGKIMRRL 631
Cdd:PRK06018 454 GHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATRE------EILKYMDGKIAKwwmPDDVAFVDAIPHTATGKILKTA 527
|
..
gi 20137268 632 LK 633
Cdd:PRK06018 528 LR 529
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
33-87 |
3.23e-24 |
|
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: 95.62 E-value: 3.23e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 20137268 33 YFKFHRQTVENLESFWESVAKELEWFKPWDKVLDASNPPFYKWFVGGRLNLSYLA 87
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPFDKVLDGSNGPFAKWFVGGKLNVCYNC 55
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
98-636 |
6.28e-24 |
|
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: 105.70 E-value: 6.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 98 NKLAIE-WEGEpvdengyptdrrkLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAItsVV 176
Cdd:cd05918 14 DAPAVCaWDGS-------------LTYAELDRLSSRLAHHL-RSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGA--FV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 177 FSGFS--ADALAERINDSQSRIVITADgfwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmtegrdywwnklm 254
Cdd:cd05918 78 PLDPShpLQRLQEILQDTGAKVVLTSS----------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 255 qgippnayiepepveSEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKwVFDIRDDDIFWCTA----DIgwvtgHSY 330
Cdd:cd05918 105 ---------------PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGR-ALGLTSESRVLQFAsytfDV-----SIL 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 331 VVLGPLLMGATEVIyegAPDYpqpDRWWSI---IERYGVTIFYTSPTAIRMFmrygeewpRKHDLSTLRIIHSVGEPINP 407
Cdd:cd05918 164 EIFTTLAAGGCLCI---PSEE---DRLNDLagfINRLRVTWAFLTPSVARLL--------DPEDVPSLRTLVLGGEALTQ 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 408 EAW-RWAYRV-LGNekvAFGST-WWMTETGGIVISHApglylvpmKPGTNGPPLPG--FEVDVVDENgNPAPPGVKGYLV 482
Cdd:cd05918 230 SDVdTWADRVrLIN---AYGPAeCTIAATVSPVVPST--------DPRNIGRPLGAtcWVVDPDNHD-RLVPIGAVGELL 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 483 IKKPwpGMLHGIWGDPER----YIKT-YW-----SRFPGMFY-AGDYAIKDKDGYIWVLGRADEVIKVAGHR--LGtyEL 549
Cdd:cd05918 298 IEGP--ILARGYLNDPEKtaaaFIEDpAWlkqegSGRGRRLYrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRveLG--EI 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 550 ESALISHPAVAESAVVGV---PDAIKGEVPIAFVVLKQG-----------VAPSDELR---KELREHVRRTIGPIAEPAQ 612
Cdd:cd05918 374 EHHLRQSLPGAKEVVVEVvkpKDGSSSPQLVAFVVLDGSssgsgdgdslfLEPSDEFRalvAELRSKLRQRLPSYMVPSV 453
|
570 580
....*....|....*....|....
gi 20137268 613 IFFVTKLPKTRSGKIMRRLLKAVA 636
Cdd:cd05918 454 FLPLSHLPLTASGKIDRRALRELA 477
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
118-636 |
1.47e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 105.03 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 118 RRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIV 197
Cdd:PRK08162 41 DRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 198 ITADGFwrrgrvvrlKEVVDAALEKATGVESVIVlprlGLKDVPMTEGR-----DY--WwnkLMQGIPPNAYIEPEpveS 270
Cdd:PRK08162 120 IVDTEF---------AEVAREALALLPGPKPLVI----DVDDPEYPGGRfigalDYeaF---LASGDPDFAWTLPA---D 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 271 EHPSFIL-YTSGTTGKPKGIV-HDTGG----------WAVHVYATMKWVFDIrdddiFWCTadiGWvtGHSYVVLgplLM 338
Cdd:PRK08162 181 EWDAIALnYTSGTTGNPKGVVyHHRGAylnalsnilaWGMPKHPVYLWTLPM-----FHCN---GW--CFPWTVA---AR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 339 GATEVIYEGApdypQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDlSTLRIIHSVGEPinPEAwrwayrVL- 417
Cdd:PRK08162 248 AGTNVCLRKV----DPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGID-HPVHAMVAGAAP--PAA------VIa 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 418 GNEKVAFGST--WWMTETGG--IVISHAPGLYLVPM-----KPGTNGPPLPGFE-VDVVD-ENGNPAPPG---------- 476
Cdd:PRK08162 315 KMEEIGFDLThvYGLTETYGpaTVCAWQPEWDALPLderaqLKARQGVRYPLQEgVTVLDpDTMQPVPADgetigeimfr 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 477 ----VKGYLVIKKPWPGMLHGIWgdperyiktywsrfpgmFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESA 552
Cdd:PRK08162 395 gnivMKGYLKNPKATEEAFAGGW-----------------FHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 553 LISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDElrkELREHVRRTIGPIAEPAQIFFvTKLPKTRSGKIMRRLL 632
Cdd:PRK08162 458 LYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEE---EIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVL 533
|
....
gi 20137268 633 KAVA 636
Cdd:PRK08162 534 REQA 537
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
117-632 |
1.71e-23 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 106.28 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRI 196
Cdd:PRK10252 480 ARYQFSYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSL 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VITADGFwrrgrvvrlkevvdaalekatgvesvivLPRLGLKDVPMTEGRDYWWnklmqgiPPNAYIEPEPVESEHPSFI 276
Cdd:PRK10252 559 LITTADQ----------------------------LPRFADVPDLTSLCYNAPL-------APQGAAPLQLSQPHHTAYI 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIV--HDTggwAVHVYATMKWVFDIRDDDIFW----CTADIG-----WvtghsyvvlgPLLMGATEVIY 345
Cdd:PRK10252 604 IFTSGSTGRPKGVMvgQTA---IVNRLLWMQNHYPLTADDVVLqktpCSFDVSvweffW----------PFIAGAKLVMA 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 346 EgaPD-YPQPDRWWSIIERYGVTIFYTSPTAIRMFMryGEEWPR--KHDLSTLRIIHSVGEPINPEAWRWAYRVLGNE-- 420
Cdd:PRK10252 671 E--PEaHRDPLAMQQFFAEYGVTTTHFVPSMLAAFV--ASLTPEgaRQSCASLRQVFCSGEALPADLCREWQQLTGAPlh 746
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 421 ------KVAFGSTWWMTEtggivishAPGLYLVPmkpgtnGPPLP-GFEV-----DVVDENGNPAPPGVKGYLVIKkpwp 488
Cdd:PRK10252 747 nlygptEAAVDVSWYPAF--------GEELAAVR------GSSVPiGYPVwntglRILDARMRPVPPGVAGDLYLT---- 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 489 G--MLHGIWGDP----ERYIKTYWSrfPG--MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVA 560
Cdd:PRK10252 809 GiqLAQGYLGRPdltaSRFIADPFA--PGerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVE 886
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20137268 561 ESAVVGV----PDAIKGEVP--IAFVVLKQGVAPSDELrkeLREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:PRK10252 887 QAVTHACvinqAAATGGDARqlVGYLVSQSGLPLDTSA---LQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
119-634 |
1.76e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 106.79 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:PRK05691 2212 QTLSYAELDARANRLARALRER-GVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLL 2290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TadgfwrrgrvvrlkevvDAALEKATGvesvivlprlglkDVPMTEGRdywWNkLMQGIPPNAYIEPEPVES----EHPS 274
Cdd:PRK05691 2291 S-----------------DRALFEALG-------------ELPAGVAR---WC-LEDDAAALAAYSDAPLPFlslpQHQA 2336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 275 FILYTSGTTGKPKGIVHDTGGWAVHVYATMKwVFDIRDDDifwCTAdigwvtgHSYVV---------LGPLLMGATEVIY 345
Cdd:PRK05691 2337 YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADD---CEL-------HFYSInfdaaserlLVPLLCGARVVLR 2405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 346 E----GAPDYPQpdrwwsIIERYGVTIFYTSPTairmfmrYGEEWPR----KHDLSTLRIIHSVGEPINPEAWRWAYRVL 417
Cdd:PRK05691 2406 AqgqwGAEEICQ------LIREQQVSILGFTPS-------YGSQLAQwlagQGEQLPVRMCITGGEALTGEHLQRIRQAF 2472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 418 GNEkvAFGSTWWMTETggIVIshaPGLYLVP--MKPGTNGPPLP---GFEVD-VVDENGNPAPPGVKGYLVIKKPwpGML 491
Cdd:PRK05691 2473 APQ--LFFNAYGPTET--VVM---PLACLAPeqLEEGAASVPIGrvvGARVAyILDADLALVPQGATGELYVGGA--GLA 2543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 492 HGIWGDP----ERYIKTYWSRFPGMFY-AGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVG 566
Cdd:PRK05691 2544 QGYHDRPgltaERFVADPFAADGGRLYrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLA 2623
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20137268 567 VpDAIKGEVPIAFVV---LKQGVAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:PRK05691 2624 L-DTPSGKQLAGYLVsavAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPA 2693
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
101-632 |
3.25e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 103.92 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 101 AIEWEGEP--VDENGyptdrrKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFS 178
Cdd:PRK13383 45 AARWPGRTaiIDDDG------ALSYRELQRATESLARRLTRD-GVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIST 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 179 GFSADALAERINDSQSRIVITADGFWRRgrvvrlkevvdaaleKATGVESVIVLPrlglkdvPMTEGRDYWWNKlmqgip 258
Cdd:PRK13383 118 EFRSDALAAALRAHHISTVVADNEFAER---------------IAGADDAVAVID-------PATAGAEESGGR------ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 259 pnayiepePVESEHPSFILYTSGTTGKPKGIVHDTG-GWAVHVYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLL 337
Cdd:PRK13383 170 --------PAVAAPGRIVLLTSGTTGKPKGVPRAPQlRSAVGVWVTILDRTRLRTGSRISVAMPMFHGLGLGMLMLTIAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 338 MGA--TEVIYEGAPDYPQPdrwwSIIERYGVTIFytsPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYR 415
Cdd:PRK13383 242 GGTvlTHRHFDAEAALAQA----SLHRADAFTAV---PVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 416 VLGNEKV-AFGSTwwmtETGgivishaPGLYLVPMK----PGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKkpwpGM 490
Cdd:PRK13383 315 TYGDILYnGYGST----EVG-------IGALATPADlrdaPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVG----GE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 491 LHGiwgdpERYIKTYW-SRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPD 569
Cdd:PRK13383 380 LAG-----TRYTDGGGkAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPD 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20137268 570 AIKGEVPIAFVVLKQGVA-PSDELRKELREHVRRtigpIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:PRK13383 455 ERFGHRLAAFVVLHPGSGvDAAQLRDYLKDRVSR----FEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
276-636 |
5.07e-23 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 104.62 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 276 ILYTSGTTGKPKGIV--HDtggwavHVYATMKW---VFDIRDDD-------IFwctadigwvtgHS--YVV--LGPLLMG 339
Cdd:PRK08633 787 IIFSSGSEGEPKGVMlsHH------NILSNIEQisdVFNLRNDDvilsslpFF-----------HSfgLTVtlWLPLLEG 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 340 ATeVIYegapdYPQPDRWWSI---IERYGVTIFYTSPTAIRMFMRYgeewPRKH--DLSTLRIIHSVGEPINPEAwRWAY 414
Cdd:PRK08633 850 IK-VVY-----HPDPTDALGIaklVAKHRATILLGTPTFLRLYLRN----KKLHplMFASLRLVVAGAEKLKPEV-ADAF 918
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 415 RvlgnEKvaFGST----WWMTETGGIVISHAP------GLYLVPMKPGTNGPPLPGFEVDVVD-ENGNPAPPGVKGYLVI 483
Cdd:PRK08633 919 E----EK--FGIRilegYGATETSPVASVNLPdvlaadFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILI 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 484 KKpwPGMLHGIWGDPER---YIKTYWSRfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHR--LGTYELESALISHPA 558
Cdd:PRK08633 993 GG--PQVMKGYLGDPEKtaeVIKDIDGI--GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMvpLGAVEEELAKALGGE 1068
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20137268 559 VAESAVVGVPDAIKGEVPIafVVLKQGVAPSDELRKELREhvrRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVA 636
Cdd:PRK08633 1069 EVVFAVTAVPDEKKGEKLV--VLHTCGAEDVEELKRAIKE---SGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELA 1141
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
273-625 |
6.91e-23 |
|
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: 100.07 E-value: 6.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 273 PSFILYTSGTTGKPKGIVHDTGGWAVHVYATMkWVFDIRDDDIFWCTADIGWVtGHSYVVLGPLLMGATEVIYEGApdyp 352
Cdd:cd17636 2 PVLAIYTAAFSGRPNGALLSHQALLAQALVLA-VLQAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRV---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 353 QPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEwpRKHDLSTLRI---IHSVGEPINPEAWRWAYRVLGnekvaFGSTww 429
Cdd:cd17636 76 DAEEVLELIEAERCTHAFLLPPTIDQIVELNAD--GLYDLSSLRSspaAPEWNDMATVDTSPWGRKPGG-----YGQT-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 430 mtETGGIVISHAPGLYLVpmkpGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpgMLH-GIWGDPEryIKTYWSR 508
Cdd:cd17636 147 --EVMGLATFAALGGGAI----GGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGP---TVMaGYWNRPE--VNARRTR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 509 FpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAP 588
Cdd:cd17636 216 G-GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASV 294
|
330 340 350
....*....|....*....|....*....|....*..
gi 20137268 589 SDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSG 625
Cdd:cd17636 295 TEA---ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
118-626 |
1.41e-22 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 102.17 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 118 RRKLTYYDLYREVNRVAYMLKQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRiV 197
Cdd:PRK05620 36 QEQTTFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDE-V 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 198 ITADGfwrrgrvvRLKEVVDAALEKATGVESVIVLprlGLKDVPMTEGRD------YWWNKLMQGippNAYIEPEPVESE 271
Cdd:PRK05620 115 IVADP--------RLAEQLGEILKECPCVRAVVFI---GPSDADSAAAHMpegikvYSYEALLDG---RSTVYDWPELDE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 272 H-PSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKW-VFDIRDDDIFWCTADIgwvtghsYVVLG---PL--LMGATEVI 344
Cdd:PRK05620 181 TtAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTdSLAVTHGESFLCCVPI-------YHVLSwgvPLaaFMSGTPLV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 345 YEGAPdyPQPDRWWSIIERYGVTIFYTSPTA-IRMFMRYGEEWPRKhdlSTLRIIHSVGEPINP---EAWRWAYrvlgne 420
Cdd:PRK05620 254 FPGPD--LSAPTLAKIIATAMPRVAHGVPTLwIQLMVHYLKNPPER---MSLQEIYVGGSAVPPiliKAWEERY------ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 421 KVAFGSTWWMTETGGI-VISHAPG--------LYLVpmkpgTNGPPLPGFEVDVVDE-------NGNPAPPGVKGYLVI- 483
Cdd:PRK05620 323 GVDVVHVWGMTETSPVgTVARPPSgvsgearwAYRV-----SQGRFPASLEYRIVNDgqvmestDRNEGEIQVRGNWVTa 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 484 ---KKPWP---GMLHGIWGDPERYIKtywSRFP--GMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALIS 555
Cdd:PRK05620 398 syyHSPTEeggGAASTFRGEDVEDAN---DRFTadGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMA 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20137268 556 HPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGK 626
Cdd:PRK05620 475 APEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGK 545
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
119-631 |
1.52e-22 |
|
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: 101.32 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:cd17648 11 KRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 TadgfwrrgrvvrlkevvdaalekatgvesvivlprlGLKDVpmtegrdywwnklmqgippnAYIepepvesehpsfiLY 278
Cdd:cd17648 91 T------------------------------------NSTDL--------------------AYA-------------IY 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 279 TSGTTGKPKGIVHDTGGwAVHVYATMKWVFDIRDD-------------DIFWCTADIGWVTGHSYVVLGPllmgateviy 345
Cdd:cd17648 102 TSGTTGKPKGVLVEHGS-VVNLRTSLSERYFGRDNgdeavlffsnyvfDFFVEQMTLALLNGQKLVVPPD---------- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 346 EGAPDypqPDRWWSIIERYGVTIFYTSPTAIRMFmrygeEWPRkhdLSTLRIIHSVGEPINP---EAWRWAYRVLGNEKV 422
Cdd:cd17648 171 EMRFD---PDRFYAYINREKVTYLSGTPSVLQQY-----DLAR---LPHLKRVDAAGEEFTApvfEKLRSRFAGLIINAY 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 423 AFgstwwmTETGgiVISHAPGLYLVPMKPGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPW--PGMLHGIWGDPER 500
Cdd:cd17648 240 GP------TETT--VTNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGvaRGYLNRPELTAER 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 501 YIKTYW--------SRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIK 572
Cdd:cd17648 312 FLPNPFqteqerarGRNARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQ 391
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20137268 573 GEVPI-----AFVVLKQGVAPSdelrKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKI-MRRL 631
Cdd:cd17648 392 AQSRIqkylvGYYLPEPGHVPE----SDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLdVRAL 452
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
118-667 |
2.81e-22 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 101.25 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 118 RRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIV 197
Cdd:PLN03102 37 KTRFTWPQTYDRCCRLAASL-ISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKIL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 198 ITADGFWRRGR-VVRLKEVVDAALEKatgveSVIVLPRLGLKDVPMTEGRDYwwNKLMQ-GIP-PNAYIEPEPVESEH-P 273
Cdd:PLN03102 116 FVDRSFEPLAReVLHLLSSEDSNLNL-----PVIFIHEIDFPKRPSSEELDY--ECLIQrGEPtPSLVARMFRIQDEHdP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 274 SFILYTSGTTGKPKGIV--HDTG---------GWAVHVYATMKWVFDIrdddiFWCTadiGWVtgHSYvvlGPLLMGATE 342
Cdd:PLN03102 189 ISLNYTSGTTADPKGVVisHRGAylstlsaiiGWEMGTCPVYLWTLPM-----FHCN---GWT--FTW---GTAARGGTS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 343 VI--YEGAPDYpqpdrwWSIIERYGVTIFYTSPTAIRMFMRyGEEWPRKHDLSTLRIIHSVGEPinPEAWRWAYRVLGNE 420
Cdd:PLN03102 256 VCmrHVTAPEI------YKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVLTGGSPP--PAALVKKVQRLGFQ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 421 KV-AFGstwwMTETGGIVI--------SHAPGLYLVPMKPGTNGPPLPGFEVDVVDENGNPAPP---GVKGYLVIKKPwp 488
Cdd:PLN03102 327 VMhAYG----LTEATGPVLfcewqdewNRLPENQQMELKARQGVSILGLADVDVKNKETQESVPrdgKTMGEIVIKGS-- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 489 GMLHGIWGDPEryiKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVP 568
Cdd:PLN03102 401 SIMKGYLKNPK---ATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMP 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 569 DAIKGEVPIAFVVLKQGVAPSDEL-------RKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVATGAPL 641
Cdd:PLN03102 478 HPTWGETPCAFVVLEKGETTKEDRvdklvtrERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGLVV 557
|
570 580
....*....|....*....|....*.
gi 20137268 642 GDvttlEDETSVEEAKRAYEEIKAEM 667
Cdd:PLN03102 558 ED----EDNVIKKVHQRPVEHFSSRL 579
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
120-632 |
4.68e-22 |
|
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: 99.82 E-value: 4.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 120 KLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVIT 199
Cdd:cd05914 7 PLTYKDLADNIAKFALLLKIN-GVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 200 ADgfwrrgrvvrlKEvvDAALekatgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepvesehpsfILYT 279
Cdd:cd05914 86 SD-----------ED--DVAL-------------------------------------------------------INYT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 280 SGTTGKPKGIV--HDTGGWAVHVYATMKWVfdiRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVI------------- 344
Cdd:cd05914 98 SGTTGNSKGVMltYRNIVSNVDGVKEVVLL---GKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFldkipsakiiala 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 345 -YEGAPDYPQPdRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRK---------HDL--STLRIIHSVGEPINPEAWRW 412
Cdd:cd05914 175 fAQVTPTLGVP-VPLVIEKIFKMDIIPKLTLKKFKFKLAKKINNRKirklafkkvHEAfgGNIKEFVIGGAKINPDVEEF 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 413 AYRVlgNEKVAFGstWWMTETGGIVISHAPGlylvPMKPGTNGPPLPGFEVDVVDENgnpaPPGVKGYLVIKKPwpGMLH 492
Cdd:cd05914 254 LRTI--GFPYTIG--YGMTETAPIISYSPPN----RIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGP--NVMK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 493 GIWGDPE----RYIKTYWsrfpgmFYAGDYAIKDKDGYIWVLGRADEVIKV-AGHRLGTYELESALISHPAVAESAVVGV 567
Cdd:cd05914 320 GYYKNPEataeAFDKDGW------FHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESLVVVQ 393
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 568 PDAIKGEVPI----AFVVLKQGVAPSDELRKELREHVRRTIGPIAEPAQIFFV-TKLPKTRSGKIMRRLL 632
Cdd:cd05914 394 EKKLVALAYIdpdfLDVKALKQRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKRFLY 463
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
121-645 |
4.13e-21 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 97.39 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITsvvfsgfsadalaerindsqsrivITA 200
Cdd:PRK05857 42 LRYRELVAEVGGLAADLRAQ-SVSRGSRVLVISDNGPETYLSVLACAKLGAIA------------------------VMA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 201 DGFWRRGRVVRLKEVVDAA---LEKATGVESViVLPRlGLKDVPMTEGRDYWWNKLMQGIPPNAYIEPEP-VESEHPSFI 276
Cdd:PRK05857 97 DGNLPIAAIERFCQITDPAaalVAPGSKMASS-AVPE-ALHSIPVIAVDIAAVTRESEHSLDAASLAGNAdQGSEDPLAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIVHDTggwavhvyATMKWVFDI-RDDDIFWctadIGWVTGhsyvvlgpllmgatEVIYEGAPDYPQPD 355
Cdd:PRK05857 175 IFTSGTTGEPKAVLLAN--------RTFFAVPDIlQKEGLNW----VTWVVG--------------ETTYSPLPATHIGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 356 RWWSI--IERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTL--RIIHSV--GEPINPEAWRWAY----------RVLGN 419
Cdd:PRK05857 229 LWWILtcLMHGGLCVTGGENTTSLLEILTTNAVATTCLVPTLlsKLVSELksANATVPSLRLVGYggsraiaadvRFIEA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 420 EKVAFGSTWWMTETG--GIVISHAPGlYLVPMKPGTNGPPLPGFEVDVVDENG-NPAPPGVK-----GYLVIKKPwPGML 491
Cdd:PRK05857 309 TGVRTAQVYGLSETGctALCLPTDDG-SIVKIEAGAVGRPYPGVDVYLAATDGiGPTAPGAGpsasfGTLWIKSP-ANML 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 492 hGIWGDPERyikTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAI 571
Cdd:PRK05857 387 -GYWNNPER---TAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEE 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20137268 572 KGE-VPIAFVVLKQ-GVAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVATGAPLGDVT 645
Cdd:PRK05857 463 FGAlVGLAVVASAElDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARVVV 538
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
219-604 |
5.15e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 96.38 E-value: 5.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 219 ALEKAtGVESVIVLPRLGLKDVpmtegrdywwNKLMQGIPPNAYI-EPEpveSEHPSFILYTSGTTGKPKGIVHDTGGWA 297
Cdd:cd05910 46 ALFKA-GAVPVLIDPGMGRKNL----------KQCLQEAEPDAFIgIPK---ADEPAAILFTSGSTGTPKGVVYRHGTFA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 298 VHVyATMKWVFDIRDDDIFWCTADIgwvtghsYVVLGPLLmGATEVIYEGAPDYP---QPDRWWSIIERYGVTIFYTSPT 374
Cdd:cd05910 112 AQI-DALRQLYGIRPGEVDLATFPL-------FALFGPAL-GLTSVIPDMDPTRParaDPQKLVGAIRQYGVSIVFGSPA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 375 AIRMFMRYGEEwpRKHDLSTLRIIHSVGEPInPEAWRWAYRVLGNEKVAFGSTWWMTET------GGIVISHAPGLYLVP 448
Cdd:cd05910 183 LLERVARYCAQ--HGITLPSLRRVLSAGAPV-PIALAARLRKMLSDEAEILTPYGATEAlpvssiGSRELLATTTAATSG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 449 MKPGTNGPPLPGFEVDVVDENGNP---------APPGVKGYLVIK----------KPWPGMLHGIWGDPERyiktYWSRF 509
Cdd:cd05910 260 GAGTCVGRPIPGVRVRIIEIDDEPiaewddtleLPRGEIGEITVTgptvtptyvnRPVATALAKIDDNSEG----FWHRM 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 510 pgmfyaGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIkGEVPIAFVVLKQGVA-P 588
Cdd:cd05910 336 ------GDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPG-CQLPVLCVEPLPGTItP 408
|
410
....*....|....*.
gi 20137268 589 SDELRKELREHVRRTI 604
Cdd:cd05910 409 RARLEQELRALAKDYP 424
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
121-617 |
1.01e-20 |
|
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: 96.00 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLKqNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVIta 200
Cdd:cd05932 7 FTWGEVADKARRLAAALR-ALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 201 dgfwrrgrVVRLKEVVDAALEKATGVESVIVLPRLGLKDvpmtegrDYWWNKLMQGIPPNayIEPEPVESEHPSFILYTS 280
Cdd:cd05932 84 --------VGKLDDWKAMAPGVPEGLISISLPPPSAANC-------QYQWDDLIAQHPPL--EERPTRFPEQLATLIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 281 GTTGKPKGIVHDTG--GWAVHVYATMkwvFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAPDYPQPdrww 358
Cdd:cd05932 147 GTTGQPKGVMLTFGsfAWAAQAGIEH---IGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFVED---- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 359 siIERYGVTIFYTSPTAIRMF-MRYGEEWPRK-------------------HD---LSTLRIIHSVGEPINPEAWRWaYR 415
Cdd:cd05932 220 --VQRARPTLFFSVPRLWTKFqQGVQDKIPQQklnlllkipvvnslvkrkvLKglgLDQCRLAGCGSAPVPPALLEW-YR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 416 VLGNEkvaFGSTWWMTETGGIVISHAPGlylvPMKPGTNGPPLPGFEVDVVDEngnpappgvkGYLVIKKpwPGMLHGIW 495
Cdd:cd05932 297 SLGLN---ILEAYGMTENFAYSHLNYPG----RDKIGTVGNAGPGVEVRISED----------GEILVRS--PALMMGYY 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 496 GDPERYIKTYWSrfPGMFYAGDYAIKDKDGYIWVLGRADEVIKVA-GHRLGTYELESALISHPAVAESAVVG--VPDAIK 572
Cdd:cd05932 358 KDPEATAEAFTA--DGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGsgLPAPLA 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 20137268 573 GEVPIAFVVLKQGVAPSDELRKELREHVRRTIGPIAEPAQIFFVT 617
Cdd:cd05932 436 LVVLSEEARLRADAFARAELEASLRAHLARVNSTLDSHEQLAGIV 480
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
235-645 |
1.45e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 95.86 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 235 LGLKDVPMTEGRDYWWNKLMQGIPPnayIEP-EPVESEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKwVFDIRDD 313
Cdd:PRK13388 116 LDLPGVRVLDVDTPAYAELVAAAGA---LTPhREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTE-RFGLTRD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 314 DIFWCTADIGwvtgHSYVVL---GPLLM-GATEVIyegaPDYPQPDRWWSIIERYGVTIFYTSPTAIRMFMRyGEEWPRK 389
Cdd:PRK13388 192 DVCYVSMPLF----HSNAVMagwAPAVAsGAAVAL----PAKFSASGFLDDVRRYGATYFNYVGKPLAYILA-TPERPDD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 390 HDlSTLRiiHSVGEPINPEAWRWAYRVLGNEKV-AFGSTwwmteTGGIVISHAPGlylVPmkPGTNGPPLPGFE------ 462
Cdd:PRK13388 263 AD-NPLR--VAFGNEASPRDIAEFSRRFGCQVEdGYGSS-----EGAVIVVREPG---TP--PGSIGRGAPGVAiynpet 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 463 -----VDVVDENG---NPAPpgVKGYLVIKKPwPGMLHGIWGDPERYIKtywsRFP-GMFYAGDYAIKDKDGYIWVLGRA 533
Cdd:PRK13388 330 ltecaVARFDAHGallNADE--AIGELVNTAG-AGFFEGYYNNPEATAE----RMRhGMYWSGDLAYRDADGWIYFAGRT 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 534 DEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPS-DELRKELreHVRRTIGPIAEPAQ 612
Cdd:PRK13388 403 ADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDpDAFAAFL--AAQPDLGTKAWPRY 480
|
410 420 430
....*....|....*....|....*....|...
gi 20137268 613 IFFVTKLPKTRSGKIMRRLLKAVATGAPLGDVT 645
Cdd:PRK13388 481 VRIAADLPSTATNKVLKRELIAQGWATGDPVTL 513
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
427-634 |
2.68e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 93.19 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 427 TWWMTET-GGIVishapglYlvpmkpgtNGPPLPGFEVDVVDENGNPAPPGV-KGYLVIKKPWPgmlhgiwgdperyikt 504
Cdd:PRK07824 181 TYGMSETsGGCV-------Y--------DGVPLDGVRVRVEDGRIALGGPTLaKGYRNPVDPDP---------------- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 505 ywsrF--PGMFYAGDYAIKDkDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVL 582
Cdd:PRK07824 230 ----FaePGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVG 304
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 20137268 583 KQGVAPSDElrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:PRK07824 305 DGGPAPTLE---ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
132-633 |
4.72e-20 |
|
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: 94.03 E-value: 4.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 132 RVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITADGFWrrgrvvr 211
Cdd:cd05915 36 RLMGGL-RALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLL------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 212 lkevvdaalekATGVESVIVLPRLglKDVPMTEGRDYWWNKLMQGIPPNaYIEPEPVESEHPSFILYTSGTTGKPKGIVH 291
Cdd:cd05915 108 -----------PLVEAIRGELKTV--QHFVVMDEKAPEGYLAYEEALGE-EADPVRVPERAACGMAYTTGTTGLPKGVVY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 292 DTGGwaVHVYATMKWVFD---IRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEVIYEGAPDypqpDRWWSIIERYGVTI 368
Cdd:cd05915 174 SHRA--LVLHSLAASLVDgtaLSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDP----ASLVELFDGEGVTF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 369 FYTSPTAIRMFMRyGEEWPRKHDLSTLRIIHSVGEPinPEAwRWAYRVLGNEKVAFGSTWWMTETGGIVISHAPGLYLVP 448
Cdd:cd05915 248 TAGVPTVWLALAD-YLESTGHRLKTLRRLVVGGSAA--PRS-LIARFERMGVEVRQGYGLTETSPVVVQNFVKSHLESLS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 449 MKPGTNGPPLPGFE-----VDVVDENGNPAPPGVKGYLVIKKPWPGMLHGIWGDPEryiKTYWSRFPGMFY-AGDYAIKD 522
Cdd:cd05915 324 EEEKLTLKAKTGLPiplvrLRVADEEGRPVPKDGKALGEVQLKGPWITGGYYGNEE---ATRSALTPDGFFrTGDIAVWD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 523 KDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDelrkELREHVRR 602
Cdd:cd05915 401 EEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPE----ELNEHLLK 476
|
490 500 510
....*....|....*....|....*....|..
gi 20137268 603 TIGPIAE-PAQIFFVTKLPKTRSGKIMRRLLK 633
Cdd:cd05915 477 AGFAKWQlPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
266-636 |
1.18e-19 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 92.99 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 266 EPVESEHPSFIL-YTSGTTGKPKGIV-HDTGG----------WAVHVYATMKWVFDIrdddiFWCTadiGWVTGHSYVVL 333
Cdd:PLN02479 189 KPPADEWQSIALgYTSGTTASPKGVVlHHRGAylmalsnaliWGMNEGAVYLWTLPM-----FHCN---GWCFTWTLAAL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 334 GP----LLMGATEVIYEGapdypqpdrwwsiIERYGVTIFYTSPTAIRMFMRYgeewPRKHDLSTL-RIIHSVGEPINPE 408
Cdd:PLN02479 261 CGtnicLRQVTAKAIYSA-------------IANYGVTHFCAAPVVLNTIVNA----PKSETILPLpRVVHVMTAGAAPP 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 409 AWRWAYRVLGNEKVAfgSTWWMTETGG--IVISHAPGLYLVPMKP-----GTNGPPLPGFE-VDVVD-ENGNPAPPGVKG 479
Cdd:PLN02479 324 PSVLFAMSEKGFRVT--HTYGLSETYGpsTVCAWKPEWDSLPPEEqarlnARQGVRYIGLEgLDVVDtKTMKPVPADGKT 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 480 YLVIKKPWPGMLHGIWGDPERYIKTYWSrfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAV 559
Cdd:PLN02479 402 MGEIVMRGNMVMKGYLKNPKANEEAFAN---GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAV 478
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20137268 560 AESAVVGVPDAIKGEVPIAFVVLKQGVAPSDE--LRKELREHVRRTIGPIAEPAQIFFvTKLPKTRSGKIMRRLLKAVA 636
Cdd:PLN02479 479 LEASVVARPDERWGESPCAFVTLKPGVDKSDEaaLAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAKA 556
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
274-633 |
2.69e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 91.69 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 274 SFILYTSGTTGKPKGIVHDTGGWAVHVYAT-MKWVFDIRDDDIF-----------WCTADIGWVTGHSYVVLGPLLMGAT 341
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALYSHRSTVLHAYGAaLPDAMGLSARDAVlpvvpmfhvnaWGLPYSAPLTGAKLVLPGPDLDGKS 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 342 evIYEgapdypqpdrwwsIIERYGVTIFYTSPTAIRMFMRYGEEWPRKhdLSTLRIIHSVGEPINPEAWRWAYRVLGNEK 421
Cdd:PRK07008 259 --LYE-------------LIEAERVTFSAGVPTVWLGLLNHMREAGLR--FSTLRRTVIGGSACPPAMIRTFEDEYGVEV 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 422 VafgSTWWMTEtggivishapglylvpMKP-GT----------------------NGPPLPGFEVDVVDENGNPAPPGVK 478
Cdd:PRK07008 322 I---HAWGMTE----------------MSPlGTlcklkwkhsqlpldeqrkllekQGRVIYGVDMKIVGDDGRELPWDGK 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 479 GY--LVIKKPWPgmlhgiwgdPERYIKTYWSRF-PGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALIS 555
Cdd:PRK07008 383 AFgdLQVRGPWV---------IDRYFRGDASPLvDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVA 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 556 HPAVAESAVVGVPDAIKGEVPIAFVVLKQGVapsDELRKELREHVRrtiGPIAE---PAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:PRK07008 454 HPAVAEAACIACAHPKWDERPLLVVVKRPGA---EVTREELLAFYE---GKVAKwwiPDDVVFVDAIPHTATGKLQKLKL 527
|
.
gi 20137268 633 K 633
Cdd:PRK07008 528 R 528
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
119-634 |
3.36e-19 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 91.72 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAItSVvfsGFSADALAERI----NDSQS 194
Cdd:cd17641 10 QEFTWADYADRVRAFALGL-LALGVGRGDVVAILGDNRPEWVWAELAAQAIGAL-SL---GIYQDSMAEEVayllNYTGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 195 RIVITADgfwrrgrvvrlKEVVDAALEKAT---GVESVIVLPRLGLKDvpMTEGRDYWWNKLMQGIPPNAYIEPEPVESE 271
Cdd:cd17641 85 RVVIAED-----------EEQVDKLLEIADripSVRYVIYCDPRGMRK--YDDPRLISFEDVVALGRALDRRDPGLYERE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 272 ----HP---SFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDDIFwCTADIGWVTGHSYVVLGPLLMGAT--- 341
Cdd:cd17641 152 vaagKGedvAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYV-SVLPLPWIGEQMYSVGQALVCGFIvnf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 342 --------EVIYEGAPDY--PQPDRWWSIIERYGVTIFYTSPTAIRMF---MRYGEE-------------WPRKH----- 390
Cdd:cd17641 231 peepetmmEDLREIGPTFvlLPPRVWEGIAADVRARMMDATPFKRFMFelgMKLGLRaldrgkrgrpvslWLRLAswlad 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 391 -----------DLSTLRIIHSVGEPINPEAWRWaYRVLG-NEKVAFGSTwwmtETGGIVISHAPGlylvPMKPGTNGPPL 458
Cdd:cd17641 311 allfrplrdrlGFSRLRSAATGGAALGPDTFRF-FHAIGvPLKQLYGQT----ELAGAYTVHRDG----DVDPDTVGVPF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 459 PGFEVDvVDENGNpappgvkgyLVIKKpwPGMLHGIWGDPERYIKTYWSRfpGMFYAGDYAIKDKDGYIWVLGRADEVIK 538
Cdd:cd17641 382 PGTEVR-IDEVGE---------ILVRS--PGVFVGYYKNPEATAEDFDED--GWLHTGDAGYFKENGHLVVIDRAKDVGT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 539 VA-GHRLGTYELESALISHPAVAESAVVG-----------VPDAIKG----EVPIAFVVLkQGVAPSDELRKELREHVRR 602
Cdd:cd17641 448 TSdGTRFSPQFIENKLKFSPYIAEAVVLGagrpyltaficIDYAIVGkwaeQRGIAFTTY-TDLASRPEVYELIRKEVEK 526
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 20137268 603 TIGPIAEPAQIFFVTKLPK---------TRSGKIMRRLLKA 634
Cdd:cd17641 527 VNASLPEAQRIRRFLLLYKeldaddgelTRTRKVRRGVIAE 567
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
276-634 |
1.91e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 89.09 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 276 ILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVfDIRDDDIFWCTADIGWVTGHSyVVLGPLLMGATEVIYegapdyPQPD 355
Cdd:PLN02860 177 ICFTSGTTGRPKGVTISHSALIVQSLAKIAIV-GYGEDDVYLHTAPLCHIGGLS-SALAMLMVGACHVLL------PKFD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 356 RWWSI--IERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKVAfgSTWWMTET 433
Cdd:PLN02860 249 AKAALqaIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLF--SAYGMTEA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 434 ggivishAPGLYLVPM-KPGTNGPPLPGFEVDVVDENGNPAPPGVkgylVIKKPWPGMLHGIWGD---PERYIKT----- 504
Cdd:PLN02860 327 -------CSSLTFMTLhDPTLESPKQTLQTVNQTKSSSVHQPQGV----CVGKPAPHVELKIGLDessRVGRILTrgphv 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 505 ---YWSRFP---------GMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIK 572
Cdd:PLN02860 396 mlgYWGQNSetasvlsndGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRL 475
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20137268 573 GEVPIAFVVLKQGVAPSD---ELRK--------ELREHVRRTIGPIAEPAQIFFVTK--LPKTRSGKIMRRLLKA 634
Cdd:PLN02860 476 TEMVVACVRLRDGWIWSDnekENAKknltlsseTLRHHCREKNLSRFKIPKLFVQWRkpFPLTTTGKIRRDEVRR 550
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
113-630 |
1.61e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 83.12 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 113 GYPTDRRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDS 192
Cdd:PRK07768 22 GEPDAPVRHTWGEVHERARRIAGGL-AAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 193 QSRI-VITAdgfwrrgRVVRLKEVVDAALEkatgvesviVLPRLGLKDVPMTEgrdywwnkLMQGIPpnayIEPEPVESE 271
Cdd:PRK07768 101 LRVIgMIGA-------KAVVVGEPFLAAAP---------VLEEKGIRVLTVAD--------LLAADP----IDPVETGED 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 272 HPSFILYTSGTTGKPKG--IVHdtGGWAVHVYATMKWV-FDIRDDDIF-W--CTADIGWVtghSYVVLgPLLMGAtEVIY 345
Cdd:PRK07768 153 DLALMQLTSGSTGSPKAvqITH--GNLYANAEAMFVAAeFDVETDVMVsWlpLFHDMGMV---GFLTV-PMYFGA-ELVK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 346 EGAPDY-PQPDRWWSIIERYGVTI-----FYTSPTAIRMfmRYGEEwPRKHDLSTLRIIHSVGEPINP---EAWRWAYRV 416
Cdd:PRK07768 226 VTPMDFlRDPLLWAELISKYRGTMtaapnFAYALLARRL--RRQAK-PGAFDLSSLRFALNGAEPIDPadvEDLLDAGAR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 417 LGNEKVAFGSTWWMTETGGIVISHAPGLYL----------------VPMKPG------TNGPPLPGFEVDVVDENGNPAP 474
Cdd:PRK07768 303 FGLRPEAILPAYGMAEATLAVSFSPCGAGLvvdevdadllaalrraVPATKGntrrlaTLGPPLPGLEVRVVDEDGQVLP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 475 P---GV---------KGYLVIKKPWPGMlhgiwgDPEryiktywsrfpGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGH 542
Cdd:PRK07768 383 PrgvGVielrgesvtPGYLTMDGFIPAQ------DAD-----------GWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGR 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 543 RLGTYELESALISHPAVAESAVVGVP-DAIKGEVPIAFVV---LKQGVAPSDELRKELREHVRRTIGpiAEPAQIFFVTK 618
Cdd:PRK07768 446 NIYPTDIERAAARVEGVRPGNAVAVRlDAGHSREGFAVAVesnAFEDPAEVRRIRHQVAHEVVAEVG--VRPRNVVVLGP 523
|
570
....*....|....
gi 20137268 619 --LPKTRSGKIMRR 630
Cdd:PRK07768 524 gsIPKTPSGKLRRA 537
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
117-602 |
1.84e-16 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 83.00 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRI 196
Cdd:PRK08279 59 EDQSISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKH 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 VITADGFWrrgrvvrlkEVVDAALEKATGVESVIVL------PRLGLKDVpmtegrdywwNKLMQGIPPNAYIEPEPVES 270
Cdd:PRK08279 138 LIVGEELV---------EAFEEARADLARPPRLWVAggdtldDPEGYEDL----------AAAAAGAPTTNPASRSGVTA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 271 EHPSFILYTSGTTGKPKGIVHDTGGW--AVHVYATMkwvFDIRDDDIFWCTADIGWVTGhSYVVLGPLLM-GATEVIYE- 346
Cdd:PRK08279 199 KDTAFYIYTSGTTGLPKAAVMSHMRWlkAMGGFGGL---LRLTPDDVLYCCLPLYHNTG-GTVAWSSVLAaGATLALRRk 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 347 -GApdypqpDRWWSIIERYGVTIFYtsptAIRMFMRYGEEWP-----RKHdlsTLRIIhsVGEPINPEAW-RWAYRvLGN 419
Cdd:PRK08279 275 fSA------SRFWDDVRRYRATAFQ----YIGELCRYLLNQPpkptdRDH---RLRLM--IGNGLRPDIWdEFQQR-FGI 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 420 EKVA--FGStwwmTEtgGIVishapGLYLVPMKPGTNG--PPLPGFEVDVV-----------DENGN--PAPPGVKGYLV 482
Cdd:PRK08279 339 PRILefYAA----SE--GNV-----GFINVFNFDGTVGrvPLWLAHPYAIVkydvdtgepvrDADGRciKVKPGEVGLLI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 483 --IKKPWPgmlhgIWG--DPEryiKT-------------YWsrfpgmFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLG 545
Cdd:PRK08279 408 grITDRGP-----FDGytDPE---ASekkilrdvfkkgdAW------FNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVA 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20137268 546 TYELESALISHPAVAESAVVGVpdaikgEVP-------IAFVVLKQGVAPSdelRKELREHVRR 602
Cdd:PRK08279 474 TTEVENALSGFPGVEEAVVYGV------EVPgtdgragMAAIVLADGAEFD---LAALAAHLYE 528
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
264-634 |
3.38e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 81.24 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 264 EPEPVESEHPSFILYTSGTTGKPKGIvhdTGGWA-----VHVYaTMKWVFDIRDDDIFWCTadigwVTgHSYV----VLG 334
Cdd:PRK08308 94 EAVNYLAEEPSLLQYSSGTTGEPKLI---RRSWTeidreIEAY-NEALNCEQDETPIVACP-----VT-HSYGlicgVLA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 335 PLLMGATEVIYEGapdyPQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKHDLSTlriihsVGEPInPEAWrwaY 414
Cdd:PRK08308 164 ALTRGSKPVIITN----KNPKFALNILRNTPQHILYAVPLMLHILGRLLPGTFQFHAVMT------SGTPL-PEAW---F 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 415 RVLGNEKVAFGSTWWMTETGGIVISHapglylvPMK-PGTNGPPLPGFEVDVVDENGNPappgvkGYLVIKKPwpgmlhg 493
Cdd:PRK08308 230 YKLRERTTYMMQQYGCSEAGCVSICP-------DMKsHLDLGNPLPHVSVSAGSDENAP------EEIVVKMG------- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 494 iwgdpERYIKTywsrfpgmfyaGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKG 573
Cdd:PRK08308 290 -----DKEIFT-----------KDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAG 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20137268 574 EVPIAFVVLKQGVAPSdelrkELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKA 634
Cdd:PRK08308 354 ERVKAKVISHEEIDPV-----QLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
109-632 |
9.12e-16 |
|
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: 80.21 E-value: 9.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 109 VDENgyptdrRKLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAER 188
Cdd:cd17656 8 VFEN------QKLTYRELNERSNQLARFL-REKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 189 INDSQSRIVITAdgfwrrgrvvrlkevvdAALEKATGVESVIVLPRlglkdvpmtegrdywWNKLMQGIPPNAYIEpepV 268
Cdd:cd17656 81 MLDSGVRVVLTQ-----------------RHLKSKLSFNKSTILLE---------------DPSISQEDTSNIDYI---N 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 269 ESEHPSFILYTSGTTGKPKGIV------------------HDTGGwAVHVYATMKwvFDIRDDDIFwctadigwvtghsy 330
Cdd:cd17656 126 NSDDLLYIIYTSGTTGKPKGVQlehknmvnllhferektnINFSD-KVLQFATCS--FDVCYQEIF-------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 331 vvlGPLLMGATEVIY--EGAPDYPQpdrWWSIIERYGVTIFYTsPTAIRMFMryGEEWPRKHDLST-LRIIHSVGEPI-- 405
Cdd:cd17656 189 ---STLLSGGTLYIIreETKRDVEQ---LFDLVKRHNIEVVFL-PVAFLKFI--FSEREFINRFPTcVKHIITAGEQLvi 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 406 -NPeawrwAYRVLGNEKVAFGSTWWMTETGGIV---ISHAPGLYLVPmkpgTNGPPLPGFEVDVVDENGNPAPPGVKGYL 481
Cdd:cd17656 260 tNE-----FKEMLHEHNVHLHNHYGPSETHVVTtytINPEAEIPELP----PIGKPISNTWIYILDQEQQLQPQGIVGEL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 482 VIKKPwpGMLHGIWGDP----ERYIKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHP 557
Cdd:cd17656 331 YISGA--SVARGYLNRQeltaEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHP 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20137268 558 AVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDelrkeLREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLL 632
Cdd:cd17656 409 GVSEAVVLDKADDKGEKYLCAYFVMEQELNISQ-----LREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
117-640 |
2.97e-15 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 80.01 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 117 DRRKLTYYDLYREVNRVAYMLKQNFGVkkGDKITLYLPMVPELPITMLAAWRIGAITSVV-FSGFSADALAE-RIndSQS 194
Cdd:PRK06814 655 VNGPLTYRKLLTGAFVLGRKLKKNTPP--GENVGVMLPNANGAAVTFFALQSAGRVPAMInFSAGIANILSAcKA--AQV 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 195 RIVITADGFWRRGRvvrLKEVVdAALEKATGVesvivlprLGLKDVPMTEGrdyWWNKLMQGI----PPNAYIEPEPves 270
Cdd:PRK06814 731 KTVLTSRAFIEKAR---LGPLI-EALEFGIRI--------IYLEDVRAQIG---LADKIKGLLagrfPLVYFCNRDP--- 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 271 EHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDDIFWCTADIgwvtgHSYVVLGPLLMgateVIYEGAPD 350
Cdd:PRK06814 793 DDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVF-----HSFGLTGGLVL----PLLSGVKV 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 351 --YPQPDRWWSIIER-YGV--TIFYTSPTAIRMFMRYGEEWprkhDLSTLRIIHSVGEPINPEAWR-WAyrvlgnEKvaF 424
Cdd:PRK06814 864 flYPSPLHYRIIPELiYDTnaTILFGTDTFLNGYARYAHPY----DFRSLRYVFAGAEKVKEETRQtWM------EK--F 931
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 425 G----STWWMTETggivishAPGLYL-VPM--KPGTNGPPLPGFE-----VDVVDENGN---PAPPGVKGYLVIKKPwpG 489
Cdd:PRK06814 932 GirilEGYGVTET-------APVIALnTPMhnKAGTVGRLLPGIEyrlepVPGIDEGGRlfvRGPNVMLGYLRAENP--G 1002
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 490 MLH---GIWGDperyiktywsrfpgmfyAGDYAIKDKDGYIWVLGRADEVIKVAGHrlgtyelesaLISHPAV------- 559
Cdd:PRK06814 1003 VLEppaDGWYD-----------------TGDIVTIDEEGFITIKGRAKRFAKIAGE----------MISLAAVeelaael 1055
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 560 ---AESAVVGVPDAIKGEvpiAFVVLKQGvapSDELRKELREHVR-RTIGPIAEPAQIFFVTKLPKTRSGKI----MRRL 631
Cdd:PRK06814 1056 wpdALHAAVSIPDARKGE---RIILLTTA---SDATRAAFLAHAKaAGASELMVPAEIITIDEIPLLGTGKIdyvaVTKL 1129
|
....*....
gi 20137268 632 LKAVATGAP 640
Cdd:PRK06814 1130 AEEAAAKPE 1138
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
120-604 |
9.24e-15 |
|
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: 77.01 E-value: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 120 KLTYYDLYREVNRVAYMLkQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVIt 199
Cdd:cd17640 5 RITYKDLYQEILDFAAGL-RSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 200 adgfwrrgrvvrlkevvdaalekatgVESvivlprlGLKDVpmtegrdywwnklmqgippnayiepepvesehpSFILYT 279
Cdd:cd17640 83 --------------------------VEN-------DSDDL---------------------------------ATIIYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 280 SGTTGKPKGIV--HDTGGWAVHVYATMkwvFDIRDDDIFWCTADIgWvtgHSYvvlgpllmgateviyEGAPDYpqpdrw 357
Cdd:cd17640 97 SGTTGNPKGVMltHANLLHQIRSLSDI---VPPQPGDRFLSILPI-W---HSY---------------ERSAEY------ 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 358 wsIIERYGVTIFYTSPTAIrmfmrygeewprKHDLSTLR--IIHSVgepinPEAWRWAYR-------------------- 415
Cdd:cd17640 149 --FIFACGCSQAYTSIRTL------------KDDLKRVKphYIVSV-----PRLWESLYSgiqkqvsksspikqflflff 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 416 VLGNEKVA---------------FGST-------WWMTETGGIVISHAPGLYLVpmkpGTNGPPLPGFEVDVVDENGN-P 472
Cdd:cd17640 210 LSGGIFKFgisgggalpphvdtfFEAIgievlngYGLTETSPVVSARRLKCNVR----GSVGRPLPGTEIKIVDPEGNvV 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 473 APPGVKGYLVIKKPwPGMLhGIWGDPERYIKTYWSRfpGMFYAGDYAIKDKDGYIWVLGRA-DEVIKVAGHRLGTYELES 551
Cdd:cd17640 286 LPPGEKGIVWVRGP-QVMK-GYYKNPEATSKVLDSD--GWFNTGDLGWLTCGGELVLTGRAkDTIVLSNGENVEPQPIEE 361
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20137268 552 ALISHPAVAESAVVG----------VP--DAIKGEVPIAFVVLKQGVAP---SDELRKELREHVRRTI 604
Cdd:cd17640 362 ALMRSPFIEQIMVVGqdqkrlgaliVPnfEELEKWAKESGVKLANDRSQllaSKKVLKLYKNEIKDEI 429
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
269-632 |
1.18e-14 |
|
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: 76.82 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 269 ESEHPSFILYTSGTTGKPKGIV--HDTggwAVHVYATMKWVFDIRDDDIFWCTADIGWvTGHSYVVLGPLLMGATEVIYE 346
Cdd:cd17645 102 NPDDLAYVIYTSGSTGLPKGVMieHHN---LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLTAGAALHVVP 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 347 GAPDYpQPDRWWSIIERYGVTIFYTSPTAIRMFMRYgeewprkhDLSTLRIIHSVGEPINpEAWRWAYRVLGNekvaFGS 426
Cdd:cd17645 178 SERRL-DLDALNDYFNQEGITISFLPTGAAEQFMQL--------DNQSLRVLLTGGDKLK-KIERKGYKLVNN----YGP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 427 TwwmteTGGIVISHAPglylvPMKPGTN---GPPLPGFEVDVVDENGNPAPPGVKGYLVIKKPwpGMLHGIWGDPERYIK 503
Cdd:cd17645 244 T-----ENTVVATSFE-----IDKPYANipiGKPIDNTRVYILDEALQLQPIGVAGELCIAGE--GLARGYLNRPELTAE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 504 TYWSR--FPG--MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAF 579
Cdd:cd17645 312 KFIVHpfVPGerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAY 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 20137268 580 VVLKQGVAPsdelrKELREHVRRTIGPIAEPAqiFFVT--KLPKTRSGKIMRRLL 632
Cdd:cd17645 392 VTAPEEIPH-----EELREWLKNDLPDYMIPT--YFVHlkALPLTANGKVDRKAL 439
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
274-639 |
2.16e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.52 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 274 SFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVfDIRDDDIFWCTA----DIG-WvtghsYVVLGPLLMGATEVIYEGA 348
Cdd:PRK05691 3872 AYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYL-ALSEADVIAQTAsqsfDISvW-----QFLAAPLFGARVEIVPNAI 3945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 349 PDYPQPdrWWSIIERYGVTIFYTSPTAIRMFMryGEEwprKHDLSTLRIIHSVGEPINPE-AWRWAYRVLGNekvafgst 427
Cdd:PRK05691 3946 AHDPQG--LLAHVQAQGITVLESVPSLIQGML--AED---RQALDGLRWMLPTGEAMPPElARQWLQRYPQI-------- 4010
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 428 wwmtetgGIVISHAPG-------LYLVPMKpGTNGPPLP-GFEVD-----VVDENGNPAPPGVKGYLVIKKPwpGMLHGI 494
Cdd:PRK05691 4011 -------GLVNAYGPAecsddvaFFRVDLA-STRGSYLPiGSPTDnnrlyLLDEALELVPLGAVGELCVAGT--GVGRGY 4080
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 495 WGDPERYIKTYWSR---FPG--MFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAvVGVPD 569
Cdd:PRK05691 4081 VGDPLRTALAFVPHpfgAPGerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQE 4159
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 570 AIKGEVPIAFVVLKQGVAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKTRSGKIMRRLLKAVATGA 639
Cdd:PRK05691 4160 GVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQ 4229
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
119-633 |
7.70e-14 |
|
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: 74.39 E-value: 7.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:cd05937 4 KTWTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 tadgfwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepVESEHPSFILY 278
Cdd:cd05937 84 ---------------------------------------------------------------------VDPDDPAILIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 279 TSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDDIFWC-------TADIGWVT---GHSYVVLGP-----------LL 337
Cdd:cd05937 95 TSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCmplyhgtAAFLGACNclmSGGTLALSRkfsasqfwkdvRD 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 338 MGATEVIYEG--------APDYP---------------QPDRWWSIIERYGVTI---FYTSPTAIRMFMRYGeewprKHD 391
Cdd:cd05937 175 SGATIIQYVGelcryllsTPPSPydrdhkvrvawgnglRPDIWERFRERFNVPEigeFYAATEGVFALTNHN-----VGD 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 392 LSTLRIIHSvgEPInpeaWRWayrVLGNekvafgstwwmtetggivishapGLYLVPMKPGTNGP---PLPGFEVDvvde 468
Cdd:cd05937 250 FGAGAIGHH--GLI----RRW---KFEN-----------------------QVVLVKMDPETDDPirdPKTGFCVR---- 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 469 ngnpAPPGVKGYLVIKKP------WPGMLHGIWGDPERYIKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGH 542
Cdd:cd05937 294 ----APVGEPGEMLGRVPfknreaFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSE 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 543 RLGTYELESALISHPAVAESAVVGV--PDAiKGEVPIAFVVLKQGVAPSDELRK-ELREHVRRTIGPIAEPAQIFFVTKL 619
Cdd:cd05937 370 NVSTTEVADVLGAHPDIAEANVYGVkvPGH-DGRAGCAAITLEESSAVPTEFTKsLLASLARKNLPSYAVPLFLRLTEEV 448
|
570
....*....|....
gi 20137268 620 PKTRSGKIMRRLLK 633
Cdd:cd05937 449 ATTDNHKQQKGVLR 462
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
112-629 |
1.62e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 74.43 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 112 NGYPTDRRKLTYYDLYREVNRVAYMLKQNFGVkkGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSA-----DALA 186
Cdd:PRK05691 32 ADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESArrhhqERLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 187 ERINDSQSRIVITADGFwrRGRVVRLKEVVDAALEKATGVESvivlprlglkdvpmtegrdywwnklMQGIPPNAYIEPE 266
Cdd:PRK05691 110 SIIADAEPRLLLTVADL--RDSLLQMEELAAANAPELLCVDT-------------------------LDPALAEAWQEPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 267 pVESEHPSFILYTSGTTGKPKGIVHDTGGW-AVHVYATMKWVFDIRDDDIF--WCTA--DIGWVTGhsyvVLGPLLMGAT 341
Cdd:PRK05691 163 -LQPDDIAFLQYTSGSTALPKGVQVSHGNLvANEQLIRHGFGIDLNPDDVIvsWLPLyhDMGLIGG----LLQPIFSGVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 342 EVIYegAPDY--PQPDRWWSIIERYGVTIFYTSPTAIRMFM-RYGEEWPRKHDLSTLRIIHSVGEPINP---EAWRWAYR 415
Cdd:PRK05691 238 CVLM--SPAYflERPLRWLEAISEYGGTISGGPDFAYRLCSeRVSESALERLDLSRWRVAYSGSEPIRQdslERFAEKFA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 416 VLGNEKVAFGSTWWMTE-----TGGIVISHAPGLYLVP-------MKPGTnGPPL-------PGFEVDVVDengnPAPPG 476
Cdd:PRK05691 316 ACGFDPDSFFASYGLAEatlfvSGGRRGQGIPALELDAealarnrAEPGT-GSVLmscgrsqPGHAVLIVD----PQSLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 477 VKGYLVIKKPW---PGMLHGIWGDPERYIKTY-------WSRfpgmfyAGDYAIKdKDGYIWVLGRADEVIKVAGHRLGT 546
Cdd:PRK05691 391 VLGDNRVGEIWasgPSIAHGYWRNPEASAKTFvehdgrtWLR------TGDLGFL-RDGELFVTGRLKDMLIVRGHNLYP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 547 YELESALISHPAVAES---AVVGVPDAIKGEVPIAFVVLK--QGVAPSDELRKELREHVrrtigpiAE-----PAQIFFV 616
Cdd:PRK05691 464 QDIEKTVEREVEVVRKgrvAAFAVNHQGEEGIGIAAEISRsvQKILPPQALIKSIRQAV-------AEacqeaPSVVLLL 536
|
570
....*....|....*
gi 20137268 617 T--KLPKTRSGKIMR 629
Cdd:PRK05691 537 NpgALPKTSSGKLQR 551
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
121-599 |
2.07e-13 |
|
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: 73.02 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLKqNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITa 200
Cdd:cd17639 6 MSYAEVWERVLNFGRGLV-ELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFT- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 201 DGfwrrgrvvrlkevvdaalekatgvesvivlprlglkdvpmtegrdywwnklmqgippnayiepepvESEHPSFILYTS 280
Cdd:cd17639 84 DG------------------------------------------------------------------KPDDLACIMYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 281 GTTGKPKGIVHDTGGWAVHVYATMKWVFD-IRDDD----------IFWCTAD---------IGW-----VTGHSY----- 330
Cdd:cd17639 98 GSTGNPKGVMLTHGNLVAGIAGLGDRVPElLGPDDrylaylplahIFELAAEnvclyrggtIGYgsprtLTDKSKrgckg 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 331 --VVLGPLLMGAT----EVIYEGAPD-YPQPdrwwSIIERygvTIFYTSPTAIRMFMRYGEEWP----------RKHDLS 393
Cdd:cd17639 178 dlTEFKPTLMVGVpaiwDTIRKGVLAkLNPM----GGLKR---TLFWTAYQSKLKALKEGPGTPlldelvfkkvRAALGG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 394 TLRIIHSVGEPINPEAWRWAYRVLGnekvAFGSTWWMTETGGIVISHAPGlylvPMKPGTNGPPLPGFEVDVVD--ENG- 470
Cdd:cd17639 251 RLRYMLSGGAPLSADTQEFLNIVLC----PVIQGYGLTETCAGGTVQDPG----DLETGRVGPPLPCCEIKLVDweEGGy 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 471 ---NPAPpgvKGYLVIKKPWPGMlhGIWGDPEryiKTYWSRFP-GMFYAGDYAIKDKDGYIWVLGRADEVIKVAghrLGT 546
Cdd:cd17639 323 stdKPPP---RGEILIRGPNVFK--GYYKNPE---KTKEAFDGdGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQ---NGE 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 20137268 547 Y----ELESALISHPAVAESAVVGVPDAIKgevPIAFVVLKQGvapsdELRKELREH 599
Cdd:cd17639 392 YialeKLESIYRSNPLVNNICVYADPDKSY---PVAIVVPNEK-----HLTKLAEKH 440
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
271-629 |
1.16e-12 |
|
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: 70.59 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 271 EHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWV-FDIRDDDIFW--CTADIGWVTGHsyvvLGPLLMGATEVIYEG 347
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTeWKTKDRILSWmpLTHDMGLIAFH----LAPLIAGMNQYLMPT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 348 APDYPQPDRWWSIIERYGVTIFYTSPTAIRMFM-RYGEEWPRKHDLSTLRIIHSVGEPINPE---AWRWAYRVLGNEKVA 423
Cdd:cd05908 182 RLFIRRPILWLKKASEHKATIVSSPNFGYKYFLkTLKPEKANDWDLSSIRMILNGAEPIDYElchEFLDHMSKYGLKRNA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 424 FGSTWWMTE-TGGIVI----SHAPGLYL----------VPMKPGTN---------GPPLPGFEVDVVDENGNPAPPGVKG 479
Cdd:cd05908 262 ILPVYGLAEaSVGASLpkaqSPFKTITLgrrhvthgepEPEVDKKDsecltfvevGKPIDETDIRICDEDNKILPDGYIG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 480 YLVIKKpwPGMLHGIWGDPERYIKTYWSrfPGMFYAGDYAIKdKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAV 559
Cdd:cd05908 342 HIQIRG--KNVTPGYYNNPEATAKVFTD--DGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGV 416
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20137268 560 --AESAVVGVPDA-IKGEVPIAFVVLKQGVAPSDELRKELREHV-RRTIGPIAEpaqIFFVTKLPKTRSGKIMR 629
Cdd:cd05908 417 elGRVVACGVNNSnTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLnKRGGWQINE---VLPIRRIPKTTSGKVKR 487
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
249-637 |
3.31e-12 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 69.25 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 249 WWNKLMQGIPPNAYIEPEPVESEHPSFILY-TSGTTGKPKgivhdtggWAVHVYATMkwvfdirdddifwcTA------- 320
Cdd:PRK07445 97 WGLDQLKLSHPPPLPSQGILPNLETGWIMIpTGGSSGQIR--------FAIHTWETL--------------TAsvqgfqr 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 321 --DIGWVtgHSYVVLgPL-----LMGATEVIYEGAPDYPQPdrwWSIIERY-----GVTIFYTS--PTAIRMFMRYGEEW 386
Cdd:PRK07445 155 yfQLQQV--NSFCVL-PLyhvsgLMQFMRSFLTGGKLVILP---YKRLKSGqelppNPSDFFLSlvPTQLQRLLQLRPQW 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 387 prkhdLSTLRIIHSVGEPinpeAWRWAYRVLGNEKVAFGSTWWMTETGGIVISHAPGLYLVpmkpGTN--GPPLPGFEVD 464
Cdd:PRK07445 229 -----LAQFRTILLGGAP----AWPSLLEQARQLQLRLAPTYGMTETASQIATLKPDDFLA----GNNssGQVLPHAQIT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 465 VVdengnpapPGVKGYLVIKKP------WPGMLhgiwgDPERYIKTywsrfpgmfyaGDYAIKDKDGYIWVLGRADEVIK 538
Cdd:PRK07445 296 IP--------ANQTGNITIQAQslalgyYPQIL-----DSQGIFET-----------DDLGYLDAQGYLHILGRNSQKII 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 539 VAGHRLGTYELESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVaPSDElrkELREHVRRTIGPIAEPAQIFFVTK 618
Cdd:PRK07445 352 TGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPS-ISLE---ELKTAIKDQLSPFKQPKHWIPVPQ 427
|
410
....*....|....*....
gi 20137268 619 LPKTRSGKIMRRLLKAVAT 637
Cdd:PRK07445 428 LPRNPQGKINRQQLQQIAV 446
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
136-626 |
2.52e-11 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 67.04 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 136 MLKQNFGV--------KKGDKITLYLPMVpelpiTMLAAWRIGAITS---VVFSGFSADA--LAERINDSQSRIVITADG 202
Cdd:PRK08043 237 LLKKTLFVgrilekysVEGERIGLMLPNA-----TISAAVIFGASLRrriPAMMNYTAGVkgLTSAITAAEIKTIFTSRQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 203 FWRRGRVVRLKEVVDAA----LEKatgvesvivlprlgLKDVpMTEGRDYW--WNKLMqgiPPNAYIEPEPvesEHPSFI 276
Cdd:PRK08043 312 FLDKGKLWHLPEQLTQVrwvyLED--------------LKDD-VTTADKLWifAHLLM---PRLAQVKQQP---EDAALI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 277 LYTSGTTGKPKGIVHDTGGWAVHVyATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGAtEVIYegapdYPQPDR 356
Cdd:PRK08043 371 LFTSGSEGHPKGVVHSHKSLLANV-EQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGA-EVFL-----YPSPLH 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 357 WWSIIE----RYGVTIFYTSpTAIRMFMRYGEEWprkhDLSTLRiihsvgepinpeawrwaYRVLGNEKVAFGSTWWMTE 432
Cdd:PRK08043 444 YRIVPElvydRNCTVLFGTS-TFLGNYARFANPY----DFARLR-----------------YVVAGAEKLQESTKQLWQD 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 433 TGGI-------VISHAPGLYL-VPM--KPGTNGPPLPGFEVDVVD----ENGN----PAPPGVKGYLVIKKPwpGMLhgi 494
Cdd:PRK08043 502 KFGLrilegygVTECAPVVSInVPMaaKPGTVGRILPGMDARLLSvpgiEQGGrlqlKGPNIMNGYLRVEKP--GVL--- 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 495 wgDPERYIKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGVPDAIKGE 574
Cdd:PRK08043 577 --EVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE 654
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 20137268 575 VPIAFVVlkqgvapSDELRKELREHVRRTIG--PIAEPAQIFFVTKLPKTRSGK 626
Cdd:PRK08043 655 ALVLFTT-------DSELTREKLQQYAREHGvpELAVPRDIRYLKQLPLLGSGK 701
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
119-622 |
3.11e-11 |
|
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: 65.84 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 119 RKLTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVI 198
Cdd:cd05940 2 EALTYAELDAMANRYARWLKS-LGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 199 tadgfwrrgrvvrlkevVDAALekatgvesvivlprlglkdvpmtegrdywwnklmqgippnaYIepepvesehpsfilY 278
Cdd:cd05940 81 -----------------VDAAL-----------------------------------------YI--------------Y 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 279 TSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDDIFWC------TADI-GWVTGhsyvvlgpLLMGATEVIYE--GAP 349
Cdd:cd05940 89 TSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTClplyhsTALIvGWSAC--------LASGATLVIRKkfSAS 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 350 DYpqpdrwWSIIERYGVTIF-YtsptaIRMFMRY-----GEEWPRKHdlsTLRIIhsVGEPINPEAWRWAYRVLGNEKVA 423
Cdd:cd05940 161 NF------WDDIRKYQATIFqY-----IGELCRYllnqpPKPTERKH---KVRMI--FGNGLRPDIWEEFKERFGVPRIA 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 424 --FGSTwwmteTGGIvishapGLYLVPMKPGTNG--PPLPGF-------EVDVvdENGNP----------APPGVKGYLV 482
Cdd:cd05940 225 efYAAT-----EGNS------GFINFFGKPGAIGrnPSLLRKvaplalvKYDL--ESGEPirdaegrcikVPRGEPGLLI 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 483 --IKKPWP------------GMLHGIWGDPERYiktywsrfpgmFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYE 548
Cdd:cd05940 292 srINPLEPfdgytdpaatekKILRDVFKKGDAW-----------FNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTE 360
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20137268 549 LESALISHPAVAESAVVGV--PDAiKGEVPIAFVVLKqgvAPSDELRKELREHVRRTIGPIAEPAQIFFVTKLPKT 622
Cdd:cd05940 361 VAAVLGAFPGVEEANVYGVqvPGT-DGRAGMAAIVLQ---PNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEIT 432
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
258-629 |
1.02e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 64.64 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 258 PPNAYIEPEPVESEHPSFILYTSGTTGKPKGIV--HDTG--GWAVHVYATMKwvfdIRDDD--IFWCT--ADIGWVTghs 329
Cdd:PRK09192 163 LPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIitHRALmaNLRAISHDGLK----VRPGDrcVSWLPfyHDMGLVG--- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 330 yVVLGPLlmgATEViyegAPDY-------PQPDRWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPRKH-DLSTLRIIHSV 401
Cdd:PRK09192 236 -FLLTPV---ATQL----SVDYlptrdfaRRPLQWLDLISRNRGTISYSPPFGYELCARRVNSKDLAElDLSCWRVAGIG 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 402 GEPINPE---AWRWAYRVLGNEKVAFGSTWWMTETGgIVISHAP------------------GLYLVPMKPGT------- 453
Cdd:PRK09192 308 ADMIRPDvlhQFAEAFAPAGFDDKAFMPSYGLAEAT-LAVSFSPlgsgivveevdrdrleyqGKAVAPGAETRrvrtfvn 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 454 NGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKpwPGMLHGIWGDPE--RYIKTywsrfPGMFYAGD--YAIkdkDGYIWV 529
Cdd:PRK09192 387 CGKALPGHEIEIRNEAGMPLPERVVGHICVRG--PSLMSGYFRDEEsqDVLAA-----DGWLDTGDlgYLL---DGYLYI 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 530 LGRADEVIKVAGHRLGTYELESALISHPAV--AESAVVGVPDAiKGEVPiafVVLKQGVAPSDE----LRKELREHVRRT 603
Cdd:PRK09192 457 TGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQE-NGEKI---VLLVQCRISDEErrgqLIHALAALVRSE 532
|
410 420
....*....|....*....|....*...
gi 20137268 604 IGpiaEPAQIFFVT--KLPKTRSGKIMR 629
Cdd:PRK09192 533 FG---VEAAVELVPphSLPRTSSGKLSR 557
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
120-635 |
1.28e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 61.06 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 120 KLTYYDLYREVNRVAYMLKQNfgvKKGDK--ITLYLPMVPELPITMLAAWRIG-AITSVVFSgfSAdalAERINDsqsri 196
Cdd:PRK04813 27 KLTYGQLKEDSDALAAFIDSL---KLPDKspIIVFGHMSPEMLATFLGAVKAGhAYIPVDVS--SP---AERIEM----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 197 vitadgfwrrgrvvrLKEVVDAALEKATGVESVIVL--PRLGLKDVPMtegrdywwnklmQGIPPNAYIEPEPVESEHPS 274
Cdd:PRK04813 94 ---------------IIEVAKPSLIIATEELPLEILgiPVITLDELKD------------IFATGNPYDFDHAVKGDDNY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 275 FILYTSGTTGKPKG--IVHDT----GGWAVHVYATMK---WV------FDIRDDDIFWCTAdigwvTGHSYVVLgpllmg 339
Cdd:PRK04813 147 YIIFTSGTTGKPKGvqISHDNlvsfTNWMLEDFALPEgpqFLnqapysFDLSVMDLYPTLA-----SGGTLVAL------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 340 ATEVIYEgapdypqPDRWWSIIERYGVTIFYTSPTAIRM-----------------FMRYGEEWPRKhDLSTL------- 395
Cdd:PRK04813 216 PKDMTAN-------FKQLFETLPQLPINVWVSTPSFADMclldpsfneehlpnlthFLFCGEELPHK-TAKKLlerfpsa 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 396 RIIHSVGepinPeawrwayrvlgnekvafgstwwmTETGGIVIShapglylVPMKPG--TNGPPLP-GF-----EVDVVD 467
Cdd:PRK04813 288 TIYNTYG----P-----------------------TEATVAVTS-------IEITDEmlDQYKRLPiGYakpdsPLLIID 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 468 ENGNPAPPGVKGYLVIKKpwPGMLHGIWGDPERYIKTYWSrFPGM--FYAGDYAIKDkDGYIWVLGRADEVIKVAGHRLg 545
Cdd:PRK04813 334 EEGTKLPDGEQGEIVISG--PSVSKGYLNNPEKTAEAFFT-FDGQpaYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRI- 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 546 tyELESalISH-----PAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSD-ELRKELREHVRRTIGPIAEPAQIFFVTKL 619
Cdd:PRK04813 409 --ELEE--IEQnlrqsSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREfELTKAIKKELKERLMEYMIPRKFIYRDSL 484
|
570
....*....|....*..
gi 20137268 620 PKTRSGKIMR-RLLKAV 635
Cdd:PRK04813 485 PLTPNGKIDRkALIEEV 501
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
274-627 |
2.17e-09 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 60.18 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 274 SFILYTSGTTGKPKgIVHDTGGWAVHVYATMKWVFDIRDDDIFWCTADIgwVTGHSYV-VLGPLLMGATEVIYEGAPDyP 352
Cdd:cd17654 121 AYVIHTSGTTGTPK-IVAVPHKCILPNIQHFRSLFNITSEDILFLTSPL--TFDPSVVeIFLSLSSGATLLIVPTSVK-V 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 353 QPDRWWSII-ERYGVTIFYTSPTAIRMFmryGEEWPRKHDLS---TLRIIHSVGEPINPEAWRWAYRVLGNEKVAFgSTW 428
Cdd:cd17654 197 LPSKLADILfKRHRITVLQATPTLFRRF---GSQSIKSTVLSatsSLRVLALGGEPFPSLVILSSWRGKGNRTRIF-NIY 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 429 WMTETGGIVIshapgLYLVPMK--PGTNGPPLPGFEVDVVDENGNPAPPGVKGYLVIKKpwpGMLHGIWGDPEryiktyw 506
Cdd:cd17654 273 GITEVSCWAL-----AYKVPEEdsPVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGLNRV---CILDDEVTVPK------- 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 507 srfpGMFYA-GDYaIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVgvpdAIKGEVPIAFVVLKQG 585
Cdd:cd17654 338 ----GTMRAtGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVT----LSDQQRLIAFIVGESS 408
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 20137268 586 vapSDELRKELREHVrrtIGPIAEPAQIFFVTKLPKTRSGKI 627
Cdd:cd17654 409 ---SSRIHKELQLTL---LSSHAIPDTFVQIDKLPLTSHGKV 444
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
121-610 |
1.02e-08 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 58.07 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLKQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITA 200
Cdd:cd05938 6 YTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 201 dgfwrrgrvvrlKEVVDAALEkatgvesviVLPRLGLKDVPM--------TEGRDYWWNKLmQGIPPnayiepEPVESEH 272
Cdd:cd05938 86 ------------PELQEAVEE---------VLPALRADGVSVwylshtsnTEGVISLLDKV-DAASD------EPVPASL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 273 PSFI--------LYTSGTTGKPK-GIVHDTGGWAVhvyATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATEV 343
Cdd:cd05938 138 RAHVtikspalyIYTSGTTGLPKaARISHLRVLQC---SGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 344 IyegAPDYpQPDRWWSIIERYGVTIF-YtsptaIRMFMRYGEEWPRKHDLSTLRIIHSVGEPINPEAWRWAYRVLGNEKV 422
Cdd:cd05938 215 L---KPKF-SASQFWDDCRKHNVTVIqY-----IGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 423 --AFGST----WWMTETGGI-VISHAPGLY-------LVPMKPGTNGPplpgfevdVVDENGN--PAPPGVKGYLVIKKP 486
Cdd:cd05938 286 reFYGSTegniGFFNYTGKIgAVGRVSYLYkllfpfeLIKFDVEKEEP--------VRDAQGFciPVAKGEPGLLVAKIT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 487 WPGMLHGIWGDPE----RYIKTYWSRFPGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAES 562
Cdd:cd05938 358 QQSPFLGYAGDKEqtekKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEV 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 20137268 563 AVVGVP-DAIKGEVPIAFVVLKqgvaPSDELR-KELREHVRRTIGPIAEP 610
Cdd:cd05938 438 NVYGVTvPGHEGRIGMAAVKLK----PGHEFDgKKLYQHVREYLPAYARP 483
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
78-310 |
1.19e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 58.06 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 78 GGRLNLSYLAVDRHVKTWRK--NKLAIEWEgepvdeNGYPTDRRKLTYYDLYREVnrvaymlkQNF-------GVKKGDK 148
Cdd:PTZ00216 83 GDRRALAYRPVERVEKEVVKdaDGKERTME------VTHFNETRYITYAELWERI--------VNFgrglaelGLTKGSN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 149 ITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVITadgfwrRGRVVrlKEVVDAALEKATGVES 228
Cdd:PTZ00216 149 VAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC------NGKNV--PNLLRLMKSGGMPNTT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 229 VIVLPRLGLkDVPMTEGRDYWWNKLMQ--GIPPNAYIEPEPVESEHPSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKW 306
Cdd:PTZ00216 221 IIYLDSLPA-SVDTEGCRLVAWTDVVAkgHSAGSHHPLNIPENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDR 299
|
....
gi 20137268 307 VFDI 310
Cdd:PTZ00216 300 LNDL 303
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
266-631 |
3.12e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 56.70 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 266 EPVESEHPSFILYTSGTTGKPKGIVHDTGGwavhVYATMKWVFDIRDDDifwCTADIG--WVTGHSYVVLGPLLMGAtev 343
Cdd:PRK05851 147 TPPDSGGPAVLQGTAGSTGTPRTAILSPGA----VLSNLRGLNARVGLD---AATDVGcsWLPLYHDMGLAFLLTAA--- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 344 iYEGAPDYPQPD--------RWWSIIERYGVTIFYTSPTAIRMFMRYGEEWPrKHDLSTLRIIHSVGEPINPEAwrwaYR 415
Cdd:PRK05851 217 -LAGAPLWLAPTtafsaspfRWLSWLSDSRATLTAAPNFAYNLIGKYARRVS-DVDLGALRVALNGGEPVDCDG----FE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 416 VLGNEKVAFG-------STWWMTETGGIVISHAPGLYL----VPMKPGTN-------GPPLPGFEVDVVDENGnPAPPGV 477
Cdd:PRK05851 291 RFATAMAPFGfdagaaaPSYGLAESTCAVTVPVPGIGLrvdeVTTDDGSGarrhavlGNPIPGMEVRISPGDG-AAGVAG 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 478 KGYLVIKKPWPGMLHGIWG----DPERYIKTywsrfpgmfyaGDYAIKDKDGYIwVLGRADEVIKVAGHRLGTYELESAL 553
Cdd:PRK05851 370 REIGEIEIRGASMMSGYLGqapiDPDDWFPT-----------GDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVA 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 554 ISHPAVAESAVVGVPDAIKGEVPIAFVVLKQGVAPSDELRKELREHVRRTIGPIaePAQIFFVT--KLPKTRSGKiMRRL 631
Cdd:PRK05851 438 AQVRGVREGAVVAVGTGEGSARPGLVIAAEFRGPDEAGARSEVVQRVASECGVV--PSDVVFVApgSLPRTSSGK-LRRL 514
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
279-605 |
1.72e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 50.92 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 279 TSGTTGKPKGIV---HDTGGWAVHVYATMKWVfDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATeVIYEGApdyPQPD 355
Cdd:COG1541 91 SSGTTGKPTVVGytrKDLDRWAELFARSLRAA-GVRPGDRVQNAFGYGLFTGGLGLHYGAERLGAT-VIPAGG---GNTE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 356 RWWSIIERYGVTIFYTSPT-AIRMfMRYGEEwpRKHDLSTLRI---IHSvGEPInPEAWR------WAYRVLgnekvafg 425
Cdd:COG1541 166 RQLRLMQDFGPTVLVGTPSyLLYL-AEVAEE--EGIDPRDLSLkkgIFG-GEPW-SEEMRkeieerWGIKAY-------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 426 STWWMTETG-GIVI--SHAPGLYLvpmkpgtngpplpgFE----VDVVD-ENGNPAPPGVKGYLVI----KKPWPgMLhg 493
Cdd:COG1541 233 DIYGLTEVGpGVAYecEAQDGLHI--------------WEdhflVEIIDpETGEPVPEGEEGELVVttltKEAMP-LI-- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 494 iwgdpeRYiKTywsrfpgmfyaGDYA---------------IKdkdgyiWVLGRADEVIKVAGHRLGTYELESALISHPA 558
Cdd:COG1541 296 ------RY-RT-----------GDLTrllpepcpcgrthprIG------RILGRADDMLIIRGVNVFPSQIEEVLLRIPE 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 20137268 559 VAESAVVGVPDAIKGEVPIAFVVLKQGvAPSDELRKELREHVRRTIG 605
Cdd:COG1541 352 VGPEYQIVVDREGGLDELTVRVELAPG-ASLEALAEAIAAALKAVLG 397
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
107-311 |
9.44e-06 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 48.61 E-value: 9.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 107 EPV-DENGYPTDRRKL------TYYDLYREVNRVAYMLKQNFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSG 179
Cdd:cd17632 47 ELVtDPATGRTTLRLLprfetiTYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 180 FSADALAERINDSQSRIvITADgfwrrgrvvrlKEVVDAALE---KATGVESVIVL---------------PRLGLKDVP 241
Cdd:cd17632 127 ASAAQLAPILAETEPRL-LAVS-----------AEHLDLAVEavlEGGTPPRLVVFdhrpevdahraalesARERLAAVG 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 242 MTEGRDYWWNKLMQGIPPNAYIEPEPvESEHPSFILYTSGTTGKPKGIVHdTGGWAVHVYATMKWVFDIR 311
Cdd:cd17632 195 IPVTTLTLIAVRGRDLPPAPLFRPEP-DDDPLALLIYTSGSTGTPKGAMY-TERLVATFWLKVSSIQDIR 262
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
120-299 |
2.09e-05 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 47.74 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 120 KLTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRIGAITSVVFSGFSADALAERINDSQSRIVit 199
Cdd:cd05933 8 TLTYKEYYEACRQAAKAFLK-LGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANIL-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 200 adgfwrrgrvvrlkeVVDAA--LEKATGVESVivLPRLglKDV-----PMTEGRD--YWWNKLMQ---GIPPNAYIEPEp 267
Cdd:cd05933 85 ---------------VVENQkqLQKILQIQDK--LPHL--KAIiqykePLKEKEPnlYSWDEFMElgrSIPDEQLDAII- 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 20137268 268 vESEHPS---FILYTSGTTGKPKGIV--HDTGGWAVH 299
Cdd:cd05933 145 -SSQKPNqccTLIYTSGTTGMPKGVMlsHDNITWTAK 180
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
121-316 |
4.04e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 47.03 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 121 LTYYDLYREVNRVAYMLKQnFGVKKGDKITLYLPMVPELPITMLAAWRiGAITSV-VFSGFSADALAERINDSQSRIVIT 199
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVA-LGHNKEERVAIFADTRAEWLIALQGCFR-QNITVVtIYASLGEEALCHSLNETEVTTVIC 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 200 ADGfwrrgrvvRLKEVVDAAlEKATGVESVIVLPRLGLKDVPMTEGRDYWW-------NKLMQGIPpnayIEPEPVESEH 272
Cdd:PLN02387 185 DSK--------QLKKLIDIS-SQLETVKRVIYMDDEGVDSDSSLSGSSNWTvssfsevEKLGKENP----VDPDLPSPND 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 20137268 273 PSFILYTSGTTGKPKGIVHDTGGWAVHVYATMKWVFDIRDDDIF 316
Cdd:PLN02387 252 IAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVY 295
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
92-290 |
8.73e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 45.86 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 92 VKTWRKNKlaieWEGEPVDENGYPTDRRKLTYYDLYREVNRVAYMLKQNfGVKKGDKITLYLPMVPELPITMLAAWRIGA 171
Cdd:PLN02736 54 VETFRDYK----YLGTRIRVDGTVGEYKWMTYGEAGTARTAIGSGLVQH-GIPKGACVGLYFINRPEWLIVDHACSAYSY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 172 ITSVVFSGFSADALAERINDSQ-SRIVITAD------GFWRRGRVVRLKEVVDAA------LEKATGVEsVIVLPRLglk 238
Cdd:PLN02736 129 VSVPLYDTLGPDAVKFIVNHAEvAAIFCVPQtlntllSCLSEIPSVRLIVVVGGAdeplpsLPSGTGVE-IVTYSKL--- 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 20137268 239 dvpMTEGRdywwnklmqgIPPNAYIEPEPvesEHPSFILYTSGTTGKPKGIV 290
Cdd:PLN02736 205 ---LAQGR----------SSPQPFRPPKP---EDVATICYTSGTTGTPKGVV 240
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
493-627 |
1.17e-04 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 45.20 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 493 GIWGDPERYIKTYWSRF-----PGMFYAGDYAIKDKDGYIWVLGRADEVIKVAGHRLGTYELESALISHPAVAESAVVGV 567
Cdd:cd17647 349 DHWNYLDKDNNEPWRQFwlgprDRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 568 PDAIKGEVPIAFVV----------LKQGVAPSD--------------ELRKELREHVRRTIGPIAEPAQIFFVTKLPKTR 623
Cdd:cd17647 429 RDKDEEPTLVSYIVprfdkpddesFAQEDVPKEvstdpivkgligyrKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNP 508
|
....
gi 20137268 624 SGKI 627
Cdd:cd17647 509 NGKV 512
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
549-636 |
8.55e-04 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 42.06 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 549 LESALISHPAVAESAVVGVPDAIKGEVPIAFVVLKQgvaPSDElrKELREHVRRTIGPIAePAQIFFVTKLPKTRSGKIM 628
Cdd:PRK09188 245 IQAALKSDPAVSDVAIALFSLPAKGVGLYAFVEAEL---PADE--KSLRARLAGAKPPKP-PEHIQPVAALPRDADGTVR 318
|
....*...
gi 20137268 629 RRLLKAVA 636
Cdd:PRK09188 319 DDILRLIA 326
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
279-633 |
1.01e-03 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 42.23 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 279 TSGTTGKPKGIVHDTGGWAV--HVYATMKWVFDIRDDDIFWCTADIGWVTGHSYVVLGPLLMGATeVIYEGApdyPQPDR 356
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDLDVwaELVARCLDAAGVTPGDRVQNAYGYGLFTGGLGFHYGAERLGAL-VIPAGG---GNTER 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 357 WWSIIERYGVTIFYTSPT----AIRMFMRYGEEwPRKHDLSTLrIIHSvgepinpEAWRWAYR----VLGNEKvAFGSTw 428
Cdd:cd05913 162 QLQLIKDFGPTVLCCTPSyalyLAEEAEEEGID-PRELSLKVG-IFGA-------EPWTEEMRkrieRRLGIK-AYDIY- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 429 WMTETGGivishaPGlylVPMK-PGTNGPPL--PGFEVDVVD-ENGNPAPPGVKGYLVI----KKPWP------GMLHGI 494
Cdd:cd05913 231 GLTEIIG------PG---VAFEcEEKDGLHIweDHFIPEIIDpETGEPVPPGEVGELVFttltKEAMPliryrtRDITRL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137268 495 WGDPERYIKTYwsrfpgMFYAGdyaikdkdgyiwVLGRADEVIKVAGHRLGTYELESALISHPAVAESA--VVGVPDA-- 570
Cdd:cd05913 302 LPGPCPCGRTH------RRIDR------------ITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYqlILTRQEHld 363
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20137268 571 ---IKGEVPIAFVvlkqGVAPSDELRKELREHVRRTIGPIAEpaqIFFVTKLPKTRSGKIMRRLLK 633
Cdd:cd05913 364 eltIKVEVRPEAD----DDEKLEALKQRLERHIKSVLGVTVE---VELVEPGSLPRSEGKAKRVID 422
|
|
| |
