|
Name |
Accession |
Description |
Interval |
E-value |
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
22-632 |
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: 1123.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 22 MKSLGYEDYEIFYNKSIEETAWFWGEAEKAVGYQWMKPYTEVLDLENGTPFAQWYNGGTCNVVESALSRWLADEETriQP 101
Cdd:cd05968 1 MASLGIPDLEAFLERSAEDNAWFWGEFVKDVGIEWYEPPYQTLDLSGGKPWAAWFVGGRMNIVEQLLDKWLADTRT--RP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 102 ALQYEGENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTR 181
Cdd:cd05968 79 ALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 182 VQAAGSKMIITADGFSRRGKIVSLKDEVDKACEHCPTVEKVVIVRHAGNDFTPHNYDFSWSTLEKEKPFIHAEEMQSDDP 261
Cdd:cd05968 159 LQDAEAKALITADGFTRRGREVNLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSYDEEKETAGDGAERTESEDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 262 LMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGVPDFPEA 341
Cdd:cd05968 239 LMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDGAPDHPKA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 342 DRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKGNVPICNYSGGTEIS 421
Cdd:cd05968 319 DRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEIS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 422 GGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGKPIRDEVGELCLEKPWVGMTKSFWEDDERYVNTYWSRFENKWVHGDW 501
Cdd:cd05968 399 GGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPARPEVGELVLLAPWPGMTRGFWRDEDRYLETYWSRFDNVWVHGDF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 502 VIYD-GEQYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGELKKELMS 580
Cdd:cd05968 479 AYYDeEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELME 558
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 446729146 581 LVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELGDLSSLVNP 632
Cdd:cd05968 559 RVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKELGDLSSLENP 610
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
74-639 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 729.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 74 QWYNGGTCNVVESALSRWLADEETRiqPALQYEGENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETV 153
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGRGDK--VALIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 154 VAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRRGKIVSLKDEVDKACEHCPTVEKVVIVRHAGNDFT 233
Cdd:COG0365 79 IAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPSLEHVIVVGRTGADVP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 234 PHNyDFSWSTL-EKEKPFIHAEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDMGW 312
Cdd:COG0365 159 MEG-DLDWDELlAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 313 MMG-PFLLFGSLINGATMVMYEGVPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEP 391
Cdd:COG0365 238 ATGhSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 392 WNPDPWMWLFETVGkgnVPICNYSGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGKPIRD-EVGELCLEKPW 470
Cdd:COG0365 318 LNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPgEEGELVIKGPW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 471 VGMTKSFWEDDERYVNTYWSRFENKWVHGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGV 549
Cdd:COG0365 395 PGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFwILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 550 PDEVKGEVCHCFVVLRDHVTFTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELGDLSSL 629
Cdd:COG0365 475 PDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRPLGDTSTL 554
|
570
....*....|
gi 446729146 630 VNPEVVPFIQ 639
Cdd:COG0365 555 EDPEALDEIK 564
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
28-631 |
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: 652.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 28 EDYEIFYNKSIEETAWFWGEAEKAVgyQWMKPYTEVLDLENGTPFAQWYNGGTCNVVESALSRWLadEETRIQPALQYEG 107
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKEL--DWFKPWDKVLDWSKGPPFIKWFEGGKLNISYNCLDRHL--KERGDKVAIIWEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 108 ENGT-SKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAG 186
Cdd:cd05966 77 DEPDqSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 187 SKMIITADGFSRRGKIVSLKDEVDKACEHCPTVEKVVIVRHAGNDFTPHN-YDFSWSTL-EKEKPFIHAEEMQSDDPLML 264
Cdd:cd05966 157 CKLVITADGGYRGGKVIPLKEIVDEALEKCPSVEKVLVVKRTGGEVPMTEgRDLWWHDLmAKQSPECEPEWMDSEDPLFI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 265 IYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDrVLWVT-DMGWMMG-PFLLFGSLINGATMVMYEGVPDFPEAD 342
Cdd:cd05966 237 LYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDD-IYWCTaDIGWITGhSYIVYGPLANGATTVMFEGTPTYPDPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 343 RLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKGNVPICNYSGGTEiSG 422
Cdd:cd05966 316 RYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIVDTWWQTE-TG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 423 GIfgnvLIKPIA------PISFNASLPGMAAVVLDDQGKPIRDEV-GELCLEKPWVGMTKSFWEDDERYVNTYWSRFENK 495
Cdd:cd05966 395 GI----MITPLPgatplkPGSATRPFFGIEPAILDEEGNEVEGEVeGYLVIKRPWPGMARTIYGDHERYEDTYFSKFPGY 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 496 WVHGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGEL 574
Cdd:cd05966 471 YFTGDGARRDEDGYYwITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDEL 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 446729146 575 KKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLG-KELGDLSSLVN 631
Cdd:cd05966 551 RKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGeEELGDTSTLAD 608
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
28-635 |
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: 630.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 28 EDYEIFYNKSIEETAWFWGEAEKAVgYQWMKPYTEVLDlENGTPFAQWYNGGTCNVVESALSRWLADEETRIqpALQYEG 107
Cdd:TIGR02188 5 EQYKELYEESIEDPDKFWAKLAREL-LDWFKPFTKVLD-WSFPPFYKWFVGGELNVSYNCVDRHLEARPDKV--AIIWEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 108 EN-GTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAG 186
Cdd:TIGR02188 81 DEpGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 187 SKMIITADGFSRRGKIVSLKDEVDKACEHCP-TVEKVVIVRHAGNDFTP--HNYDFSWSTL-EKEKPFIHAEEMQSDDPL 262
Cdd:TIGR02188 161 AKLVITADEGLRGGKVIPLKAIVDEALEKCPvSVEHVLVVRRTGNPVVPwvEGRDVWWHDLmAKASAYCEPEPMDSEDPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 263 MLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDrVLWVT-DMGWMMG-PFLLFGSLINGATMVMYEGVPDFPE 340
Cdd:TIGR02188 241 FILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGD-IFWCTaDVGWITGhSYIVYGPLANGATTVMFEGVPTYPD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 341 ADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKGNVPICNYSGGTEi 420
Cdd:TIGR02188 320 PGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKERCPIVDTWWQTE- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 421 SGGIfgnvLIKPIA------PISFNASLPGMAAVVLDDQGKPIR--DEVGELCLEKPWVGMTKSFWEDDERYVNTYWSRF 492
Cdd:TIGR02188 399 TGGI----MITPLPgatptkPGSATLPFFGIEPAVVDEEGNPVEgpGEGGYLVIKQPWPGMLRTIYGDHERFVDTYFSPF 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 493 ENKWVHGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFT 571
Cdd:TIGR02188 475 PGYYFTGDGARRDKDGYIwITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPD 554
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446729146 572 GELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKE--LGDLSSLVNPEVV 635
Cdd:TIGR02188 555 DELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAeiLGDTSTLEDPSVV 620
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
8-645 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 622.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 8 PTEEYKEKTRLygwmkslGYEDYEIFYNKSIEETAWFWGEAEKAVgyQWMKPYTEVLDLENgtPFAQWYNGGTCNVVESA 87
Cdd:PRK00174 4 PPAEFAANALI-------DMEQYKALYQESVEDPEGFWAEQAKRL--DWFKPFDTVLDWNA--PFIKWFEDGELNVSYNC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 88 LSRWLadEETRIQPALQYEGEN-GTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAII 166
Cdd:PRK00174 73 LDRHL--KTRGDKVAIIWEGDDpGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 167 SPIFSGFASDAVMTRVQAAGSKMIITADGFSRRGKIVSLKDEVDKACEHCPTVEKVVIVRHAGND--FTPHNyDFSWSTL 244
Cdd:PRK00174 151 SVVFGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCPSVEKVIVVRRTGGDvdWVEGR-DLWWHEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 245 -EKEKPFIHAEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAA------FDagfgmnIKQGDrVLWVT-DMGWMMG- 315
Cdd:PRK00174 230 vAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAmtmkyvFD------YKDGD-VYWCTaDVGWVTGh 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 316 PFLLFGSLINGATMVMYEGVPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPD 395
Cdd:PRK00174 303 SYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGSVGEPINPE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 396 PWMWLFETVGKGNVPICNYSGGTEiSGGIfgnvLIKPIA------PISFNASLPGMAAVVLDDQGKPIRDEV-GELCLEK 468
Cdd:PRK00174 383 AWEWYYKVVGGERCPIVDTWWQTE-TGGI----MITPLPgatplkPGSATRPLPGIQPAVVDEEGNPLEGGEgGNLVIKD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 469 PWVGMTKSFWEDDERYVNTYWSRFENKWVHGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAI 547
Cdd:PRK00174 458 PWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYwITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVV 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 548 GVPDEVKGEVCHCFVVLRDHVTFTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKE-LGDL 626
Cdd:PRK00174 538 GRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEEiLGDT 617
|
650 660
....*....|....*....|
gi 446729146 627 SSLVNPEVVP-FIQGLQSSK 645
Cdd:PRK00174 618 STLADPSVVEkLIEARQNRK 637
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
30-610 |
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: 612.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 30 YEIFYNKSIEETAWFWGEAEKAVGYQWMKPYTEVLDLENGTPFAQWYNGGTCNVVESALSRWLADEETRIqpALQYEGEN 109
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQKVKNTSFAPGAPSIKWFEDATLNLAANALDRHLRENGDRT--AIIYEGDD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 110 GT-SKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSK 188
Cdd:cd17634 79 TSqSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 189 MIITADGFSRRGKIVSLKDEVDKACE-HCPTVEKVVIVRHAGNDF--TPhNYDFSWSTL-EKEKPFIHAEEMQSDDPLML 264
Cdd:cd17634 159 LLITADGGVRAGRSVPLKKNVDDALNpNVTSVEHVIVLKRTGSDIdwQE-GRDLWWRDLiAKASPEHQPEAMNAEDPLFI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 265 IYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDMGWMMG-PFLLFGSLINGATMVMYEGVPDFPEADR 343
Cdd:cd17634 238 LYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLLYEGVPNWPTPAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 344 LWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKGNVPICNYSGGTEISGG 423
Cdd:cd17634 318 MWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDTWWQTETGGF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 424 IFGN--VLIKPIAPISFNAsLPGMAAVVLDDQGKPIR-DEVGELCLEKPWVGMTKSFWEDDERYVNTYWSRFENKWVHGD 500
Cdd:cd17634 398 MITPlpGAIELKAGSATRP-VFGVQPAVVDNEGHPQPgGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTFKGMYFSGD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 501 WVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGELKKELM 579
Cdd:cd17634 477 GARRDEDGYYwITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELR 556
|
570 580 590
....*....|....*....|....*....|.
gi 446729146 580 SLVNSHIGKALCPKDIHVVEDLPKTRNSKVM 610
Cdd:cd17634 557 NWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
30-638 |
1.15e-153 |
|
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: 456.78 E-value: 1.15e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 30 YEIFYNKSIEETAWFWGEAekAVGYQWMKPYTEVLDLENGtPFAQWYNGGTCNVVESALSRWlADEETRIQPALQYE-GE 108
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQ--ARLIDWFKPPEKILDNSNP-PFTRWFVGGRLNTCYNALDRH-VEAGRGDQIALIYDsPV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 109 NGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSK 188
Cdd:cd05967 77 TGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 189 MIITADGFSRRGKIVSLKDEVDKACEHCPTVEKVVIVRHAGN---DFTPHNYDFSWSTLEKEKPFIHAEEMQSDDPLMLI 265
Cdd:cd05967 157 LIVTASCGIEPGKVVPYKPLLDKALELSGHKPHHVLVLNRPQvpaDLTKPGRDLDWSELLAKAEPVDCVPVAATDPLYIL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 266 YTSGTTGKPKGTVHTHAGF--PLKAAFDAGFGMniKQGDrVLWVT-DMGWMMG-PFLLFGSLINGATMVMYEGVPDF-PE 340
Cdd:cd05967 237 YTSGTTGKPKGVVRDNGGHavALNWSMRNIYGI--KPGD-VWWAAsDVGWVVGhSYIVYGPLLHGATTVLYEGKPVGtPD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 341 ADRLWETVDKYEITHLGISPTLIRALmAKGD---EYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGkgnVPICNYSGG 417
Cdd:cd05967 314 PGAFWRVIEKYQVNALFTAPTAIRAI-RKEDpdgKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG---VPVIDHWWQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 418 TEISGGIFGN---VLIKPIAPISFNASLPGMAAVVLDDQGKPIR-DEVGELCLEKPWV-GMTKSFWEDDERYVNTYWSRF 492
Cdd:cd05967 390 TETGWPITANpvgLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGpNELGNIVIKLPLPpGCLLTLWKNDERFKKLYLSKF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 493 ENKWVHGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFT 571
Cdd:cd05967 470 PGYYDTGDAGYKDEDGYLfIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKIT 549
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446729146 572 GE-LKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELGDLSSLVNPEVVPFI 638
Cdd:cd05967 550 AEeLEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDYTIPSTIEDPSVLDEI 617
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
28-635 |
6.45e-139 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 420.84 E-value: 6.45e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 28 EDYEIFYNKSIEETAWFWgeAEKAVGYQWMKPY------TEVLDLENGTPFAQWYNGGTCNVVESALSRWL-ADEETRIq 100
Cdd:PLN02654 30 QQYMEMYKRSVDDPAGFW--SDIASQFYWKQKWegdevcSENLDVRKGPISIEWFKGGKTNICYNCLDRNVeAGNGDKI- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 pALQYEG-ENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM 179
Cdd:PLN02654 107 -AIYWEGnEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 180 TRVQAAGSKMIITADGFSRRGKIVSLKDEVDKACEH----------CPTVEKVVIVRHAGNDFTPHNyDFSWSTLEKEKP 249
Cdd:PLN02654 186 QRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDEsakngvsvgiCLTYENQLAMKREDTKWQEGR-DVWWQDVVPNYP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 250 F-IHAEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDrVLWVT-DMGWMMG-PFLLFGSLING 326
Cdd:PLN02654 265 TkCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTD-VYWCTaDCGWITGhSYVTYGPMLNG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 327 ATMVMYEGVPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGK 406
Cdd:PLN02654 344 ATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 407 GNVPICNYSGGTEiSGGIFGNVL--IKPIAPISfnASLP--GMAAVVLDDQGKPIRDEV-GELCLEKPWVGMTKSFWEDD 481
Cdd:PLN02654 424 SRCPISDTWWQTE-TGGFMITPLpgAWPQKPGS--ATFPffGVQPVIVDEKGKEIEGECsGYLCVKKSWPGAFRTLYGDH 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 482 ERYVNTYWSRFENKWVHGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHC 560
Cdd:PLN02654 501 ERYETTYFKPFAGYYFSGDGCSRDKDGYYwLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYA 580
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446729146 561 FVVLRDHVTFTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK--AAYLGKELGDLSSLVNPEVV 635
Cdd:PLN02654 581 FVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRkiASRQLDELGDTSTLADPGVV 657
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
28-632 |
1.25e-138 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 418.58 E-value: 1.25e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 28 EDYEIFYNKSIEETAWFWGEAEKAVgyQWMKPYTEVLDLENgTPFAQWYNGGTCNVVESALSRWLADEETriQPALQY-E 106
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRI--DWQTPFTQVLDYSN-PPFARWFVGGRTNLCHNAVDRHLAKRPE--QLALIAvS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 107 GENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAG 186
Cdd:PRK10524 77 TETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 187 SKMIITADGFSRRGKIVSLKDEVDKAC---EHCPtvEKVVIV-RHAGNDFTPHNYDFSWSTLEKekpfIHAEE------M 256
Cdd:PRK10524 157 PVLIVSADAGSRGGKVVPYKPLLDEAIalaQHKP--RHVLLVdRGLAPMARVAGRDVDYATLRA----QHLGArvpvewL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 257 QSDDPLMLIYTSGTTGKPKGTVHTHAGF--PLKAAFDAGFGMniKQGDRVLWVTDMGWMMG-PFLLFGSLINGATMVMYE 333
Cdd:PRK10524 231 ESNEPSYILYTSGTTGKPKGVQRDTGGYavALATSMDTIFGG--KAGETFFCASDIGWVVGhSYIVYAPLLAGMATIMYE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 334 GVPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKgnvPIC- 412
Cdd:PRK10524 309 GLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGV---PVId 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 413 NY----SGGTEISggIFGNVLIKPIAPISFNASLPGMAAVVLDDQ-GKPIR-DEVGELCLEKPW-VGMTKSFWEDDERYV 485
Cdd:PRK10524 386 NYwqteTGWPILA--IARGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGpNEKGVLVIEGPLpPGCMQTVWGDDDRFV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 486 NTYWSRFeNKWVHG--DWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFV 562
Cdd:PRK10524 464 KTYWSLF-GRQVYStfDWGIRDADGYYfILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFV 542
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446729146 563 VLRDHVTFTGE-----LKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELGDLSSLVNP 632
Cdd:PRK10524 543 VPKDSDSLADRearlaLEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGRDPGDLTTIEDP 617
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
1-641 |
1.64e-133 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 406.10 E-value: 1.64e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 1 MKQAVWFPTEEYKEKTRLYGWM------KSLGYEDYEIFYNKSIEETAWFWGEAEKAVGYQWMKPYTEVLDlENGTPFAQ 74
Cdd:PRK03584 1 MGDPLWTPSAERIAASRMTAFIrwlaarRGLSFDDYAALWRWSVEDLEAFWQSVWDFFGVIGSTPYTVVLA-GRRMPGAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 75 WYNGGTCNVVESALsRWLADEEtriqPALQYEGENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVV 154
Cdd:PRK03584 80 WFPGARLNYAENLL-RHRRDDR----PAIIFRGEDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 155 AMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRRGKIVSLKDEVDKACEHCPTVEKVVIVRHAGN--DF 232
Cdd:PRK03584 155 AMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDRRAKVAELRAALPSLEHVVVVPYLGPaaAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 233 TPHNYDFSWSTL--EKEKPFIHAEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDM 310
Cdd:PRK03584 235 AALPGALLWEDFlaPAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDRFFWYTTC 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 311 GWMMGPFLLfGSLINGATMVMYEGVPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGE 390
Cdd:PRK03584 315 GWMMWNWLV-SGLLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 391 PWNPDPWMWLFETVgKGNVPICNYSGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGKPIRDEVGELCLEKPW 470
Cdd:PRK03584 394 PLPPEGFDWVYEHV-KADVWLASISGGTDICSCFVGGNPLLPVYRGEIQCRGLGMAVEAWDEDGRPVVGEVGELVCTKPF 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 471 VGMTKSFW--EDDERYVNTYWSRFENKWVHGDWV-IYDGEQYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAI 547
Cdd:PRK03584 473 PSMPLGFWndPDGSRYRDAYFDTFPGVWRHGDWIeITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVI 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 548 GVPDEVKGEVCHCFVVLRDHVTFTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLG---KELG 624
Cdd:PRK03584 553 GQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKVELPVKKLLHGrpvKKAV 632
|
650
....*....|....*..
gi 446729146 625 DLSSLVNPEVVPFIQGL 641
Cdd:PRK03584 633 NRDALANPEALDWFADL 649
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
22-633 |
1.92e-125 |
|
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: 384.70 E-value: 1.92e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 22 MKSLGYEDYEIFYNKSIEETAWFWGEAEKAVGYQWMKPYTEVLDLENGTPFAQWYNGGTCNVVESALSRWLADEetriqP 101
Cdd:cd05943 11 RHGLSLADYAALHRWSVDDPGAFWAAVWDFSGVRGSKPYDVVVVSGRIMPGARWFPGARLNYAENLLRHADADD-----P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 102 ALQYEGENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTR 181
Cdd:cd05943 86 AAIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 182 VQAAGSKMIITADGFSRRGKIVSLKDEVDKACEHCPTVEKVVIVrhaGNDFTPHNYDFS----WSTLEKEK-----PFIH 252
Cdd:cd05943 166 FGQIEPKVLFAVDAYTYNGKRHDVREKVAELVKGLPSLLAVVVV---PYTVAAGQPDLSkiakALTLEDFLatgaaGELE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 253 AEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLfGSLINGATMVMY 332
Cdd:cd05943 243 FEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGWMMWNWLV-SGLAVGATIVLY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 333 EGVPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVgKGNVPIC 412
Cdd:cd05943 322 DGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHI-KPDVLLA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 413 NYSGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGKPIRDEVGELCLEKPWVGMTKSFWEDDE--RYVNTYWS 490
Cdd:cd05943 401 SISGGTDIISCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPVWGEKGELVCTKPFPSMPVGFWNDPDgsRYRAAYFA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 491 RFENKWVHGDWVIYDGE-QYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVT 569
Cdd:cd05943 481 KYPGVWAHGDWIEITPRgGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVE 560
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446729146 570 FTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELGDLSSLVNPE 633
Cdd:cd05943 561 LDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGRPVKNAGALANPE 624
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
75-629 |
5.83e-120 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 368.45 E-value: 5.83e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 75 WYNGGTCNVVESALSRWlADEETRIQPALQYEGENgTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVV 154
Cdd:PRK04319 36 WLETGKVNIAYEAIDRH-ADGGRKDKVALRYLDAS-RKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 155 AMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRRGKIVSLkdevdkacehcPTVEKVVIVRHAGnDFTP 234
Cdd:PRK04319 114 ALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERKPADDL-----------PSLKHVLLVGEDV-EEGP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 235 HNYDFsWSTLEKEKPFIHAEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAfDAGFGMNIKQGDrVLWVT-DMGWM 313
Cdd:PRK04319 182 GTLDF-NALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQ-TGKYVLDLHEDD-VYWCTaDPGWV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 314 MG-PFLLFGSLINGATMVMYEGvpDFpEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPW 392
Cdd:PRK04319 259 TGtSYGIFAPWLNGATNVIDGG--RF-SPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDLVKKYDLSSLRHILSVGEPL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 393 NP---------------DPWmWLFETvgkGNVPICNYSGgteisggifgnvliKPIAPISFNASLPGMAAVVLDDQGKPI 457
Cdd:PRK04319 336 NPevvrwgmkvfglpihDNW-WMTET---GGIMIANYPA--------------MDIKPGSMGKPLPGIEAAIVDDQGNEL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 458 -RDEVGELCLEKPWVGMTKSFWEDDERYvNTYwsrFENKW-VHGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESI 534
Cdd:PRK04319 398 pPNRMGNLAIKKGWPSMMRGIWNNPEKY-ESY---FAGDWyVSGDSAYMDEDGYFwFQGRVDDVIKTSGERVGPFEVESK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 535 LVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVI 614
Cdd:PRK04319 474 LMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVL 553
|
570
....*....|....*
gi 446729146 615 KAAYLGKELGDLSSL 629
Cdd:PRK04319 554 KAWELGLPEGDLSTM 568
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
3-645 |
1.52e-107 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 338.78 E-value: 1.52e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 3 QAVWFPTEEYKEKTRLYGWMKSLG------YEDYEIFYNKSIEETAWFWGEAEKAVGYQWMKPYTEVLDLENGtPFAQWY 76
Cdd:TIGR01217 4 QPLWQPDAQRIAQARMTRFQAWAGehhgaaEGGYDALHRWSVDELDTFWKAVWEWFDVRFSTPCARVVDDRTM-PGAQWF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 77 NGGTCNVVESALsrwladEETRIQPALQYEGENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAM 156
Cdd:TIGR01217 83 PGARLNYAENLL------RAAGTEPALLYVDETHEPAPVTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 157 LAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRRGKIVSLKDEVDKACEHCPTVEKVVIVRHAGNDFT--- 233
Cdd:TIGR01217 157 LATASVGAIWSSCSPDFGARGVLDRFQQIEPKLLFTVDGYRYNGKEHDRRDKVAEVRKELPTLRAVVHIPYLGPRETeap 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 234 --PHNYDFSWSTLEKEKPFIHAEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDMG 311
Cdd:TIGR01217 237 kiDGALDLEDFTAAAQAAELVFEQLPFDHPLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTTTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 312 WMMGPFLLFGsLINGATMVMYEGVPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEP 391
Cdd:TIGR01217 317 WMMWNWLVSG-LATGATLVLYDGSPGFPATNVLWDIAERTGATLFGTSAKYVMACRKAGVHPARTHDLSALQCVASTGSP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 392 WNPDPWMWLFETVgKGNVPICNYSGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGKPIRDEVGELCLEKPWV 471
Cdd:TIGR01217 396 LPPDGFRWVYDEI-KADVWLASISGGTDICSCFAGANPTLPVHIGEIQAPGLGTAVQSWDPEGKPVTGEVGELVCTNPMP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 472 GMTKSFW--EDDERYVNTYWSRFENKWVHGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIG 548
Cdd:TIGR01217 475 SMPIRFWndPDGSKYRDAYFDTYPGVWRHGDWITLTPRGGIvIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIG 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 549 VPDEVKGEVCHCFVVLRDHVTFTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELGDLSS 628
Cdd:TIGR01217 555 QEQPDGGYRVVLFVHLAPGATLDDALLDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKRVLQGTPVDNPGA 634
|
650
....*....|....*..
gi 446729146 629 LVNPEVVPFIQGLQSSK 645
Cdd:TIGR01217 635 IDNPELLDLYEELAELR 651
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
115-616 |
3.63e-101 |
|
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: 315.60 E-value: 3.63e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 115 FTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITad 194
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 195 gfsrrgkivslkdevdkacehcptvekvvivrhagndfTPHNYdfswstlekekpfihaEEMQSDDPLMLIYTSGTTGKP 274
Cdd:cd05969 79 --------------------------------------TEELY----------------ERTDPEDPTLLHYTSGTTGTP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 275 KGTVHTHAGFpLKAAFDAGFGMNIKQGDrVLWVT-DMGWMMGPFL-LFGSLINGATMVMYEGvpDFpEADRLWETVDKYE 352
Cdd:cd05969 105 KGVLHVHDAM-IFYYFTGKYVLDLHPDD-IYWCTaDPGWVTGTVYgIWAPWLNGVTNVVYEG--RF-DAESWYGIIERVK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 353 ITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVgkgNVPICNYSGGTEISGGIFGNVLIKP 432
Cdd:cd05969 180 VTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVF---GVPIHDTWWQTETGSIMIANYPCMP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 433 IAPISFNASLPGMAAVVLDDQGKPIR-DEVGELCLEKPWVGMTKSFWEDDERYVNTywsrFENKW-VHGDWVIYDGEQYI 510
Cdd:cd05969 257 IKPGSMGKPLPGVKAAVVDENGNELPpGTKGILALKPGWPSMFRGIWNDEERYKNS----FIDGWyLTGDLAYRDEDGYF 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 511 -ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGELKKELMSLVNSHIGKA 589
Cdd:cd05969 333 wFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAH 412
|
490 500
....*....|....*....|....*..
gi 446729146 590 LCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:cd05969 413 VAPREIEFVDNLPKTRSGKIMRRVLKA 439
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
115-616 |
1.54e-95 |
|
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: 300.41 E-value: 1.54e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 115 FTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITad 194
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 195 gfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihaeemQSDDPLMLIYTSGTTGKP 274
Cdd:cd05972 79 --------------------------------------------------------------DAEDPALIYFTSGTTGLP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 275 KGTVHTHAgFPLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGP-FLLFGSLINGATMVMYEGVPdFpEADRLWETVDKYEI 353
Cdd:cd05972 97 KGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAwSSFFGPWLLGATVFVYEGPR-F-DAERILELLERYGV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 354 THLGISPTLIRALMAKG-DEYVnkhsLKSLEVFASTGEPWNPDPWMWLFETVGkgnVPICNYSGGTEiSGGIFGNVLIKP 432
Cdd:cd05972 174 TSFCGPPTAYRMLIKQDlSSYK----FSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTE-TGLTVGNFPDMP 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 433 IAPISFNASLPGMAAVVLDDQGKPIRD-EVGELCLEKPWVGMTKSFWEDDERYVntywSRFENKWVH-GDWVIYDGEQYI 510
Cdd:cd05972 246 VKPGSMGRPTPGYDVAIIDDDGRELPPgEEGDIAIKLPPPGLFLGYVGDPEKTE----ASIRGDYYLtGDRAYRDEDGYF 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 511 -ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGELKKELMSLVNSHIGKA 589
Cdd:cd05972 322 wFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPY 401
|
490 500
....*....|....*....|....*..
gi 446729146 590 LCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:cd05972 402 KYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
100-624 |
3.97e-89 |
|
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: 284.40 E-value: 3.97e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 100 QPALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM 179
Cdd:COG0318 15 RPALVFGGR-----RLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 180 TRVQAAGSKMIITAdgfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihaeemqsd 259
Cdd:COG0318 90 YILEDSGARALVTA------------------------------------------------------------------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 260 dplMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVT----DMGWMMGpflLFGSLINGATMVMyegV 335
Cdd:COG0318 104 ---LILYTSGTTGRPKGVMLTHRNL-LANAAAIAAALGLTPGDVVLVALplfhVFGLTVG---LLAPLLAGATLVL---L 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 336 PDFpEADRLWETVDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGkgnVPICNYS 415
Cdd:COG0318 174 PRF-DPERVLELIERERVTVLFGVPTMLARLLRHPE--FARYDLSSLRLVVSGGAPLPPELLERFEERFG---VRIVEGY 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 416 GGTEISGGIFGNVLIKPIAPIsfnAS----LPGMAAVVLDDQGKPI-RDEVGELCLEKPWVgmTKSFWEDDERYVNTyws 490
Cdd:COG0318 248 GLTETSPVVTVNPEDPGERRP---GSvgrpLPGVEVRIVDEDGRELpPGEVGEIVVRGPNV--MKGYWNDPEATAEA--- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 491 rFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHV 568
Cdd:COG0318 320 -FRDGWLRtGDLGRLDEDGYLyIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGA 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446729146 569 TFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELG 624
Cdd:COG0318 399 ELDAE---ELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
5-616 |
2.24e-82 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 274.65 E-value: 2.24e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 5 VWFPTEEYKEKTRLYGWMKSLGYE-----------DYEIFYNKSIEETAWFWGEAEKAVGYQWMKPYTEVLDLENGT-PF 72
Cdd:PLN03052 86 AWFPSPEIAKLTNLGRLLEARGKEllgskykdpisSFSEFQRFSVENPEVYWSIVLDELSLVFSVPPRCILDTSDESnPG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 73 AQWYNGGTCNVVESALSrwLADEETRIQPALQY--EGENGTSKSF-TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMI 149
Cdd:PLN03052 166 GQWLPGAVLNVAECCLT--PKPSKTDDSIAIIWrdEGSDDLPVNRmTLSELRSQVSRVANALDALGFEKGDAIAIDMPMN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 150 PETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRRGKIVSLKDEVDKACEHcptveKVVIVRHAG 229
Cdd:PLN03052 244 VHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYSRVVEAKAP-----KAIVLPADG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 230 NDFTP--HNYDFSW-------STLEKEKPFIHAEemQSDDPLMLI-YTSGTTGKPKGTVHTHAGfPLKAAFDAGFGMNIK 299
Cdd:PLN03052 319 KSVRVklREGDMSWddflaraNGLRRPDEYKAVE--QPVEAFTNIlFSSGTTGEPKAIPWTQLT-PLRAAADAWAHLDIR 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 300 QGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGVPDFPEADRLwetVDKYEITHLGISPTLIRALmaKGDEYVNKHSL 379
Cdd:PLN03052 396 KGDIVCWPTNLGWMMGPWLVYASLLNGATLALYNGSPLGRGFAKF---VQDAKVTMLGTVPSIVKTW--KNTNCMAGLDW 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 380 KSLEVFASTGEPWNPDPWMWLfetVGKGNV-PICNYSGGTEISGGIFGNVLIKPIAPISFnaSLPGM--AAVVLDDQGKP 456
Cdd:PLN03052 471 SSIRCFGSTGEASSVDDYLWL---MSRAGYkPIIEYCGGTELGGGFVTGSLLQPQAFAAF--STPAMgcKLFILDDSGNP 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 457 IRDEV---GELCLEKPWVGMTKSFWEDDerYVNTYWS---RFENKWV--HGDwvIYD---GEQYIITGRSDDTLNIAGKR 525
Cdd:PLN03052 546 YPDDApctGELALFPLMFGASSTLLNAD--HYKVYFKgmpVFNGKILrrHGD--IFErtsGGYYRAHGRADDTMNLGGIK 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 526 IGPAEYESILVK-HNDVIEAAAIGVPDEVKG-EVCHCFVVLRDHVTFTGELkKELMSLVNSHIGKALCP----KDIHVVE 599
Cdd:PLN03052 622 VSSVEIERVCNAaDESVLETAAIGVPPPGGGpEQLVIAAVLKDPPGSNPDL-NELKKIFNSAIQKKLNPlfkvSAVVIVP 700
|
650
....*....|....*..
gi 446729146 600 DLPKTRNSKVMRRVIKA 616
Cdd:PLN03052 701 SFPRTASNKVMRRVLRQ 717
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
109-616 |
5.47e-77 |
|
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: 252.35 E-value: 5.47e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 109 NGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSK 188
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 189 MIITaDGfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihaeemqSDDPLMLIYTS 268
Cdd:cd05971 81 ALVT-DG--------------------------------------------------------------SDDPALIIYTS 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 269 GTTGKPKGTVHTHAgFPLKAAFDAGFGMNI-KQGDRVLWVT-DMGWMMGPF-LLFGSLINGATMVMYEGVPdFpEADRLW 345
Cdd:cd05971 98 GTTGPPKGALHAHR-VLLGHLPGVQFPFNLfPRDGDLYWTPaDWAWIGGLLdVLLPSLYFGVPVLAHRMTK-F-DPKAAL 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 346 ETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLEVFASTGEPWNPDPWMWLFETVGkgnVPICNYSGGTEISGGIF 425
Cdd:cd05971 175 DLMSRYGVTTAFLPPTALKMMRQQGEQ--LKHAQVKLRAIATGGESLGEELLGWAREQFG---VEVNEFYGQTECNLVIG 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 426 GNVLIKPIAPISFNASLPGMAAVVLDDQGKPI-RDEVGELCLEKPWVGMTKSFWEDDERYVntywSRFENKW-VHGDWVI 503
Cdd:cd05971 250 NCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLpPGEVGEIAVELPDPVAFLGYWNNPSATE----KKMAGDWlLTGDLGR 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 504 YDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGELKKELMSLV 582
Cdd:cd05971 326 KDSDGYFwYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELV 405
|
490 500 510
....*....|....*....|....*....|....
gi 446729146 583 NSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:cd05971 406 KTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
108-522 |
1.95e-75 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 247.61 E-value: 1.95e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 108 ENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGS 187
Cdd:pfam00501 15 EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 188 KMIITADGFsrrgkivslkdEVDKACEHCPTVEKVVIVRHAGNDFTPHNYDFSWSTLEKEKPFIHAEEMQSDDPLMLIYT 267
Cdd:pfam00501 95 KVLITDDAL-----------KLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 268 SGTTGKPKGTVHTHAG-----FPLKAAFDAGFGMNikQGDRVLWVTDMGWMMG-PFLLFGSLINGATMVMYEGVPDFPeA 341
Cdd:pfam00501 164 SGTTGKPKGVMLTHRNlvanvLSIKRVRPRGFGLG--PDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALD-P 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 342 DRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSlkSLEVFASTGEPWNPDPWMWLFETVGkgnVPICNYSGGTEIS 421
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLS--SLRLVLSGGAPLPPELARRFRELFG---GALVNGYGLTETT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 422 GGIFGNVLikPIAPISFNAS----LPGMAAVVLDDQ-GKPIRD-EVGELCLEKPWVgmTKSFWEDDERYVNTYWsrfENK 495
Cdd:pfam00501 316 GVVTTPLP--LDEDLRSLGSvgrpLPGTEVKIVDDEtGEPVPPgEPGELCVRGPGV--MKGYLNDPELTAEAFD---EDG 388
|
410 420
....*....|....*....|....*....
gi 446729146 496 WVH-GDWVIYDGEQYI-ITGRSDDTLNIA 522
Cdd:pfam00501 389 WYRtGDLGRRDEDGYLeIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
260-610 |
4.21e-71 |
|
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: 233.33 E-value: 4.21e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 260 DPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGvpdfP 339
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK----F 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 340 EADRLWETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLEVFASTGEPWNPDPWMWLFETVGkgnVPICNYSGGTE 419
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPES--AGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLTE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 420 ISGGI-FGNVLIKPIAPISFNASLPGMAAVVLDDQGKPIRD-EVGELCLEKPWVgmTKSFWEDDERyvnTYwSRFENKWV 497
Cdd:cd04433 151 TGGTVaTGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPgEIGELVVRGPSV--MKGYWNNPEA---TA-AVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 498 H-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGElk 575
Cdd:cd04433 225 RtGDLGRLDEDGYLyIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAE-- 302
|
330 340 350
....*....|....*....|....*....|....*
gi 446729146 576 kELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVM 610
Cdd:cd04433 303 -ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
115-615 |
2.39e-70 |
|
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: 234.72 E-value: 2.39e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 115 FTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIIT-A 193
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTdA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 194 DgfsRRGKIvslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihaeemqSDDPLMLIYTSGTTGK 273
Cdd:cd05973 81 A---NRHKL-------------------------------------------------------DSDPFVMMFTSGTTGL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 274 PKGTVHthagfPLKA--AFDA--GFGMNIKQGDRVLWVTDMGWMMGPFL-LFGSLINGATMVMYEGvpDFpEADRLWETV 348
Cdd:cd05973 103 PKGVPV-----PLRAlaAFGAylRDAVDLRPEDSFWNAADPGWAYGLYYaITGPLALGHPTILLEG--GF-SVESTWRVI 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 349 DKYEITHLGISPTLIRALMAKGDEYVNKHSLKsLEVFASTGEPWNPDPWMWLFETVGkgnVPICNYSGGTEIsGGIFGN- 427
Cdd:cd05973 175 ERLGVTNLAGSPTAYRLLMAAGAEVPARPKGR-LRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTEL-GMVLANh 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 428 -VLIKPIAPISFNASLPGMAAVVLDDQGK-PIRDEVGELCLE---KP--WVGmtkSFWEDDERYVNTYWSRfenkwvHGD 500
Cdd:cd05973 250 hALEHPVHAGSAGRAMPGWRVAVLDDDGDeLGPGEPGRLAIDianSPlmWFR---GYQLPDTPAIDGGYYL------TGD 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 501 WVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGELKKELM 579
Cdd:cd05973 321 TVEFDPDGSFsFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQ 400
|
490 500 510
....*....|....*....|....*....|....*.
gi 446729146 580 SLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05973 401 LHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
111-610 |
2.40e-70 |
|
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: 235.96 E-value: 2.40e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 111 TSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMI 190
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 191 ITAdgfsrrgkiVSLKDEVDKACEHCPTVEKVVIVRHAGnDFTPHNYDFSWSTLEKEKPFIHAEEMQS-DDPLMLIYTSG 269
Cdd:cd05911 87 FTD---------PDGLEKVKEAAKELGPKDKIIVLDDKP-DGVLSIEDLLSPTLGEEDEDLPPPLKDGkDDTAAILYSSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 270 TTGKPKGTVHTH----AGFPLKAAFdagFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMyegVPDFpEADRLW 345
Cdd:cd05911 157 TTGLPKGVCLSHrnliANLSQVQTF---LYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVII---MPKF-DSELFL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 346 ETVDKYEITHLGISPTLIrALMAKgDEYVNKHSLKSLEVFASTGEPWNPDpwmwLFETVGK--GNVPICNYSGGTEISGG 423
Cdd:cd05911 230 DLIEKYKITFLYLVPPIA-AALAK-SPLLDKYDLSSLRVILSGGAPLSKE----LQELLAKrfPNATIKQGYGMTETGGI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 424 IFgnvlIKPIAPISFNAS---LPGMAAVVLDDQGKPI--RDEVGELCLEKPwvGMTKSFWEDDEryvNTYWSRFENKWVH 498
Cdd:cd05911 304 LT----VNPDGDDKPGSVgrlLPNVEAKIVDDDGKDSlgPNEPGEICVRGP--QVMKGYYNNPE---ATKETFDEDGWLH 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 499 -GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTgelKK 576
Cdd:cd05911 375 tGDIGYFDEDGYLyIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLT---EK 451
|
490 500 510
....*....|....*....|....*....|....*...
gi 446729146 577 ELMSLVNSHIGKAlcpKDIH----VVEDLPKTRNSKVM 610
Cdd:cd05911 452 EVKDYVAKKVASY---KQLRggvvFVDEIPKSASGKIL 486
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
146-616 |
3.00e-70 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 236.25 E-value: 3.00e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 146 MPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRRGKIVSLKDEVDKACEHcptveKVVIV 225
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAAPA-----KAIVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 226 RHAGNDFTP--HNYDFSW---------STLEKEKPFiHAEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGfPLKAAFDAGF 294
Cdd:PLN03051 76 PAAGEPVAVplREQDLSWcdflgvaaaQGSVGGNEY-SPVYAPVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 295 GMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGVP------DFPEADRlwetvdkyeITHLGISPTLIRALMA 368
Cdd:PLN03051 154 HMDIQPGDVVCWPTNLGWMMGPWLLYSAFLNGATLALYGGAPlgrgfgKFVQDAG---------VTVLGLVPSIVKAWRH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 369 KGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLfeTVGKGNV-PICNYSGGTEISGGIFGNVLIKPIAPISFNASLPGMAA 447
Cdd:PLN03051 225 TGAFAMEGLDWSKLRVFASTGEASAVDDVLWL--SSVRGYYkPVIEYCGGTELASGYISSTLLQPQAPGAFSTASLGTRF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 448 VVLDDQGKPIRDE---VGELCLEKPWVGMTKSFWEDDERYVntYWS---RFENKWV----HGDWVI-YDGEQYIITGRSD 516
Cdd:PLN03051 303 VLLNDNGVPYPDDqpcVGEVALAPPMLGASDRLLNADHDKV--YYKgmpMYGSKGMplrrHGDIMKrTPGGYFCVQGRAD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 517 DTLNIAGKRIGPAEYESILVKHND-VIEAAAIGVPDEVKG-EVCHCFVvlrdhvtFTGELKK--------ELMSLVNSHI 586
Cdd:PLN03051 381 DTMNLGGIKTSSVEIERACDRAVAgIAETAAVGVAPPDGGpELLVIFL-------VLGEEKKgfdqarpeALQKKFQEAI 453
|
490 500 510
....*....|....*....|....*....|....
gi 446729146 587 GKALCP----KDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:PLN03051 454 QTNLNPlfkvSRVKIVPELPRNASNKLLRRVLRD 487
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
115-622 |
1.05e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 227.38 E-value: 1.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 115 FTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITAD 194
Cdd:PRK06187 32 TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 195 GFSrrgkivslkDEVDKACEHCPTVEKVVIVRHAGNDFTP---HNYDFSWSTLEKEKPFIHAEEmqsDDPLMLIYTSGTT 271
Cdd:PRK06187 112 EFV---------PLLAAILPQLPTVRTVIVEGDGPAAPLApevGEYEELLAAASDTFDFPDIDE---NDAAAMLYTSGTT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 272 GKPKGTVHTHAGFPLKAAFDAGfGMNIKQGDRVLWVTDM------GWMMGPFLLfgslinGATMVMyegvPDFPEADRLW 345
Cdd:PRK06187 180 GHPKGVVLSHRNLFLHSLAVCA-WLKLSRDDVYLVIVPMfhvhawGLPYLALMA------GAKQVI----PRRFDPENLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 346 ETVDKYEITHLGISPTLIRALMAKGDEYvnKHSLKSLEVFASTGEPWNPDpwmWLFETVGKGNVPICNYSGGTEISGGIF 425
Cdd:PRK06187 249 DLIETERVTFFFAVPTIWQMLLKAPRAY--FVDFSSLRLVIYGGAALPPA---LLREFKEKFGIDLVQGYGMTETSPVVS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 426 GNVL---IKPIAPISFNA--SLPGMAAVVLDDQGKPI-RD--EVGELCLEKPWvgMTKSFWEDDERYVNTywsrFENKWV 497
Cdd:PRK06187 324 VLPPedqLPGQWTKRRSAgrPLPGVEARIVDDDGDELpPDggEVGEIIVRGPW--LMQGYWNRPEATAET----IDGGWL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 498 H-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTgelK 575
Cdd:PRK06187 398 HtGDVGYIDEDGYLyITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLD---A 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 446729146 576 KELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKE 622
Cdd:PRK06187 475 KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAEGK 521
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
88-615 |
6.77e-66 |
|
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: 225.84 E-value: 6.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 88 LSRWLADEETRIqpALQYEGENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIIS 167
Cdd:cd05970 23 VDAMAKEYPDKL--ALVWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 168 PIFSGFASDAVMTRVQAAGSKMIITADGfsrrgkiVSLKDEVDKACEHCPTVEKVVIVrhaGNDFTPHNYDFSwSTLEKE 247
Cdd:cd05970 101 PATHQLTAKDIVYRIESADIKMIVAIAE-------DNIPEEIEKAAPECPSKPKLVWV---GDPVPEGWIDFR-KLIKNA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 248 KPFI---HAE-EMQSDDPLMLIYTSGTTGKPKGTVHTHAgFPLKAAFDAGFGMNIKQGDRVLWVTDMGW---MMGPFllF 320
Cdd:cd05970 170 SPDFerpTANsYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWgkaVWGKI--Y 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 321 GSLINGATMVMYEGVPDFPEAdrLWETVDKYEITHLGISPTLIRALMakgDEYVNKHSLKSLEVFASTGEPWNPDpwmwL 400
Cdd:cd05970 247 GQWIAGAAVFVYDYDKFDPKA--LLEKLSKYGVTTFCAPPTIYRFLI---REDLSRYDLSSLRYCTTAGEALNPE----V 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 401 FETV-GKGNVPICNYSGGTEISGGIfGNVLIKPIAPISFNASLPGMAAVVLDDQGKPIR-DEVGELCL---EKPWVGMTK 475
Cdd:cd05970 318 FNTFkEKTGIKLMEGFGQTETTLTI-ATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEaGEEGEIVIrtsKGKPVGLFG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 476 SFWEDDERYVNTYwsrFENKWVHGD--WVIYDGEQYIItGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEV 553
Cdd:cd05970 397 GYYKDAEKTAEVW---HDGYYHTGDaaWMDEDGYLWFV-GRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPI 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446729146 554 KGEVCHCFVVLRDHVTFTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05970 473 RGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
100-611 |
7.44e-63 |
|
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: 214.78 E-value: 7.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 100 QPALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM 179
Cdd:cd17631 11 RTALVFGGR-----SLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 180 TRVQAAGSKMIItadgfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihaeemqsD 259
Cdd:cd17631 86 YILADSGAKVLF-------------------------------------------------------------------D 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 260 DPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDM--GWMMGPFLLFGsLINGATMVMYEGvpd 337
Cdd:cd17631 99 DLALLMYTSGTTGRPKGAMLTHRNL-LWNAVNALAALDLGPDDVLLVVAPLfhIGGLGVFTLPT-LLRGGTVVILRK--- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 338 fPEADRLWETVDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFASTGEPWnPDPwmwLFETVGKGNVPICNYSGG 417
Cdd:cd17631 174 -FDPETVLDLIERHRVTSFFLVPTMIQALLQHPR--FATTDLSSLRAVIYGGAPM-PER---LLRALQARGVKFVQGYGM 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 418 TEISGGIFGN----VLIKPIapiSFNASLPGMAAVVLDDQGKPIRD-EVGELCLEKPwvGMTKSFWEDDERYVNTywsrF 492
Cdd:cd17631 247 TETSPGVTFLspedHRRKLG---SAGRPVFFVEVRIVDPDGREVPPgEVGEIVVRGP--HVMAGYWNRPEATAAA----F 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 493 ENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTF 570
Cdd:cd17631 318 RDGWFHtGDLGRLDEDGYLyIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAEL 397
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 446729146 571 TGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:cd17631 398 DED---ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
100-616 |
1.88e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 204.75 E-value: 1.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 100 QPALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAI---ISPIFSGFASD 176
Cdd:PRK07656 21 KEAYVFGDQ-----RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVvvpLNTRYTADEAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 177 AVMTRvqaAGSKMIITADGFsrRGKIVSLKDEVdkacehcPTVEKVVIVR-HAGNDFTPHNYDFSwSTLEKEKPFIHAEE 255
Cdd:PRK07656 96 YILAR---GDAKALFVLGLF--LGVDYSATTRL-------PALEHVVICEtEEDDPHTEKMKTFT-DFLAAGDPAERAPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 256 MQSDDPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDMgwmmgpFLLFG-------SLINGAT 328
Cdd:PRK07656 163 VDPDDVADILFTSGTTGRPKGAMLTHRQL-LSNAADWAEYLGLTEGDRYLAANPF------FHVFGykagvnaPLMRGAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 329 MVMyegVPDFpEADRLWETVDKYEITHLGISPTLIRALMA--KGDEYvnkhSLKSLEVFASTG------------EPWNp 394
Cdd:PRK07656 236 ILP---LPVF-DPDEVFRLIETERITVLPGPPTMYNSLLQhpDRSAE----DLSSLRLAVTGAasmpvallerfeSELG- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 395 dpwmwlFETVGKGnvpicnYsGGTEISggifGNVLIKPI------APISFNASLPGMAAVVLDDQGKPI-RDEVGELCLE 467
Cdd:PRK07656 307 ------VDIVLTG------Y-GLSEAS----GVTTFNRLdddrktVAGTIGTAIAGVENKIVNELGEEVpVGEVGELLVR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 468 KPWVgMtKSFWEDDERYVNTYwsRFENkWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAA 545
Cdd:PRK07656 370 GPNV-M-KGYYDDPEATAAAI--DADG-WLHtGDLGRLDEEGYLyIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAA 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446729146 546 AIGVPDEVKGEVCHCFVVLRDHVTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:PRK07656 445 VIGVPDERLGEVGKAYVVLKPGAELTEE---ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
100-615 |
7.27e-58 |
|
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: 202.02 E-value: 7.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 100 QPALQYEGengtsKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM 179
Cdd:cd05936 15 KTALIFMG-----RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 180 TRVQAAGSKMIITADGFSRRGKIvslkdevdkacehcptvekvvivrhagndftphnydfswSTLEKEKPFIHAeemqsD 259
Cdd:cd05936 90 HILNDSGAKALIVAVSFTDLLAA---------------------------------------GAPLGERVALTP-----E 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 260 DPLMLIYTSGTTGKPKGTVHTHAGFplkaafdagfGMNIKQGDRvlWVTDMGW----MMGP---FLLFG-------SLIN 325
Cdd:cd05936 126 DVAVLQYTSGTTGVPKGAMLTHRNL----------VANALQIKA--WLEDLLEgddvVLAAlplFHVFGltvalllPLAL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 326 GATMVMyegVPDFpEADRLWETVDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFASTGEPWNPDpwmwLFETVG 405
Cdd:cd05936 194 GATIVL---IPRF-RPIGVLKEIRKHRVTIFPGVPTMYIALLNAPE--FKKRDFSSLRLCISGGAPLPVE----VAERFE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 406 K-GNVPICNYSGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGKPI-RDEVGELCLEKPWVgmTKSFWEDDER 483
Cdd:cd05936 264 ElTGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELpPGEVGELWVRGPQV--MKGYWNRPEE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 484 YVNTywsrFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCF 561
Cdd:cd05936 342 TAEA----FVDGWLRtGDIGYMDEDGYFfIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAF 417
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446729146 562 VVLRDHVTFTgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05936 418 VVLKEGASLT---EEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
101-615 |
1.91e-56 |
|
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: 200.00 E-value: 1.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYEGENGTSKSFTYEELDNWVSRVANGLKHA-GIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM 179
Cdd:cd05928 28 PALWWVNGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDIL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 180 TRVQAAGSKMIITADgfsrrgkivSLKDEVDKACEHCPTVEKVVIVrhagndfTPHNYDfSW----STLEKEKPFIHAEE 255
Cdd:cd05928 108 YRLQASKAKCIVTSD---------ELAPEVDSVASECPSLKTKLLV-------SEKSRD-GWlnfkELLNEASTEHHCVE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 256 MQSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDrVLW-VTDMGWMMGPF-LLFGSLINGATMVMYE 333
Cdd:cd05928 171 TGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASD-IMWnTSDTGWIKSAWsSLFEPWIQGACVFVHH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 334 gVPDFpEADRLWETVDKYEITHLGISPTLIRALMAKGdeyVNKHSLKSLEVFASTGEPWNPD---PW-----MWLFETVG 405
Cdd:cd05928 250 -LPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQQD---LSSYKFPSLQHCVTGGEPLNPEvleKWkaqtgLDIYEGYG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 406 KGN-VPICNYSGGTEISGGIFGnvliKPIapisfnaslPGMAAVVLDDQGK--PIRDEvGELCL----EKPwVGMTKSFW 478
Cdd:cd05928 325 QTEtGLICANFKGMKIKPGSMG----KAS---------PPYDVQIIDDNGNvlPPGTE-GDIGIrvkpIRP-FGLFSGYV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 479 EDDERYVNTYWSRFenkWVHGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEV 557
Cdd:cd05928 390 DNPEKTAATIRGDF---YLTGDRGIMDEDGYFwFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEV 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446729146 558 CHCFVVL------RDHvtftGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05928 467 VKAFVVLapqflsHDP----EQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELR 526
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
100-612 |
1.55e-53 |
|
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: 189.66 E-value: 1.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 100 QPALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDavm 179
Cdd:cd05930 3 AVAVVDGDQ-----SLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 180 tRVQA----AGSKMIITadgfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihaee 255
Cdd:cd05930 75 -RLAYiledSGAKLVLT--------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 256 mQSDDPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVT----DMGWMMgpflLFGSLINGATMVM 331
Cdd:cd05930 91 -DPDDLAYVIYTSGSTGKPKGVMVEHRGL-VNLLLWMQEAYPLTPGDRVLQFTsfsfDVSVWE----IFGALLAGATLVV 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 332 yegVPDFPEAD--RLWETVDKYEITHLGISPTLIRALMakgdEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVgkGNV 409
Cdd:cd05930 165 ---LPEEVRKDpeALADLLAEEGITVLHLTPSLLRLLL----QELELAALPSLRLVLVGGEALPPDLVRRWRELL--PGA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 410 PICNYSGGTEISGGI-FGNVL--IKPIAPISFNASLPGMAAVVLDDQGKPIRD-EVGELCLEKPwvGMTKSFWED----D 481
Cdd:cd05930 236 RLVNLYGPTEATVDAtYYRVPpdDEEDGRVPIGRPIPNTRVYVLDENLRPVPPgVPGELYIGGA--GLARGYLNRpeltA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 482 ERYVNTYWsrFENKWVH--GDWVIY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGE 556
Cdd:cd05930 314 ERFVPNPF--GPGERMYrtGDLVRWlpDGNlEFL--GRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEK 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 446729146 557 VCHCFVVLRDHVTFT-GELKKELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd05930 390 RLVAYVVPDEGGELDeEELRAHLAERLPDY----MVPSAFVVLDALPLTPNGKVDRK 442
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
113-611 |
2.59e-53 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 188.82 E-value: 2.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 113 KSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIispifsgfasdAVMTRVQAAgskmiit 192
Cdd:cd05919 9 RSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAI-----------AVVINPLLH------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 193 adgfsrrgkivslKDEVDKACEHCptvEKVVIVRHAgndftphnydfswstlekekpfihaeemqsDDPLMLIYTSGTTG 272
Cdd:cd05919 71 -------------PDDYAYIARDC---EARLVVTSA------------------------------DDIAYLLYSSGTTG 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 273 KPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDM--GWMMGPFLLFGsLINGATMVMYEGVPDfpeADRLWETVDK 350
Cdd:cd05919 105 PPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNSLWFP-LAVGASAVLNPGWPT---AERVLATLAR 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 351 YEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGkgnVPICNYSGGTEIsGGIFGNVLI 430
Cdd:cd05919 181 FRPTVLYGVPTFYANLLDSCA--GSPDALRSLRLCVSAGEALPRGLGERWMEHFG---GPILDGIGATEV-GHIFLSNRP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 431 KPIAPISFNASLPGMAAVVLDDQGKPIR-DEVGELCLEKPwvGMTKSFWEDDERYVntywSRFENKWVH-GDWVIYDGEQ 508
Cdd:cd05919 255 GAWRLGSTGRPVPGYEIRLVDEEGHTIPpGEEGDLLVRGP--SAAVGYWNNPEKSR----ATFNGGWYRtGDKFCRDADG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 509 -YIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGELKKELMSLVNSHIG 587
Cdd:cd05919 329 wYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLS 408
|
490 500
....*....|....*....|....
gi 446729146 588 KALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:cd05919 409 AHKVPRRIAFVDELPRTATGKLQR 432
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
113-615 |
5.49e-49 |
|
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: 177.29 E-value: 5.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 113 KSFTYEELDNWVSRVANGLKHA-GIEKGDRVTIYMPMIPETVVAMLAVMKIGAIispifsgfaSDAVMTRVQAAGSKMII 191
Cdd:cd05958 9 REWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAI---------AVATMPLLRPKELAYIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 192 tadgfsRRGKIVslkdevdkacehcptvekVVIVRHAgndftphnydfswstlekekpfihaeEMQSDDPLMLIYTSGTT 271
Cdd:cd05958 80 ------DKARIT------------------VALCAHA--------------------------LTASDDICILAFTSGTT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 272 GKPKGTVHTHAGfpLKAAFDaGFGMNI---KQGDRVLWVTDM--GWMMGPFLLFgSLINGATMVMYEGVpdfpEADRLWE 346
Cdd:cd05958 110 GAPKATMHFHRD--PLASAD-RYAVNVlrlREDDRFVGSPPLafTFGLGGVLLF-PFGVGASGVLLEEA----TPDLLLS 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 347 TVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLEVFASTGEPWNPDPWMWLFETVGkgnVPICNYSGGTEISGgIFG 426
Cdd:cd05958 182 AIARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATG---IPIIDGIGSTEMFH-IFI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 427 NVLIKPIAPISFNASLPGMAAVVLDDQGKPIRD-EVGELCLEKPwvgmtKSFWEDDERYVNTYwsrFENKW-VHGDWVIY 504
Cdd:cd05958 256 SARPGDARPGATGKPVPGYEAKVVDDEGNPVPDgTIGRLAVRGP-----TGCRYLADKRQRTY---VQGGWnITGDTYSR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 505 DGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGELKKELMSLVN 583
Cdd:cd05958 328 DPDGYFrHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHAK 407
|
490 500 510
....*....|....*....|....*....|..
gi 446729146 584 SHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05958 408 AHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
110-615 |
1.24e-48 |
|
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: 177.95 E-value: 1.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 110 GTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKM 189
Cdd:cd05959 25 DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 190 IITADGFSRRGKIVSLKDEvdkacehcPTVEKVVIVRHAGNDFTPHNYDFSWSTLEKEKPfihAEEMQSDDPLMLIYTSG 269
Cdd:cd05959 105 VVVSGELAPVLAAALTKSE--------HTLVVLIVSGGAGPEAGALLLAELVAAEAEQLK---PAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 270 TTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDM--GWMMGPFLLFgSLINGATMVMYegvPDFPEADRLWET 347
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLffAYGLGNSLTF-PLSVGATTVLM---PERPTPAAVFKR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 348 VDKYEITHLGISPTLIRALMAkgDEYVNKHSLKSLEVFASTGEPwnpdpwmwLFETVGKG-----NVPICNYSGGTEIsG 422
Cdd:cd05959 250 IRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEA--------LPAEVGERwkarfGLDILDGIGSTEM-L 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 423 GIFGNVLIKPIAPISFNASLPGMAAVVLDDQGKPIRD-EVGELCLEKPWVGMtkSFWEDDERYVNT---YWSRFENKWVH 498
Cdd:cd05959 319 HIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADgEPGELYVRGPSSAT--MYWNNRDKTRDTfqgEWTRTGDKYVR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 499 GDwviyDGeQYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGELKKEL 578
Cdd:cd05959 397 DD----DG-FYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEALEEEL 471
|
490 500 510
....*....|....*....|....*....|....*..
gi 446729146 579 MSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05959 472 KEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
111-612 |
2.95e-48 |
|
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: 176.66 E-value: 2.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 111 TSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMI 190
Cdd:cd05904 29 TGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 191 ITAdgfsrrgkivslkdevdkacehCPTVEK-------VVIVRHAgnDFTPHNYDFswSTLEKEKPFIHAEEMQSDDPLM 263
Cdd:cd05904 109 FTT----------------------AELAEKlaslalpVVLLDSA--EFDSLSFSD--LLFEADEAEPPVVVIKQDDVAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 264 LIYTSGTTGKPKGTVHTHAGF-PLKAAFDAGFGMNIKQGDRVLWVTDMGWMMG-PFLLFGSLINGATMVMyegVPDFpEA 341
Cdd:cd05904 163 LLYSSGTTGRSKGVMLTHRNLiAMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGlSSFALGLLRLGATVVV---MPRF-DL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 342 DRLWETVDKYEITHLGISPTLIRAlMAKGDEyVNKHSLKSLEVFASTGEPWNPDpwmwLFETVGK--GNVPICNYSGGTE 419
Cdd:cd05904 239 EELLAAIERYKVTHLPVVPPIVLA-LVKSPI-VDKYDLSSLRQIMSGAAPLGKE----LIEAFRAkfPNVDLGQGYGMTE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 420 ISGGI--FGNVLIKPIAPISFNASLPGMAAVVLD-DQGKPI-RDEVGELCLEKPWVgMTKsfwedderYVN----TYWSR 491
Cdd:cd05904 313 STGVVamCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLpPNQTGELWIRGPSI-MKG--------YLNnpeaTAATI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 492 FENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVT 569
Cdd:cd05904 384 DKEGWLHtGDLCYIDEDGYLfIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSS 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 446729146 570 FTGelkKELMSLVNSHIG--KALcpKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd05904 464 LTE---DEIMDFVAKQVApyKKV--RKVAFVDAIPKSPSGKILRK 503
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
110-615 |
3.95e-48 |
|
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: 175.96 E-value: 3.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 110 GTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKM 189
Cdd:cd05926 10 GSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 190 IITADGFSrrgkivslkDEVDKACEHcptvEKVVIVRHAGNDFTPHNYD--FSWSTLEKEKPFIHAE-EMQSDDPLMLIY 266
Cdd:cd05926 90 VLTPKGEL---------GPASRAASK----LGLAILELALDVGVLIRAPsaESLSNLLADKKNAKSEgVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 267 TSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDM----GWMMGpflLFGSLINGATMVMyegvPDFPEAD 342
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNL-AASATNITNTYKLTPDDRTLVVMPLfhvhGLVAS---LLSTLAAGGSVVL----PPRFSAS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 343 RLWETVDKYEITHLGISPTLIRAL--MAKGDEYVNKHSLKslevFA-STGEPWNPDPWMWLFETVGkgnVP-ICNYsGGT 418
Cdd:cd05926 229 TFWPDVRDYNATWYTAVPTIHQILlnRPEPNPESPPPKLR----FIrSCSASLPPAVLEALEATFG---APvLEAY-GMT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 419 EISGGIFGNVLikPIAPISF-NASLP-GMAAVVLDDQGKPIRD-EVGELCLEKPWVgmTKSFWEDDEryvNTYWSRFENK 495
Cdd:cd05926 301 EAAHQMTSNPL--PPGPRKPgSVGKPvGVEVRILDEDGEILPPgVVGEICLRGPNV--TRGYLNNPE---ANAEAAFKDG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 496 WVH-GDWVIYDGEQY-IITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTge 573
Cdd:cd05926 374 WFRtGDLGYLDADGYlFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVT-- 451
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 446729146 574 lKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05926 452 -EEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
29-614 |
1.20e-46 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 174.93 E-value: 1.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 29 DYEIFYNKSIEETAWFWGEAEKAVGYqWMKPYTEVLDLENGTPfaQWYNGGTCNVVESALSRWLADEETRIQPALQYEGE 108
Cdd:PTZ00237 9 DYENDSNYANSNPESFWDEVAKKYVH-WDKMYDKVYSGDEIYP--DWFKGGELNTCYNVLDIHVKNPLKRDQDALIYECP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 109 --NGTSKsFTYEELDNWV---SRVangLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQ 183
Cdd:PTZ00237 86 ylKKTIK-LTYYQLYEKVcefSRV---LLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 184 AAGSKMIITADGFSRRGKIVSLKDEVDKACEhCPTVEKVVIVRHAGNDFTPHNYD------------FSW-STLEK---- 246
Cdd:PTZ00237 162 TITPKLIITTNYGILNDEIITFTPNLKEAIE-LSTFKPSNVITLFRNDITSESDLkkietiptipntLSWyDEIKKiken 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 247 -EKPFIHAEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLIN 325
Cdd:PTZ00237 241 nQSPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 326 GATMVMYEG--VPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHS---LKSLEVFASTGEPWNPDPWMWL 400
Cdd:PTZ00237 321 GNTFVMFEGgiIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSkydLSNLKEIWCGGEVIEESIPEYI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 401 FEtvgKGNVPICNYSGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGKPIRD-EVGELCLEKPW-VGMTKSFW 478
Cdd:PTZ00237 401 EN---KLKIKSSRGYGQTEIGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVnEIGEVAFKLPMpPSFATTFY 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 479 EDDERYVNTYwSRFENKWVHGDWVIYDGEQ-YIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEV 557
Cdd:PTZ00237 478 KNDEKFKQLF-SKFPGYYNSGDLGFKDENGyYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNV 556
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446729146 558 CHCFVVLR----DHVTFTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVI 614
Cdd:PTZ00237 557 PIGLLVLKqdqsNQSIDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
116-546 |
5.61e-46 |
|
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: 168.21 E-value: 5.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLK-HAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDavmtRVQA----AGSKMI 190
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAE----RLAFiledAGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 191 ITADGFSrrgkivSLKDEVDKACEHCPTVEKVVIVRhAGNDFTPhnydfswstlekekpfihAEEMQSDDPLMLIYTSGT 270
Cdd:TIGR01733 77 LTDSALA------SRLAGLVLPVILLDPLELAALDD-APAPPPP------------------DAPSGPDDLAYVIYTSGS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 271 TGKPKGTVHTHAGFplkAAFDAGFG--MNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGVPDFPEADRLWETV 348
Cdd:TIGR01733 132 TGRPKGVVVTHRSL---VNLLAWLArrYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALI 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 349 DKYEITHLGISPTLIRALMAKGDEyvnkhSLKSLEVFASTGEPWNP---DPWMWLFetvgkGNVPICNYSGGTEISGGIF 425
Cdd:TIGR01733 209 AEHPVTVLNLTPSLLALLAAALPP-----ALASLRLVILGGEALTPalvDRWRARG-----PGARLINLYGPTETTVWST 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 426 GNVLIKPIAPISFNAS----LPGMAAVVLDDQGKPI-RDEVGELCLEKPWVGmtKSFWEDD----ERYV-NTYWSRFENK 495
Cdd:TIGR01733 279 ATLVDPDDAPRESPVPigrpLANTRLYVLDDDLRPVpVGVVGELYIGGPGVA--RGYLNRPeltaERFVpDPFAGGDGAR 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 446729146 496 WVH-GDWVIY--DGEqYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAA 546
Cdd:TIGR01733 357 LYRtGDLVRYlpDGN-LEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
101-617 |
3.60e-44 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 167.44 E-value: 3.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQY---EGENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGaIISPIFSGFASDA 177
Cdd:PRK07529 42 PALSFlldADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 178 VMTRVQAAGSKMIITADGFSRrgkiVSLKDEVDKACEHCPTVEKVVIVRHAGNDFTP------------HNYDFSWSTLE 245
Cdd:PRK07529 121 IAELLRAAGAKVLVTLGPFPG----TDIWQKVAEVLAALPELRTVVEVDLARYLPGPkrlavplirrkaHARILDFDAEL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 246 KEKPFIH---AEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGfPLKAAFDAGFGMNIKQGDRVLWVTDMgwmmgpFLLFGS 322
Cdd:PRK07529 197 ARQPGDRlfsGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFCGLPL------FHVNAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 323 LIN-------GATMVM-----YEGvpdfPEA-DRLWETVDKYEITHLGISPTLIRALMAKGdeyVNKHSLKSLEVFASTG 389
Cdd:PRK07529 270 LVTglaplarGAHVVLatpqgYRG----PGViANFWKIVERYRINFLSGVPTVYAALLQVP---VDGHDISSLRYALCGA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 390 EPWNPDpwmwLFETV-GKGNVPICNYSGGTEISGGIFGNVLIKPIAPISFNASLPG--MAAVVLDDQGKPIRD----EVG 462
Cdd:PRK07529 343 APLPVE----VFRRFeAATGVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYqrVRVVILDDAGRYLRDcavdEVG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 463 ELCLEKPWV--GMT-----KSFWEDDeRYVNTywsrfenkwvhGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESI 534
Cdd:PRK07529 419 VLCIAGPNVfsGYLeaahnKGLWLED-GWLNT-----------GDLGRIDADGYFwLTGRAKDLIIRGGHNIDPAAIEEA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 535 LVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGElkkELMSLVNSHIG-KALCPKDIHVVEDLPKTRNSKV---- 609
Cdd:PRK07529 487 LLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEA---ELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIfkpa 563
|
570
....*....|...
gi 446729146 610 -----MRRVIKAA 617
Cdd:PRK07529 564 lrrdaIRRVLRAA 576
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
111-611 |
1.80e-43 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 163.47 E-value: 1.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 111 TSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGaiISPIfsgfasdAVMTRVQAAGSKMI 190
Cdd:TIGR02262 27 DISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAG--IVPV-------ALNTLLTADDYAYM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 191 ITadgfSRRGKIVSLKDE----VDKACEHCPTVEKVVIVrhagNDFTPHNYDFSwSTLEKEKPFIHAEEMQSDDPLMLIY 266
Cdd:TIGR02262 98 LE----DSRARVVFVSGAllpvIKAALGKSPHLEHRVVV----GRPEAGEVQLA-ELLATESEQFKPAATQADDPAFWLY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 267 TSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDM--GWMMGPFLLFGSLInGATMVMYegvPDFPEADRL 344
Cdd:TIGR02262 169 SSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKLffAYGLGNALTFPMSV-GATTVLM---GERPTPDAV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 345 WETVDKYEITHLGISPTLIRALMAkgDEYVNKHSLKSLEVFASTGEPwnpdpwmwLFETVGKG-----NVPICNYSGGTE 419
Cdd:TIGR02262 245 FDRLRRHQPTIFYGVPTLYAAMLA--DPNLPSEDQVRLRLCTSAGEA--------LPAEVGQRwqarfGVDIVDGIGSTE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 420 IsGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGKPIRD-EVGELCLEKPWVGmtKSFWEDDERYVNTY---WSRFENK 495
Cdd:TIGR02262 315 M-LHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADgEPGELLISGPSSA--TMYWNNRAKSRDTFqgeWTRSGDK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 496 WVHGDwviyDGeQYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHvtfTGELK 575
Cdd:TIGR02262 392 YVRND----DG-SYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPG---QTALE 463
|
490 500 510
....*....|....*....|....*....|....*.
gi 446729146 576 KELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:TIGR02262 464 TELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
101-618 |
1.99e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 163.56 E-value: 1.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:PRK08316 28 TALVFGDR-----SWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 181 RVQAAGSKMIITADGFSRRgkivsLKDEVDKACEHCPTVEKVVIVRHAGNDFTPHNydfSWstLEKEKPFIHAEEMQSDD 260
Cdd:PRK08316 103 ILDHSGARAFLVDPALAPT-----AEAALALLPVDTLILSLVLGGREAPGGWLDFA---DW--AEAGSVAEPDVELADDD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 261 PLMLIYTSGTTGKPKGTVHTHAGFP---LKAAFDAGfgmnIKQGDRVLWV------TDMGWMMGPFLLFGslingATMVM 331
Cdd:PRK08316 173 LAQILYTSGTESLPKGAMLTHRALIaeyVSCIVAGD----MSADDIPLHAlplyhcAQLDVFLGPYLYVG-----ATNVI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 332 YEGvpdfPEADRLWETVDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSL------------EVFASTGEPWnPDPWMW 399
Cdd:PRK08316 244 LDA----PDPELILRTIEAERITSFFAPPTVWISLLRHPD--FDTRDLSSLrkgyygasimpvEVLKELRERL-PGLRFY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 400 lfetvgkgnvpicNYSGGTEIsgGIFGNVLiKP----IAPISfnASLPG--MAAVVLDDQGKPI-RDEVGELCLEKPWVg 472
Cdd:PRK08316 317 -------------NCYGQTEI--APLATVL-GPeehlRRPGS--AGRPVlnVETRVVDDDGNDVaPGEVGEIVHRSPQL- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 473 MTkSFWEDDERYVNTywsrFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVP 550
Cdd:PRK08316 378 ML-GYWDDPEKTAEA----FRGGWFHsGDLGVMDEEGYItVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLP 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446729146 551 DEVKGEVCHCFVVLRDHVTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAY 618
Cdd:PRK08316 453 DPKWIEAVTAVVVPKAGATVTED---ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERY 517
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
115-615 |
2.96e-43 |
|
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: 160.92 E-value: 2.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 115 FTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITad 194
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 195 gfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihaeemqsdDPLMLIYTSGTTGKP 274
Cdd:cd05934 82 -----------------------------------------------------------------DPASILYTSGTTGPP 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 275 KGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWV--------TDMGWMmgpfllfGSLINGATMVMyegVPDFpEADRLWE 346
Cdd:cd05934 97 KGVVITHANL-TFAGYYSARRFGLGEDDVYLTVlplfhinaQAVSVL-------AALSVGATLVL---LPRF-SASRFWS 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 347 TVDKYEITHLGISPTLIRALMAKGD-EYVNKHSLKslEVFAStgePWNPDPWMWLFETVGkgnVPICNYSGGTEISGGIF 425
Cdd:cd05934 165 DVRRYGATVTNYLGAMLSYLLAQPPsPDDRAHRLR--AAYGA---PNPPELHEEFEERFG---VRLLEGYGMTETIVGVI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 426 GNVlIKPIAPISFNASLPGMAAVVLDDQGKPIRD-EVGELCL--EKPWvGMTKSFWEDDERYVntywSRFENKWVH-GDW 501
Cdd:cd05934 237 GPR-DEPRRPGSIGRPAPGYEVRIVDDDGQELPAgEPGELVIrgLRGW-GFFKGYYNMPEATA----EAMRNGWFHtGDL 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 502 VIYDGEQYII-TGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGElkkELMS 580
Cdd:cd05934 311 GYRDADGFFYfVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE---ELFA 387
|
490 500 510
....*....|....*....|....*....|....*
gi 446729146 581 LVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05934 388 FCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
115-613 |
5.04e-43 |
|
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: 160.43 E-value: 5.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 115 FTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQaagskmiitad 194
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVD----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 195 gfsRRGKIVSLKDEVDKAcehcptvekvvivrhagndftphnydfswstlekekpfihaeemqsDDPLMLIYTSGTTGKP 274
Cdd:cd05974 70 ---RGGAVYAAVDENTHA----------------------------------------------DDPMLLYFTSGTTSKP 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 275 KGTVHTHAGFPLkAAFDAGFGMNIKQGDRVLWVTDMGWMMGPF-LLFGSLINGATMVMYEgVPDFpEADRLWETVDKYEI 353
Cdd:cd05974 101 KLVEHTHRSYPV-GHLSTMYWIGLKPGDVHWNISSPGWAKHAWsCFFAPWNAGATVFLFN-YARF-DAKRVLAALVRYGV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 354 THLGISPTLIRALMakgDEYVNKHSLKSLEVFAStGEPWNPDpwmwLFETVGKG-NVPICNYSGGTEISGGIfGNVLIKP 432
Cdd:cd05974 178 TTLCAPPTVWRMLI---QQDLASFDVKLREVVGA-GEPLNPE----VIEQVRRAwGLTIRDGYGQTETTALV-GNSPGQP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 433 IAPISFNASLPGMAAVVLDDQGKPIRDevGELCLE----KPwVGMTKSFWEDDERyvnTYWSRFENKWVHGDWVIYDGEQ 508
Cdd:cd05974 249 VKAGSMGRPLPGYRVALLDPDGAPATE--GEVALDlgdtRP-VGLMKGYAGDPDK---TAHAMRGGYYRTGDIAMRDEDG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 509 YII-TGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGELKKELMslvnSHIG 587
Cdd:cd05974 323 YLTyVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIF----RFSR 398
|
490 500
....*....|....*....|....*....
gi 446729146 588 KALCP-KDIHVVE--DLPKTRNSKVmRRV 613
Cdd:cd05974 399 ERLAPyKRIRRLEfaELPKTISGKI-RRV 426
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
95-612 |
3.64e-40 |
|
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: 152.79 E-value: 3.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 95 EETRIQPALQYEGengtsKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFA 174
Cdd:cd05945 2 AANPDRPAVVEGG-----RTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 175 SDAVMTRVQAAGSKMIITADgfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihae 254
Cdd:cd05945 77 AERIREILDAAKPALLIADG------------------------------------------------------------ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 255 emqsDDPLMLIYTSGTTGKPKGTVHTHAGFplkAAF----DAGFgmNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMV 330
Cdd:cd05945 97 ----DDNAYIIFTSGSTGRPKGVQISHDNL---VSFtnwmLSDF--PLGPGDVFLNQAPFSFDLSVMDLYPALASGATLV 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 331 MyegVPDFPEAD--RLWETVDKYEITHLGISPTLIRalMAKGDEYVNKHSLKSLEVFASTGEPWnPDP----WMWLFEtv 404
Cdd:cd05945 168 P---VPRDATADpkQLFRFLAEHGITVWVSTPSFAA--MCLLSPTFTPESLPSLRHFLFCGEVL-PHKtaraLQQRFP-- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 405 gkgNVPICNYSGGTEISGGIFGNVLIKPIA------PISFnaSLPGMAAVVLDDQGKPIRD-EVGELCLEKPWVgmTKSF 477
Cdd:cd05945 240 ---DARIYNTYGPTEATVAVTYIEVTPEVLdgydrlPIGY--AKPGAKLVILDEDGRPVPPgEKGELVISGPSV--SKGY 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 478 WEDDERyVNTYWSRFENKWVH--GDWVIYDGE-QYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVK 554
Cdd:cd05945 313 LNNPEK-TAAAFFPDEGQRAYrtGDLVRLEADgLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEK 391
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 555 GEVCHCFVVLRDHVTF--TGELKKELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd05945 392 VTELIAFVVPKPGAEAglTKAIKAELAERLPPY----MIPRRFVYLDELPLNANGKIDRK 447
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
115-614 |
1.04e-39 |
|
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: 152.78 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 115 FTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITAD 194
Cdd:cd12119 26 YTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 195 GFSRRgkivslkdeVDKACEHCPTVEKVVIV---RHAGNDFTPHNYDFsWSTLEKEKPFIHAEEMQSDDPLMLIYTSGTT 271
Cdd:cd12119 106 DFLPL---------LEAIAPRLPTVEHVVVMtddAAMPEPAGVGVLAY-EELLAAESPEYDWPDFDENTAAAICYTSGTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 272 GKPKGTVHTHAGFPLKA----AFDagfGMNIKQGDRVLWVTDM----GWMMgPFLLFGSlinGATMVMyegvPD-FPEAD 342
Cdd:cd12119 176 GNPKGVVYSHRSLVLHAmaalLTD---GLGLSESDVVLPVVPMfhvnAWGL-PYAAAMV---GAKLVL----PGpYLDPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 343 RLWETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLEVFASTGEPWNPDpwmwLFETVGKGNVPICNYSGGTEISG 422
Cdd:cd12119 245 SLAELIEREGVTFAAGVPTVWQGLLDHLEA--NGRDLSSLRRVVIGGSAVPRS----LIEAFEERGVRVIHAWGMTETSP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 423 -GIFG---------------NVLIKPIAPIsfnaslPGMAAVVLDDQGKPI-RD--EVGELCLEKPWVgmTKSFWEDDER 483
Cdd:cd12119 319 lGTVArppsehsnlsedeqlALRAKQGRPV------PGVELRIVDDDGRELpWDgkAVGELQVRGPWV--TKSYYKNDEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 484 YVNTywsrFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCF 561
Cdd:cd12119 391 SEAL----TEDGWLRtGDVATIDEDGYLtITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAV 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446729146 562 VVLRDHVTFTgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVI 614
Cdd:cd12119 467 VVLKEGATVT---AEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
100-612 |
1.52e-39 |
|
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: 151.73 E-value: 1.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 100 QPALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM 179
Cdd:cd17651 11 APALVAEGR-----RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 180 TRVQAAGSKMIITADGFSRRGkivslkdevdkacehcpTVEKVVIVRHAgndftphnyDFSWSTLEKEKPFIhaeEMQSD 259
Cdd:cd17651 86 FMLADAGPVLVLTHPALAGEL-----------------AVELVAVTLLD---------QPGAAAGADAEPDP---ALDAD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 260 DPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFgMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMyegVPD-- 337
Cdd:cd17651 137 DLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARA-SSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVL---PPEev 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 338 FPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSlkSLEVFASTGEPWNPDPWMWLFeTVGKGNVPICNYSGG 417
Cdd:cd17651 213 RTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLA--ALRYLLTGGEQLVLTEDLREF-CAGLPGLRLHNHYGP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 418 TE---ISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGKPI-RDEVGELC----------LEKPwvGMTKsfweddER 483
Cdd:cd17651 290 TEthvVTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVpPGVPGELYiggaglargyLNRP--ELTA------ER 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 484 YVNTYWSRFENKWVHGDWVIY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHC 560
Cdd:cd17651 362 FVPDPFVPGARMYRTGDLARWlpDGElEFL--GRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVA 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446729146 561 FVVLR-DHVTFTGELKKELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd17651 440 YVVGDpEAPVDAAELRAALATHLPEY----MVPSAFVLLDALPLTPNGKLDRR 488
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
70-618 |
3.14e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 151.68 E-value: 3.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 70 TPFAQWYNGGT-CNVVESALSRWladeetRIQPALqYEGEngtsKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPM 148
Cdd:PRK06188 3 TMADLLHSGATyGHLLVSALKRY------PDRPAL-VLGD----TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 149 IPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADG-FSRRGkiVSLKdevdkacEHCPTVEKVVIVRH 227
Cdd:PRK06188 72 RPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDPApFVERA--LALL-------ARVPSLKHVLTLGP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 228 A--GNDFtphnydfsWSTLEKEKPFIHAEEMQSDDPLMLIYTSGTTGKPKGTVHTH---AGFP--LKAAFDagfgmnIKQ 300
Cdd:PRK06188 143 VpdGVDL--------LAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHrsiATMAqiQLAEWE------WPA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 301 GDRVLWVTDMGWMMGPFLLfGSLINGATMVMYEGvpdFpEADRLWETVDKYEITHLGISPTLIRALMAKGDeyVNKHSLK 380
Cdd:PRK06188 209 DPRFLMCTPLSHAGGAFFL-PTLLRGGTVIVLAK---F-DPAEVLRAIEEQRITATFLVPTMIYALLDHPD--LRTRDLS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 381 SLEVFASTGEPWNPDPWMWLFETVGkgnvPI-CNYSGGTEISGGIfgNVLIK----PIAPISFnAS----LPGMAAVVLD 451
Cdd:PRK06188 282 SLETVYYGASPMSPVRLAEAIERFG----PIfAQYYGQTEAPMVI--TYLRKrdhdPDDPKRL-TScgrpTPGLRVALLD 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 452 DQGKPI-RDEVGELCLEKPWVgmtksfwedderyVNTYWSR-------FENKWVH-GDWVIYDGEQYI-ITGRSDDTLNI 521
Cdd:PRK06188 355 EDGREVaQGEVGEICVRGPLV-------------MDGYWNRpeetaeaFRDGWLHtGDVAREDEDGFYyIVDRKKDMIVT 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 522 AGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGElkkELMSLVNSHIGKALCPKDIHVVEDL 601
Cdd:PRK06188 422 GGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAA---ELQAHVKERKGSVHAPKQVDFVDSL 498
|
570
....*....|....*..
gi 446729146 602 PKTRNSKVMRRVIKAAY 618
Cdd:PRK06188 499 PLTALGKPDKKALRARY 515
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
111-616 |
6.16e-38 |
|
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: 147.62 E-value: 6.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 111 TSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMI 190
Cdd:TIGR03098 22 HDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 191 ITAdgfSRRgkIVSLKDevdkACEHCPTVEKVVIV--RHAGNDFTPHNYDFSWSTLEKEKPFIHAEEMQSDDPLMLIYTS 268
Cdd:TIGR03098 102 VTS---SER--LDLLHP----ALPGCHDLRTLIIVgdPAHASEGHPGEEPASWPKLLALGDADPPHPVIDSDMAAILYTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 269 GTTGKPKGTVHTHAGFPLKAAFDAGFgMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYegvpDFPEADRLWETV 348
Cdd:TIGR03098 173 GSTGRPKGVVLSHRNLVAGAQSVATY-LENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLH----DYLLPRDVLKAL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 349 DKYEITHLGISPTLIrALMAKGDeyVNKHSLKSLEVFASTGepwnpdpwmwlfetvgkGNVPICNYS------------- 415
Cdd:TIGR03098 248 EKHGITGLAAVPPLW-AQLAQLD--WPESAAPSLRYLTNSG-----------------GAMPRATLSrlrsflpnarlfl 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 416 --GGTEisggIFGNVLIKPIA----PISFNASLPGMAAVVLDDQGK---PirDEVGELCLEKPWVgmTKSFWEDDERYVN 486
Cdd:TIGR03098 308 myGLTE----AFRSTYLPPEEvdrrPDSIGKAIPNAEVLVLREDGSecaP--GEEGELVHRGALV--AMGYWNDPEKTAE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 487 TY-----------------WSrfenkwvhGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIG 548
Cdd:TIGR03098 380 RFrplppfpgelhlpelavWS--------GDTVRRDEEGFLyFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFG 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446729146 549 VPDEVKGEVCHCFVVLRDHVTFTgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:TIGR03098 452 VPDPTLGQAIVLVVTPPGGEELD---RAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
101-612 |
1.05e-37 |
|
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: 146.28 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:cd12116 4 TAVRDDDR-----SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 181 RVQAAGSKMIITADgfsrrgkivslkDEVDKACEHCPTVEKVVIVRHAGndftPHNYDfswstlekekpfihaEEMQSDD 260
Cdd:cd12116 79 ILEDAEPALVLTDD------------ALPDRLPAGLPVLLLALAAAAAA----PAAPR---------------TPVSPDD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 261 PLMLIYTSGTTGKPKGTVHTHAGFplkAAFDAGFG--MNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGvPDF 338
Cdd:cd12116 128 LAYVIYTSGSTGRPKGVVVSHRNL---VNFLHSMRerLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPR-ETQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 339 PEADRLWETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLevfaSTGEPWNPDPWMWLFETVGKgnvpICNYSGGT 418
Cdd:cd12116 204 RDPEALARLIEAHSITVMQATPATWRMLLDAGWQ--GRAGLTAL----CGGEALPPDLAARLLSRVGS----LWNLYGPT 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 419 EISggIFGNV--LIKPIAPISFNASLPGMAAVVLDDQGKPI-RDEVGELCLEKPwvGMTKSFWED----DERYV-NTYWS 490
Cdd:cd12116 274 ETT--IWSTAarVTAAAGPIPIGRPLANTQVYVLDAALRPVpPGVPGELYIGGD--GVAQGYLGRpaltAERFVpDPFAG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 491 RFENKWVHGDWVIYDGE---QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVChCFVVLRDH 567
Cdd:cd12116 350 PGSRLYRTGDLVRRRADgrlEYL--GRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKAG 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446729146 568 VTF-TGELKKELmslvNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd12116 427 AAPdAAALRAHL----RATLPAYMVPSAFVRLDALPLTANGKLDRK 468
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
101-612 |
4.46e-37 |
|
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: 144.65 E-value: 4.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:cd12117 14 VAVVYGDR-----SLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 181 RVQAAGSKMIITADGFSRRgkivslkdevdkACEHCPTVEkvvivrhagndftphnYDFSWSTLEKEKPfihAEEMQSDD 260
Cdd:cd12117 89 MLADAGAKVLLTDRSLAGR------------AGGLEVAVV----------------IDEALDAGPAGNP---AVPVSPDD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 261 PLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFgMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEgvPDFPE 340
Cdd:cd12117 138 LAYVMYTSGSTGRPKGVAVTHRGV-VRLVKNTNY-VTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAP--KGTLL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 341 -ADRLWETVDKYEITHLGISPTLIRALMakgDEYVNkhSLKSLEVFASTGEPWNPdPWM--WLfETVGKGNVPICnYsGG 417
Cdd:cd12117 214 dPDALGALIAEEGVTVLWLTAALFNQLA---DEDPE--CFAGLRELLTGGEVVSP-PHVrrVL-AACPGLRLVNG-Y-GP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 418 TE---------ISGGIF--GNVLI-KPIApisfnaslpGMAAVVLDDQGKPIR-DEVGELCLEKPwvGMTKSFWED---- 480
Cdd:cd12117 285 TEnttfttshvVTELDEvaGSIPIgRPIA---------NTRVYVLDEDGRPVPpGVPGELYVGGD--GLALGYLNRpalt 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 481 DERYVNTYWSRFENKWVHGDWVIY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDE-VKGE 556
Cdd:cd12117 354 AERFVADPFGPGERLYRTGDLARWlpDGRlEFL--GRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAgGDKR 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 557 VChCFVVLRDHVTfTGELKKelmslvnsHIGKAL----CPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd12117 432 LV-AYVVAEGALD-AAELRA--------FLRERLpaymVPAAFVVLDELPLTANGKVDRR 481
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
101-609 |
7.63e-37 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 145.20 E-value: 7.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PAL-QYEGENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM 179
Cdd:PRK13295 41 TAVtAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 180 TRVQAAGSKMII---TADGFSRRGKIVSLKDEVdkacehcPTVEKVVIVRHAG-NDFTPHNYDFSWSTLEKEKPFIHAEE 255
Cdd:PRK13295 121 FMLKHAESKVLVvpkTFRGFDHAAMARRLRPEL-------PALRHVVVVGGDGaDSFEALLITPAWEQEPDAPAILARLR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 256 MQSDDPLMLIYTSGTTGKPKGTVHTH-----AGFPLKAAFDAGfgmnikQGDRVLWVTDM----GWMMG---PFLLfgsl 323
Cdd:PRK13295 194 PGPDDVTQLIYTSGTTGEPKGVMHTAntlmaNIVPYAERLGLG------ADDVILMASPMahqtGFMYGlmmPVML---- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 324 inGATMVMYegvpDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLEVFASTGEPWnPDPwmwLFET 403
Cdd:PRK13295 264 --GATAVLQ----DIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKE--SGRPVSSLRTFLCAGAPI-PGA---LVER 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 404 VGKG-NVPICNYSGGTE---ISGGIFGNVLIKPIAPISFnaSLPGMAAVVLDDQGKPI-RDEVGEL----C------LEK 468
Cdd:PRK13295 332 ARAAlGAKIVSAWGMTEngaVTLTKLDDPDERASTTDGC--PLPGVEVRVVDADGAPLpAGQIGRLqvrgCsnfggyLKR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 469 P-WVGMtksfweDDERYVNTywsrfenkwvhGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAA 546
Cdd:PRK13295 410 PqLNGT------DADGWFDT-----------GDLARIDADGYIrISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAI 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446729146 547 IGVPDEVKGEVCHCFVVLRDHVTFTGELKKELmsLVNSHIGKALCPKDIHVVEDLPKTRNSKV 609
Cdd:PRK13295 473 VAYPDERLGERACAFVVPRPGQSLDFEEMVEF--LKAQKVAKQYIPERLVVRDALPRTPSGKI 533
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
114-617 |
9.37e-37 |
|
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: 144.52 E-value: 9.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 114 SFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIisPIFSGFAS-----DAVMTRVQAAGsk 188
Cdd:COG1021 50 RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--PVFALPAHrraeiSHFAEQSEAVA-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 189 mIITAD---GFSRRGkivsLKDEVdkaCEHCPTVEKVVIVRHAGnDFTphnydfSWSTLEKEKPFIHAEEMQSDDPLMLI 265
Cdd:COG1021 126 -YIIPDrhrGFDYRA----LAREL---QAEVPSLRHVLVVGDAG-EFT------SLDALLAAPADLSEPRPDPDDVAFFQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 266 YTSGTTGKPKGTVHTHA--GFPLKAAFDAgfgMNIKQGDRVLWVTDMG--WMMGPFLLFGSLINGATMVMyegVPDfPEA 341
Cdd:COG1021 191 LSGGTTGLPKLIPRTHDdyLYSVRASAEI---CGLDADTVYLAALPAAhnFPLSSPGVLGVLYAGGTVVL---APD-PSP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 342 DRLWETVDKYEITHLGISPTLIRALMAKGDEYvnKHSLKSLEVFASTGEPWNP--------------------------- 394
Cdd:COG1021 264 DTAFPLIERERVTVTALVPPLALLWLDAAERS--RYDLSSLRVLQVGGAKLSPelarrvrpalgctlqqvfgmaeglvny 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 395 ----DPWMWLFETVGKgnvPICNYSggtEISggifgnvlikpiapisfnaslpgmaavVLDDQGKPIRD-EVGELCLEKP 469
Cdd:COG1021 342 trldDPEEVILTTQGR---PISPDD---EVR---------------------------IVDEDGNPVPPgEVGELLTRGP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 470 WvgmT------------KSFweDDERYvntYWSrfenkwvhGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILV 536
Cdd:COG1021 389 Y---TirgyyrapehnaRAF--TPDGF---YRT--------GDLVRRTPDGYLvVEGRAKDQINRGGEKIAAEEVENLLL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 537 KHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGELKKELMSLvnsHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:COG1021 453 AHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPLTLAELRRFLRER---GLAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
|
.
gi 446729146 617 A 617
Cdd:COG1021 530 A 530
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
100-574 |
2.52e-36 |
|
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: 146.54 E-value: 2.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 100 QPALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASD--A 177
Cdd:COG1020 492 AVAVVFGDQ-----SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAErlA 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 178 VMtrVQAAGSKMIITADgfsrrgkivSLKDEVDKACEHCPTVEKVVIVRHAGNDFTPhnydfswstlekekpfihaeEMQ 257
Cdd:COG1020 567 YM--LEDAGARLVLTQS---------ALAARLPELGVPVLALDALALAAEPATNPPV--------------------PVT 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 258 SDDPLMLIYTSGTTGKPKGTVHTHAGFP-LKAAFDAGFGMNikQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMY--EG 334
Cdd:COG1020 616 PDDLAYVIYTSGSTGRPKGVMVEHRALVnLLAWMQRRYGLG--PGDRVLQFASLSFDASVWEIFGALLSGATLVLAppEA 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 335 VPDfpeADRLWETVDKYEITHLGISPTLIRALMAKGDEyvnkhSLKSLEVFASTGEPWNPDPWMWLFETVgkGNVPICN- 413
Cdd:COG1020 694 RRD---PAALAELLARHRVTVLNLTPSLLRALLDAAPE-----ALPSLRLVLVGGEALPPELVRRWRARL--PGARLVNl 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 414 YsGGTEISggIFgnVLIKPIAPISFNAS-------LPGMAAVVLDDQGKPIRDEV-GELC----------LEKPwvGMTK 475
Cdd:COG1020 764 Y-GPTETT--VD--STYYEVTPPDADGGsvpigrpIANTRVYVLDAHLQPVPVGVpGELYiggaglargyLNRP--ELTA 836
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 476 S------FWEDDERYVNTywsrfenkwvhGDWVIY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAA 546
Cdd:COG1020 837 ErfvadpFGFPGARLYRT-----------GDLARWlpDGNlEFL--GRADDQVKIRGFRIELGEIEAALLQHPGVREAVV 903
|
490 500
....*....|....*....|....*...
gi 446729146 547 IGVPDEVKGEVCHCFVVLRDHVTFTGEL 574
Cdd:COG1020 904 VAREDAPGDKRLVAYVVPEAGAAAAAAL 931
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
82-615 |
5.47e-36 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 142.13 E-value: 5.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 82 NVVESALSRWLADEETRI---QPALQYEGENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLA 158
Cdd:PRK08008 2 DIVGGQHLRQMWDDLADVyghKTALIFESSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 159 VMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSrrGKIVSLKDEVDKACEHcptvekVVIVRHAGNDFTP-HNY 237
Cdd:PRK08008 82 LAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFY--PMYRQIQQEDATPLRH------ICLTRVALPADDGvSSF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 238 DfswsTLEKEKP--FIHAEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLwvtdmgWMMG 315
Cdd:PRK08008 154 T----QLKAQQPatLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNL-RFAGYYSAWQCALRDDDVYL------TVMP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 316 PF-------LLFGSLINGATMVMYEGVpdfpEADRLWETVDKYEITHLGISPTLIRALM---AKGDEyvNKHSLKSLEVF 385
Cdd:PRK08008 223 AFhidcqctAAMAAFSAGATFVLLEKY----SARAFWGQVCKYRATITECIPMMIRTLMvqpPSAND--RQHCLREVMFY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 386 ASTGEPWNPDpwmwlFETvgKGNVPICNYSGGTEISGGIFGNvliKPIAPISF-NASLPGMA--AVVLDDQGKPI-RDEV 461
Cdd:PRK08008 297 LNLSDQEKDA-----FEE--RFGVRLLTSYGMTETIVGIIGD---RPGDKRRWpSIGRPGFCyeAEIRDDHNRPLpAGEI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 462 GELCLeKPWVGMT--KSFWEDDERYVNTYwsrFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVK 537
Cdd:PRK08008 367 GEICI-KGVPGKTifKEYYLDPKATAKVL---EADGWLHtGDTGYVDEEGFFyFVDRRCNMIKRGGENVSCVELENIIAT 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446729146 538 HNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:PRK08008 443 HPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
114-611 |
5.89e-36 |
|
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: 140.59 E-value: 5.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 114 SFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITA 193
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 194 DGFSRRgkivslkdevdkacehcptvekvvivRHAGndftphnydfswstlekekpfihaeemQSDDPLMLIYTSGTTGK 273
Cdd:cd05903 81 ERFRQF--------------------------DPAA---------------------------MPDAVALLLFTSGTTGE 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 274 PKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGpfllfgsLINGATMVMYEGVP----DFPEADRLWETVD 349
Cdd:cd05903 108 PKGVMHSHNTL-SASIRQYAERLGLGPGDVFLVASPMAHQTG-------FVYGFTLPLLLGAPvvlqDIWDPDKALALMR 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 350 KYEITHLGISPT----LIRALMAKGDEyvnkhsLKSLEVFASTGEPWNPDPWMWLFETVGkgnVPICNYSGGTEISGGIf 425
Cdd:cd05903 180 EHGVTFMMGATPfltdLLNAVEEAGEP------LSRLRTFVCGGATVPRSLARRAAELLG---AKVCSAYGSTECPGAV- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 426 gnVLIKPIAPISFNAS----LPGMAAVVLDDQGKPI-RDEVGELCLEKPWV--GMTK----SFWEDDERYVNTywsrfen 494
Cdd:cd05903 250 --TSITPAPEDRRLYTdgrpLPGVEIKVVDDTGATLaPGVEGELLSRGPSVflGYLDrpdlTADAAPEGWFRT------- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 495 kwvhGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGE 573
Cdd:cd05903 321 ----GDLARLDEDGYLrITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFD 396
|
490 500 510
....*....|....*....|....*....|....*...
gi 446729146 574 LKKELMSLVNshIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:cd05903 397 ELVAYLDRQG--VAKQYWPERLVHVDDLPRTPSGKVQK 432
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
114-611 |
1.07e-35 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 141.81 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 114 SFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITA 193
Cdd:PRK06087 49 SYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 194 DGFSRRG---KIVSLKDEVdkacehcPTVEKVVIVRHAGndftPHNYDFSWS-TLEKEKPFIHAEEMQSDDPLMLIYTSG 269
Cdd:PRK06087 129 TLFKQTRpvdLILPLQNQL-------PQLQQIVGVDKLA----PATSSLSLSqIIADYEPLTTAITTHGDELAAVLFTSG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 270 TTGKPKGTVHTHAGFPL-KAAFDAGFGMNikqgdrvlWvTDMGWMMGP------FL--LFGSLINGATMVMYEgvpDFpE 340
Cdd:PRK06087 198 TEGLPKGVMLTHNNILAsERAYCARLNLT--------W-QDVFMMPAPlghatgFLhgVTAPFLIGARSVLLD---IF-T 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 341 ADRLWETVDKYEIT-HLGISPtLIRALMAKGDEyvNKHSLKSLEVFASTGEPWNPDpwmwLFETVGKGNVPICNYSGGTE 419
Cdd:PRK06087 265 PDACLALLEQQRCTcMLGATP-FIYDLLNLLEK--QPADLSALRFFLCGGTTIPKK----VARECQQRGIKLLSVYGSTE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 420 ISGGIFgnvlIKPIAPISFNASLPGMAAV-----VLDDQGKPI-RDEVGELCLEKPWVGMtkSFWEDDERyvnTYWSRFE 493
Cdd:PRK06087 338 SSPHAV----VNLDDPLSRFMHTDGYAAAgveikVVDEARKTLpPGCEGEEASRGPNVFM--GYLDEPEL---TARALDE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 494 NKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTfT 571
Cdd:PRK06087 409 EGWYYsGDLCRMDEAGYIkITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHH-S 487
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446729146 572 GELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:PRK06087 488 LTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQK 527
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
115-615 |
1.60e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 141.45 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 115 FTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITAD 194
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICAD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 195 GFsRRGKIVSLKDEVDK----------ACEHCPTVEKVviVRHAGNDfTPHNydFSWSTLEKEKPFIHAEE-------MQ 257
Cdd:PRK12583 126 AF-KTSDYHAMLQELLPglaegqpgalACERLPELRGV--VSLAPAP-PPGF--LAWHELQARGETVSREAlaerqasLD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 258 SDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFdAGFGMNIKQGDRVLWVTDMGWMMGPFLL-FGSLINGATMVMyegvP 336
Cdd:PRK12583 200 RDDPINIQYTSGTTGFPKGATLSHHNILNNGYF-VAESLGLTEHDRLCVPVPLYHCFGMVLAnLGCMTVGACLVY----P 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 337 -DFPEADRLWETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKGNVPICnYs 415
Cdd:PRK12583 275 nEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQR--GNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIA-Y- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 416 GGTEISGGIFGNVLIKPIAP--ISFNASLPGMAAVVLDDQGKPI-RDEVGELCLEKPWVgmTKSFWEDDERyvnTYWSRF 492
Cdd:PRK12583 351 GMTETSPVSLQTTAADDLERrvETVGRTQPHLEVKVVDPDGATVpRGEIGELCTRGYSV--MKGYWNNPEA---TAESID 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 493 ENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTF 570
Cdd:PRK12583 426 EDGWMHtGDLATMDEQGYVrIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAA 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 446729146 571 TGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:PRK12583 506 SEE---ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
110-611 |
1.75e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 140.38 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 110 GTSKSFTYEELDNWVSRVANGLKHA-GIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSK 188
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 189 MIITADGFSrrGKIVSLKDEVdkacehcpTVEKVVIVRhagndftphnydfSWSTLEKEKPfIHAEEMQSDDPLMLIYTS 268
Cdd:PRK06839 103 VLFVEKTFQ--NMALSMQKVS--------YVQRVISIT-------------SLKEIEDRKI-DNFVEKNESASFIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 269 GTTGKPKGTVHTHAGFPLKAAFDAgFGMNIKQGDRVLWVTDMGWMMGPFLL-FGSLINGATMVmyegVPDFPEADRLWET 347
Cdd:PRK06839 159 GTTGKPKGAVLTQENMFWNALNNT-FAIDLTMHDRSIVLLPLFHIGGIGLFaFPTLFAGGVII----VPRKFEPTKALSM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 348 VDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFASTGEPWnPDPWMWLFETVGkgnVPICNYSGGTEISGGIFgn 427
Cdd:PRK06839 234 IEKHKVTVVMGVPTIHQALINCSK--FETTNLQSVRWFYNGGAPC-PEELMREFIDRG---FLFGQGFGMTETSPTVF-- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 428 VLIKPIA---PISFNASLPGMAAVVLDDQGKPI-RDEVGELCLEKPWVgmTKSFWEDDERYVNTywsrFENKWVH-GDWV 502
Cdd:PRK06839 306 MLSEEDArrkVGSIGKPVLFCDYELIDENKNKVeVGEVGELLIRGPNV--MKEYWNRPDATEET----IQDGWLCtGDLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 503 IYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTgelKKELMSL 581
Cdd:PRK06839 380 RVDEDGFVyIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLI---EKDVIEH 456
|
490 500 510
....*....|....*....|....*....|
gi 446729146 582 VNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:PRK06839 457 CRLFLAKYKIPKEIVFLKELPKNATGKIQK 486
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
114-614 |
4.99e-35 |
|
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: 137.61 E-value: 4.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 114 SFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIIta 193
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 194 dgfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfIHAEEmqsDDPLMLIYTSGTTGK 273
Cdd:cd05935 79 ---------------------------------------------------------VGSEL---DDLALIPYTSGTTGL 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 274 PKGTVHTHAGFPLKAAFDAgFGMNIKQGDRVL------WVTDM-GWMMGPfllfgsLINGATMVMYEGVpdfpEADRLWE 346
Cdd:cd05935 99 PKGCMHTHFSAAANALQSA-VWTGLTPSDVILaclplfHVTGFvGSLNTA------VYVGGTYVLMARW----DRETALE 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 347 TVDKYEITHLGISPTLIRALMAkgDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKGNVPIcnySGGTEISGGIFG 426
Cdd:cd05935 168 LIEKYKVTFWTNIPTMLVDLLA--TPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEG---YGLTETMSQTHT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 427 NvliKPIAPISFNASLP--GMAAVVLD-DQGKPIRD-EVGELCLEKPWV---------GMTKSFWEDD-ERYVNTywsrf 492
Cdd:cd05935 243 N---PPLRPKLQCLGIP*fGVDARVIDiETGRELPPnEVGEIVVRGPQIfkgywnrpeETEESFIEIKgRRFFRT----- 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 493 enkwvhGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHvtFT 571
Cdd:cd05935 315 ------GDLGYMDEEGYFfFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPE--YR 386
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446729146 572 GELKKE-LMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVI 614
Cdd:cd05935 387 GKVTEEdIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
113-614 |
1.20e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 139.01 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 113 KSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIIT 192
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 193 AD-GFSRRGKIVSlkdevdkacehCPTVEKVVIVRHAgnDFTPHN----YDFS-------------------WSTLEKEK 248
Cdd:PRK06710 128 LDlVFPRVTNVQS-----------ATKIEHVIVTRIA--DFLPFPknllYPFVqkkqsnlvvkvsesetihlWNSVEKEV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 249 PfiHAEEMQSD---DPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLwvtdMGWMmgPFL-LFG--- 321
Cdd:PRK06710 195 N--TGVEVPCDpenDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVV----LGVL--PFFhVYGmta 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 322 ----SLINGATMVMyegVPDFpEADRLWETVDKYEITHLGISPTLIRALMakGDEYVNKHSLKSLEVFASTGEPWnPDPW 397
Cdd:PRK06710 267 vmnlSIMQGYKMVL---IPKF-DMKMVFEAIKKHKVTLFPGAPTIYIALL--NSPLLKEYDISSIRACISGSAPL-PVEV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 398 MWLFETVGKGNVpICNYsGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLD-DQGKPIR-DEVGELCLEKPWVgmTK 475
Cdd:PRK06710 340 QEKFETVTGGKL-VEGY-GLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPpGEIGEIVVKGPQI--MK 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 476 SFWEDDERYVntywSRFENKWVHGDWVIYDGEQ--YIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEV 553
Cdd:PRK06710 416 GYWNKPEETA----AVLQDGWLHTGDVGYMDEDgfFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPY 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446729146 554 KGEVCHCFVVLRDHVTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVI 614
Cdd:PRK06710 492 RGETVKAFVVLKEGTECSEE---ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
113-626 |
2.76e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 137.09 E-value: 2.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 113 KSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIIT 192
Cdd:PRK07470 31 RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIC 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 193 ADGFSrrgkivslkDEVDKACEHCPTVEKVVIVrhAGNDFTPhnydfSWSTLEKEKPFIHAEEMQ--SDDPLMLIYTSGT 270
Cdd:PRK07470 111 HADFP---------EHAAAVRAASPDLTHVVAI--GGARAGL-----DYEALVARHLGARVANAAvdHDDPCWFFFTSGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 271 TGKPKGTVHTHAgfplKAAF-------DAGFGMNikQGDRVLWVTDMGWMMGPFLLFgSLINGATMVMYEGVP-DFPEAd 342
Cdd:PRK07470 175 TGRPKAAVLTHG----QMAFvitnhlaDLMPGTT--EQDASLVVAPLSHGAGIHQLC-QVARGAATVLLPSERfDPAEV- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 343 rlWETVDKYEITHLGISPTLIRALMAkgDEYVNKHSLKSLEVFASTGEP-WNPDPWMWLfETVGKGNVpicNYSGGTEIS 421
Cdd:PRK07470 247 --WALVERHRVTNLFTVPTILKMLVE--HPAVDRYDHSSLRYVIYAGAPmYRADQKRAL-AKLGKVLV---QYFGLGEVT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 422 GGIfgNVLikpiaPISFNASLP--------------GMAAVVLDDQGKPIR-DEVGELCLEKPWVGMtkSFWEDDEryVN 486
Cdd:PRK07470 319 GNI--TVL-----PPALHDAEDgpdarigtcgfertGMEVQIQDDEGRELPpGETGEICVIGPAVFA--GYYNNPE--AN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 487 TywSRFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVL 564
Cdd:PRK07470 388 A--KAFRDGWFRtGDLGHLDARGFLyITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVA 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446729146 565 RDHVTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELGDL 626
Cdd:PRK07470 466 RDGAPVDEA---ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEERGLLDL 524
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
111-615 |
4.08e-34 |
|
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: 136.89 E-value: 4.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 111 TSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMI 190
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 191 ITadgfSRRG--KIVSLKDEVdkacehcPTVEKVVIVrHAGNDFTPHNYDFSWSTLE-----KEKPFIHAEEMQSDDPLM 263
Cdd:cd17642 121 FC----SKKGlqKVLNVQKKL-------KIIKTIIIL-DSKEDYKGYQCLYTFITQNlppgfNEYDFKPPSFDRDEQVAL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 264 LIYTSGTTGKPKGTVHTHAGF--PLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMyegVPDFPEA 341
Cdd:cd17642 189 IMNSSGSTGLPKGVQLTHKNIvaRFSHARDPIFGNQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVL---MYKFEEE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 342 DRLwETVDKYEITHLGISPTLIrALMAKgDEYVNKHSLKSLEVFASTGEPWNPDpwmwLFETVGKG-NVP-ICNYSGGTE 419
Cdd:cd17642 266 LFL-RSLQDYKVQSALLVPTLF-AFFAK-STLVDKYDLSNLHEIASGGAPLSKE----VGEAVAKRfKLPgIRQGYGLTE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 420 ISGGIfgnvLIKP---IAPISFNASLPGMAAVVLD-DQGKPI-RDEVGELCLEKPwvGMTKSFWEDDEryvNTYWSRFEN 494
Cdd:cd17642 339 TTSAI----LITPegdDKPGAVGKVVPFFYAKVVDlDTGKTLgPNERGELCVKGP--MIMKGYVNNPE---ATKALIDKD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 495 KWVH-GDWVIYDGE-QYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTg 572
Cdd:cd17642 410 GWLHsGDIAYYDEDgHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMT- 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446729146 573 elKKELMSLVNSHIGKALCPK-DIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd17642 489 --EKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
115-616 |
1.07e-33 |
|
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: 134.73 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 115 FTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIItad 194
Cdd:cd12118 30 YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 195 gfsrrgkivslkdeVDKACEHcptvEKVVIvrhAGNDftphnyDFSWstlekEKPfihAEEmqsDDPLMLIYTSGTTGKP 274
Cdd:cd12118 107 --------------VDREFEY----EDLLA---EGDP------DFEW-----IPP---ADE---WDPIALNYTSGTTGRP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 275 KGTVHTHAGFPLkAAFDAGFGMNIKQGDRVLWVTDM----GWMmGPFLLFGsliNGATMVMYEGVpdfpEADRLWETVDK 350
Cdd:cd12118 149 KGVVYHHRGAYL-NALANILEWEMKQHPVYLWTLPMfhcnGWC-FPWTVAA---VGGTNVCLRKV----DAKAIYDLIEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 351 YEITHLGISPTLIRALmAKGDEYVNKHSLKSLEVFaSTGEPwnPDPWMwlFETVGKGNVPICNYSGGTEISGgifgnvli 430
Cdd:cd12118 220 HKVTHFCGAPTVLNML-ANAPPSDARPLPHRVHVM-TAGAP--PPAAV--LAKMEELGFDVTHVYGLTETYG-------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 431 kpiaPISFNASLPGMAAVVLDDQGKPI-RDEVGELCLEK------------PWVGMT------------KSFWEDDERyv 485
Cdd:cd12118 286 ----PATVCAWKPEWDELPTEERARLKaRQGVRYVGLEEvdvldpetmkpvPRDGKTigeivfrgnivmKGYLKNPEA-- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 486 nTYWSrFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVV 563
Cdd:cd12118 360 -TAEA-FRGGWFHsGDLAVIHPDGYIeIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVE 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446729146 564 LRDHVTFTGElkkELMSLVNSHIGKALCPKDIhVVEDLPKTRNSKVMRRVIKA 616
Cdd:cd12118 438 LKEGAKVTEE---EIIAFCREHLAGFMVPKTV-VFGELPKTSTGKIQKFVLRD 486
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
101-612 |
2.80e-33 |
|
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: 132.88 E-value: 2.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:cd17649 4 VALVFGDQ-----SLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 181 RVQAAGSKMIITADGfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihaeemqsDD 260
Cdd:cd17649 79 MLEDSGAGLLLTHHP---------------------------------------------------------------RQ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 261 PLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFgMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMyEGVPDFPE 340
Cdd:cd17649 96 LAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVL-RPDELWAS 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 341 ADRLWETVDKYEITHLGISPTLIRALMAKGDEyVNKHSLKSLEVFASTGEPWNPDPW-MWLfetvgKGNVPICNYSGGTE 419
Cdd:cd17649 174 ADELAEMVRELGVTVLDLPPAYLQQLAEEADR-TGDGRPPSLRLYIFGGEALSPELLrRWL-----KAPVRLFNAYGPTE 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 420 --ISGGIF----GNVLIKPIAPISfnASLPGMAAVVLDDQGKPI-RDEVGEL-----CL-----EKPwvGMTKsfweddE 482
Cdd:cd17649 248 atVTPLVWkceaGAARAGASMPIG--RPLGGRSAYILDADLNPVpVGVTGELyiggeGLargylGRP--ELTA------E 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 483 RYVNTYWSRFENKWVH-GDWVIY--DGeQYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCH 559
Cdd:cd17649 318 RFVPDPFGAPGSRLYRtGDLARWrdDG-VIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVA 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446729146 560 CfVVLRDHVTfTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd17649 397 Y-VVLRAAAA-QPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRK 447
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
112-615 |
3.89e-33 |
|
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: 132.43 E-value: 3.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 112 SKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMII 191
Cdd:cd17653 20 GGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 192 TADGfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihaeemqSDDPLMLIYTSGTT 271
Cdd:cd17653 100 TTDS--------------------------------------------------------------PDDLAYIIFTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 272 GKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEgvPDFPeadrlWETVDKy 351
Cdd:cd17653 118 GIPKGVMVPHRGV-LNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLAD--PSDP-----FAHVAR- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 352 EITHLGISPTLIRALmaKGDEYVNkhslksLEVFASTGEPWNP---DPWmwlfetvgKGNVPICNYSGGTEISGGIFgNV 428
Cdd:cd17653 189 TVDALMSTPSILSTL--SPQDFPN------LKTIFLGGEAVPPsllDRW--------SPGRRLYNAYGPTECTISST-MT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 429 LIKPIAPISFNASLPGMAAVVLDDQGKPI-RDEVGELCLEKPwvGMTKSFWEDDERYVntywSRF-ENKWVHGdWVIY-- 504
Cdd:cd17653 252 ELLPGQPVTIGKPIPNSTCYILDADLQPVpEGVVGEICISGV--QVARGYLGNPALTA----SKFvPDPFWPG-SRMYrt 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 505 --------DGEQYIItGRSDDTLNIAGKRIG-PAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDhvtftgeLK 575
Cdd:cd17653 325 gdygrwteDGGLEFL-GREDNQVKVRGFRINlEEIEEVVLQSQPEVTQAAAIVVNGRLVAFVTPETVDVDG-------LR 396
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446729146 576 KELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd17653 397 SELAKHLPSY----AVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
101-613 |
5.09e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 133.93 E-value: 5.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYEGengtsKSFTYEELDNWVSRVANGLKHA-GIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM 179
Cdd:PRK08314 27 TAIVFYG-----RAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 180 TRVQAAGSKMIITADgfsrrgkivSLKDEVDKAceHCPTVEKVVIVRHAGNDFTPHNYDF--SWSTLEKEKPFIHAE--- 254
Cdd:PRK08314 102 HYVTDSGARVAIVGS---------ELAPKVAPA--VGNLRLRHVIVAQYSDYLPAEPEIAvpAWLRAEPPLQALAPGgvv 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 255 ---------------EMQSDDPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVL------WVTDM-GW 312
Cdd:PRK08314 171 awkealaaglappphTAGPDDLAVLPYTSGTTGVPKGCMHTHRTV-MANAVGSVLWSNSTPESVVLavlplfHVTGMvHS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 313 MMGPfllfgsLINGATMVMyegvpdFPEADR--LWETVDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFASTGE 390
Cdd:PRK08314 250 MNAP------IYAGATVVL------MPRWDReaAARLIERYRVTHWTNIPTMVVDFLASPG--LAERDLSSLRYIGGGGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 391 PwnpdpwM------WLFETVGkgnVPICNYSGGTEISGGIFGNVLIKP------IApiSFNASlpgmAAVVLDDQGKPI- 457
Cdd:PRK08314 316 A------MpeavaeRLKELTG---LDYVEGYGLTETMAQTHSNPPDRPklqclgIP--TFGVD----ARVIDPETLEELp 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 458 RDEVGELCLEKPWV---------GMTKSFWE-DDERYVNTywsrfenkwvhGDWVIYDGEQY-IITGRSDDTLNIAGKRI 526
Cdd:PRK08314 381 PGEVGEIVVHGPQVfkgywnrpeATAEAFIEiDGKRFFRT-----------GDLGRMDEEGYfFITDRLKRMINASGFKV 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 527 GPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGElKKELMSLVNSHIGKALCPKDIHVVEDLPKTRN 606
Cdd:PRK08314 450 WPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTT-EEEIIAWAREHMAAYKYPRIVEFVDSLPKSGS 528
|
....*..
gi 446729146 607 SKVMRRV 613
Cdd:PRK08314 529 GKILWRQ 535
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
100-618 |
9.39e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 132.98 E-value: 9.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 100 QPALQYEGengtsKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM 179
Cdd:PRK07786 33 APALRFLG-----NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 180 TRVQAAGSKMIITADgfsrrgKIVSLKDEVDKAcehCPTVEKVVIVRHAGNDFTphnydFSWSTLEKEKPFIHAE-EMQS 258
Cdd:PRK07786 108 FLVSDCGAHVVVTEA------ALAPVATAVRDI---VPLLSTVVVAGGSSDDSV-----LGYEDLLAEAGPAHAPvDIPN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 259 DDPLMLIYTSGTTGKPKGTVHTHAGFplkaafdAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYeGVPD- 337
Cdd:PRK07786 174 DSPALIMYTSGTTGRPKGAVLTHANL-------TGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLL-GAPTv 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 338 -FP----EADRLWETVDKYEITHLGISPTLIRALMAkgDEYVNKHSLKsLEVFASTGEPWNPDPWMWLFETVGKGNvpIC 412
Cdd:PRK07786 246 iYPlgafDPGQLLDVLEAEKVTGIFLVPAQWQAVCA--EQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQ--IL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 413 NYSGGTEISG---GIFGNVLIKPIApiSFNASLPGMAAVVLDDQGKPI-RDEVGELCLEKPwvGMTKSFWEDDERYVNTy 488
Cdd:PRK07786 321 AAFGQTEMSPvtcMLLGEDAIRKLG--SVGKVIPTVAARVVDENMNDVpVGEVGEIVYRAP--TLMSGYWNNPEATAEA- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 489 wsrFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRD 566
Cdd:PRK07786 396 ---FAGGWFHsGDLVRQDEEGYVwVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRN 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446729146 567 HvtfTGELK-KELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAY 618
Cdd:PRK07786 473 D---DAALTlEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERY 522
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
108-616 |
1.08e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 132.74 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 108 ENGTsksFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGS 187
Cdd:PRK07788 71 ERGT---LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 188 KMIITADGFSRRgkIVSLKDEVDKAcehcptvekVVIVRHAGNDFTPhnyDFSWSTLEKekpFIHAEemqSDDPL----- 262
Cdd:PRK07788 148 KALVYDDEFTDL--LSALPPDLGRL---------RAWGGNPDDDEPS---GSTDETLDD---LIAGS---STAPLpkppk 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 263 ---MLIYTSGTTGKPKGTVHTHagfPLKAAFDAGFGmnikqgDRVLWVTDM----------GWMMGPFLLfgSLINGATM 329
Cdd:PRK07788 208 pggIVILTSGTTGTPKGAPRPE---PSPLAPLAGLL------SRVPFRAGEttllpapmfhATGWAHLTL--AMALGSTV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 330 VMYEgvpDF-PEAdrLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPdpwmWLFETVGK-- 406
Cdd:PRK07788 277 VLRR---RFdPEA--TLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSP----ELATRALEaf 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 407 GNVpICNYSGGTEISggiFGNVlIKP----IAPISFNASLPGMAAVVLDDQGKPI-RDEVGELclekpWVGMTKSFwedd 481
Cdd:PRK07788 348 GPV-LYNLYGSTEVA---FATI-ATPedlaEAPGTVGRPPKGVTVKILDENGNEVpRGVVGRI-----FVGNGFPF---- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 482 ERYVNTYWSRFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCH 559
Cdd:PRK07788 414 EGYTDGRDKQIIDGLLSsGDVGYFDEDGLLfVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLR 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 446729146 560 CFVVLRDHVTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:PRK07788 494 AFVVKAPGAALDED---AIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
100-620 |
5.06e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 130.01 E-value: 5.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 100 QPALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM 179
Cdd:PRK06145 18 RAALVYRDQ-----EISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 180 TRVQAAGSKMIITADGFsrrgkivslkdEVDKACEHcptvEKVVIVRHAGNDFT----PHnydfswstlekeKPFIHAEE 255
Cdd:PRK06145 93 YILGDAGAKLLLVDEEF-----------DAIVALET----PKIVIDAAAQADSRrlaqGG------------LEIPPQAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 256 MQSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAaFDAGFGMNIKQGDRVLWVtdmgwmmGPFLLFGSLINGATMVMYEG- 334
Cdd:PRK06145 146 VAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKS-IDHVIALGLTASERLLVV-------GPLYHVGAFDLPGIAVLWVGg 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 335 ----VPDFpEADRLWETVDKYEITHLGISPTLIRALMAKGDEYvnKHSLKSLEVFASTGEPwNPDPWMWLFETVGKGNVP 410
Cdd:PRK06145 218 tlriHREF-DPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRD--RFDLDSLAWCIGGGEK-TPESRIRDFTRVFTRARY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 411 ICNYsGGTEISGGifgNVLI---KPIAPI-SFNASLPGMAAVVLDDQGKPIRDEV-GELCLEKPWVgmTKSFWEDDERYV 485
Cdd:PRK06145 294 IDAY-GLTETCSG---DTLMeagREIEKIgSTGRALAHVEIRIADGAGRWLPPNMkGEICMRGPKV--TKGYWKDPEKTA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 486 NTywsrFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVV 563
Cdd:PRK06145 368 EA----FYGDWFRsGDVGYLDEEGFLyLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVV 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 446729146 564 LRDHVTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLG 620
Cdd:PRK06145 444 LNPGATLTLE---ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELNG 497
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
101-612 |
1.21e-31 |
|
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: 128.19 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:cd17643 4 VAVVDEDR-----RLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 181 RVQAAGSKMIITadgfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihaeemQSDD 260
Cdd:cd17643 79 ILADSGPSLLLT----------------------------------------------------------------DPDD 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 261 PLMLIYTSGTTGKPKGTVHTHAGF-PLKAAFDAGFGMNikQGDRVLWVTDMG-----WMMgpfllFGSLINGATMVMyeg 334
Cdd:cd17643 95 LAYVIYTSGSTGRPKGVVVSHANVlALFAATQRWFGFN--EDDVWTLFHSYAfdfsvWEI-----WGALLHGGRLVV--- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 335 VPdfPEADR----LWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFAstGEPWNPD---PWmwlFETVGKG 407
Cdd:cd17643 165 VP--YEVARspedFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFG--GEALEAAmlrPW---AGRFGLD 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 408 NVPICNYSGGTEISggIFgnVLIKPIAPISFNAS--------LPGMAAVVLDDQGKPI-RDEVGELCLEKPWV------- 471
Cdd:cd17643 238 RPQLVNMYGITETT--VH--VTFRPLDAADLPAAaaspigrpLPGLRVYVLDADGRPVpPGVVGELYVSGAGVargylgr 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 472 -GMTKS------FWEDDERYVNTywsrfenkwvhGDWVIY--DGEqYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVI 542
Cdd:cd17643 314 pELTAErfvanpFGGPGSRMYRT-----------GDLARRlpDGE-LEYLGRADEQVKIRGFRIELGEIEAALATHPSVR 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446729146 543 EAAAIGVPDEVKGEVCHCFVVLRDHVTFT-GELKKELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd17643 382 DAAVIVREDEPGDTRLVAYVVADDGAAADiAELRALLKELLPDY----MVPARYVPLDALPLTVNGKLDRA 448
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
101-612 |
1.28e-31 |
|
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: 128.93 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:cd17646 15 PAVVDEGR-----TLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 181 RVQAAGSKMIITADGFSRRGkivslkdevdkACEHCPTVekVVIVRHAGNDFTPHnydfswstlekekpfihAEEMQSDD 260
Cdd:cd17646 90 MLADAGPAVVLTTADLAARL-----------PAGGDVAL--LGDEALAAPPATPP-----------------LVPPRPDN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 261 PLMLIYTSGTTGKPKGTVHTHAGFP-----LKAAFDAGfgmnikQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEgv 335
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHAGIVnrllwMQDEYPLG------PGDRVLQKTPLSFDVSVWELFWPLVAGARLVVAR-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 336 pdfPEADR----LWETVDKYEITHLGISPTLIRALMAKGDeyvnKHSLKSLEVFASTGEPWNPDPWMWLFETVGkgnVPI 411
Cdd:cd17646 212 ---PGGHRdpayLAALIREHGVTTCHFVPSMLRVFLAEPA----AGSCASLRRVFCSGEALPPELAARFLALPG---AEL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 412 CNYSGGTEISGGI-----FGNVLIKPIaPISfnASLPGMAAVVLDDQGKPIRDEV-GELCLEKPWV--------GMTKsf 477
Cdd:cd17646 282 HNLYGPTEAAIDVthwpvRGPAETPSV-PIG--RPVPNTRLYVLDDALRPVPVGVpGELYLGGVQLargylgrpALTA-- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 478 weddERYVntywsrfENKWVHGDWViY----------DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAA 546
Cdd:cd17646 357 ----ERFV-------PDPFGPGSRM-YrtgdlarwrpDGAlEFL--GRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVV 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446729146 547 IGVPDEVKGEVCHCFVVLRDhvTFTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd17646 423 VARAAPAGAARLVGYVVPAA--GAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRA 486
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
114-616 |
1.66e-31 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 129.11 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 114 SFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITA 193
Cdd:PRK13382 68 TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 194 DGFSrrgkivslkDEVDKACEHCPTVEKVVivrhagnDFTPHNYDfswSTLEKekpFIHAEEMQSDDPL-----MLIYTS 268
Cdd:PRK13382 148 EEFS---------ATVDRALADCPQATRIV-------AWTDEDHD---LTVEV---LIAAHAGQRPEPTgrkgrVILLTS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 269 GTTGKPKGTVHTHAG--FPLKAAFDAgfgMNIKQGDRVLWVTDM--GWMMGPFLLFGSLINgaTMVMYEgvpDF-PEADr 343
Cdd:PRK13382 206 GTTGTPKGARRSGPGgiGTLKAILDR---TPWRAEEPTVIVAPMfhAWGFSQLVLAASLAC--TIVTRR---RFdPEAT- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 344 lWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGkgNVPICNYsGGTEISgg 423
Cdd:PRK13382 277 -LDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFG--DVIYNNY-NATEAG-- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 424 ifgnvLIKPIAPISF-----NASLPGMAAV--VLDDQGKPIRD-EVGELclekpWV-----------GMTKSFwedDERY 484
Cdd:PRK13382 351 -----MIATATPADLraapdTAGRPAEGTEirILDQDFREVPTgEVGTI-----FVrndtqfdgytsGSTKDF---HDGF 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 485 VNTywsrfenkwvhGDWVIYDGE-QYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVV 563
Cdd:PRK13382 418 MAS-----------GDVGYLDENgRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVV 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446729146 564 LRDHVTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:PRK13382 487 LKPGASATPE---TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
114-616 |
2.12e-31 |
|
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: 126.69 E-value: 2.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 114 SFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIfsgfasdavmtrvqaagskmiita 193
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLL------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 194 dgfSRRGKIVSLKDEVDKAcehcptvekvvivrhagndftphnydfswstlekekpfihaeEMQSDDPLMLIYTSGTTGK 273
Cdd:cd05912 57 ---NTRLTPNELAFQLKDS------------------------------------------DVKLDDIATIMYTSGTTGK 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 274 PKGTVHThAGFPLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEgvpDFpEADRLWETVDKYEI 353
Cdd:cd05912 92 PKGVQQT-FGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRSVIYGMTVYLVD---KF-DAEQVLHLINSGKV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 354 THLGISPTLIRALMAKGDEYVNKHslksLEVFASTGEPWNPDpwmwLFETVGKGNVPICNYSGGTEISGGIfgnvlikpi 433
Cdd:cd05912 167 TIISVVPTMLQRLLEILGEGYPNN----LRCILLGGGPAPKP----LLEQCKEKGIPVYQSYGMTETCSQI--------- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 434 apISFNaslPGMAAVVLDDQGKP-------IRD------EVGELCLEKPWVgmTKSFWEDDERyvnTYWSrFENKWVH-G 499
Cdd:cd05912 230 --VTLS---PEDALNKIGSAGKPlfpvelkIEDdgqppyEVGEILLKGPNV--TKGYLNRPDA---TEES-FENGWFKtG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 500 D--WVIYDGEQYIITGRSDdtLNIAG-KRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTftgelKK 576
Cdd:cd05912 299 DigYLDEEGFLYVLDRRSD--LIISGgENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPIS-----EE 371
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446729146 577 ELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:cd05912 372 ELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
110-621 |
2.55e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 128.10 E-value: 2.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 110 GTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKM 189
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 190 IITADGFSrrgkivslkDEVDKACEHCPT-VEKVVIVRHAGNDFTPhnydfswstlekekpFIHAEEMQSDDPL------ 262
Cdd:PRK08276 87 LIVSAALA---------DTAAELAAELPAgVPLLLVVAGPVPGFRS---------------YEEALAAQPDTPIadetag 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 263 -MLIYTSGTTGKPKGT------VHTHAGfPLKAAFDAGFGMNIKQGDRVLwvtdmgwMMGPF-----LLFG--SLINGAT 328
Cdd:PRK08276 143 aDMLYSSGTTGRPKGIkrplpgLDPDEA-PGMMLALLGFGMYGGPDSVYL-------SPAPLyhtapLRFGmsALALGGT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 329 MVMYEGvpdFpEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGkgn 408
Cdd:PRK08276 215 VVVMEK---F-DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWG--- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 409 vPICN-YSGGTEISGGIFGNV---LIKPiapisFNASLPGMAAV-VLDDQGKPI-RDEVGELCLEKPwvGMTKSFWEDDE 482
Cdd:PRK08276 288 -PIIHeYYASSEGGGVTVITSedwLAHP-----GSVGKAVLGEVrILDEDGNELpPGEIGTVYFEMD--GYPFEYHNDPE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 483 RyvnTYWSRFENKWVH-GD--WVIYDGEQYIiTGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCH 559
Cdd:PRK08276 360 K---TAAARNPHGWVTvGDvgYLDEDGYLYL-TDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVK 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446729146 560 CFVVLRDHVTFTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGK 621
Cdd:PRK08276 436 AVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEG 497
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
113-616 |
3.63e-31 |
|
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: 126.64 E-value: 3.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 113 KSFTYEELDNWVSRVANGLKHAG-IEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIfsgfasdavmtrvqaagskmii 191
Cdd:cd05941 10 DSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPL---------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 192 tadgfsrrgkivslkdevdkacehCPtvekvvivrhagnDFTPHNYDFswsTLEKEKPFIHAeemqsdDPLMLIYTSGTT 271
Cdd:cd05941 68 ------------------------NP-------------SYPLAELEY---VITDSEPSLVL------DPALILYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 272 GKPKGTVHTHA--GFPLKAAFDAgfgMNIKQGDRVLWVTDMGWMMGPFL-LFGSLINGATMVMyegVPDFpEADRLWETV 348
Cdd:cd05941 102 GRPKGVVLTHAnlAANVRALVDA---WRWTEDDVLLHVLPLHHVHGLVNaLLCPLFAGASVEF---LPKF-DPKEVAISR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 349 DKYEITHLGISPT----LIRA--LMAKGDEYVNKHSLKSLEVFASTGEPWnPDPWMWLFETVGkGNVPICNYsGGTEIsG 422
Cdd:cd05941 175 LMPSITVFMGVPTiytrLLQYyeAHFTDPQFARAAAAERLRLMVSGSAAL-PVPTLEEWEAIT-GHTLLERY-GMTEI-G 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 423 GIFGNVLIKPIAPISFNASLPGMAAVVLDDQGKPI--RDEVGELCLEKPwvGMTKSFWEDDERyvnTYWSRFENKW-VHG 499
Cdd:cd05941 251 MALSNPLDGERRPGTVGMPLPGVQARIVDEETGEPlpRGEVGEIQVRGP--SVFKEYWNKPEA---TKEEFTDDGWfKTG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 500 DWVIYDGE-QYIITGR-SDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRD--HVTFTGELK 575
Cdd:cd05941 326 DLGVVDEDgYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAgaAALSLEELK 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446729146 576 ---KELMSlvnshigKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:cd05941 406 ewaKQRLA-------PYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
116-608 |
7.05e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 127.31 E-value: 7.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADG 195
Cdd:PRK07798 30 TYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYERE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 196 FSrrGKIVSLKDEvdkacehCPTVEKVVIVRHA-GNDFTP--HNYDFSWSTLEKEKPFIhaeEMQSDDpLMLIYTSGTTG 272
Cdd:PRK07798 110 FA--PRVAEVLPR-------LPKLRTLVVVEDGsGNDLLPgaVDYEDALAAGSPERDFG---ERSPDD-LYLLYTGGTTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 273 KPKGTVHTHAGFpLKAAF---DAGFGMNIK----QGDRVLWVTDMGWMMGPFLL--------FGSLINGATMVMYEgVPD 337
Cdd:PRK07798 177 MPKGVMWRQEDI-FRVLLggrDFATGEPIEdeeeLAKRAAAGPGMRRFPAPPLMhgagqwaaFAALFSGQTVVLLP-DVR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 338 FpEADRLWETVDKYEITHLGI------SPtLIRALMAKGDeyvnkHSLKSLEVFASTGEPWNP---DPWMWLFEtvgkgN 408
Cdd:PRK07798 255 F-DADEVWRTIEREKVNVITIvgdamaRP-LLDALEARGP-----YDLSSLFAIASGGALFSPsvkEALLELLP-----N 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 409 VPICNYSGGTEisGGIFGNVLIKPIAPISFNASL-PGMAAVVLDDQGKPIR---DEVGelclekpWVGMT---------- 474
Cdd:PRK07798 323 VVLTDSIGSSE--TGFGGSGTVAKGAVHTGGPRFtIGPRTVVLDEDGNPVEpgsGEIG-------WIARRghiplgyykd 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 475 -----KSFWE-DDERYVntywsrfenkwVHGDW--VIYDGeqyIIT--GRSDDTLNIAGKRIGPAEYESILVKHNDVIEA 544
Cdd:PRK07798 394 pektaETFPTiDGVRYA-----------IPGDRarVEADG---TITllGRGSVCINTGGEKVFPEEVEEALKAHPDVADA 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446729146 545 AAIGVPDEVKGEVCHCFVVLRDHVTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSK 608
Cdd:PRK07798 460 LVVGVPDERWGQEVVAVVQLREGARPDLA---ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
116-612 |
9.00e-31 |
|
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: 126.23 E-value: 9.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITAdg 195
Cdd:cd12114 14 TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTD-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 196 fsrrgkivslkDEVDKACEHCPTVEKVVIVRHAGNDFTPhnydfswstlekekpfihAEEMQSDDPLMLIYTSGTTGKPK 275
Cdd:cd12114 92 -----------GPDAQLDVAVFDVLILDLDALAAPAPPP------------------PVDVAPDDLAYVIFTSGSTGTPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 276 GTVHTHAG-FPLKAAFDAGFGMNIKqgDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGVPDfPEADRLWETVDKYEIT 354
Cdd:cd12114 143 GVMISHRAaLNTILDINRRFAVGPD--DRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARR-RDPAHWAELIERHGVT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 355 HLGISPTLIRALMAKGdEYVNKHsLKSLEVFASTGEpW----NPDPWMWLFetvgkgnvPICNY---SGGTEisGGIFGN 427
Cdd:cd12114 220 LWNSVPALLEMLLDVL-EAAQAL-LPSLRLVLLSGD-WipldLPARLRALA--------PDARLislGGATE--ASIWSI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 428 VLikPIAP-------ISFNASLPGMAAVVLDDQGKPIRDEV-GELclekpW---VGMTKSFWED----DERYVN----TY 488
Cdd:cd12114 287 YH--PIDEvppdwrsIPYGRPLANQRYRVLDPRGRDCPDWVpGEL-----WiggRGVALGYLGDpeltAARFVThpdgER 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 489 WSRfenkwvHGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDevkGEVCH--CFVVLR 565
Cdd:cd12114 360 LYR------TGDLGRYRPDGTLeFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGD---PGGKRlaAFVVPD 430
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 446729146 566 DHVTFTGELkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd12114 431 NDGTPIAPD--ALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRA 475
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
69-609 |
2.14e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 126.31 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 69 GTPFAQWYNGGTCNVVESaLSRWLADEETRiqPALQYEGengtsKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPM 148
Cdd:PRK06178 21 GIPREPEYPHGERPLTEY-LRAWARERPQR--PAIIFYG-----HVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 149 IPETVVAMLAVMKIGAI---ISPIFSGFasdAVMTRVQAAGSKMIITADGFS------------RRGKIVSLKDEVDKAc 213
Cdd:PRK06178 93 CPQFHIVFFGILKLGAVhvpVSPLFREH---ELSYELNDAGAEVLLALDQLApvveqvraetslRHVIVTSLADVLPAE- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 214 ehcPTVEKVVIVR-----HAG-NDFTPHnydfswstLEKEKPFIHAEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGFPLK 287
Cdd:PRK06178 169 ---PTLPLPDSLRaprlaAAGaIDLLPA--------LRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 288 AAFDAGFGMNIKQGDRVLWVTDMGWMMGP-FLLFGSLINGATMVMYEGVpdfpEADRLWETVDKYEITHLGISPTLIRAL 366
Cdd:PRK06178 238 AAAAYAVAVVGGEDSVFLSFLPEFWIAGEnFGLLFPLFSGATLVLLARW----DAVAFMAAVERYRVTRTVMLVDNAVEL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 367 MAKGDeyVNKHSLKSLEVF--ASTGEPWNPD---PWMWLfetvgKGNVPICNYSGGTE------ISGGIFGNVLIKPIAP 435
Cdd:PRK06178 314 MDHPR--FAEYDLSSLRQVrvVSFVKKLNPDyrqRWRAL-----TGSVLAEAAWGMTEthtcdtFTAGFQDDDFDLLSQP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 436 ISFNASLPGMAAVVLD-DQGK--PIRDEvGELCLEKPwvGMTKSFWEDDERYVNTywsrFENKWVH-GDWVIYDGEQYI- 510
Cdd:PRK06178 387 VFVGLPVPGTEFKICDfETGEllPLGAE-GEIVVRTP--SLLKGYWNKPEATAEA----LRDGWLHtGDIGKIDEQGFLh 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 511 ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGElkkELMSLVNSHIGKAL 590
Cdd:PRK06178 460 YLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAA---ALQAWCRENMAVYK 536
|
570
....*....|....*....
gi 446729146 591 CPkDIHVVEDLPKTRNSKV 609
Cdd:PRK06178 537 VP-EIRIVDALPMTATGKV 554
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
56-622 |
2.43e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 125.88 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 56 WMKPYTEvldlenGTPFAQWYNGGT-CNVVESALSRWLADeetriqPALQYEGengtsKSFTYEELDNWVSRVANGLKHA 134
Cdd:PRK05605 15 WLQSYAP------WTPHDLDYGDTTlVDLYDNAVARFGDR------PALDFFG-----ATTTYAELGKQVRRAAAGLRAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 135 GIEKGDRVTIYMPMIPETVVAMLAVMKIGAII---SPIFSG------FASDAvmTRVQAAGSKMIITADGFSRRG---KI 202
Cdd:PRK05605 78 GVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVvehNPLYTAhelehpFEDHG--ARVAIVWDKVAPTVERLRRTTpleTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 203 VSlkdeVDkACEHCPTVEK------VVIVRHAGNDFTPHNYDF-SWSTLEK-----EKPFIHAEEMQSDDPLMLIYTSGT 270
Cdd:PRK05605 156 VS----VN-MIAAMPLLQRlalrlpIPALRKARAALTGPAPGTvPWETLVDaaiggDGSDVSHPRPTPDDVALILYTSGT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 271 TGKPKGTVHTHAGfpLKAafdagfgmNIKQG-----------DRVLWVTDM----GWMMGpfLLFGSLInGATMVMYegv 335
Cdd:PRK05605 231 TGKPKGAQLTHRN--LFA--------NAAQGkawvpglgdgpERVLAALPMfhayGLTLC--LTLAVSI-GGELVLL--- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 336 PDfPEADRLWETVDKYEITHLGISPTLIRALMAKGDEY-VNKHSLK-------SLEVfaSTGEPWnpdpwmwlfETVGKG 407
Cdd:PRK05605 295 PA-PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERgVDLSGVRnafsgamALPV--STVELW---------EKLTGG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 408 NVpICNYsGGTEISGGIFGNvlikpiaPISfNASLPGMAAVVLD-------DQGKPIRD----EVGELCLEKPWVgmTKS 476
Cdd:PRK05605 363 LL-VEGY-GLTETSPIIVGN-------PMS-DDRRPGYVGVPFPdtevrivDPEDPDETmpdgEEGELLVRGPQV--FKG 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 477 FWEDDERYVNTywsrFENKWVH-GDWVIYDGEQY----------IITGrsddtlniaGKRIGPAEYESILVKHNDVIEAA 545
Cdd:PRK05605 431 YWNRPEETAKS----FLDGWFRtGDVVVMEEDGFirivdrikelIITG---------GFNVYPAEVEEVLREHPGVEDAA 497
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446729146 546 AIGVPDEVKGEVCHCFVVLRDHVTFTGELKKElmsLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKE 622
Cdd:PRK05605 498 VVGLPREDGSEEVVAAVVLEPGAALDPEGLRA---YCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEKL 571
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
124-615 |
3.28e-30 |
|
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: 124.09 E-value: 3.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 124 VSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIF---SGFASDAVMTRVQA-AGSKMIITADGfsrr 199
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFvplNPTLKESVLRYLVAdAGGRIVLADAG---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 200 gkivsLKDEVDKACEHCPTVEKVVIV---RHAGNDFTPHnydfswstlekekpfihaeEMQSDDPLMLIYTSGTTGKPKG 276
Cdd:cd05922 79 -----AADRLRDALPASPDPGTVLDAdgiRAARASAPAH-------------------EVSHEDLALLLYTSGSTGSPKL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 277 TVHTHAGFPLKAAFDAGFgMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYE-GVPDfpeaDRLWETVDKYEITH 355
Cdd:cd05922 135 VRLSHQNLLANARSIAEY-LGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNdGVLD----DAFWEDLREHGATG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 356 LGISPTLIRALMAKGdeyVNKHSLKSLEVFASTGEPWnPDPWMWLFETVGKGNVPICNYsGGTEisggIFGNVLIKPI-- 433
Cdd:cd05922 210 LAGVPSTYAMLTRLG---FDPAKLPSLRYLTQAGGRL-PQETIARLRELLPGAQVYVMY-GQTE----ATRRMTYLPPer 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 434 ---APISFNASLPGMAAVVLDDQGKPIR-DEVGELCLEKPWVgmTKSFWeDDERYVnTYWSRFENKWVHGDWVIYDGEQY 509
Cdd:cd05922 281 ileKPGSIGLAIPGGEFEILDDDGTPTPpGEPGEIVHRGPNV--MKGYW-NDPPYR-RKEGRGGGVLHTGDLARRDEDGF 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 510 I-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVkGEVCHCFVVLRDHVTftgelKKELMSLVNSHIGK 588
Cdd:cd05922 357 LfIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKID-----PKDVLRSLAERLPP 430
|
490 500
....*....|....*....|....*..
gi 446729146 589 ALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05922 431 YKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
101-617 |
3.84e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 124.30 E-value: 3.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYEGengtsKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:PRK03640 19 TAIEFEE-----KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 181 RVQAAGSKMIITADGFsrrgkivslKDEVdkacehcpTVEKVVIvrhagndftphnydfsWSTLEK--EKPFIHAEEMQS 258
Cdd:PRK03640 94 QLDDAEVKCLITDDDF---------EAKL--------IPGISVK----------------FAELMNgpKEEAEIQEEFDL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 259 DDPLMLIYTSGTTGKPKGTVHTHaGFPLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEgvpDF 338
Cdd:PRK03640 141 DEVATIMYTSGTTGKPKGVIQTY-GNHWWSAVGSALNLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVLVE---KF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 339 pEADRLWETVDKYEITHLGISPTLIRALMAK--GDEYVNkhslkSLEVFASTGEPWNPDpwmwLFETVGKGNVPICNYSG 416
Cdd:PRK03640 217 -DAEKINKLLQTGGVTIISVVSTMLQRLLERlgEGTYPS-----SFRCMLLGGGPAPKP----LLEQCKEKGIPVYQSYG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 417 GTEISggifgnvliKPIAPISFNASLPGMAAVvlddqGKP-------IRD--------EVGELCLEKPWVgmTKSFWEDD 481
Cdd:PRK03640 287 MTETA---------SQIVTLSPEDALTKLGSA-----GKPlfpcelkIEKdgvvvppfEEGEIVVKGPNV--TKGYLNRE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 482 ERyvnTYWSrFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCH 559
Cdd:PRK03640 351 DA---TRET-FQDGWFKtGDIGYLDEEGFLyVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPV 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446729146 560 CFVVLRDHVTftgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAA 617
Cdd:PRK03640 427 AFVVKSGEVT-----EEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
116-612 |
5.27e-30 |
|
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: 124.16 E-value: 5.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAV--------MTRVQAAGS 187
Cdd:cd05923 30 TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELaeliergeMTAAVIAVD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 188 KMIITADgFSRRGKIVSLKDEVDkacehcptvekvvivrhagndfTPHNYDFSwstlekekPFIHAEEMQSDDPLMLIYT 267
Cdd:cd05923 110 AQVMDAI-FQSGVRVLALSDLVG----------------------LGEPESAG--------PLIEDPPREPEQPAFVFYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 268 SGTTGKPKGTVHTHAGFPLKAAFDAG-FGMNIKQGDRVLWVTDMGWMMGPF-LLFGSLINGATMVMyegVPDFPEADRLw 345
Cdd:cd05923 159 SGTTGLPKGAVIPQRAAESRVLFMSTqAGLRHGRHNVVLGLMPLYHVIGFFaVLVAALALDGTYVV---VEEFDPADAL- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 346 ETVDKYEITHLGISPTLIRALMAKgdEYVNKHSLKSLE--VFASTGEpwnPDPwmwLFETVGKG-NVPICNYSGGTEI-- 420
Cdd:cd05923 235 KLIEQERVTSLFATPTHLDALAAA--AEFAGLKLSSLRhvTFAGATM---PDA---VLERVNQHlPGEKVNIYGTTEAmn 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 421 -------------SGGIFGNVLIKPIAPISFNASLPGmaavvldDQGKPIRDEVGelclekpwvgmtksfwedDERYVNt 487
Cdd:cd05923 307 slymrdartgtemRPGFFSEVRIVRIGGSPDEALANG-------EEGELIVAAAA------------------DAAFTG- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 488 YWSRFE--------NKWVHGDWVIYDGE-QYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVC 558
Cdd:cd05923 361 YLNQPEatakklqdGWYRTGDVGYVDPSgDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSV 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446729146 559 HCFVVLRDHVTFTGELKKELMSlvnSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd05923 441 TACVVPREGTLSADELDQFCRA---SELADFKRPRRYFFLDELPKNAMNKVLRR 491
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
101-616 |
7.53e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 126.61 E-value: 7.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYeGEngtsKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:PRK12316 528 PALAF-GE----ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAY 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 181 RVQAAGSKMIITAdgfSRRGKIVSLKDEVDKACEHCPTvekvvivrhagndftphnydfSW-STLEKEKPFIHAEemqSD 259
Cdd:PRK12316 603 MLEDSGVQLLLSQ---SHLGRKLPLAAGVQVLDLDRPA---------------------AWlEGYSEENPGTELN---PE 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 260 DPLMLIYTSGTTGKPKGTVHTHAGFP--LKAAFDAgFGMNIkqGDRVLWVTDMGWMMGPFLLFGSLINGATMVMyEGVPD 337
Cdd:PRK12316 656 NLAYVIYTSGSTGKPKGAGNRHRALSnrLCWMQQA-YGLGV--GDTVLQKTPFSFDVSVWEFFWPLMSGARLVV-AAPGD 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 338 FPEADRLWETVDKYEITHLGISPTLIRALMAKGDEyvnkHSLKSLEVFASTGEPWNPDPWMWLFETvgKGNVPICNYSGG 417
Cdd:PRK12316 732 HRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDV----ASCTSLRRIVCSGEALPADAQEQVFAK--LPQAGLYNLYGP 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 418 TEISGGIFGNVLIKPIA-PISFNASLPGMAAVVLDDQGKPIRDEV-GELCLEKpwVGMTKSFWE----DDERYVNTYWSR 491
Cdd:PRK12316 806 TEAAIDVTHWTCVEEGGdSVPIGRPIANLACYILDANLEPVPVGVlGELYLAG--RGLARGYHGrpglTAERFVPSPFVA 883
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 492 FENKWVHGDWVIY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGvpdeVKGEVCHCFVVLRDHv 568
Cdd:PRK12316 884 GERMYRTGDLARYraDGViEYA--GRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLESE- 956
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 446729146 569 tfTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:PRK12316 957 --GGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPA 1002
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
101-612 |
2.03e-29 |
|
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: 121.59 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:cd17652 4 PAVVFGDE-----TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 181 RVQAAGSKMIITadgfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihaeemQSDD 260
Cdd:cd17652 79 MLADARPALLLT----------------------------------------------------------------TPDN 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 261 PLMLIYTSGTTGKPKGTVHTHAGFP-LKAAFDAGFgmNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVM---YEGVP 336
Cdd:cd17652 95 LAYVIYTSGSTGRPKGVVVTHRGLAnLAAAQIAAF--DVGPGSRVLQFASPSFDASVWELLMALLAGATLVLapaEELLP 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 337 DFPEADRLWEtvdkYEITHLGISPTLIRALMAKGdeyvnkhsLKSLEVFASTGEPWNPDpwmwLFETVGKGNVPICNYsG 416
Cdd:cd17652 173 GEPLADLLRE----HRITHVTLPPAALAALPPDD--------LPDLRTLVVAGEACPAE----LVDRWAPGRRMINAY-G 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 417 GTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGKPIRDEV-GELCLEKPwvGMTKSFWE----DDERYV-NTYWS 490
Cdd:cd17652 236 PTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVpGELYIAGA--GLARGYLNrpglTAERFVaDPFGA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 491 RFENKWVHGDWVIY--DGeQYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIgVPDEVKGE--VCHCFVVLRD 566
Cdd:cd17652 314 PGSRMYRTGDLARWraDG-QLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVV-VRDDRPGDkrLVAYVVPAPG 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446729146 567 HVTFTGELKKELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd17652 392 AAPTAAELRAHLAERLPGY----MVPAAFVVLDALPLTPNGKLDRR 433
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
110-621 |
2.61e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 122.11 E-value: 2.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 110 GTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKM 189
Cdd:PRK13391 20 STGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 190 IITAdgfSRRGKIVSLkdevdkACEHCPTVEKVVIVRHAGndftphnydfswsTLEKEKPFIHAEEMQSDDPL------- 262
Cdd:PRK13391 100 LITS---AAKLDVARA------LLKQCPGVRHRLVLDGDG-------------ELEGFVGYAEAVAGLPATPIadeslgt 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 263 MLIYTSGTTGKPKGTVHTHAGFPLKAAFD-AGFGMNIKQGDRvlwvtDMGWM-------MGPfLLFGSLIN--GATMVMY 332
Cdd:PRK13391 158 DMLYSSGTTGRPKGIKRPLPEQPPDTPLPlTAFLQRLWGFRS-----DMVYLspaplyhSAP-QRAVMLVIrlGGTVIVM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 333 EgvpDFpEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPD------PWmWlfetvgk 406
Cdd:PRK13391 232 E---HF-DAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQvkeqmiDW-W------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 407 GNVpICNYSGGTEISGGIFGNVLIKPIAPISFNASLPGMAaVVLDDQGKPI-RDEVGELCLEKpwvGMTKSFWEDDERyv 485
Cdd:PRK13391 300 GPI-IHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFGDL-HILDDDGAELpPGEPGTIWFEG---GRPFEYLNDPAK-- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 486 nTYWSRFEnkwvHGDW-----VIY-DGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVC 558
Cdd:PRK13391 373 -TAEARHP----DGTWstvgdIGYvDEDGYLyLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEV 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446729146 559 HCFVVLRDHVTFTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGK 621
Cdd:PRK13391 448 KAVVQPVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWGN 510
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
116-612 |
4.56e-29 |
|
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: 120.65 E-value: 4.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITadg 195
Cdd:cd17650 14 TYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLT--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 196 fsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihaeemQSDDPLMLIYTSGTTGKPK 275
Cdd:cd17650 91 -------------------------------------------------------------QPEDLAYVIYTSGTTGKPK 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 276 GTVHTHAGFP-LKAAFDAGFGMNIKQgDRVLWVTDMGW--MMGPFLLfgSLINGATMVMyegVPDFPEAD--RLWETVDK 350
Cdd:cd17650 110 GVMVEHRNVAhAAHAWRREYELDSFP-VRLLQMASFSFdvFAGDFAR--SLLNGGTLVI---CPDEVKLDpaALYDLILK 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 351 YEITHLGISPTLIRALMakgdEYVNKHSLK--SLEVFASTGEPWNPDPWMWLFETVGKGNVPICNYsGGTE--ISGGIF- 425
Cdd:cd17650 184 SRITLMESTPALIRPVM----AYVYRNGLDlsAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSY-GVTEatIDSTYYe 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 426 -GNVLIKPIAPISFNASLPGMAAVVLD--DQGKPIrDEVGELCLEKPwvGMTKSFWEDDE----RYVNTYWSRFENKWVH 498
Cdd:cd17650 259 eGRDPLGDSANVPIGRPLPNTAMYVLDerLQPQPV-GVAGELYIGGA--GVARGYLNRPEltaeRFVENPFAPGERMYRT 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 499 GD---WvIYDGEQYIItGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIgVPDEVKGEVCHCFVVLRDHVTFTGELK 575
Cdd:cd17650 336 GDlarW-RADGNVELL-GRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VREDKGGEARLCAYVVAAATLNTAELR 412
|
490 500 510
....*....|....*....|....*....|....*..
gi 446729146 576 KELMslvnSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd17650 413 AFLA----KELPSYMIPSYYVQLDALPLTPNGKVDRR 445
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
111-616 |
1.08e-28 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 120.47 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 111 TSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMI 190
Cdd:PLN02246 47 TGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 191 ITADGFSrrGKIVSLKDEVDKacehcptveKVVIVrhagnDFTPHNYDFSWSTLEKEKPFIHAEEMQSDDPLMLIYTSGT 270
Cdd:PLN02246 127 ITQSCYV--DKLKGLAEDDGV---------TVVTI-----DDPPEGCLHFSELTQADENELPEVEISPDDVVALPYSSGT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 271 TGKPKGTVHTHAGFPLKAA--FDagfGMN----IKQGDRVLWVTDMgwmmgpF-------LLFGSLINGATMVMyegVPD 337
Cdd:PLN02246 191 TGLPKGVMLTHKGLVTSVAqqVD---GENpnlyFHSDDVILCVLPM------FhiyslnsVLLCGLRVGAAILI---MPK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 338 FpEADRLWETVDKYEITHLGISPTLIRALmAKGDEyVNKHSLKSLEVFASTGEPWNPDpwmwLFETV---------GKGn 408
Cdd:PLN02246 259 F-EIGALLELIQRHKVTIAPFVPPIVLAI-AKSPV-VEKYDLSSIRMVLSGAAPLGKE----LEDAFraklpnavlGQG- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 409 vpicnYsGGTEIsggifGNVL------------IKPIA--PISFNASLpgmaAVVLDDQGKPI-RDEVGELCLEKPWVgM 473
Cdd:PLN02246 331 -----Y-GMTEA-----GPVLamclafakepfpVKSGScgTVVRNAEL----KIVDPETGASLpRNQPGEICIRGPQI-M 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 474 tKSFWEDDERYVNTYwsrFENKWVH-GD-WVIYDGEQYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPD 551
Cdd:PLN02246 395 -KGYLNDPEATANTI---DKDGWLHtGDiGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKD 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446729146 552 EVKGEVCHCFVVLRDHVTFTGELKKElmslvnsHIGKALC-PKDIHVV---EDLPKTRNSKVMRRVIKA 616
Cdd:PLN02246 471 EVAGEVPVAFVVRSNGSEITEDEIKQ-------FVAKQVVfYKRIHKVffvDSIPKAPSGKILRKDLRA 532
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
112-618 |
1.99e-28 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 119.42 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 112 SKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMII 191
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 192 T-ADGFSrrgkivSLKDEVDKACE--HCPT-VEKVVIVRHAGNDFTPHNYDFSWST-LEKEKPFihaEEMQSDDPLMLIY 266
Cdd:PRK12406 89 AhADLLH------GLASALPAGVTvlSVPTpPEIAAAYRISPALLTPPAGAIDWEGwLAQQEPY---DGPPVPQPQSMIY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 267 TSGTTGKPKGtVHTHAGFPLKAAFD---AGFGMNIKQGDRVLwvtdmgwMMGPflLFGSLIN---------GATMVMyeg 334
Cdd:PRK12406 160 TSGTTGHPKG-VRRAAPTPEQAAAAeqmRALIYGLKPGIRAL-------LTGP--LYHSAPNayglragrlGGVLVL--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 335 VPDFpEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPD------PWmWlfetvgkGN 408
Cdd:PRK12406 227 QPRF-DPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADvkramiEW-W-------GP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 409 VpICNYSGGTEISGGIFGN---VLIKpiaPISFNASLPGMAAVVLDDQGKPIRD-EVGELCLEKPwvGMtksfweDDERY 484
Cdd:PRK12406 298 V-IYEYYGSTESGAVTFATsedALSH---PGTVGKAAPGAELRFVDEDGRPLPQgEIGEIYSRIA--GN------PDFTY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 485 VNTYWSRFE---NKWVH-GD--WVIYDGEQYIITGRSDDTLNiAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVC 558
Cdd:PRK12406 366 HNKPEKRAEidrGGFITsGDvgYLDADGYLFLCDRKRDMVIS-GGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEAL 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446729146 559 HCFVVLRDHVTF-TGELKKELmslvNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAY 618
Cdd:PRK12406 445 MAVVEPQPGATLdEADIRAQL----KARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPY 501
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
100-618 |
3.24e-28 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 119.82 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 100 QPALQYEgENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM 179
Cdd:COG1022 27 RVALREK-EDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 180 TRVQAAGSKMIITADGFsrrgkivsLKDEVDKACEHCPTVEKVVIVRHAGNDFTPHNYdfSWSTLEKE-KPFIHAEEMQS 258
Cdd:COG1022 106 YILNDSGAKVLFVEDQE--------QLDKLLEVRDELPSLRHIVVLDPRGLRDDPRLL--SLDELLALgREVADPAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 259 -------DDPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVL------WVtdMGWMMGpfllFGSLIN 325
Cdd:COG1022 176 rraavkpDDLATIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDRTLsflplaHV--FERTVS----YYALAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 326 GATMVMYEGVPDFPEA------------DRLWETVdkYE--ITHLGISPTLIRAL----MAKGDEYVN------------ 375
Cdd:COG1022 249 GATVAFAESPDTLAEDlrevkptfmlavPRVWEKV--YAgiQAKAEEAGGLKRKLfrwaLAVGRRYARarlagkspslll 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 376 --KHSL--------------KSLEVFASTGEPWNPDpwmwL---FETVGkgnVPICN-YsGGTEISGGIFGNvlikpiap 435
Cdd:COG1022 327 rlKHALadklvfsklrealgGRLRFAVSGGAALGPE----LarfFRALG---IPVLEgY-GLTETSPVITVN-------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 436 iSFNASLPGmaAVvlddqGKPIRD-EV-----GELCLEKPwvGMTKSFWEDDERYVNTYwsrFENKWVH-GDWVIYDGEQ 508
Cdd:COG1022 391 -RPGDNRIG--TV-----GPPLPGvEVkiaedGEILVRGP--NVMKGYYKNPEATAEAF---DADGWLHtGDIGELDEDG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 509 YI-ITGRSDDTL-NIAGKRIGPAEYESILVKHNDVIEAAAIG----------VPD--------EVKGEVCHCFVVLRDHV 568
Cdd:COG1022 458 FLrITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVGdgrpflaaliVPDfealgewaEENGLPYTSYAELAQDP 537
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 446729146 569 TFTGELKKELMSlVNSHIGKALCPKDIHVvedLPK---------TRNSKVMRRVIKAAY 618
Cdd:COG1022 538 EVRALIQEEVDR-ANAGLSRAEQIKRFRL---LPKeftiengelTPTLKLKRKVILEKY 592
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
114-618 |
5.58e-28 |
|
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: 117.64 E-value: 5.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 114 SFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIfsgfasDAVMTR------VQAAGS 187
Cdd:cd05918 24 SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPL------DPSHPLqrlqeiLQDTGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 188 KMIITAdgfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihaeemQSDDPLMLIYT 267
Cdd:cd05918 98 KVVLTS---------------------------------------------------------------SPSDAAYVIFT 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 268 SGTTGKPKGTVHTHAGFplKAAFDAgFG--MNIKQGDRVLW---------VTDMgwmmgpfllFGSLINGATMVmyegVP 336
Cdd:cd05918 115 SGSTGKPKGVVIEHRAL--STSALA-HGraLGLTSESRVLQfasytfdvsILEI---------FTTLAAGGCLC----IP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 337 dfPEADR---LWETVDKYEITHLGISPTLIRALmakgdeyvNKHSLKSLEVFASTGEPWNP---DPWmwlfetvgKGNVP 410
Cdd:cd05918 179 --SEEDRlndLAGFINRLRVTWAFLTPSVARLL--------DPEDVPSLRTLVLGGEALTQsdvDTW--------ADRVR 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 411 ICNYSGGTEISggIFGNVlikPIAPISFNASLPGMAA------VVLDDQGKPI-RDEVGELCLEKPWVGmtKSFWEDDER 483
Cdd:cd05918 241 LINAYGPAECT--IAATV---SPVVPSTDPRNIGRPLgatcwvVDPDNHDRLVpIGAVGELLIEGPILA--RGYLNDPEK 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 484 -----YVNTYWSRFENKWVH------GDWVIY--DGEQYIItGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGV- 549
Cdd:cd05918 314 taaafIEDPAWLKQEGSGRGrrlyrtGDLVRYnpDGSLEYV-GRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVv 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 550 --PDEVKGEVCHCFVVLRDHVTFTG----------ELKKELMSLVNSHIGKAL----CPKDIHVVEDLPKTRNSKVMRRV 613
Cdd:cd05918 393 kpKDGSSSPQLVAFVVLDGSSSGSGdgdslflepsDEFRALVAELRSKLRQRLpsymVPSVFLPLSHLPLTASGKIDRRA 472
|
....*
gi 446729146 614 IKAAY 618
Cdd:cd05918 473 LRELA 477
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
113-548 |
3.03e-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: 115.39 E-value: 3.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 113 KSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIIT 192
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 193 adgfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekEKPfihaeemqsDDPLMLIYTSGTTG 272
Cdd:cd05907 84 ------------------------------------------------------EDP---------DDLATIIYTSGTTG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 273 KPKGTVHTHAGF--PLKAAFDAgfgMNIKQGDRVLWVTDMGWMMGP-FLLFGSLINGATMVMYE----GVPDFPEAD--- 342
Cdd:cd05907 101 RPKGVMLSHRNIlsNALALAER---LPATEGDRHLSFLPLAHVFERrAGLYVPLLAGARIYFASsaetLLDDLSEVRptv 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 343 -----RLWETVdkYEITHLGISPTLIRALMAkgdeyvnKHSLKSLEVFASTGEPWNPDPWMWlFETVGkgnVPICNYSGG 417
Cdd:cd05907 178 flavpRVWEKV--YAAIKVKAVPGLKRKLFD-------LAVGGRLRFAASGGAPLPAELLHF-FRALG---IPVYEGYGL 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 418 TEISGGIFGNvlikpiapisfnasLPGmaAVVLDDQGKPIR------DEVGELCLEKPwvGMTKSFWEDDERyvnTYWSR 491
Cdd:cd05907 245 TETSAVVTLN--------------PPG--DNRIGTVGKPLPgvevriADDGEILVRGP--NVMLGYYKNPEA---TAEAL 303
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 492 FENKWVH-GDWVIYDGEQYI-ITGRSDDTL-NIAGKRIGPAEYESILVKHNDVIEAAAIG 548
Cdd:cd05907 304 DADGWLHtGDLGEIDEDGFLhITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
95-612 |
3.35e-27 |
|
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: 115.50 E-value: 3.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 95 EETRIQPALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFA 174
Cdd:cd17655 8 EKTPDHTAVVFEDQ-----TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 175 SDAVMTRVQAAGSKMIITadgfsrrgkivslkdevdkaceHCPTVEKVVIVRHAGNDFTPHNYDFSWSTLEKEKpfihae 254
Cdd:cd17655 83 EERIQYILEDSGADILLT----------------------QSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVS------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 255 emQSDDPLMLIYTSGTTGKPKGTVHTHAGFP-LKAAFDAgfGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYE 333
Cdd:cd17655 135 --KSDDLAYVIYTSGSTGKPKGVMIEHRGVVnLVEWANK--VIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 334 GVPDFPeADRLWETVDKYEITHLGISPTLIRALmakgdEYVNKHSLKSLEVFASTGEPWNPD---PWMWLFETvgkgNVP 410
Cdd:cd17655 211 KETVLD-GQALTQYIRQNRITIIDLTPAHLKLL-----DAADDSEGLSLKHLIVGGEALSTElakKIIELFGT----NPT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 411 ICNYSGGTE-----ISGGIFGNVLIKPIAPISfnASLPGMAAVVLDDQGKPIR-DEVGELCLEKPwvGMTKSFWE----D 480
Cdd:cd17655 281 ITNAYGPTEttvdaSIYQYEPETDQQVSVPIG--KPLGNTRIYILDQYGRPQPvGVAGELYIGGE--GVARGYLNrpelT 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 481 DERYVNTYWSRFENKWVHGD---WvIYDGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGE 556
Cdd:cd17655 357 AEKFVDDPFVPGERMYRTGDlarW-LPDGNiEFL--GRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQN 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446729146 557 VCHCFVVLRDHVTfTGELKKELmslvNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd17655 434 YLCAYIVSEKELP-VAQLREFL----ARELPDYMIPSYFIKLDEIPLTPNGKVDRK 484
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
111-615 |
2.71e-26 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 113.40 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 111 TSKSFTYEELDNWVSRVANGLKHA-GIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKM 189
Cdd:PLN02574 63 TGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 190 IITadgfsrrgkivslkdEVDKACEHCPTVEKVVIVRHAG--NDFTPHNYDFSWSTLEKEKPFIhAEEMQSDDPLMLIYT 267
Cdd:PLN02574 143 AFT---------------SPENVEKLSPLGVPVIGVPENYdfDSKRIEFPKFYELIKEDFDFVP-KPVIKQDDVAAIMYS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 268 SGTTGKPKGTVHTHAGF----PLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLIN-GATMVMYEGVpdfpEAD 342
Cdd:PLN02574 207 SGTTGASKGVVLTHRNLiamvELFVRFEASQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSlGSTIVVMRRF----DAS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 343 RLWETVDKYEITHLGISPTLIRALM--AKGdeyVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGkgNVPICNYSGGTEi 420
Cdd:PLN02574 283 DMVKVIDRFKVTHFPVVPPILMALTkkAKG---VCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLP--HVDFIQGYGMTE- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 421 SGGI----FGNVLIKPIAPISFNAslPGMAAVVLDDQGKPI--RDEVGELCLEKPwvGMTKSFWEDDERyvnTYWSRFEN 494
Cdd:PLN02574 357 STAVgtrgFNTEKLSKYSSVGLLA--PNMQAKVVDWSTGCLlpPGNCGELWIQGP--GVMKGYLNNPKA---TQSTIDKD 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 495 KWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTG 572
Cdd:PLN02574 430 GWLRtGDIAYFDEDGYLyIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQ 509
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446729146 573 ElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:PLN02574 510 E---AVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
113-619 |
3.63e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 112.59 E-value: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 113 KSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPI---FSGFASDAVMTRVQAAgskM 189
Cdd:PRK09088 21 RRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLnwrLSASELDALLQDAEPR---L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 190 IITADGFSRRGKI-VSLKDEVDKACEHCPtvekvvivrhagnDFTPHnydfswstlekekpfihaeeMQSDDPLMLIYTS 268
Cdd:PRK09088 98 LLGDDAVAAGRTDvEDLAAFIASADALEP-------------ADTPS--------------------IPPERVSLILFTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 269 GTTGKPKGTVHTHagfplKAAFDAG--FGMNIKQGDRVLWVTD--MGWMMGpflLFGS----LINGATMVMYEGVPdfPE 340
Cdd:PRK09088 145 GTSGQPKGVMLSE-----RNLQQTAhnFGVLGRVDAHSSFLCDapMFHIIG---LITSvrpvLAVGGSILVSNGFE--PK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 341 ADRLWETVDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFASTGEPW-NPDPWMWLFEtvgkgNVPICNYSGGTE 419
Cdd:PRK09088 215 RTLGRLGDPALGITHYFCVPQMAQAFRAQPG--FDAAALRHLTALFTGGAPHaAEDILGWLDD-----GIPMVDGFGMSE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 420 iSGGIFG-NVLIKPIAPISFNASL--PGMAAVVLDDQGKPIRDEV-GELCLEKPwvGMTKSFWEDDEryvNTYWSRFENK 495
Cdd:PRK09088 288 -AGTVFGmSVDCDVIRAKAGAAGIptPTVQTRVVDDQGNDCPAGVpGELLLRGP--NLSPGYWRRPQ---ATARAFTGDG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 496 WVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGE 573
Cdd:PRK09088 362 WFRtGDIARRDADGFFwVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLE 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446729146 574 lkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYL 619
Cdd:PRK09088 442 ---RIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALA 484
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
260-616 |
4.04e-25 |
|
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: 106.65 E-value: 4.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 260 DPLMLIYTSGTTGKPKGTVHTHAGfpLKAAFDAGfGMNIKQGDRVLWVTDM--GWMMGPFLLFGSLINGATMVMYEGVPD 337
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAN--LLASAAGL-HSRLGFGGGDSWLLSLplYHVGGLAILVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 338 fpeadrLWETVDKYEITHLGISPT-LIRALMAKGDeyvnKHSLKSLEVFASTGEPWNPDpwmwLFETVGKGNVPICNYSG 416
Cdd:cd17630 78 ------LAEDLAPPGVTHVSLVPTqLQRLLDSGQG----PAALKSLRAVLLGGAPIPPE----LLERAADRGIPLYTTYG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 417 GTEISGGIFGNVLIKPIAPISFNAsLPGmAAVVLDDQGkpiRDEVGELCLEKpwvGMTKSFWEDDeryvntywsRFENKW 496
Cdd:cd17630 144 MTETASQVATKRPDGFGRGGVGVL-LPG-RELRIVEDG---EIWVGGASLAM---GYLRGQLVPE---------FNEDGW 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 497 VH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTftgel 574
Cdd:cd17630 207 FTtKDLGELHADGRLtVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPAD----- 281
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446729146 575 KKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:cd17630 282 PAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
530-608 |
1.14e-24 |
|
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: 97.62 E-value: 1.14e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446729146 530 EYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTftgELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSK 608
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVE---LLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
95-619 |
1.22e-24 |
|
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: 108.48 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 95 EETRIQPALQY-EGENGTSKSFTYEELDNWVSRVANGLKHAGiEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIF--- 170
Cdd:cd05931 4 AARPDRPAYTFlDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPppt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 171 SGFASDAVMTRVQAAGSKMIITADGFsrrgkivslKDEVDKACEHCPTVEKVVIVRH------AGNDFTPhnydfswstl 244
Cdd:cd05931 83 PGRHAERLAAILADAGPRVVLTTAAA---------LAAVRAFAASRPAAGTPRLLVVdllpdtSAADWPP---------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 245 ekekpfihaEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGfpLKAAFDAGF-GMNIKQGDR-VLWVT---DMGWMMGpflL 319
Cdd:cd05931 144 ---------PSPDPDDIAYLQYTSGSTGTPKGVVVTHRN--LLANVRQIRrAYGLDPGDVvVSWLPlyhDMGLIGG---L 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 320 FGSLINGATMVMYEGVpDFPEADRLW-ETVDKYEITHLGiSPT-----LIRALMAKGDEYVNKHSLK------------S 381
Cdd:cd05931 210 LTPLYSGGPSVLMSPA-AFLRRPLRWlRLISRYRATISA-APNfaydlCVRRVRDEDLEGLDLSSWRvalngaepvrpaT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 382 LEVFASTGEPWNPDPWMW----------LFETVG-KGNVPICNYSGGTEISGGIFGNVLIKPIAP--ISFNASLPGMAAV 448
Cdd:cd05931 288 LRRFAEAFAPFGFRPEAFrpsyglaeatLFVSGGpPGTGPVVLRVDRDALAGRAVAVAADDPAARelVSCGRPLPDQEVR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 449 VLDDQGKPIR--DEVGELCLEKPwvGMTKSFWEDDERYVNTYWSRFENKwvHGDW-------VIYDGEQYiITGRSDDTL 519
Cdd:cd05931 368 IVDPETGRELpdGEVGEIWVRGP--SVASGYWGRPEATAETFGALAATD--EGGWlrtgdlgFLHDGELY-ITGRLKDLI 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 520 NIAGKRIGPAEYESILVKHNDVIE---AAAIGVPDEVKGEVchcfVVLRDHVTFTG-----ELKKELMSLVNSHIGkaLC 591
Cdd:cd05931 443 IVRGRNHYPQDIEATAEEAHPALRpgcVAAFSVPDDGEERL----VVVAEVERGADpadlaAIAAAIRAAVAREHG--VA 516
|
570 580 590
....*....|....*....|....*....|
gi 446729146 592 PKDIHVVE--DLPKTRNSKVMRRVIKAAYL 619
Cdd:cd05931 517 PADVVLVRpgSIPRTSSGKIQRRACRAAYL 546
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
258-611 |
1.56e-24 |
|
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: 105.64 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 258 SDDPLMLIYTSGTTGKPKGTVHTHAGfplkaafdagfgmnikqgdrvlwVTDMGWMMGPFLLFGS--------------- 322
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSN-----------------------EVYNAWMLALNSLFDPddvllcglplfhvng 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 323 --------LINGATMVM-----YEGVPDFpeaDRLWETVDKYEITHLGISPTLIRALMAKGDEyVNKHSLKslevFASTG 389
Cdd:cd05944 58 svvtlltpLASGAHVVLagpagYRNPGLF---DNFWKLVERYRITSLSTVPTVYAALLQVPVN-ADISSLR----FAMSG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 390 EPWNPDPWMWLFETvgKGNVPICNYSGGTEISGGIFGNVLIKPIAPISFNASLP--GMAAVVLDDQGKPIRD----EVGE 463
Cdd:cd05944 130 AAPLPVELRARFED--ATGLPVVEGYGLTEATCLVAVNPPDGPKRPGSVGLRLPyaRVRIKVLDGVGRLLRDcapdEVGE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 464 LCLEKPWV--GMTksfweDDERYVNTYwsrFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHN 539
Cdd:cd05944 208 ICVAGPGVfgGYL-----YTEGNKNAF---VADGWLNtGDLGRLDADGYLfITGRAKDLIIRGGHNIDPALIEEALLRHP 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446729146 540 DVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGElkkELMSLVNSHIG-KALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:cd05944 280 AVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEE---ELLAWARDHVPeRAAVPKHIEVLEELPVTAVGKVFK 349
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
115-611 |
2.61e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 107.59 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 115 FTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAI---ISPIFSGFASDAVMTRVqaaGSKMII 191
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIlvtINPAYRLSELEYALNQS---GCKALI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 192 TADGFsRRGKIVSLKDEVDKACEHC----------PTVEKVVIVrhaGNDFTPHNYdfSWSTLEKEKPFIH-------AE 254
Cdd:PRK08315 121 AADGF-KDSDYVAMLYELAPELATCepgqlqsarlPELRRVIFL---GDEKHPGML--NFDELLALGRAVDdaelaarQA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 255 EMQSDDPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRV-LWVtdmgwmmgPFL-LFG-------SLIN 325
Cdd:PRK08315 195 TLDPDDPINIQYTSGTTGFPKGATLTHRNI-LNNGYFIGEAMKLTEEDRLcIPV--------PLYhCFGmvlgnlaCVTH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 326 GATMV-MYEGvpdF-PEAdrLWETVDKYEITHL-GIsPTLIRALMAKGDeyVNKHSLKSLEVFASTGEPWnPDPWMWlfE 402
Cdd:PRK08315 266 GATMVyPGEG---FdPLA--TLAAVEEERCTALyGV-PTMFIAELDHPD--FARFDLSSLRTGIMAGSPC-PIEVMK--R 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 403 TVGKGN---VPICnYsGGTEISggifgnvlikpiaPISFNAS---------------LPGMAAVVLD-DQGKPI-RDEVG 462
Cdd:PRK08315 335 VIDKMHmseVTIA-Y-GMTETS-------------PVSTQTRtddplekrvttvgraLPHLEVKIVDpETGETVpRGEQG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 463 ELCLEKPWVgMtKSFWEDDERyvnTYWSRFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHND 540
Cdd:PRK08315 400 ELCTRGYSV-M-KGYWNDPEK---TAEAIDADGWMHtGDLAVMDEEGYVnIVGRIKDMIIRGGENIYPREIEEFLYTHPK 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446729146 541 VIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKV----MR 611
Cdd:PRK08315 475 IQDVQVVGVPDEKYGEEVCAWIILRPGATLTEE---DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIqkfkMR 546
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
259-615 |
2.97e-24 |
|
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: 104.67 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 259 DDPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDM----GWMMGpflLFGSLINGATMVMYEg 334
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNI-VNNGYFIGERLGLTEQDRLCIPVPLfhcfGSVLG---VLACLTHGATMVFPS- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 335 vPDFPEADRLwETVDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFASTGEPWnPDPWM-WLFETVGKGNVPICn 413
Cdd:cd05917 77 -PSFDPLAVL-EAIEKEKCTALHGVPTMFIAELEHPD--FDKFDLSSLRTGIMAGAPC-PPELMkRVIEVMNMKDVTIA- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 414 YsGGTEISGGIFGNVLIKPIAP--ISFNASLPGMAAVVLDDQGK--PIRDEVGELCLEKpwVGMTKSFWEDDERyvnTYW 489
Cdd:cd05917 151 Y-GMTETSPVSTQTRTDDSIEKrvNTVGRIMPHTEAKIVDPEGGivPPVGVPGELCIRG--YSVMKGYWNDPEK---TAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 490 SRFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDH 567
Cdd:cd05917 225 AIDGDGWLHtGDLAVMDEDGYCrIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEG 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446729146 568 VTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:cd05917 305 AELTEE---DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
116-609 |
4.16e-24 |
|
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: 106.26 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIisPIFsgfasdAVmtrvqaagskmiitadg 195
Cdd:cd05920 42 TYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVL------AL----------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 196 FSRRGKivslkdEVDKACEHCPTVEKVVIVRHAGNDFTPHnydfswstlekekpfihAEEMQSD--DPLMLIYTSGTTGK 273
Cdd:cd05920 97 PSHRRS------ELSAFCAHAEAVAYIVPDRHAGFDHRAL-----------------ARELAESipEVALFLLSGGTTGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 274 PKGTVHTHA--GFPLKAAFDAgfgMNIKQGDRVLWVTDMGW---MMGPFLLfGSLINGATMVMyegVPDfPEADRLWETV 348
Cdd:cd05920 154 PKLIPRTHNdyAYNVRASAEV---CGLDQDTVYLAVLPAAHnfpLACPGVL-GTLLAGGRVVL---APD-PSPDAAFPLI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 349 DKYEITHLGISPTLIRALMAKGDEYvnKHSLKSLEVFASTGEPWNPDPWMWLFETVG----------KGNVpicNYsggT 418
Cdd:cd05920 226 EREGVTVTALVPALVSLWLDAAASR--RADLSSLRLLQVGGARLSPALARRVPPVLGctlqqvfgmaEGLL---NY---T 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 419 EI--SGGIFGNVLIKPIAPisfnaslpGMAAVVLDDQGKPIRD-EVGELCLEKPWV--GM-------TKSFWEDderyvN 486
Cdd:cd05920 298 RLddPDEVIIHTQGRPMSP--------DDEIRVVDEEGNPVPPgEEGELLTRGPYTirGYyrapehnARAFTPD-----G 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 487 TYWSrfenkwvhGDWVIYDGEQYII-TGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLR 565
Cdd:cd05920 365 FYRT--------GDLVRRTPDGYLVvEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446729146 566 DHVTFTGELKKELMslvNSHIGKALCPKDIHVVEDLPKTRNSKV 609
Cdd:cd05920 437 DPPPSAAQLRRFLR---ERGLAAYKLPDRIEFVDSLPLTAVGKI 477
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
116-615 |
4.43e-24 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 106.51 E-value: 4.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMII---- 191
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLidad 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 192 ----TADGFSRRGKIVSLKDEVDKACEHCPTVekvvivrHAGNDFTPHnydfswstlekekPFIHAEEMQSDDPLMLIYT 267
Cdd:PRK05852 125 gphdRAEPTTRWWPLTVNVGGDSGPSGGTLSV-------HLDAATEPT-------------PATSTPEGLRPDDAMIMFT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 268 SGTTGKPKGTVHTHAGFPLKA-AFDAGFGMnikqGDRVLWVTDMGWMMGPFL---LFGSLINGATmVMYEGVPDFpEADR 343
Cdd:PRK05852 185 GGTTGLPKMVPWTHANIASSVrAIITGYRL----SPRDATVAVMPLYHGHGLiaaLLATLASGGA-VLLPARGRF-SAHT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 344 LWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGkgnVPICNYSGGTEISGG 423
Cdd:PRK05852 259 FWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFA---APVVCAFGMTEATHQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 424 IfGNVLIKPIAPISFNASLPGMAA--------VVLDDQGKPIRDEVGELCLEKPWVgmTKSFWEDDEryvNTYwSRFENK 495
Cdd:PRK05852 336 V-TTTQIEGIGQTENPVVSTGLVGrstgaqirIVGSDGLPLPAGAVGEVWLRGTTV--VRGYLGDPT---ITA-ANFTDG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 496 WVH-GDWVIYDGE-QYIITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGE 573
Cdd:PRK05852 409 WLRtGDLGSLSAAgDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAE 488
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 446729146 574 lkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:PRK05852 489 ---ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVA 527
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
114-612 |
4.49e-24 |
|
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: 105.48 E-value: 4.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 114 SFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITa 193
Cdd:cd12115 24 SLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 194 dgfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihaeemQSDDPLMLIYTSGTTGK 273
Cdd:cd12115 103 ---------------------------------------------------------------DPDDLAYVIYTSGSTGR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 274 PKGTVHTHAG-----FPLKAAFDAgfgmniKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGV---PDFPEADrlw 345
Cdd:cd12115 120 PKGVAIEHRNaaaflQWAAAAFSA------EELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVlalPDLPAAA--- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 346 etvdkyEITHLGISPTLIRALMAKGDeyvnkhSLKSLEVFASTGEPWNPDpwmwLFETV-GKGNVP-ICN---------Y 414
Cdd:cd12115 191 ------EVTLINTVPSAAAELLRHDA------LPASVRVVNLAGEPLPRD----LVQRLyARLQVErVVNlygpsedttY 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 415 SGGTEISGGIFGnvlikpiaPISFNASLPGMAAVVLDDQGKPIRD-EVGELCLEKPwvGMTKSFWEDD----ERYVNTYW 489
Cdd:cd12115 255 STVAPVPPGASG--------EVSIGRPLANTQAYVLDRALQPVPLgVPGELYIGGA--GVARGYLGRPgltaERFLPDPF 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 490 SRFENKWVHGDWVIYDGE---QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVL-R 565
Cdd:cd12115 325 GPGARLYRTGDLVRWRPDgllEFL--GRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAeP 402
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 446729146 566 DHVTFTGELKKELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd12115 403 GAAGLVEDLRRHLGTRLPAY----MVPSRFVRLDALPLTPNGKIDRS 445
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
108-615 |
9.35e-24 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 105.45 E-value: 9.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 108 ENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIispiFSGFASDAVMT----RVQ 183
Cdd:PLN02330 49 EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV----FSGANPTALESeikkQAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 184 AAGSKMIITADgfSRRGKIVSLkdevdkacehcptvEKVVIVRHAGNDFTPHNYDFSWSTLEKEKPFIHAEEMQSDDPLM 263
Cdd:PLN02330 125 AAGAKLIVTND--TNYGKVKGL--------------GLPVIVLGEEKIEGAVNWKELLEAADRAGDTSDNEEILQTDLCA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 264 LIYTSGTTGKPKGTVHTHAGFP---LKAAFDAGFGMnIKQgdrvlwVTDMGWMmgPF--------LLFGSLINGATMVMy 332
Cdd:PLN02330 189 LPFSSGTTGISKGVMLTHRNLVanlCSSLFSVGPEM-IGQ------VVTLGLI--PFfhiygitgICCATLRNKGKVVV- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 333 egVPDFpEADRLWETVDKYEITHLGISPTLIRALMAkgDEYVNKHSLKSLEVFA--STGEPWNPDpWMWLFETVGKGnVP 410
Cdd:PLN02330 259 --MSRF-ELRTFLNALITQEVSFAPIVPPIILNLVK--NPIVEEFDLSKLKLQAimTAAAPLAPE-LLTAFEAKFPG-VQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 411 ICNYSGGTEIS---------------------GGIFGNVLIKPIAPISfNASLPgmaavvlddqgkpiRDEVGELCLEKP 469
Cdd:PLN02330 332 VQEAYGLTEHScitlthgdpekghgiakknsvGFILPNLEVKFIDPDT-GRSLP--------------KNTPGELCVRSQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 470 WVgmTKSFWEDDERYVNTYwsrFENKWVH-GD--WVIYDGEQYIITgRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAA 546
Cdd:PLN02330 397 CV--MQGYYNNKEETDRTI---DEDGWLHtGDigYIDDDGDIFIVD-RIKELIKYKGFQVAPAELEAILLTHPSVEDAAV 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446729146 547 IGVPDEVKGEVCHCFVVLRDHVTftgELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:PLN02330 471 VPLPDEEAGEIPAACVVINPKAK---ESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLK 536
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
260-611 |
1.00e-23 |
|
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: 102.48 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 260 DPLMLIYTSGTTGKPKGTVHTHAGFplKAAFDAG-FGMNIKQGDRVLwvtdmgwMMGPFLLFGSLiNGATMVMYEG---- 334
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSW--IESFVCNeDLFNISGEDAIL-------APGPLSHSLFL-YGAISALYLGgtfi 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 335 VPDFPEADRLWETVDKYEITHLGISPTLIRALMAkgdEYVNKHSLKSlevFASTGEPWNPDpwmwLFETVGKG--NVPIC 412
Cdd:cd17633 71 GQRKFNPKSWIRKINQYNATVIYLVPTMLQALAR---TLEPESKIKS---IFSSGQKLFES----TKKKLKNIfpKANLI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 413 NYSGGTEISGgIFGNVLIKPIAPISFNASLPGMAAVVLDDQGkpirDEVGELCLEKPwvgMTKSFWEDDERYVNTYWSrf 492
Cdd:cd17633 141 EFYGTSELSF-ITYNFNQESRPPNSVGRPFPNVEIEIRNADG----GEIGKIFVKSE---MVFSGYVRGGFSNPDGWM-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 493 enkwVHGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVChCFVVLRDHVTft 571
Cdd:cd17633 211 ----SVGDIGYVDEEGYLyLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA-VALYSGDKLT-- 283
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446729146 572 gelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:cd17633 284 ---YKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
101-612 |
1.71e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 106.78 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:PRK12467 3112 PALVFGDQ-----QLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAY 3186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 181 RVQAAGSKMIITADGFSRRGKIVSlkdeVDKAcehcptvekVVIVRHAGNDFTPHNYDfswstlekekPFIHAEEMQsdd 260
Cdd:PRK12467 3187 MIEDSGVKLLLTQAHLLEQLPAPA----GDTA---------LTLDRLDLNGYSENNPS----------TRVMGENLA--- 3240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 261 plMLIYTSGTTGKPKGTVHTHAGFPLK-AAFDAGFGMNIkqGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGvpDFP 339
Cdd:PRK12467 3241 --YVIYTSGSTGKPKGVGVRHGALANHlCWIAEAYELDA--NDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDN--DLW 3314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 340 EADRLWETVDKYEITHLGISPTLIRALMAKGDeyvnKHSLKSLEVFASTGEPWNPDPWMWLFETVgkGNVPICNYSGGTE 419
Cdd:PRK12467 3315 DPEELWQAIHAHRISIACFPPAYLQQFAEDAG----GADCASLDIYVFGGEAVPPAAFEQVKRKL--KPRGLTNGYGPTE 3388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 420 IS--------GGifGNVLIKPIAPISfnASLPGMAAVVLDDQGKPIRDEV-GELCLEKpwVGMTKSFWE----DDERYV- 485
Cdd:PRK12467 3389 AVvtvtlwkcGG--DAVCEAPYAPIG--RPVAGRSIYVLDGQLNPVPVGVaGELYIGG--VGLARGYHQrpslTAERFVa 3462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 486 NTYWSRFENKWVHGDWVIY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEvKGEVCHCFV 562
Cdd:PRK12467 3463 DPFSGSGGRLYRTGDLARYraDGViEYL--GRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGA-GGKQLVAYV 3539
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 446729146 563 VLRDHvtfTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:PRK12467 3540 VPADP---QGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRK 3586
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
260-611 |
2.16e-23 |
|
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: 101.58 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 260 DPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSL-INGATMVMyegvPDF 338
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNL-IAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFhAGGANVVM----EKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 339 PEADRLwETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLEVFASTGEPwnpdpwmwlfETVGK--GNVPICNYS- 415
Cdd:cd17637 76 DPAEAL-ELIEEEKVTLMGSFPPILSNLLDAAEK--SGVDLSSLRHVLGLDAP----------ETIQRfeETTGATFWSl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 416 -GGTEISGGI-FGNVLIKPIApisfnASLPGMAAVV--LDDQGKPI-RDEVGELCLEKPWVgmTKSFWEDDEryVNTYws 490
Cdd:cd17637 143 yGQTETSGLVtLSPYRERPGS-----AGRPGPLVRVriVDDNDRPVpAGETGEIVVRGPLV--FQGYWNLPE--LTAY-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 491 RFENKWVH-GDWVIYDGEQYI-ITGRS--DDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRD 566
Cdd:cd17637 212 TFRNGWHHtGDLGRFDEDGYLwYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKP 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 446729146 567 HVTFTgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:cd17637 292 GATLT---ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
113-621 |
4.37e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 103.69 E-value: 4.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 113 KSFTYEELDNWVSRVANGL-KHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAII---SPIFSgfaSDAVMTRVQAAGSK 188
Cdd:PRK05677 48 KTLTYGELYKLSGAFAAWLqQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVvntNPLYT---AREMEHQFNDSGAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 189 MIitadgfsrrgkiVSLKDEVDKACEHCP-TVEKVVIVRHAGNDFTPHN---YDFSWSTLEKEKPFIH------------ 252
Cdd:PRK05677 125 AL------------VCLANMAHLAEKVLPkTGVKHVIVTEVADMLPPLKrllINAVVKHVKKMVPAYHlpqavkfndala 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 253 --------AEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGFPLK-AAFDAGFGMNIKQGDRVLwvtdmgwmMGPFLLFG-- 321
Cdd:PRK05677 193 kgagqpvtEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmLQCRALMGSNLNEGCEIL--------IAPLPLYHiy 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 322 --SLINGATMVMYEG---VPDFPEADRLWETVDKYEIT-HLGISpTLIRALMakGDEYVNKHSLKSLEVFASTGepwnpd 395
Cdd:PRK05677 265 afTFHCMAMMLIGNHnilISNPRDLPAMVKELGKWKFSgFVGLN-TLFVALC--NNEAFRKLDFSALKLTLSGG------ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 396 pwMWLFETVGK-----GNVPICNYSGGTEISGGIFGNVlIKPIAPISFNASLPGMAAVVLDDQGKPI-RDEVGELCLEKP 469
Cdd:PRK05677 336 --MALQLATAErwkevTGCAICEGYGMTETSPVVSVNP-SQAIQVGTIGIPVPSTLCKVIDDDGNELpLGEVGELCVKGP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 470 WVgmTKSFWEDDEryvNTYWSRFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAI 547
Cdd:PRK05677 413 QV--MKGYWQRPE---ATDEILDSDGWLKtGDIALIQEDGYMrIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAI 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446729146 548 GVPDEVKGEVCHCFVVLRDHVTFTgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGK 621
Cdd:PRK05677 488 GVPDEKSGEAIKVFVVVKPGETLT---KEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKK 558
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
20-616 |
1.86e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.50 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 20 GWMKSLGYeDYEIFYNKSIEETAWFWGEAEKAVGYQWMKPYTEVLDL---ENGTPFAQWYNGGTCNVVESALSRWLADEE 96
Cdd:PRK12316 2989 GLGASLTY-ATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLdaeERGQLLEAWNATAAEYPLERGVHRLFEEQV 3067
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 97 TRI--QPALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFA 174
Cdd:PRK12316 3068 ERTpdAVALAFGEQ-----RLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYP 3142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 175 SDAVMTRVQAAGSKMIITADGFSrrgkivslkdevdkaCEHCPTVEKVVIVRHAGNdftphnydfswstLEKEKPFIHae 254
Cdd:PRK12316 3143 EERLAYMLEDSGAQLLLSQSHLR---------------LPLAQGVQVLDLDRGDEN-------------YAEANPAIR-- 3192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 255 eMQSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFgMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMyEG 334
Cdd:PRK12316 3193 -TMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQA-YGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVL-AG 3269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 335 VPDFPEADRLWETVDKYEITHLGISPTLIRALMakgdEYVNKHSLKSLEVFASTGEPWNPDPWMWLFetvgkGNVPICNY 414
Cdd:PRK12316 3270 PEDWRDPALLVELINSEGVDVLHAYPSMLQAFL----EEEDAHRCTSLKRIVCGGEALPADLQQQVF-----AGLPLYNL 3340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 415 SGGTEISGGIFGNVLIKPIAPISFNAS-LPGMAAVVLDDQGKPI-RDEVGELCLEKpwVGMTKSFWE----DDERYVNTY 488
Cdd:PRK12316 3341 YGPTEATITVTHWQCVEEGKDAVPIGRpIANRACYILDGSLEPVpVGALGELYLGG--EGLARGYHNrpglTAERFVPDP 3418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 489 WSRFENKWVHGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIgvpdEVKGEVCHCFVVLRDH 567
Cdd:PRK12316 3419 FVPGERLYRTGDLARYRADGVIeYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDE 3494
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 446729146 568 vtfTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:PRK12316 3495 ---AGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
115-617 |
2.11e-22 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 101.37 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 115 FTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPI---FSGFASDAVMTRVQAAgsKMII 191
Cdd:PRK06155 47 WTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPIntaLRGPQLEHILRNSGAR--LLVV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 192 TADGFsrrgkivslkDEVDKACEHCPTVEKVVIVRHAGNDFTPHNYDFSwsTLEKEKPFIHAEEMQSDDPLMLIYTSGTT 271
Cdd:PRK06155 125 EAALL----------AALEAADPGDLPLPAVWLLDAPASVSVPAGWSTA--PLPPLDAPAPAAAVQPGDTAAILYTSGTT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 272 GKPKGTVHTHAGFPLKAAFDAGFgMNIKQGDrVLWVTdmgwmmgpFLLF---------GSLINGATMVMyegVPDFpEAD 342
Cdd:PRK06155 193 GPSKGVCCPHAQFYWWGRNSAED-LEIGADD-VLYTT--------LPLFhtnalnaffQALLAGATYVL---EPRF-SAS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 343 RLWETVDKYEIT---HLGISPTLIRALMAKGDEyvNKHSLKsleVFASTGEPwnPDPWMWLFETVGkgnVPICNYSGGTE 419
Cdd:PRK06155 259 GFWPAVRRHGATvtyLLGAMVSILLSQPARESD--RAHRVR---VALGPGVP--AALHAAFRERFG---VDLLDGYGSTE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 420 iSGGIFGNVLIKPiAPISFNASLPGMAAVVLDDQGKPIRD-EVGELCL--EKPWVGMTKSFwEDDERYVNTyWsrfENKW 496
Cdd:PRK06155 329 -TNFVIAVTHGSQ-RPGSMGRLAPGFEARVVDEHDQELPDgEPGELLLraDEPFAFATGYF-GMPEKTVEA-W---RNLW 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 497 VH-GDWVI--YDGEQYIItGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGE 573
Cdd:PRK06155 402 FHtGDRVVrdADGWFRFV-DRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPV 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446729146 574 lkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAA 617
Cdd:PRK06155 481 ---ALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
113-550 |
4.38e-22 |
|
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: 99.74 E-value: 4.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 113 KSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIfsgfasdavmtrvqaagskmiit 192
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALI----------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 193 adGFSRRGKivslkdevdkACEHCPTV--EKVVIVrhagndftphnydfswstlekekpfihaeemqsdDPLMLIYTSGT 270
Cdd:cd05940 59 --NYNLRGE----------SLAHCLNVssAKHLVV----------------------------------DAALYIYTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 271 TGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGdrVLWVT-----DMGWMMGpflLFGSLINGATMVMYEgvpDFpEADRLW 345
Cdd:cd05940 93 TGLPKAAIISHRRAWRGGAFFAGSGGALPSD--VLYTClplyhSTALIVG---WSACLASGATLVIRK---KF-SASNFW 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 346 ETVDKYEITHLGISPTLIRALM-AKGDEYVNKHSLKslevfASTGEPWNPDPWMwlfETVGKGNVP-ICNYSGGTEISGG 423
Cdd:cd05940 164 DDIRKYQATIFQYIGELCRYLLnQPPKPTERKHKVR-----MIFGNGLRPDIWE---EFKERFGVPrIAEFYAATEGNSG 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 424 iFGNVLIKPIApISFNASLP----GMAAVVLD-DQGKPIRD-----------EVGELCLE----KPWVGMTKS------- 476
Cdd:cd05940 236 -FINFFGKPGA-IGRNPSLLrkvaPLALVKYDlESGEPIRDaegrcikvprgEPGLLISRinplEPFDGYTDPaatekki 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446729146 477 ---FWEDDERYVNTywsrfenkwvhGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVP 550
Cdd:cd05940 314 lrdVFKKGDAWFNT-----------GDLMRLDGEGFWyFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQ 380
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
109-618 |
5.96e-22 |
|
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: 99.85 E-value: 5.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 109 NGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSK 188
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 189 MIITadgfsrrGKIvslkdevdkacEHCPTVEKVV---IVRHAGNDFTPHNYDFSWSTLEKEKPFIHAEEMQSDDPLM-L 264
Cdd:cd05932 81 ALFV-------GKL-----------DDWKAMAPGVpegLISISLPPPSAANCQYQWDDLIAQHPPLEERPTRFPEQLAtL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 265 IYTSGTTGKPKGTVHTHAGFplkaAFDAGFGMN---IKQGDRVLWVTDMGWMMGPFLLF-GSLINGATMVMYEGVPDFPE 340
Cdd:cd05932 143 IYTSGTTGQPKGVMLTFGSF----AWAAQAGIEhigTEENDRMLSYLPLAHVTERVFVEgGSLYGGVLVAFAESLDTFVE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 341 ------------ADRLWETVDKYEITHLGISP-----------TLIRALMAKGdeyvnkHSLKSLEVFASTGEPWNPDPW 397
Cdd:cd05932 219 dvqrarptlffsVPRLWTKFQQGVQDKIPQQKlnlllkipvvnSLVKRKVLKG------LGLDQCRLAGCGSAPVPPALL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 398 MWlFETVGkgnVPICNYSGGTEISGGIFGNVlikpiaPISFNASLPGMAAvvlddQGKPIR-DEVGELCLEKPwvGMTKS 476
Cdd:cd05932 293 EW-YRSLG---LNILEAYGMTENFAYSHLNY------PGRDKIGTVGNAG-----PGVEVRiSEDGEILVRSP--ALMMG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 477 FWEDDERyvnTYWSRFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIA-GKRIGPAEYESILVKHnDVIEAAAI---GVP 550
Cdd:cd05932 356 YYKDPEA---TAEAFTADGFLRtGDKGELDADGNLtITGRVKDIFKTSkGKYVAPAPIENKLAEH-DRVEMVCVigsGLP 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446729146 551 DEVKGEVCHCFVVLRDHVTFTGELK---KELMSLVNSHIGKALCPKDIHVVEDLPKTRNS------KVMRRVIKAAY 618
Cdd:cd05932 432 APLALVVLSEEARLRADAFARAELEaslRAHLARVNSTLDSHEQLAGIVVVKDPWSIDNGiltptlKIKRNVLEKAY 508
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
101-612 |
6.00e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 101.57 E-value: 6.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYEGEngtskSFTYEELDnwvsRVANGLKHAGIEKG----DRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASD 176
Cdd:PRK12316 4568 VAVVFDEE-----KLTYAELN----RRANRLAHALIARGvgpeVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRE 4638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 177 AVMTRVQAAGSKMIITADGFSRRgkiVSLKDEVdkaceHCPTVEKvvivrhagndftphnyDFSWSTLEKEKPfihAEEM 256
Cdd:PRK12316 4639 RLAYMMEDSGAALLLTQSHLLQR---LPIPDGL-----ASLALDR----------------DEDWEGFPAHDP---AVRL 4691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 257 QSDDPLMLIYTSGTTGKPKGTVHTHAGF-PLKAAFDAGFGMNikQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEgv 335
Cdd:PRK12316 4692 HPDNLAYVIYTSGSTGRPKGVAVSHGSLvNHLHATGERYELT--PDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRD-- 4767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 336 PDFPEADRLWETVDKYEITHLGISPTLIRALmAKGDEyvNKHSLKSLEVFASTGEPWNPDPWMWLFETVgkGNVPICNYS 415
Cdd:PRK12316 4768 DSLWDPERLYAEIHEHRVTVLVFPPVYLQQL-AEHAE--RDGEPPSLRVYCFGGEAVAQASYDLAWRAL--KPVYLFNGY 4842
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 416 GGTEISGGIF------GNVLIKPIAPISfnASLPGMAAVVLDDQGKPIR-DEVGELCLEKPwvGMTKSFWE----DDERY 484
Cdd:PRK12316 4843 GPTETTVTVLlwkardGDACGAAYMPIG--TPLGNRSGYVLDGQLNPLPvGVAGELYLGGE--GVARGYLErpalTAERF 4918
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 485 V-NTYWSRFENKWVHGDWVIY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVkGEVCHC 560
Cdd:PRK12316 4919 VpDPFGAPGGRLYRTGDLARYraDGViDYL--GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAV-GKQLVG 4995
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 446729146 561 FVV-----LRDHVTFTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:PRK12316 4996 YVVpqdpaLADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRK 5052
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
101-555 |
1.97e-21 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 98.79 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYEGengtsKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:PRK08279 54 PALLFED-----QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 181 RVQAAGSKMIITADGFSRRgkIVSLKDEVDKACEHCPTVEKVVIVRHAGNDftphnYDFSWSTLEKEKPfIHAEEMQSDD 260
Cdd:PRK08279 129 SLNLVDAKHLIVGEELVEA--FEEARADLARPPRLWVAGGDTLDDPEGYED-----LAAAAAGAPTTNP-ASRSGVTAKD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 261 PLMLIYTSGTTGKPKGTVHTHAGFpLKAAfdAGFG--MNIKQGDRVLWVTDMGWMMGPFLLFGSLIN-GATMVMYEgvpD 337
Cdd:PRK08279 201 TAFYIYTSGTTGLPKAAVMSHMRW-LKAM--GGFGglLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAaGATLALRR---K 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 338 FpEADRLWETVDKYEITHLGISPTLIRALM---AKGDEyvNKHSLKSLevfasTGEPWNPDPWMWLFETVGkgnVP-ICN 413
Cdd:PRK08279 275 F-SASRFWDDVRRYRATAFQYIGELCRYLLnqpPKPTD--RDHRLRLM-----IGNGLRPDIWDEFQQRFG---IPrILE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 414 YSGGTEISGGIFgNVLIKPIApISF-NASLPGMAAVV-LD-DQGKPIRD-----------EVGELcLEK-----PWVGMT 474
Cdd:PRK08279 344 FYAASEGNVGFI-NVFNFDGT-VGRvPLWLAHPYAIVkYDvDTGEPVRDadgrcikvkpgEVGLL-IGRitdrgPFDGYT 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 475 KS-----------FwEDDERYVNTywsrfenkwvhGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVI 542
Cdd:PRK08279 421 DPeasekkilrdvF-KKGDAWFNT-----------GDLMRDDGFGHAqFVDRLGDTFRWKGENVATTEVENALSGFPGVE 488
|
490
....*....|...
gi 446729146 543 EAAAIGVpdEVKG 555
Cdd:PRK08279 489 EAVVYGV--EVPG 499
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
258-608 |
3.65e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 95.53 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 258 SDDPLMLIYTSGTTGKPKGTVHTHAGFP--LKAAFDAGFG---MNIKQGDRVLWVTDMGWMMGPFLL--------FGSLI 324
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVMWRQEDIFrmLMGGADFGTGeftPSEDAHKAAAAAAGTVMFPAPPLMhgtgswtaFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 325 NGATMVmyegVPDFP-EADRLWETVDKYEITHLGI-----SPTLIRALMAKGDeyvnkHSLKSLEVFASTGEPWNPDPWM 398
Cdd:cd05924 82 GGQTVV----LPDDRfDPEEVWRTIEKHKVTSMTIvgdamARPLIDALRDAGP-----YDLSSLFAISSGGALLSPEVKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 399 WLFETVGkgNVPICNYSGGTEISGGIFGNVliKPIAPISFNASLPGMAAVVLDDQGKPI---RDEVGelclekpWVG--- 472
Cdd:cd05924 153 GLLELVP--NITLVDAFGSSETGFTGSGHS--AGSGPETGPFTRANPDTVVLDDDGRVVppgSGGVG-------WIArrg 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 473 -MTKSFWEDDERYVNTYWSRFENKW-VHGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGV 549
Cdd:cd05924 222 hIPLGYYGDEAKTAETFPEVDGVRYaVPGDRATVEADGTVtLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGR 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446729146 550 PDEVKGEVCHCFVVLRDHVTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSK 608
Cdd:cd05924 302 PDERWGQEVVAVVQLREGAGVDLE---ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
260-611 |
7.37e-21 |
|
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: 94.25 E-value: 7.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 260 DPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEgvpDFP 339
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGG---ENT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 340 EADRLWETVDKYEITHLGISPTLIRALMakgDEYVNK-HSLKSLEVFASTGE-PWNPDPWMWLFetvgKGNVPICNYSGG 417
Cdd:cd17635 79 TYKSLFKILTTNAVTTTCLVPTLLSKLV---SELKSAnATVPSLRLIGYGGSrAIAADVRFIEA----TGLTNTAQVYGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 418 TEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQG-KPIRDEVGELCLEKPWvgMTKSFWEDDERYVntywSRFENKW 496
Cdd:cd17635 152 SETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGiAGPSASFGTIWIKSPA--NMLGYWNNPERTA----EVLIDGW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 497 VH-GD--WVIYDGEQYIiTGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLrdhvtfTGE 573
Cdd:cd17635 226 VNtGDlgERREDGFLFI-TGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA------SAE 298
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446729146 574 LKKELMS----LVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:cd17635 299 LDENAIRalkhTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
264-611 |
1.91e-20 |
|
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: 92.95 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 264 LIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGmNIKQGDRVLWVTdmgwmmgPFL-LFG-------SLINGATMVmyegv 335
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCA-DLTEDDRYLIIN-------PFFhTFGykagivaCLLTGATVV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 336 pdfPEA----DRLWETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLEvFASTGEPWNPDPWM------WLFETVG 405
Cdd:cd17638 72 ---PVAvfdvDAILEAIERERITVLPGPPTLFQSLLDHPGR--KKFDLSSLR-AAVTGAATVPVELVrrmrseLGFETVL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 406 KGnvpicnySGGTEISGGifgnVLIKPIAPISFNAS-----LPGMAAVVLDDqgkpirdevGELCLEKPWVgmTKSFWED 480
Cdd:cd17638 146 TA-------YGLTEAGVA----TMCRPGDDAETVATtcgraCPGFEVRIADD---------GEVLVRGYNV--MQGYLDD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 481 DEryvNTYWSRFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVC 558
Cdd:cd17638 204 PE---ATAEAIDADGWLHtGDVGELDERGYLrITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVG 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446729146 559 HCFVVLRDHVTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:cd17638 281 KAFVVARPGVTLTEE---DVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
114-612 |
6.46e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 93.52 E-value: 6.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 114 SFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITA 193
Cdd:PRK13383 60 ALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVAD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 194 DGFSRR----GKIVSLKDEVDKACEHCPTVEKVvivrhagndftphnydfswstlekekpfihaeemqSDDPLMLIYTSG 269
Cdd:PRK13383 140 NEFAERiagaDDAVAVIDPATAGAEESGGRPAV-----------------------------------AAPGRIVLLTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 270 TTGKPKGTvhthagfPLKAAFDAGFGMNI--------KQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGVpdfpEA 341
Cdd:PRK13383 185 TTGKPKGV-------PRAPQLRSAVGVWVtildrtrlRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTHRHF----DA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 342 DRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKgnvPICNYSGGTEIS 421
Cdd:PRK13383 254 EAALAQASLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGD---ILYNGYGSTEVG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 422 GGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGKPIRDEV-------GELCLEKPWVGMTKSFwedderyVNTYWSRfen 494
Cdd:PRK13383 331 IGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVtgrifvgGELAGTRYTDGGGKAV-------VDGMTST--- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 495 kwvhGDWVIYD--GEQYIItGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHvtfTG 572
Cdd:PRK13383 401 ----GDMGYLDnaGRLFIV-GREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG---SG 472
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446729146 573 ELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:PRK13383 473 VDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRK 512
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
115-611 |
7.12e-20 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 93.55 E-value: 7.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 115 FTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITAD 194
Cdd:PLN03102 40 FTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 195 GFSRRGKIVSLKDEVDKACEHCPtvekvVIVRHAgNDFT--PHNYDFSWSTL-EKEKP---------FIHAEEmqsdDPL 262
Cdd:PLN03102 120 SFEPLAREVLHLLSSEDSNLNLP-----VIFIHE-IDFPkrPSSEELDYECLiQRGEPtpslvarmfRIQDEH----DPI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 263 MLIYTSGTTGKPKGTVHTHAGFPLkAAFDAGFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGVpdfpEAD 342
Cdd:PLN03102 190 SLNYTSGTTADPKGVVISHRGAYL-STLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHV----TAP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 343 RLWETVDKYEITHLGISPTLIRALMaKGDEYVNKHslKSLEVFASTGepwNPDPWMWLFETVGKGNVPICNYSGGTEISG 422
Cdd:PLN03102 265 EIYKNIEMHNVTHMCCVPTVFNILL-KGNSLDLSP--RSGPVHVLTG---GSPPPAALVKKVQRLGFQVMHAYGLTEATG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 423 gifgnvlikpiaPISFNA------SLP-----------GMAAVVLDD--------QGKPIRD--EVGELCLEKPwvGMTK 475
Cdd:PLN03102 339 ------------PVLFCEwqdewnRLPenqqmelkarqGVSILGLADvdvknketQESVPRDgkTMGEIVIKGS--SIMK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 476 SFWEDDEryvnTYWSRFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEV 553
Cdd:PLN03102 405 GYLKNPK----ATSEAFKHGWLNtGDVGVIHPDGHVeIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPT 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446729146 554 KGEVCHCFVVLRDHVTFTGEL-------KKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:PLN03102 481 WGETPCAFVVLEKGETTKEDRvdklvtrERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILK 545
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
101-590 |
7.57e-20 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 94.73 E-value: 7.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:PRK10252 475 PALADARY-----QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKM 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 181 RVQAAGSKMIITADGFSRRgkivslkdevdkacehcptvekvvivRHAGNDFTPHNYDfSWSTLEKEKPFIHAeemQSDD 260
Cdd:PRK10252 550 MLEDARPSLLITTADQLPR--------------------------FADVPDLTSLCYN-APLAPQGAAPLQLS---QPHH 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 261 PLMLIYTSGTTGKPKGTVHTHAG-----------FPLKAAfdagfgmnikqgDRVLWVTDMGWMMGPFLLFGSLINGATM 329
Cdd:PRK10252 600 TAYIIFTSGSTGRPKGVMVGQTAivnrllwmqnhYPLTAD------------DVVLQKTPCSFDVSVWEFFWPFIAGAKL 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 330 VMYEgvpdfPEADR----LWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSL-EVFAStGEPWNP---DPWMWLF 401
Cdd:PRK10252 668 VMAE-----PEAHRdplaMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLrQVFCS-GEALPAdlcREWQQLT 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 402 etvgkgNVPICNYSGGTEI---------SGGIFGNVLIKPIaPISF---NASLpgmaaVVLDDQGKPIRDEV-GELC--- 465
Cdd:PRK10252 742 ------GAPLHNLYGPTEAavdvswypaFGEELAAVRGSSV-PIGYpvwNTGL-----RILDARMRPVPPGVaGDLYltg 809
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 466 --LEKPWVGmtksfwEDD---ERYVNTYWSRFENKWVHGD---WvIYDGE-QYIitGRSDDTLNIAGKRIGPAEYESILV 536
Cdd:PRK10252 810 iqLAQGYLG------RPDltaSRFIADPFAPGERMYRTGDvarW-LDDGAvEYL--GRSDDQLKIRGQRIELGEIDRAMQ 880
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446729146 537 KHNDVIEAAAIGvpdevkgevchcfVVLRDHVTFTGElKKELMSLVNSHIGKAL 590
Cdd:PRK10252 881 ALPDVEQAVTHA-------------CVINQAAATGGD-ARQLVGYLVSQSGLPL 920
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
264-616 |
8.59e-20 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 92.83 E-value: 8.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 264 LIYTSGTTGKPKGTVHTHAGFPLKAA--FDAGFGMNIKQGDRVLWVTDM------GWMMGpfllfgSLINGATMVmyeGV 335
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDtlMAAALGFGPGADSVYLSPAPLyhaapfRWSMT------ALFMGGTLV---LM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 336 PDFpEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEP---WNPDPWM-WLFETvgkgnvpI 411
Cdd:cd05929 201 EKF-DPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPcppWVKEQWIdWGGPI-------I 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 412 CNYSGGTEISGGIF----------GNVlikpiapisfnaslpGMAAV----VLDDQGKPI-RDEVGELCLEKPwvgmtkS 476
Cdd:cd05929 273 WEYYGGTEGQGLTIingeewlthpGSV---------------GRAVLgkvhILDEDGNEVpPGEIGEVYFANG------P 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 477 FWEDDERYVNTYWSRFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVK 554
Cdd:cd05929 332 GFEYTNDPEKTAAARNEGGWSTlGDVGYLDEDGYLyLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEEL 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446729146 555 GEVCHCFVVLRDHVTFTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:cd05929 412 GQRVHAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
116-628 |
9.38e-20 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 93.56 E-value: 9.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIispifsGFASDAVMTRVQAA------GSKM 189
Cdd:PRK06060 32 THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVM------AFLANPELHRDDHAlaarntEPAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 190 IITADGFSRRGKIVSLKDEVDKACEhcptvekvvIVRHAGNDFTPHNYD-FSWSTlekekpfihaeemqsddplmliYTS 268
Cdd:PRK06060 106 VVTSDALRDRFQPSRVAEAAELMSE---------AARVAPGGYEPMGGDaLAYAT----------------------YTS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 269 GTTGKPKGTVHTHAG-FPLKAAFDAGfGMNIKQGDRVLWVTDM--GWMMGPFLLFgSLINGATMVMyEGVPDFPEADRLW 345
Cdd:PRK06060 155 GTTGPPKAAIHRHADpLTFVDAMCRK-ALRLTPEDTGLCSARMyfAYGLGNSVWF-PLATGGSAVI-NSAPVTPEAAAIL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 346 ETvdKYEITHL-GISPTLIRALMAkgdeyVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGkgNVPICNYSGGTEIsGGI 424
Cdd:PRK06060 232 SA--RFGPSVLyGVPNFFARVIDS-----CSPDSFRSLRCVVSAGEALELGLAERLMEFFG--GIPILDGIGSTEV-GQT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 425 FGNVLIKPIAPISFNASLPGMAAVVLDDQGKpirdEVGElclekpwvGMTKSFWEDDERYVNTYWSRFENKWVHGDW--- 501
Cdd:PRK06060 302 FVSNRVDEWRLGTLGRVLPPYEIRVVAPDGT----TAGP--------GVEGDLWVRGPAIAKGYWNRPDSPVANEGWldt 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 502 ---VIYDGEQYIITG-RSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGELKKE 577
Cdd:PRK06060 370 rdrVCIDSDGWVTYRcRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRD 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 446729146 578 LMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGKELGDLSS 628
Cdd:PRK06060 450 LHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKPIWELSL 500
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
129-621 |
1.10e-19 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 93.19 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 129 NGLKhagIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRrgkivSLKDE 208
Cdd:PRK08974 67 NGLG---LKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAH-----TLEKV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 209 VDKACehcptVEKVVIVRhAGN----------DFT-------------PHNYDFSwSTLEKE------KPfihaeEMQSD 259
Cdd:PRK08974 139 VFKTP-----VKHVILTR-MGDqlstakgtlvNFVvkyikrlvpkyhlPDAISFR-SALHKGrrmqyvKP-----ELVPE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 260 DPLMLIYTSGTTGKPKGTVHTHAGFPlkaafdagfgMNIKQGDrvlwvtdmgWMMGPFL---------------LFGSLI 324
Cdd:PRK08974 207 DLAFLQYTGGTTGVAKGAMLTHRNML----------ANLEQAK---------AAYGPLLhpgkelvvtalplyhIFALTV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 325 N-------GATMVMYEGVPDFPEadrLWETVDKYEITHLGISPTLIRALMAKGD-EYVNKHSLK-----SLEVFASTGEP 391
Cdd:PRK08974 268 NcllfielGGQNLLITNPRDIPG---FVKELKKYPFTAITGVNTLFNALLNNEEfQELDFSSLKlsvggGMAVQQAVAER 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 392 WnpdpwmwlfETVGKGNVpICNYsGGTEISGGIFGNvlikPIAPISFNASL----PGMAAVVLDDQGKPI-RDEVGELCL 466
Cdd:PRK08974 345 W---------VKLTGQYL-LEGY-GLTECSPLVSVN----PYDLDYYSGSIglpvPSTEIKLVDDDGNEVpPGEPGELWV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 467 EKPWVgMtKSFWEDDERYVNTywsrFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEA 544
Cdd:PRK08974 410 KGPQV-M-LGYWQRPEATDEV----IKDGWLAtGDIAVMDEEGFLrIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEV 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446729146 545 AAIGVPDEVKGEVCHCFVVLRDHvTFTgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAAYLGK 621
Cdd:PRK08974 484 AAVGVPSEVSGEAVKIFVVKKDP-SLT---EEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
115-617 |
1.76e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 92.32 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 115 FTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITAD 194
Cdd:PRK08162 44 RTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 195 GFSrrgkivslkDEVDKACEHCPTVEKVVI---------VRHAGN----DFTPH-NYDFSWSTLEKEKpfihaeemqsdD 260
Cdd:PRK08162 124 EFA---------EVAREALALLPGPKPLVIdvddpeypgGRFIGAldyeAFLASgDPDFAWTLPADEW-----------D 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 261 PLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDA-GFGMniKQGDRVLWVTDM----GWMMgPFLLfgsLINGATMVMYEGV 335
Cdd:PRK08162 184 AIALNYTSGTTGNPKGVVYHHRGAYLNALSNIlAWGM--PKHPVYLWTLPMfhcnGWCF-PWTV---AARAGTNVCLRKV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 336 pdfpEADRLWETVDKYEITHLGISPTLIRALMAKGDEYvnKHSLKSLEVFASTGEPwnpdPWMWLFETVGKGNVPICNYS 415
Cdd:PRK08162 258 ----DPKLIFDLIREHGVTHYCGAPIVLSALINAPAEW--RAGIDHPVHAMVAGAA----PPAAVIAKMEEIGFDLTHVY 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 416 GGTEISGgifgnvlikpiaPISFNASLPGMAAVVLDDQG-KPIRDEVGELCLEK------------PWVGMT-------- 474
Cdd:PRK08162 328 GLTETYG------------PATVCAWQPEWDALPLDERAqLKARQGVRYPLQEGvtvldpdtmqpvPADGETigeimfrg 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 475 ----KSFWEDDERYVNTywsrFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIG 548
Cdd:PRK08162 396 nivmKGYLKNPKATEEA----FAGGWFHtGDLAVLHPDGYIkIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVA 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446729146 549 VPDEVKGEVCHCFVVLRDHVTFTGElkkELMSLVNSHIGKALCPKDIhVVEDLPKTRNSK----VMRRVIKAA 617
Cdd:PRK08162 472 KPDPKWGEVPCAFVELKDGASATEE---EIIAHCREHLAGFKVPKAV-VFGELPKTSTGKiqkfVLREQAKSL 540
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
113-617 |
1.95e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 92.25 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 113 KSFTYEELDNWVSRVANGL-KHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMII 191
Cdd:PRK08751 49 KTITYREADQLVEQFAAYLlGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 192 TADGFSrrgkivslkDEVDKACEHCPtVEKVV------------------IVRHAgNDFTPhNYDFSWSTLEKE------ 247
Cdd:PRK08751 129 VIDNFG---------TTVQQVIADTP-VKQVIttglgdmlgfpkaalvnfVVKYV-KKLVP-EYRINGAIRFREalalgr 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 248 KPFIHAEEMQSDDPLMLIYTSGTTGKPKGTVHTH----AGFPLKAAFDAGFGmNIKQGDRVLWVTdmgwmMGPFLLFGSL 323
Cdd:PRK08751 197 KHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHrnlvANMQQAHQWLAGTG-KLEEGCEVVITA-----LPLYHIFALT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 324 INGATMVMYEGVPDFPEADR----LWETVDKYEITHLGISPTLIRALM-AKGDEYVNKHSLK-----SLEVFASTGEPWN 393
Cdd:PRK08751 271 ANGLVFMKIGGCNHLISNPRdmpgFVKELKKTRFTAFTGVNTLFNGLLnTPGFDQIDFSSLKmtlggGMAVQRSVAERWK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 394 pdpwmwlfETVGkgnVPICNYSGGTEISGGifgnVLIKPIAPISFNASL----PGMAAVVLDDQGKPIR-DEVGELCLEK 468
Cdd:PRK08751 351 --------QVTG---LTLVEAYGLTETSPA----ACINPLTLKEYNGSIglpiPSTDACIKDDAGTVLAiGEIGELCIKG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 469 PWVgmTKSFWEDDERyvnTYWSRFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAA 546
Cdd:PRK08751 416 PQV--MKGYWKRPEE---TAKVMDADGWLHtGDIARMDEQGFVyIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAA 490
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446729146 547 IGVPDEVKGEVCHCFVVLRDHVTFTGELKKElmslVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKAA 617
Cdd:PRK08751 491 VGVPDEKSGEIVKVVIVKKDPALTAEDVKAH----ARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDA 557
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
101-616 |
4.18e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 92.71 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYEGENgtsksFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:PRK12316 2020 IAVVFGDQH-----LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAY 2094
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 181 RVQAAGSKMIITADGFSRRgkivslkdevdkacehCPTVEKVVIVrhagnDFTPhnyDFSWSTLEKEKPfihAEEMQSDD 260
Cdd:PRK12316 2095 MLEDSGAALLLTQRHLLER----------------LPLPAGVARL-----PLDR---DAEWADYPDTAP---AVQLAGEN 2147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 261 PLMLIYTSGTTGKPKGTVHTHAgfPLKAAFDA-GFGMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMYEGVPDFP 339
Cdd:PRK12316 2148 LAYVIYTSGSTGLPKGVAVSHG--ALVAHCQAaGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDP 2225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 340 EadRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSL---------EVFASTGEPWNPDPWMWLF---ETVgkg 407
Cdd:PRK12316 2226 E--QLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYcfggeavpaASLRLAWEALRPVYLFNGYgptEAV--- 2300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 408 nVPICNYSGGTEISGGIFGnvlikpiAPISfnASLPGMAAVVLDDQGKPIRDE-VGELCLEKpwVGMTKSFWE----DDE 482
Cdd:PRK12316 2301 -VTPLLWKCRPQDPCGAAY-------VPIG--RALGNRRAYILDADLNLLAPGmAGELYLGG--EGLARGYLNrpglTAE 2368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 483 RYV-NTYWSRFENKWVHGDWVIY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVpDEVKGEVC 558
Cdd:PRK12316 2369 RFVpDPFSASGERLYRTGDLARYraDGVvEYL--GRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQL 2445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 446729146 559 HCFVVLRDHVT-FTGELKKELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:PRK12316 2446 VAYVVPDDAAEdLLAELRAWLAARLPAY----MVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
111-615 |
1.75e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 88.91 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 111 TSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMI 190
Cdd:PRK13390 21 TGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 191 ITAdgfsrrgkiVSLKDEVDKACEHCPtvekvviVRHAGNDFTPHNYDFSwSTLEKEKPFIHAEEMQSddplMLIYTSGT 270
Cdd:PRK13390 101 VAS---------AALDGLAAKVGADLP-------LRLSFGGEIDGFGSFE-AALAGAGPRLTEQPCGA----VMLYSSGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 271 TGKPKGTVHTHAGFPLKAAFD-----AGFGMNIKQGDrVLWVTDMGWMMGPfLLFGSLIN--GATMVMYEgvpDFPEADR 343
Cdd:PRK13390 160 TGFPKGIQPDLPGRDVDAPGDpivaiARAFYDISESD-IYYSSAPIYHAAP-LRWCSMVHalGGTVVLAK---RFDAQAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 344 LwETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGkgnvPIC-NYSGGTEISG 422
Cdd:PRK13390 235 L-GHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLG----PIVyEYYSSTEAHG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 423 GIFGNVLIKPIAPISFNASLPGMAAVVLDDQGKPIRDEVGELCLEKPwvGMTKSFWEDDERYV------NTYWSRFenkw 496
Cdd:PRK13390 310 MTFIDSPDWLAHPGSVGRSVLGDLHICDDDGNELPAGRIGTVYFERD--RLPFRYLNDPEKTAaaqhpaHPFWTTV---- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 497 vhGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGELK 575
Cdd:PRK13390 384 --GDLGSVDEDGYLyLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELA 461
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446729146 576 KELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:PRK13390 462 RELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
92-613 |
2.32e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 88.65 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 92 LADEETRIQP---ALQYEGengtsKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISP 168
Cdd:PRK06164 15 LLDAHARARPdavALIDED-----RPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 169 IFSGFASDAVMTRVQAAGSKMIITADGFsRRGKIVSLKDEVDKACEhcPTVEKVVIVRHAGNDfTPHNYDFSWSTL---- 244
Cdd:PRK06164 90 VNTRYRSHEVAHILGRGRARWLVVWPGF-KGIDFAAILAAVPPDAL--PPLRAIAVVDDAADA-TPAPAPGARVQLfalp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 245 EKEKPFIHAEEMQSDDPLMLIY-TSGTTGKPKGTVHTHAGFPLKAAFDA-GFGMNikQGDRVLWVTDMGWMMGPFLLFGS 322
Cdd:PRK06164 166 DPAPPAAAGERAADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIArAYGYD--PGAVLLAALPFCGVFGFSTLLGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 323 LINGATMVMyEGVPDFPEADRLwetVDKYEITHLGISPTLIRALMAKGDEyvnKHSLKSLEV--FASTGEPWNPdpwmwL 400
Cdd:PRK06164 244 LAGGAPLVC-EPVFDAARTARA---LRRHRVTHTFGNDEMLRRILDTAGE---RADFPSARLfgFASFAPALGE-----L 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 401 FETVGKGNVPICNYSGGTEisggIFGNVLIKPIAPISFNASLPGMAAV-------VLDDQGKPI--RDEVGELCLEKPWV 471
Cdd:PRK06164 312 AALARARGVPLTGLYGSSE----VQALVALQPATDPVSVRIEGGGRPAspearvrARDPQDGALlpDGESGEIEIRAPSL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 472 ---------GMTKSFWEDDerYVNTywsrfenkwvhGDWVIYDGE-QYIITGRSDDTLNIAGKRIGPAEYESILVKHNDV 541
Cdd:PRK06164 388 mrgyldnpdATARALTDDG--YFRT-----------GDLGYTRGDgQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGV 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446729146 542 IEAAAIGVpdEVKGE-VCHCFVVLRDHVTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTR--NSKVMRRV 613
Cdd:PRK06164 455 AAAQVVGA--TRDGKtVPVAFVIPTDGASPDEA---GLMAACREALAGFKVPARVQVVEAFPVTEsaNGAKIQKH 524
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
103-543 |
2.37e-18 |
|
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: 88.27 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 103 LQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRV 182
Cdd:cd05914 1 LYYGGE-----PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 183 QAAGSKMIITADgfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihaeemqSDDPL 262
Cdd:cd05914 76 NHSEAKAIFVSD---------------------------------------------------------------EDDVA 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 263 MLIYTSGTTGKPKGTVHTHAGfpLKAAFDAGFGMNI-KQGDRVLWVTDMGWMMGpfLLFGSLI---NGATMVMYEGVPDf 338
Cdd:cd05914 93 LINYTSGTTGNSKGVMLTYRN--IVSNVDGVKEVVLlGKGDKILSILPLHHIYP--LTFTLLLpllNGAHVVFLDKIPS- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 339 PEADRLwetvDKYEITHLGISPTLIRALMAKGDEYVNKHSLK-----------------------------SLEVFASTG 389
Cdd:cd05914 168 AKIIAL----AFAQVTPTLGVPVPLVIEKIFKMDIIPKLTLKkfkfklakkinnrkirklafkkvheafggNIKEFVIGG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 390 EPWNPDpwmwLFETVGKGNVPICNYSGGTEISggifgnvlikPIapISFNaslpGMAAVVLDDQGKPIRD-EV------- 461
Cdd:cd05914 244 AKINPD----VEEFLRTIGFPYTIGYGMTETA----------PI--ISYS----PPNRIRLGSAGKVIDGvEVridspdp 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 462 ----GELCLEKPwvGMTKSFWEDDERYVNTYwsrFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNI-AGKRIGPAEYESI 534
Cdd:cd05914 304 atgeGEIIVRGP--NVMKGYYKNPEATAEAF---DKDGWFHtGDLGKIDAEGYLyIRGRKKEMIVLsSGKNIYPEEIEAK 378
|
....*....
gi 446729146 535 LVKHNDVIE 543
Cdd:cd05914 379 INNMPFVLE 387
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
139-603 |
4.00e-18 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 87.77 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 139 GDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADGFSRRGKIvslkdevdkacEHCPT 218
Cdd:cd05909 31 GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEKLKL-----------HHLFD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 219 VEkvvivrhagndftphnYDFSW----------STLEKEKPFIHAE-------------EMQSDDPLMLIYTSGTTGKPK 275
Cdd:cd05909 100 VE----------------YDARIvyledlrakiSKADKCKAFLAGKfppkwllrifgvaPVQPDDPAVILFTSGSEGLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 276 GTVHTHAGF-----PLKAAFDAgfgmniKQGDRVLWVtdmgwmMGPFLLFG-------SLINGATMVMYegvPDFPEADR 343
Cdd:cd05909 164 GVVLSHKNLlanveQITAIFDP------NPEDVVFGA------LPFFHSFGltgclwlPLLSGIKVVFH---PNPLDYKK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 344 LWETVDKYEITHLGISPTLIRALMakgdEYVNKHSLKSLEVFASTGEPWNP---DPWMWLFetvgkgNVPICNYSGGTEI 420
Cdd:cd05909 229 IPELIYDKKATILLGTPTFLRGYA----RAAHPEDFSSLRLVVAGAEKLKDtlrQEFQEKF------GIRILEGYGTTEC 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 421 SGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGK-PIRDEVGELCLEKPwVGMTKSFWEDDERYVntywSRFENKW-VH 498
Cdd:cd05909 299 SPVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHeEVPIGEGGLLLVRG-PNVMLGYLNEPELTS----FAFGDGWyDT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 499 GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKH--NDViEAAAIGVPDEVKGEVchcfVVLrdhVTFTGELK 575
Cdd:cd05909 374 GDIGKIDGEGFLtITGRLSRFAKIAGEMVSLEAIEDILSEIlpEDN-EVAVVSVPDGRKGEK----IVL---LTTTTDTD 445
|
490 500 510
....*....|....*....|....*....|
gi 446729146 576 KELMS--LVNSHIGKALCPKDIHVVEDLPK 603
Cdd:cd05909 446 PSSLNdiLKNAGISNLAKPSYIHQVEEIPL 475
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
116-615 |
6.69e-18 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 87.50 E-value: 6.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITADG 195
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 196 FsrrgkiVSLkdeVDKACEHCPTVEKVVIVrhAGNDFTP----------------HNYDFSWSTLEKekpfihaeemqsD 259
Cdd:PRK06018 121 F------VPI---LEKIADKLPSVERYVVL--TDAAHMPqttlknavayeewiaeADGDFAWKTFDE------------N 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 260 DPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFG-MNIKQGDRVLWVTDM----GWMMGpfllFGSLINGATMVMyeg 334
Cdd:PRK06018 178 TAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANNGDaLGTSAADTMLPVVPLfhanSWGIA----FSAPSMGTKLVM--- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 335 vpdfPEAD----RLWETVDKYEITHLGISPTLIRALMakgdEYVNKHSLK--SLEVFASTGEPWnPDPWMWLFETVGkgn 408
Cdd:PRK06018 251 ----PGAKldgaSVYELLDTEKVTFTAGVPTVWLMLL----QYMEKEGLKlpHLKMVVCGGSAM-PRSMIKAFEDMG--- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 409 VPICNYSGGTEISG-GIFGnVLIKPIAPISFNASLPgmaavVLDDQGKP-------IRDEVGElclEKPWVGMT------ 474
Cdd:PRK06018 319 VEVRHAWGMTEMSPlGTLA-ALKPPFSKLPGDARLD-----VLQKQGYPpfgvemkITDDAGK---ELPWDGKTfgrlkv 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 475 ------KSFWE------DDERYVNTywsrfenkwvhGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDV 541
Cdd:PRK06018 390 rgpavaAAYYRvdgeilDDDGFFDT-----------GDVATIDAYGYMrITDRSKDVIKSGGEWISSIDLENLAVGHPKV 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446729146 542 IEAAAIGVPDEVKGEVCHCFVVLRDHVTFTgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:PRK06018 459 AEAAVIGVYHPKWDERPLLIVQLKPGETAT---REEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
114-612 |
8.44e-18 |
|
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: 86.76 E-value: 8.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 114 SFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITa 193
Cdd:cd17656 13 KLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 194 dgfsrrgkivslkdevdkaCEHCPTvekvvivrhagndftphNYDFSWSTLEKEKPFIHAEEMQ-------SDDPLMLIY 266
Cdd:cd17656 92 -------------------QRHLKS-----------------KLSFNKSTILLEDPSISQEDTSnidyinnSDDLLYIIY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 267 TSGTTGKPKGTVHTHAGFP--LKAAFDAgfgMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATM--VMYEGVPDFPEad 342
Cdd:cd17656 136 TSGTTGKPKGVQLEHKNMVnlLHFEREK---TNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLyiIREETKRDVEQ-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 343 rLWETVDKYEITHLgISPTLIRALMAKGDEYVN------KHSLKSLEVFASTGEpwnpdpwmwLFETVGKGNVPICNYSG 416
Cdd:cd17656 211 -LFDLVKRHNIEVV-FLPVAFLKFIFSEREFINrfptcvKHIITAGEQLVITNE---------FKEMLHEHNVHLHNHYG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 417 GTEISggIFGNVLIKPIAPISfnaSLP--GMAAV-----VLDDQGKPI-RDEVGELCLEKpwVGMTKSFWEDD----ERY 484
Cdd:cd17656 280 PSETH--VVTTYTINPEAEIP---ELPpiGKPISntwiyILDQEQQLQpQGIVGELYISG--ASVARGYLNRQeltaEKF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 485 VNTYWSRFENKWVHGDWVIY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKG-EVCHC 560
Cdd:cd17656 353 FPDPFDPNERMYRTGDLARYlpDGNiEFL--GRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEkYLCAY 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 446729146 561 FVVLrdhVTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd17656 431 FVME---QELNIS---QLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRK 476
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
114-612 |
1.12e-17 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 86.80 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 114 SFTYEELDNWVSRVANGL-KHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIIT 192
Cdd:PRK12492 49 TLSYAELERHSAAFAAYLqQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 193 ADGFsrrGKIVSlkdEV--DKACEHC---------PT------------VEKVVIVRHagndfTPHNYDFSWSTLEKEKP 249
Cdd:PRK12492 129 LNMF---GKLVQ---EVlpDTGIEYLieakmgdllPAakgwlvntvvdkVKKMVPAYH-----LPQAVPFKQALRQGRGL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 250 FIHAEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGF-----PLKAAF---DAGFGMNIKQGDRVlwvtdmgwMMGPFLLFG 321
Cdd:PRK12492 198 SLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLvanmlQVRACLsqlGPDGQPLMKEGQEV--------MIAPLPLYH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 322 ----------SLINGATMVMYEGVPDFPEadrLWETVDKYEITHLGISPTLIRALMAKGD-EYVNKHSLKSLE-----VF 385
Cdd:PRK12492 270 iyaftancmcMMVSGNHNVLITNPRDIPG---FIKELGKWRFSALLGLNTLFVALMDHPGfKDLDFSALKLTNsggtaLV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 386 ASTGEPWNpdpwmwlfetvgkgnvpicNYSGGTEISGgiFGNVLIKPIA---PISFNASL-------PGMAAVVLDDQGK 455
Cdd:PRK12492 347 KATAERWE-------------------QLTGCTIVEG--YGLTETSPVAstnPYGELARLgtvgipvPGTALKVIDDDGN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 456 PIR-DEVGELCLEKPWVgmTKSFWEDDERyvnTYWSRFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYE 532
Cdd:PRK12492 406 ELPlGERGELCIKGPQV--MKGYWQQPEA---TAEALDAEGWFKtGDIAVIDPDGFVrIVDRKKDLIIVSGFNVYPNEIE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 533 SILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDhvtfTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:PRK12492 481 DVVMAHPKVANCAAIGVPDERSGEAVKLFVVARD----PGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRR 556
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
24-617 |
2.27e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.14 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 24 SLGYEDyEIFYNKSIEETAWFWGEAEKAVGYQWMKPYTEV---------LDLENGTPFAQWYNGGTCnvVESALSRWLAd 94
Cdd:PRK12467 1510 SLTYAT-DLFEASTIERLAGHWLNLLQGLVADPERRLGELdlldeaerrQILEGWNATHTGYPLARL--VHQLIEDQAA- 1585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 95 eETRIQPALQYEGEngtskSFTYEELDnwvsRVANGLKHAGIEKG----DRVTIYMPMIPETVVAMLAVMKIGAIISPIF 170
Cdd:PRK12467 1586 -ATPEAVALVFGEQ-----ELTYGELN----RRANRLAHRLIALGvgpeVLVGIAVERSLEMVVGLLAILKAGGAYVPLD 1655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 171 SGFASDAVMTRVQAAGSKMIITADgfsrrgkivslkdevdKACEHCPTVEKV-VIVRHAGNDftphnydfsWstLEKEKP 249
Cdd:PRK12467 1656 PEYPRERLAYMIEDSGIELLLTQS----------------HLQARLPLPDGLrSLVLDQEDD---------W--LEGYSD 1708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 250 FIHAEEMQSDDPLMLIYTSGTTGKPKGTVHTHAgfPLKAAFDA---GFGMNikQGDRVLWVTDMGWMMGPFLLFGSLING 326
Cdd:PRK12467 1709 SNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHG--ALVNRLCAtqeAYQLS--AADVVLQFTSFAFDVSVWELFWPLING 1784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 327 ATMVMYE-GVPDFPEadRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLeVFAstGEPWNPD---PWMWLFe 402
Cdd:PRK12467 1785 ARLVIAPpGAHRDPE--QLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRV-VCG--GEALEVEalrPWLERL- 1858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 403 tvgkGNVPICNYSGGTEISggifGNVLIKPI----------APISfnASLPGMAAVVLDDQGKPI-RDEVGELCLEKpwV 471
Cdd:PRK12467 1859 ----PDTGLFNLYGPTETA----VDVTHWTCrrkdlegrdsVPIG--QPIANLSTYILDASLNPVpIGVAGELYLGG--V 1926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 472 GMTKSFWE----DDERYVNTYWSRFENK-WVHGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAA 545
Cdd:PRK12467 1927 GLARGYLNrpalTAERFVADPFGTVGSRlYRTGDLARYRADGVIeYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAV 2006
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 546 AIGVpDEVKGEVCHCFVVLRD---------HVTFTGELKKELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:PRK12467 2007 VIAQ-DGANGKQLVAYVVPTDpglvdddeaQVALRAILKNHLKASLPEY----MVPAHLVFLARMPLTPNGKLDRKALPA 2081
|
.
gi 446729146 617 A 617
Cdd:PRK12467 2082 P 2082
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
101-612 |
3.23e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 86.37 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:PRK12467 529 PALVFGEQ-----VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAY 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 181 RVQAAGSKMIITADGFSRR-----GKIVSLKDEVDKACEHCPTVekvvivrHAGNDFTPHNYDFswstlekekpfihaee 255
Cdd:PRK12467 604 MLDDSGVRLLLTQSHLLAQlpvpaGLRSLCLDEPADLLCGYSGH-------NPEVALDPDNLAY---------------- 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 256 mqsddplmLIYTSGTTGKPKGTVHTHAGFP-LKAAFDAGFGMNIKqgDRVLWVTDMGWMMGPFLLFGSLINGATMVM--Y 332
Cdd:PRK12467 661 --------VIYTSGSTGQPKGVAISHGALAnYVCVIAERLQLAAD--DSMLMVSTFAFDLGVTELFGALASGATLHLlpP 730
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 333 EGVPDfpeADRLWETVDKYEITHLGISPTLIRALM--AKGDEYVNKHSLksleVFASTGEPWN-PDPWMWLfetvgKGNV 409
Cdd:PRK12467 731 DCARD---AEAFAALMADQGVTVLKIVPSHLQALLqaSRVALPRPQRAL----VCGGEALQVDlLARVRAL-----GPGA 798
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 410 PICNYSGGTEISGGifgnVLIKPI--APISFNAS-----LPGMAAVVLDDQGKPIRDEV-GELC-----LEKPWVG---- 472
Cdd:PRK12467 799 RLINHYGPTETTVG----VSTYELsdEERDFGNVpigqpLANLGLYILDHYLNPVPVGVvGELYiggagLARGYHRrpal 874
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 473 -----MTKSFWEDDERYVNTywsrfenkwvhGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAA 546
Cdd:PRK12467 875 taerfVPDPFGADGGRLYRT-----------GDLARYRADGVIeYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVV 943
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446729146 547 IGVPDEVKGE-VCHCFVVL----RDHVTFTGELKKELMSLVNSHigkaLCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:PRK12467 944 LAQPGDAGLQlVAYLVPAAvadgAEHQATRDELKAQLRQVLPDY----MVPAHLLLLDSLPLTPNGKLDRK 1010
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
113-612 |
5.85e-17 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 84.30 E-value: 5.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 113 KSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIG-------------------------AIIs 167
Cdd:PRK07059 47 KAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGyvvvnvnplytprelehqlkdsgaeAIV- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 168 pIFSGFAS--DAVMTRVQAagsKMIITA---DGFSRRGKIVSLkdevdkacehcpTVEKVVIVRHAGNdfTPHNYDFSWS 242
Cdd:PRK07059 126 -VLENFATtvQQVLAKTAV---KHVVVAsmgDLLGFKGHIVNF------------VVRRVKKMVPAWS--LPGHVRFNDA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 243 TLEKEKPFIHAEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGFP---------LKAAFDAGfgmniKQGDRVLWVTDMgwm 313
Cdd:PRK07059 188 LAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVanvlqmeawLQPAFEKK-----PRPDQLNFVCAL--- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 314 mgPFLLFGSLINGATMVMYEG-----VPDFPEADRLWETVDKYEITHLGISPTLIRALMAKGDeyVNKHSLKSLEVFAST 388
Cdd:PRK07059 260 --PLYHIFALTVCGLLGMRTGgrnilIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPD--FDKLDFSKLIVANGG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 389 G--------EPWNPDPWMWLFETVG---KGNVPICNYSGGTEISGGIfgnvlikpiapisfNASLPGMAAVVLDDQGK-- 455
Cdd:PRK07059 336 GmavqrpvaERWLEMTGCPITEGYGlseTSPVATCNPVDATEFSGTI--------------GLPLPSTEVSIRDDDGNdl 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 456 PIrDEVGELCLEKPWVgMtKSFWE--DDERYVNTYWSRFENkwvhGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYE 532
Cdd:PRK07059 402 PL-GEPGEICIRGPQV-M-AGYWNrpDETAKVMTADGFFRT----GDVGVMDERGYTkIVDRKKDMILVSGFNVYPNEIE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 533 SILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHvtftgelkkelmSLVNSHIgKALC---------PKDIHVVEDLPK 603
Cdd:PRK07059 475 EVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDP------------ALTEEDV-KAFCkerltnykrPKFVEFRTELPK 541
|
....*....
gi 446729146 604 TRNSKVMRR 612
Cdd:PRK07059 542 TNVGKILRR 550
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
116-549 |
2.21e-16 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 82.09 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITadg 195
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 196 fsrrgkivSLKDEVDKACEHCPtvEKVVIVRHagndftphnydfswstlekekpfihaeemqsDDPLMLIYTSGTTGKPK 275
Cdd:cd05939 82 --------NLLDPLLTQSSTEP--PSQDDVNF-------------------------------RDKLFYIYTSGTTGLPK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 276 GTVHTHAGFPLKAAFdAGFGMNIKQGDRV-----LWVTDMGWM-MGPFLLFGSlingaTMVMYEGVpdfpEADRLWETVD 349
Cdd:cd05939 121 AAVIVHSRYYRIAAG-AYYAFGMRPEDVVydclpLYHSAGGIMgVGQALLHGS-----TVVIRKKF----SASNFWDDCV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 350 KYEITHLGISPTLIRALMA-KGDEYVNKHSLKSLevfasTGEPWNPDPWMwlfETVGKGNVP-ICNYSGGTEISGGIfGN 427
Cdd:cd05939 191 KYNCTIVQYIGEICRYLLAqPPSEEEQKHNVRLA-----VGNGLRPQIWE---QFVRRFGIPqIGEFYGATEGNSSL-VN 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 428 VLIKpIAPISFNA-SLPGMAAVVL----DDQGKPIRDEVGeLCLE----KPWVGMTKSFWEDDERYVNTYWSRFE-NKWV 497
Cdd:cd05939 262 IDNH-VGACGFNSrILPSVYPIRLikvdEDTGELIRDSDG-LCIPcqpgEPGLLVGKIIQNDPLRRFDGYVNEGAtNKKI 339
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446729146 498 HGDwVIYDGEQYIITG---------------RSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGV 549
Cdd:cd05939 340 ARD-VFKKGDSAFLSGdvlvmdelgylyfkdRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGV 405
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
99-419 |
4.98e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 81.48 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 99 IQPALQYEGENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAI---ISPifsGFAS 175
Cdd:PRK09274 26 AVPGGRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVpvlVDP---GMGI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 176 DAVMTRVQAAGSKMIITadgfsrrgkivslkdeVDKAceH---------CPTVEKVVIVRHAgndftphnydFSW--STL 244
Cdd:PRK09274 103 KNLKQCLAEAQPDAFIG----------------IPKA--HlarrlfgwgKPSVRRLVTVGGR----------LLWggTTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 245 EK------EKPFIHAEeMQSDDPLMLIYTSGTTGKPKGTVHTHAGF-----PLKAAFDagfgmnIKQGDRvlwvtDMGwM 313
Cdd:PRK09274 155 ATllrdgaAAPFPMAD-LAPDDMAAILFTSGSTGTPKGVVYTHGMFeaqieALREDYG------IEPGEI-----DLP-T 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 314 MGPFLLFG-SLinGATMVmyegVPDF---------PeaDRLWETVDKYEITHLGISPTLIRALMAKGDEyvNKHSLKSLE 383
Cdd:PRK09274 222 FPLFALFGpAL--GMTSV----IPDMdptrpatvdP--AKLFAAIERYGVTNLFGSPALLERLGRYGEA--NGIKLPSLR 291
|
330 340 350
....*....|....*....|....*....|....*.
gi 446729146 384 VFASTGEPWNPDPWMwLFETVGKGNVPICNYSGGTE 419
Cdd:PRK09274 292 RVISAGAPVPIAVIE-RFRAMLPPDAEILTPYGATE 326
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
106-618 |
1.19e-15 |
|
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: 80.16 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 106 EGENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAA 185
Cdd:cd17641 3 EKDFGIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 186 GSKMIITADgfsrrgkivslKDEVDKACEH---CPTVEKVVIVRHAGNDFTPHNYDFSWSTLEKEKPFIHAE-------- 254
Cdd:cd17641 83 GARVVIAED-----------EEQVDKLLEIadrIPSVRYVIYCDPRGMRKYDDPRLISFEDVVALGRALDRRdpglyere 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 255 --EMQSDDPLMLIYTSGTTGKPKGTVHTHAGFplkaafdAGFGMNIKQ------GDRVLWVTDMGWMM------GPFLLF 320
Cdd:cd17641 152 vaAGKGEDVAVLCTTSGTTGKPKLAMLSHGNF-------LGHCAAYLAadplgpGDEYVSVLPLPWIGeqmysvGQALVC 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 321 GSLIN----GATMV--MYEGVPDFP-EADRLWETVD-------------KYEITHLGIS---------------PTLIRA 365
Cdd:cd17641 225 GFIVNfpeePETMMedLREIGPTFVlLPPRVWEGIAadvrarmmdatpfKRFMFELGMKlglraldrgkrgrpvSLWLRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 366 LMAKGDEYV-----NKHSLKSLEVFASTGEPWNPDPWMWlFETVGkgnVPICNYSGGTEISGGIFgnvlIKPIAPISFNA 440
Cdd:cd17641 305 ASWLADALLfrplrDRLGFSRLRSAATGGAALGPDTFRF-FHAIG---VPLKQLYGQTELAGAYT----VHRDGDVDPDT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 441 SLPGMAavvlddqGKPIR-DEVGELCLEKPwvGMTKSFWEDDERYVNTYwsrFENKWVH-GDWVIYDGE-QYIITGRSDD 517
Cdd:cd17641 377 VGVPFP-------GTEVRiDEVGEILVRSP--GVFVGYYKNPEATAEDF---DEDGWLHtGDAGYFKENgHLVVIDRAKD 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 518 TLNIA-GKRIGPAEYESILVKHNDVIEAAAIGvpdevKG-EVCHCFVVLR----------DHVTFTG----ELKKELMSL 581
Cdd:cd17641 445 VGTTSdGTRFSPQFIENKLKFSPYIAEAVVLG-----AGrPYLTAFICIDyaivgkwaeqRGIAFTTytdlASRPEVYEL 519
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 446729146 582 VNSHIGK--------------ALCPKDIHvVEDLPKTRNSKVMRRVIKAAY 618
Cdd:cd17641 520 IRKEVEKvnaslpeaqrirrfLLLYKELD-ADDGELTRTRKVRRGVIAEKY 569
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
113-609 |
1.27e-15 |
|
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: 79.75 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 113 KSFTYEELDNWVSRVANGLKHAGIEKGD-RVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMII 191
Cdd:cd17648 11 KRLTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 192 TadgfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihaeemQSDDPLMLIYTSGTT 271
Cdd:cd17648 91 T----------------------------------------------------------------NSTDLAYAIYTSGTT 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 272 GKPKGTVHTHAG-FPLKAAFDAGFGMNIKQGDRVLWVTDmgWMMGPFL--LFGSLINGATMVMYEGvPDFPEADRLWETV 348
Cdd:cd17648 107 GKPKGVLVEHGSvVNLRTSLSERYFGRDNGDEAVLFFSN--YVFDFFVeqMTLALLNGQKLVVPPD-EMRFDPDRFYAYI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 349 DKYEITHLGISPTLIralmakgdEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGKgnvPICNYSGGTEISggiFGNV 428
Cdd:cd17648 184 NREKVTYLSGTPSVL--------QQYDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAG---LIINAYGPTETT---VTNH 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 429 LIKPIAPISFNASL----PGMAAVVLDDQGKPIR-DEVGELCLEKpwVGMTKSFWEDD----ERYV-NTYWS-------R 491
Cdd:cd17648 250 KRFFPGDQRFDKSLgrpvRNTKCYVLNDAMKRVPvGAVGELYLGG--DGVARGYLNRPeltaERFLpNPFQTeqerargR 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 492 FENKWVHGDWV--IYDGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAI-------GVPDEVKGEVCHcF 561
Cdd:cd17648 328 NARLYKTGDLVrwLPSGElEYL--GRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVakedasqAQSRIQKYLVGY-Y 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 446729146 562 VVLRDHVTftgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKV 609
Cdd:cd17648 405 LPEPGHVP-----ESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
257-612 |
2.98e-15 |
|
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: 78.63 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 257 QSDDPLMLIYTSGTTGKPKGTVHTHAGF-----PLKAAFDagfgmnIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVM 331
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLvnlshGLIKEYG------ITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 332 yegVPD--FPEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKhSLKSLEVFASTGEPWNPDPWMWLFETVGKgNV 409
Cdd:cd17644 178 ---RPEemRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTID-LPSSLRLVIVGGEAVQPELVRQWQKNVGN-FI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 410 PICNYSGGTEIS-GGIFGNVL---IKPIAPISFNASLPGMAAVVLDDQGKPIRDEV-GELCLEKpwVGMTKSFWEDD--- 481
Cdd:cd17644 253 QLINVYGPTEATiAATVCRLTqltERNITSVPIGRPIANTQVYILDENLQPVPVGVpGELHIGG--VGLARGYLNRPelt 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 482 -ERYVNT--YWSRFENKWVHGDWVIY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKG 555
Cdd:cd17644 331 aEKFISHpfNSSESERLYKTGDLARYlpDGNiEYL--GRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGN 408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 446729146 556 EVCHCFVVlrDHVTFTGeLKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRR 612
Cdd:cd17644 409 KRLVAYIV--PHYEESP-STVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRR 462
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
249-616 |
6.26e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 77.80 E-value: 6.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 249 PFIHAEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAG-FGMNikqGDRVLWVTdMGWMMGPFLLFG---SLI 324
Cdd:PRK07867 142 AEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQrFGLG---PDDVCYVS-MPLFHSNAVMAGwavALA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 325 NGATMVMYegvPDFpEADRLWETVDKYEITHLgisptliralmakgdEYVNKhslkSLEVFASTgePWNPD----PWMWL 400
Cdd:PRK07867 218 AGASIALR---RKF-SASGFLPDVRRYGATYA---------------NYVGK----PLSYVLAT--PERPDdadnPLRIV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 401 FETVGK-----------GNVPICNYsGGTEisggifGNVLIKPiAPISFNASL----PGMAAV-----------VLDDQG 454
Cdd:PRK07867 273 YGNEGApgdiarfarrfGCVVVDGF-GSTE------GGVAITR-TPDTPPGALgplpPGVAIVdpdtgtecppaEDADGR 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 455 KPIRDE-VGELC-LEKPwvGMTKSFWEDDE----RYVN-TYWSrfenkwvhGDWVIYDGEQYI-ITGRSDDTLNIAGKRI 526
Cdd:PRK07867 345 LLNADEaIGELVnTAGP--GGFEGYYNDPEadaeRMRGgVYWS--------GDLAYRDADGYAyFAGRLGDWMRVDGENL 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 527 GPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGELKKELMSlVNSHIGKALCPKDIHVVEDLPKTRN 606
Cdd:PRK07867 415 GTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLA-AQPDLGPKQWPSYVRVCAELPRTAT 493
|
410
....*....|
gi 446729146 607 SKVMRRVIKA 616
Cdd:PRK07867 494 FKVLKRQLSA 503
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
116-604 |
7.31e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 77.90 E-value: 7.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHA-GIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIItAD 194
Cdd:PRK05620 40 TFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV-AD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 195 GfsrrgkivSLKDEVDKACEHCPTVEKVVIVrhAGNDFT-------PHNYDFSWSTLEKEKPFIHA-EEMQSDDPLMLIY 266
Cdd:PRK05620 119 P--------RLAEQLGEILKECPCVRAVVFI--GPSDADsaaahmpEGIKVYSYEALLDGRSTVYDwPELDETTAAAICY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 267 TSGTTGKPKGTVHTHAGFPLKaafdagfGMNIKQGDRvLWVTD-------------MGWMMgPFLLFGSlinGATMVmye 333
Cdd:PRK05620 189 STGTTGAPKGVVYSHRSLYLQ-------SLSLRTTDS-LAVTHgesflccvpiyhvLSWGV-PLAAFMS---GTPLV--- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 334 gvpdFPEADRLWETVDKYEITHL-----GIsPTLIRALMAkgdEYVNKH----SLKSLEVFASTGEPWNPDPW------- 397
Cdd:PRK05620 254 ----FPGPDLSAPTLAKIIATAMprvahGV-PTLWIQLMV---HYLKNPpermSLQEIYVGGSAVPPILIKAWeerygvd 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 398 ---MW-LFETVGKGNV--PICNYSGGT----EISGGIFgnvlikpiaPISFNASlpgmaaVVLDDQGKPIRDE-VGELCL 466
Cdd:PRK05620 326 vvhVWgMTETSPVGTVarPPSGVSGEArwayRVSQGRF---------PASLEYR------IVNDGQVMESTDRnEGEIQV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 467 EKPWVgmTKSFWEDD------------ERYVNTYWSRF-ENKWVH-GD--WVIYDGeQYIITGRSDDTLNIAGKRIGPAE 530
Cdd:PRK05620 391 RGNWV--TASYYHSPteegggaastfrGEDVEDANDRFtADGWLRtGDvgSVTRDG-FLTIHDRARDVIRSGGEWIYSAQ 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446729146 531 YESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKT 604
Cdd:PRK05620 468 LENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKT 541
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
260-604 |
7.99e-15 |
|
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: 76.19 E-value: 7.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 260 DPLMLIYTSGTTGKPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDM---GWMMGpflLFGSLINGATMVMyegVP 336
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQAL-LAQALVLAVLQAIDEGTVFLNSGPLfhiGTLMF---TLATFHAGGTNVF---VR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 337 DFpEADRLWETVDKYEITHLGI-SPTL--IRALMAKGdeyvnKHSLKSLEVFASTgEPWN----PDPWMWlfetvgkgnv 409
Cdd:cd17636 74 RV-DAEEVLELIEAERCTHAFLlPPTIdqIVELNADG-----LYDLSSLRSSPAA-PEWNdmatVDTSPW---------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 410 piCNYSGG---TEISGGIFGNVLIKPIAPISFNASlPGMAAVVLDDQGKPIRD-EVGELCLEKPWVGmtKSFWEDDEryV 485
Cdd:cd17636 137 --GRKPGGygqTEVMGLATFAALGGGAIGGAGRPS-PLVQVRILDEDGREVPDgEVGEIVARGPTVM--AGYWNRPE--V 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 486 NTywSRFENKWVH-GDwviydgeqyiiTGR--SDDTLNIAGKR----------IGPAEYESILVKHNDVIEAAAIGVPDE 552
Cdd:cd17636 210 NA--RRTRGGWHHtND-----------LGRrePDGSLSFVGPKtrmiksgaenIYPAEVERCLRQHPAVADAAVIGVPDP 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446729146 553 VKGEVCHCFVVLRDHVTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKT 604
Cdd:cd17636 277 RWAQSVKAIVVLKPGASVTEA---ELIEHCRARIASYKKPKSVEFADALPRT 325
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
102-615 |
3.34e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 75.59 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 102 ALQYEgengtSKSFTYEELDNWVSRVANGLkHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTR 181
Cdd:PRK07638 19 AIKEN-----DRVLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 182 VQAAGSKMIITADGFSRrgkivslkdevDKACEHCPtvekVVIVRHagndftphnydfsW-STLEKEKPFIHAEEMQSDD 260
Cdd:PRK07638 93 LAISNADMIVTERYKLN-----------DLPDEEGR----VIEIDE-------------WkRMIEKYLPTYAPIENVQNA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 261 PLMLIYTSGTTGKPKGTVHTHAGFplKAAFDAG---FGMniKQGDRVLWVtdmGWMMGPFLLFG---SLINGATMVMyeg 334
Cdd:PRK07638 145 PFYMGFTSGSTGKPKAFLRAQQSW--LHSFDCNvhdFHM--KREDSVLIA---GTLVHSLFLYGaisTLYVGQTVHL--- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 335 VPDFPEADRLwETVDKYEITHLGISPTLIRALmAKGDEYVNkHSLKSLevfaSTGEPW---------NPDPWMWLFE--- 402
Cdd:PRK07638 215 MRKFIPNQVL-DKLETENISVMYTVPTMLESL-YKENRVIE-NKMKII----SSGAKWeaeakekikNIFPYAKLYEfyg 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 403 --------------------TVGK----GNVPICNySGGTEISGGIFGNVLIKpiAPISFNASLPGMAAVV-LDDQGKPI 457
Cdd:PRK07638 288 aselsfvtalvdeeserrpnSVGRpfhnVQVRICN-EAGEEVQKGEIGTVYVK--SPQFFMGYIIGGVLAReLNADGWMT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 458 RDEVGelclekpwvgmtksfWEDDERYvntywsrfenkwvhgdwvIYdgeqyiITGRSDDTLNIAGKRIGPAEYESILVK 537
Cdd:PRK07638 365 VRDVG---------------YEDEEGF------------------IY------IVGREKNMILFGGINIFPEEIESVLHE 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446729146 538 HNDVIEAAAIGVPDEVKGEVCHCFVVLRDHvtftgelKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIK 615
Cdd:PRK07638 406 HPAVDEIVVIGVPDSYWGEKPVAIIKGSAT-------KQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
95-614 |
6.09e-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: 74.51 E-value: 6.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 95 EETRIQPALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFA 174
Cdd:cd17645 9 ERTPDHVAVVDRGQ-----SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 175 SDAVMTRVQAAGSKMIITadgfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihae 254
Cdd:cd17645 84 GERIAYMLADSSAKILLT-------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 255 emQSDDPLMLIYTSGTTGKPKGT-VHTHAGFPLKAAFDAGFGMNikQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMye 333
Cdd:cd17645 102 --NPDDLAYVIYTSGSTGLPKGVmIEHHNLVNLCEWHRPYFGVT--PADKSLVYASFSFDASAWEIFPHLTAGAALHV-- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 334 gvpdFPEADRL-WETVDKYEITHlGISPTLIRALMAKGDEYVNKHSLKsleVFASTGEPWNpdpwmwlfETVGKGNVPIC 412
Cdd:cd17645 176 ----VPSERRLdLDALNDYFNQE-GITISFLPTGAAEQFMQLDNQSLR---VLLTGGDKLK--------KIERKGYKLVN 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 413 NYsGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDD--QGKPIrDEVGELCLEKPwvGMTKSFW----EDDERYVN 486
Cdd:cd17645 240 NY-GPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDEalQLQPI-GVAGELCIAGE--GLARGYLnrpeLTAEKFIV 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 487 TYWSRFENKWVHGD---WVIYDGEQYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVV 563
Cdd:cd17645 316 HPFVPGERMYRTGDlakFLPDGNIEFL--GRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 446729146 564 LRDHVTFtgelkKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVI 614
Cdd:cd17645 394 APEEIPH-----EELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
124-566 |
3.30e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 72.52 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 124 VSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPI---FSGFASDAVMTRVQAAgskMIITADGFS--- 197
Cdd:PLN02860 42 VLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLnyrWSFEEAKSAMLLVRPV---MLVTDETCSswy 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 198 ---RRGKIVSLKDEV--DKACEHcptvekvviVRHAGNDF-----------TPHNYDFSWStlekekpfihaeemqSDDP 261
Cdd:PLN02860 119 eelQNDRLPSLMWQVflESPSSS---------VFIFLNSFlttemlkqralGTTELDYAWA---------------PDDA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 262 LMLIYTSGTTGKPKGTVHTHAGFPL----KAAFdAGFGmnikqGDRVLWVTdmgwmmGPFLLFGSLINGATMVMYEG--- 334
Cdd:PLN02860 175 VLICFTSGTTGRPKGVTISHSALIVqslaKIAI-VGYG-----EDDVYLHT------APLCHIGGLSSALAMLMVGAchv 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 335 -VPDFpEADRLWETVDKYEITHLGISPTLIRALMAKGDEYVNKHSlkslevfastgepwnpdpwmwlFETVGKgnvpICN 413
Cdd:PLN02860 243 lLPKF-DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKV----------------------FPSVRK----ILN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 414 ySGGTEISGGIFGNVLIKPIAPIsFNA--------SLPGMA---------AVVLDDQGKPIRDEVGEL---CLEKP---- 469
Cdd:PLN02860 296 -GGGSLSSRLLPDAKKLFPNAKL-FSAygmteacsSLTFMTlhdptlespKQTLQTVNQTKSSSVHQPqgvCVGKPaphv 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 470 --WVGMTKS----------------FWEDDeryVNTYWSRFENKWVH-GDWVIYD--GEQYIItGRSDDTLNIAGKRIGP 528
Cdd:PLN02860 374 elKIGLDESsrvgriltrgphvmlgYWGQN---SETASVLSNDGWLDtGDIGWIDkaGNLWLI-GRSNDRIKTGGENVYP 449
|
490 500 510
....*....|....*....|....*....|....*...
gi 446729146 529 AEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRD 566
Cdd:PLN02860 450 EEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRD 487
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
113-609 |
5.47e-13 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 71.94 E-value: 5.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 113 KSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIG-AIISPIFSGFASDAVMTRVQAAGSKMII 191
Cdd:PRK10946 47 RQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGvAPVNALFSHQRSELNAYASQIEPALLIA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 192 tadgfSRRGKIVSLKDEVDKACEHCPTVEkVVIVRHagndftpHNYDFSWST-LEKEKPFIHAEEMQSDDPLMLIYTSGT 270
Cdd:PRK10946 127 -----DRQHALFSDDDFLNTLVAEHSSLR-VVLLLN-------DDGEHSLDDaINHPAEDFTATPSPADEVAFFQLSGGS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 271 TGKPKGTVHTHAGF--PLKAAFD-AGFGMNIkqgdRVLWVTDMG--WMMGPFLLFGSLINGATMVMyegVPDfPEADRLW 345
Cdd:PRK10946 194 TGTPKLIPRTHNDYyySVRRSVEiCGFTPQT----RYLCALPAAhnYPMSSPGALGVFLAGGTVVL---APD-PSATLCF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 346 ETVDKYEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPwnpdpwmwLFETVGKgNVP--------------- 410
Cdd:PRK10946 266 PLIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASLKLLQVGGAR--------LSETLAR-RIPaelgcqlqqvfgmae 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 411 -ICNYSGGTEISGGIF---GNvlikpiaPISfnaslPGMAAVVLDDQGKPI-RDEVGELCLEKPWV--GMTKS------- 476
Cdd:PRK10946 337 gLVNYTRLDDSDERIFttqGR-------PMS-----PDDEVWVADADGNPLpQGEVGRLMTRGPYTfrGYYKSpqhnasa 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 477 FweDDERYvntYWSrfenkwvhGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKG 555
Cdd:PRK10946 405 F--DANGF---YCS--------GDLVSIDPDGYItVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMG 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446729146 556 EVCHCFVVLRDHVTfTGELKKELMSLvnsHIGKALCPKDIHVVEDLPKTRNSKV 609
Cdd:PRK10946 472 EKSCAFLVVKEPLK-AVQLRRFLREQ---GIAEFKLPDRVECVDSLPLTAVGKV 521
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
265-609 |
1.45e-12 |
|
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: 70.19 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 265 IYTSGTTGKPKGTVHTHAGF-PLKAAFDAGFGM---NIKQGDRVLwVTDmgwmmgPFL--LFGSLINGATMVMyegVPDF 338
Cdd:cd17654 124 IHTSGTTGTPKIVAVPHKCIlPNIQHFRSLFNItseDILFLTSPL-TFD------PSVveIFLSLSSGATLLI---VPTS 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 339 --PEADRLWETVDK-YEITHLGISPTLIRALMAKGDEYVNKHSLKSLEVFASTGEPWNPD----PWMwlfetvGKGN-VP 410
Cdd:cd17654 194 vkVLPSKLADILFKrHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFPSLvilsSWR------GKGNrTR 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 411 ICNYSGGTEISGGIFGNVLIKPIAPISFNASLPGMAAVVLDDQGKPIRdevGELCLEkpwvGMTKSFWEDDerYVNTYWS 490
Cdd:cd17654 268 IFNIYGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSEGT---GQVFLG----GLNRVCILDD--EVTVPKG 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 491 RFENKwvhGDWV-IYDGEQYIItGRSDDTLNIAGKRIGPAEYESILVKHNDViEAAAIGVPDEvkgEVCHCFVVLRDHVT 569
Cdd:cd17654 339 TMRAT---GDFVtVKDGELFFL-GRKDSQIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSDQ---QRLIAFIVGESSSS 410
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 446729146 570 ftgELKKEL-MSLVNSHIgkalCPKDIHVVEDLPKTRNSKV 609
Cdd:cd17654 411 ---RIHKELqLTLLSSHA----IPDTFVQIDKLPLTSHGKV 444
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
30-87 |
2.40e-12 |
|
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: 61.72 E-value: 2.40e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446729146 30 YEIFYNKSIEETAWFWGEAEKAVgyQWMKPYTEVLDLENGtPFAQWYNGGTCNVVESA 87
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKEL--DWFKPFDKVLDGSNG-PFAKWFVGGKLNVCYNC 55
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
86-624 |
2.81e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 69.65 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 86 SALSRWLADEETRIQpALQYEGENGTSkSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAI 165
Cdd:PRK05857 15 TVLDRVFEQARQQPE-AIALRRCDGTS-ALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 166 ispifsgfasdAVMtrvqAAGSKMIITADGFSR----RGKIVSLKDEVDKAC--EHCPTVEKVVIVRHAGNDFTPHNYDF 239
Cdd:PRK05857 93 -----------AVM----ADGNLPIAAIERFCQitdpAAALVAPGSKMASSAvpEALHSIPVIAVDIAAVTRESEHSLDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 240 SWSTLEKEkpfihaeeMQSDDPLMLIYTSGTTGKPKGTVHTHAGFplkaafdagFGM-NIKQGDRVLWVTdmgWMMG--- 315
Cdd:PRK05857 158 ASLAGNAD--------QGSEDPLAMIFTSGTTGEPKAVLLANRTF---------FAVpDILQKEGLNWVT---WVVGett 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 316 ----PFLLFGSLINGATMVMYEG--VPDFPEADRLWETVDKYEITHLGISPTLIRALMAKgdeyvnkhsLKslevFASTG 389
Cdd:PRK05857 218 ysplPATHIGGLWWILTCLMHGGlcVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSE---------LK----SANAT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 390 EPwnpdpwmwlfetvgkgNVPICNYSGGTEISGGI-FGNVLIKPIAPIsFNASLPGMAAVVL-DDQGKPIRDEVGELCLE 467
Cdd:PRK05857 285 VP----------------SLRLVGYGGSRAIAADVrFIEATGVRTAQV-YGLSETGCTALCLpTDDGSIVKIEAGAVGRP 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 468 KPWV-----------------GMTKSF---WEDDERYVNTYWSRFE-------NKWVH-GDWVIY--DGEQYiITGRSDD 517
Cdd:PRK05857 348 YPGVdvylaatdgigptapgaGPSASFgtlWIKSPANMLGYWNNPErtaevliDGWVNtGDLLERreDGFFY-IKGRSSE 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 518 TLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTG--ELKKELMSLVNSHIGKALCPKDI 595
Cdd:PRK05857 427 MIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAarALKHTIAARFRRESEPMARPSTI 506
|
570 580
....*....|....*....|....*....
gi 446729146 596 HVVEDLPKTRNSKVMRRVIKAAYLGKELG 624
Cdd:PRK05857 507 VIVTDIPRTQSGKVMRASLAAAATADKAR 535
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
442-612 |
3.35e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 68.86 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 442 LPGMAAVVLDDQGKPIR---DEVGELCLEKPWVgmtksFWEdderYVN----TYWSRFENKWVH-GDWVIYDGEQYI-IT 512
Cdd:PRK07787 299 LAGVETRLVDEDGGPVPhdgETVGELQVRGPTL-----FDG----YLNrpdaTAAAFTADGWFRtGDVAVVDPDGMHrIV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 513 GR-SDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTftgelKKELMSLVNSHIGKALC 591
Cdd:PRK07787 370 GReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVA-----ADELIDFVAQQLSVHKR 444
|
170 180
....*....|....*....|.
gi 446729146 592 PKDIHVVEDLPKTRNSKVMRR 612
Cdd:PRK07787 445 PREVRFVDALPRNAMGKVLKK 465
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
253-616 |
4.17e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 68.90 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 253 AEEMQSDDPLMLIYTSGTTGKPKGTVHTHaGFPLKAAFDAGFGMNIKQGDrVLWVTdMGWMMGPFLLFG---SLINGATM 329
Cdd:PRK13388 144 HREVDAMDPFMLIFTSGTTGAPKAVRCSH-GRLAFAGRALTERFGLTRDD-VCYVS-MPLFHSNAVMAGwapAVASGAAV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 330 VMyegVPDFpEADRLWETVDKYEITHLgisptliralmakgdEYVNKhslkSLEVFASTgePWNPD----PWmwlfeTVG 405
Cdd:PRK13388 221 AL---PAKF-SASGFLDDVRRYGATYF---------------NYVGK----PLAYILAT--PERPDdadnPL-----RVA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 406 KGN---------------VPICNYSGGTEisGGifGNVLIKPIAPI-SFNASLPGMAAV-----------VLDDQGKPIR 458
Cdd:PRK13388 271 FGNeasprdiaefsrrfgCQVEDGYGSSE--GA--VIVVREPGTPPgSIGRGAPGVAIYnpetltecavaRFDAHGALLN 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 459 --DEVGELcLEKPWVGMTKSFWEDD----ERYVN-TYWSrfenkwvhGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAE 530
Cdd:PRK13388 347 adEAIGEL-VNTAGAGFFEGYYNNPeataERMRHgMYWS--------GDLAYRDADGWIyFAGRTADWMRVDGENLSAAP 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 531 YESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFT-GELKKELMSlvNSHIGKALCPKDIHVVEDLPKTRNSKV 609
Cdd:PRK13388 418 IERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDpDAFAAFLAA--QPDLGTKAWPRYVRIAADLPSTATNKV 495
|
....*..
gi 446729146 610 MRRVIKA 616
Cdd:PRK13388 496 LKRELIA 502
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
105-354 |
3.22e-11 |
|
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: 66.16 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 105 YEGEngtskSFTYEELDNWVSRVANGLK-HAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQ 183
Cdd:cd05938 1 FEGE-----TYTYRDVDRRSNQAARALLaHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 184 AAGSKMIITADgfsrrgkivSLKDEVDkacEHCPTV-EKVVIVRHAGNDFTPHNYDfswSTLEKEK-------PFIHAEE 255
Cdd:cd05938 76 CCGAKVLVVAP---------ELQEAVE---EVLPALrADGVSVWYLSHTSNTEGVI---SLLDKVDaasdepvPASLRAH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 256 MQSDDPLMLIYTSGTTGKPKGTVHTHagfpLKAAFDAGFGMNIK-QGDRVLWVT-----DMGWMMGpflLFGSLINGATM 329
Cdd:cd05938 141 VTIKSPALYIYTSGTTGLPKAARISH----LRVLQCSGFLSLCGvTADDVIYITlplyhSSGFLLG---IGGCIELGATC 213
|
250 260
....*....|....*....|....*
gi 446729146 330 VMYegvPDFpEADRLWETVDKYEIT 354
Cdd:cd05938 214 VLK---PKF-SASQFWDDCRKHNVT 234
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
100-282 |
4.66e-11 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 65.69 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 100 QPALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIG-AIIsPIFSGFASDAV 178
Cdd:PRK04813 18 FPAYDYLGE-----KLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhAYI-PVDVSSPAERI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 179 MTRVQAAGSKMIITADGFsrrgkivslkdevDKACEHCPTVEKVVIVRHAGNDFTPhnydfswstlekekPFIHAeeMQS 258
Cdd:PRK04813 92 EMIIEVAKPSLIIATEEL-------------PLEILGIPVITLDELKDIFATGNPY--------------DFDHA--VKG 142
|
170 180
....*....|....*....|....
gi 446729146 259 DDPLMLIYTSGTTGKPKGTVHTHA 282
Cdd:PRK04813 143 DDNYYIIFTSGTTGKPKGVQISHD 166
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
209-611 |
1.68e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 63.96 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 209 VDKACEHCPTVEKVVIV---RHAGNDFTP----------HNYDFSWSTLEkekpfihaEEMQSDdplmLIYTSGTTGKPK 275
Cdd:PRK07008 125 VDALAPQCPNVKGWVAMtdaAHLPAGSTPllcyetlvgaQDGDYDWPRFD--------ENQASS----LCYTSGTTGNPK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 276 GTVHTHAGFPLKAaFDAGF--GMNIKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVmyegvpdFPEAD----RLWETVD 349
Cdd:PRK07008 193 GALYSHRSTVLHA-YGAALpdAMGLSARDAVLPVVPMFHVNAWGLPYSAPLTGAKLV-------LPGPDldgkSLYELIE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 350 KYEITHLGISPTLIRALMakgdEYVNKHSLK--SLE--VFASTGEPwnpdPWMW--LFETVGkgnVPICNYSGGTEISG- 422
Cdd:PRK07008 265 AERVTFSAGVPTVWLGLL----NHMREAGLRfsTLRrtVIGGSACP----PAMIrtFEDEYG---VEVIHAWGMTEMSPl 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 423 GIFGNVLIKpiapisfNASLPGMAAV-VLDDQGKPI----RDEVGELCLEKPWVGmtKSF--------WEDDeRYVNTYW 489
Cdd:PRK07008 334 GTLCKLKWK-------HSQLPLDEQRkLLEKQGRVIygvdMKIVGDDGRELPWDG--KAFgdlqvrgpWVID-RYFRGDA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 490 SRFENKWVH-GDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDH 567
Cdd:PRK07008 404 SPLVDGWFPtGDVATIDADGFMqITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPG 483
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 446729146 568 VTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:PRK07008 484 AEVTRE---ELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQK 524
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
113-397 |
2.55e-10 |
|
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: 63.22 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 113 KSFTYEELDNWVSRVANGLKHA-GIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMII 191
Cdd:cd05937 4 KTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 192 TADgfsrrgkivslkdevdkacehcptvekvvivrhagndftphnydfswstlekekpfihaeemqsDDPLMLIYTSGTT 271
Cdd:cd05937 84 VDP----------------------------------------------------------------DDPAILIYTSGTT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 272 GKPKGTVHThAGFPLKAAFDAGFGMNIKQGDRvlWVTDMGWMMGPFLLFG---SLINGATMVMyegVPDFpEADRLWETV 348
Cdd:cd05937 100 GLPKAAAIS-WRRTLVTSNLLSHDLNLKNGDR--TYTCMPLYHGTAAFLGacnCLMSGGTLAL---SRKF-SASQFWKDV 172
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446729146 349 DKYEITHLGISPTLIRALMAKGDE-YVNKHSLKslevfASTGEPWNPDPW 397
Cdd:cd05937 173 RDSGATIIQYVGELCRYLLSTPPSpYDRDHKVR-----VAWGNGLRPDIW 217
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
85-618 |
4.62e-10 |
|
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: 62.30 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 85 ESALSRWLADEETRIqpaLQYEGENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGA 164
Cdd:cd05906 13 LELLLRAAERGPTKG---ITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 165 I--ISPIFSgfASDAVMTRV-------QAAGSKMIITADgfsrrgkivSLKDEVDKACEHCPTVEKVVIVRHAGNDfTPH 235
Cdd:cd05906 90 VpaPLTVPP--TYDEPNARLrklrhiwQLLGSPVVLTDA---------ELVAEFAGLETLSGLPGIRVLSIEELLD-TAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 236 NYdfswstlekekpfiHAEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGfpLKAAFDAGFGMNIKQGDRVLwvtdMGWMmg 315
Cdd:cd05906 158 DH--------------DLPQSRPDDLALLMLTSGSTGFPKAVPLTHRN--ILARSAGKIQHNGLTPQDVF----LNWV-- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 316 PFLLFGSLINGATMVMYEG-----VP--DFPEADRLW-ETVDKYEITHlGISP----TLIRALMAKGDEYvnKHSLKSLE 383
Cdd:cd05906 216 PLDHVGGLVELHLRAVYLGcqqvhVPteEILADPLRWlDLIDRYRVTI-TWAPnfafALLNDLLEEIEDG--TWDLSSLR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 384 VFASTGEPWNPDPWMWLFETVGKGNVP---ICNYSGGTEI-SGGIFGNVLIKPIAP-----ISFNASLPGMAAVVLDDQG 454
Cdd:cd05906 293 YLVNAGEAVVAKTIRRLLRLLEPYGLPpdaIRPAFGMTETcSGVIYSRSFPTYDHSqalefVSLGRPIPGVSMRIVDDEG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 455 KPI-RDEVGELCLEKPWVgmTKSFWEDD----ERYVNTYWsrFENkwvhGDWVIYDGEQYIITGRSDDTLNIAGKRIGPA 529
Cdd:cd05906 373 QLLpEGEVGRLQVRGPVV--TKGYYNNPeanaEAFTEDGW--FRT----GDLGFLDNGNLTITGRTKDTIIVNGVNYYSH 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 530 EYESILVKHNDVIE----AAAIGVPDEVKGEVCHCFVVLRDHVTFTGELKKELMSLVNSHIGKALcpkdIHVV----EDL 601
Cdd:cd05906 445 EIEAAVEEVPGVEPsftaAFAVRDPGAETEELAIFFVPEYDLQDALSETLRAIRSVVSREVGVSP----AYLIplpkEEI 520
|
570
....*....|....*..
gi 446729146 602 PKTRNSKVMRRVIKAAY 618
Cdd:cd05906 521 PKTSLGKIQRSKLKAAF 537
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
101-616 |
4.76e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 63.26 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 101 PALQYEGEngtskSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMT 180
Cdd:PRK05691 2205 PALTFAGQ-----TLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHY 2279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 181 RVQAAGSKMIIT-ADGFSRRGKivsLKDEVDKACehcptVEkvvivrhagnDFTPHNYDFSWSTLekekPFIHAEEMQSd 259
Cdd:PRK05691 2280 MIEDSGIGLLLSdRALFEALGE---LPAGVARWC-----LE----------DDAAALAAYSDAPL----PFLSLPQHQA- 2336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 260 dplMLIYTSGTTGKPKGTVHTHAGFPLK-AAFDAGFGMniKQGDRVLWVTDMGWMMGPFLLFGSLINGATMVMY-EGVPD 337
Cdd:PRK05691 2337 ---YLIYTSGSTGKPKGVVVSHGEIAMHcQAVIERFGM--RADDCELHFYSINFDAASERLLVPLLCGARVVLRaQGQWG 2411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 338 fpeADRLWETVDKYEITHLGISPT----LIRALMAKGDEYVNKHSLKSLEvfASTGEPWnpdpwmwlfETVGKGNVP--I 411
Cdd:PRK05691 2412 ---AEEICQLIREQQVSILGFTPSygsqLAQWLAGQGEQLPVRMCITGGE--ALTGEHL---------QRIRQAFAPqlF 2477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 412 CNYSGGTEisggifgnVLIKPIAPISFN------ASLP------GMAAVVLDDQGKPI-RDEVGELCL----------EK 468
Cdd:PRK05691 2478 FNAYGPTE--------TVVMPLACLAPEqleegaASVPigrvvgARVAYILDADLALVpQGATGELYVggaglaqgyhDR 2549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 469 PwvGMTKsfweddERYV-NTYWSRFENKWVHGDWVIY--DGE-QYIitGRSDDTLNIAGKRIGPAEYESILVKHNDVIEA 544
Cdd:PRK05691 2550 P--GLTA------ERFVaDPFAADGGRLYRTGDLVRLraDGLvEYV--GRIDHQVKIRGFRIELGEIESRLLEHPAVREA 2619
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446729146 545 A--AIGVPD--EVKGEVChCFVVLRDHVTfTGELKKELMSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMRRVIKA 616
Cdd:PRK05691 2620 VvlALDTPSgkQLAGYLV-SAVAGQDDEA-QAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPA 2693
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
116-611 |
6.04e-10 |
|
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: 61.71 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIisPIFSgfasDAVMTRVQAAGSKMIITADG 195
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAV--PVLI----DPGMGRKNLKQCLQEAEPDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 196 FSrrgkivslkdEVDKAcehcptvekvvivrhagndftphnydfswstlekekpfihaeemqsDDPLMLIYTSGTTGKPK 275
Cdd:cd05910 78 FI----------GIPKA----------------------------------------------DEPAAILFTSGSTGTPK 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 276 GTVHTHAGFplKAAFDA-GFGMNIKQGDRVLWVtdmgwmMGPFLLFGSLInGATMVMYEGVPDFP-EAD--RLWETVDKY 351
Cdd:cd05910 102 GVVYRHGTF--AAQIDAlRQLYGIRPGEVDLAT------FPLFALFGPAL-GLTSVIPDMDPTRPaRADpqKLVGAIRQY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 352 EITHLGISPTLIRALMAKGDEyvNKHSLKSLEVFASTGEPWnPDPWMWLFETVGKGNVPICNYSGGTE---ISgGIFGNV 428
Cdd:cd05910 173 GVSIVFGSPALLERVARYCAQ--HGITLPSLRRVLSAGAPV-PIALAARLRKMLSDEAEILTPYGATEalpVS-SIGSRE 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 429 LIKPIAPISFNAS-------LPGMAAVVLDDQGKPIRD----------EVGELCLEKPWV-----------GMTKSfWED 480
Cdd:cd05910 249 LLATTTAATSGGAgtcvgrpIPGVRVRIIEIDDEPIAEwddtlelprgEIGEITVTGPTVtptyvnrpvatALAKI-DDN 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 481 DERyvntYWSRFenkwvhGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCH 559
Cdd:cd05910 328 SEG----FWHRM------GDLGYLDDEGRLwFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVL 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446729146 560 CFVVLRDHVTFTGELKKELMSLVNSH-----IGKALC----PKDIHvvedlpktRNSKVMR 611
Cdd:cd05910 398 CVEPLPGTITPRARLEQELRALAKDYphtqrIGRFLIhpsfPVDIR--------HNAKIFR 450
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
113-548 |
7.20e-10 |
|
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: 61.61 E-value: 7.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 113 KSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIispifsgfasDAVmtrvqaagskmiit 192
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAV----------DVV-------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 193 adgfsrRGKIVSLKdevdkacehcptvEKVVIVRHAGNDFTphnydfswstlekekpFIhaeEMQSDDPLMLIYTSGTTG 272
Cdd:cd17640 60 ------RGSDSSVE-------------ELLYILNHSESVAL----------------VV---ENDSDDLATIIYTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 273 KPKGTVHTHAGFpLKAAFDAGFGMNIKQGDRVLWVTDMgWMMGPFLLFGSLINGATMVMYEGVPDFPE------------ 340
Cdd:cd17640 102 NPKGVMLTHANL-LHQIRSLSDIVPPQPGDRFLSILPI-WHSYERSAEYFIFACGCSQAYTSIRTLKDdlkrvkphyivs 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 341 ADRLWETVDKYEITHLGISPTLIRALMakgdeyvnkHSLKSLE--VFASTGEPWNPDPWMWLFETVGkgnVPICNYSGGT 418
Cdd:cd17640 180 VPRLWESLYSGIQKQVSKSSPIKQFLF---------LFFLSGGifKFGISGGGALPPHVDTFFEAIG---IEVLNGYGLT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 419 EISGGIFGNVLIKPIAPiSFNASLPGMAAVVLDDQGKPI--RDEVGELCLEKPWVgmTKSFWEDDERyvnTYWSRFENKW 496
Cdd:cd17640 248 ETSPVVSARRLKCNVRG-SVGRPLPGTEIKIVDPEGNVVlpPGEKGIVWVRGPQV--MKGYYKNPEA---TSKVLDSDGW 321
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446729146 497 VH-GD--WVIYDGEqYIITGRSDDTLNIA-GKRIGPAEYESILVKHNDVIEAAAIG 548
Cdd:cd17640 322 FNtGDlgWLTCGGE-LVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
97-299 |
1.44e-09 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 60.88 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 97 TRIQPalqyEGENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASD 176
Cdd:PLN02736 65 TRIRV----DGTVGEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 177 AVMTRVQAAGSKMI-ITADGFSrrgKIVSLKDEvdkacehCPTVEKVVIVRHAGNDFTPHNYD-----FSWSTLEKE--- 247
Cdd:PLN02736 141 AVKFIVNHAEVAAIfCVPQTLN---TLLSCLSE-------IPSVRLIVVVGGADEPLPSLPSGtgveiVTYSKLLAQgrs 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446729146 248 --KPFIHAEEmqsDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAafdAGFGMNIK 299
Cdd:PLN02736 211 spQPFRPPKP---EDVATICYTSGTTGTPKGVVLTHGNLIANV---AGSSLSTK 258
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
115-618 |
2.00e-09 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 60.27 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 115 FTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITAD 194
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 195 gfSRRGkivslkdevdkacehcpTVEKVVIVRHAGNDFTpHNYDFSWSTLE---KEKPFIHAEEMQSDDPLMLIYTSGTT 271
Cdd:PRK07514 109 --ANFA-----------------WLSKIAAAAGAPHVET-LDADGTGSLLEaaaAAPDDFETVPRGADDLAAILYTSGTT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 272 GKPKGTVHTHAgfplkaafdagfgmNIKQGDRVL---WvtdmGWMMGPFL-----------LF----GSLINGATMVMye 333
Cdd:PRK07514 169 GRSKGAMLSHG--------------NLLSNALTLvdyW----RFTPDDVLihalpifhthgLFvatnVALLAGASMIF-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 334 gVPDFpEADRLWE-----TVdkyeitHLGIsPTLIRALMAkgDEYVNKHSLKSLEVFASTGEPWNPDPWMWLFETVGK-- 406
Cdd:PRK07514 229 -LPKF-DPDAVLAlmpraTV------MMGV-PTFYTRLLQ--EPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHai 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 407 --------GNVPICN-YSGgtEISGGIFGnvliKPiapisfnasLPGMAAVVLD-DQGKPI-RDEVGELCLEKPWVgmTK 475
Cdd:PRK07514 298 lerygmteTNMNTSNpYDG--ERRAGTVG----FP---------LPGVSLRVTDpETGAELpPGEIGMIEVKGPNV--FK 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 476 SFWEDDERyvnTYWSRFENKW-VHGDWVIYDGEQYI-ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEV 553
Cdd:PRK07514 361 GYWRMPEK---TAEEFRADGFfITGDLGKIDERGYVhIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPD 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446729146 554 KGEVCHCFVVLRDHVTFTGElkkELMSLVNSHIGKALCPKDIHVVEDLPktRNS--KVMRRVIKAAY 618
Cdd:PRK07514 438 FGEGVTAVVVPKPGAALDEA---AILAALKGRLARFKQPKRVFFVDELP--RNTmgKVQKNLLREQY 499
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
75-281 |
2.85e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 59.99 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 75 WYNGGTCnvvesaLSRwLAD--EETRIQPALQY-----------EGENGTSKSF-----------TYEELDNWVSRVANG 130
Cdd:PTZ00216 65 WYYGPNF------LQR-LERicKERGDRRALAYrpvervekevvKDADGKERTMevthfnetryiTYAELWERIVNFGRG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 131 LKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITadGFSRRGKIVSLKDEvd 210
Cdd:PTZ00216 138 LAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC--NGKNVPNLLRLMKS-- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 211 KACEHCPtvekVVIVRHAGNDFTPHNYD-FSWSTLEKEkpfihAEEMQS---------DDPLMLI-YTSGTTGKPKGTVH 279
Cdd:PTZ00216 214 GGMPNTT----IIYLDSLPASVDTEGCRlVAWTDVVAK-----GHSAGShhplnipenNDDLALImYTSGTTGDPKGVMH 284
|
..
gi 446729146 280 TH 281
Cdd:PTZ00216 285 TH 286
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
116-328 |
2.89e-09 |
|
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: 60.16 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLK-HAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMI-ITA 193
Cdd:cd17632 69 TYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLaVSA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 194 DgfsrrgkivSLKDEVDKACEHcPTVEKVVIVRHAgNDFTPHNYDFSWS-----------TLEKE--------KPFIHAE 254
Cdd:cd17632 149 E---------HLDLAVEAVLEG-GTPPRLVVFDHR-PEVDAHRAALESArerlaavgipvTTLTLiavrgrdlPPAPLFR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 255 EMQSDDPL-MLIYTSGTTGKPKGTVHTHagfplKAAFDAGFGMNIKQGDR-----VLWVTDMGWMMGPFLLFGSLINGAT 328
Cdd:cd17632 218 PEPDDDPLaLLIYTSGSTGTPKGAMYTE-----RLVATFWLKVSSIQDIRppasiTLNFMPMSHIAGRISLYGTLARGGT 292
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
116-282 |
4.15e-09 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 59.54 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIE--KGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIITA 193
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 194 DGFsrrgKIVSLKDEVDKACEHcptvekvvIVRHagndftphnydfswstlEKEKPfihaeemqsDDPLMLIYTSGTTGK 273
Cdd:cd05927 87 AGV----KVYSLEEFEKLGKKN--------KVPP-----------------PPPKP---------EDLATICYTSGTTGN 128
|
....*....
gi 446729146 274 PKGTVHTHA 282
Cdd:cd05927 129 PKGVMLTHG 137
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
513-617 |
1.21e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 57.74 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 513 GRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGE-VCHCFVVlrDHVTFTGELKKELMSLVNSHigkaLC 591
Cdd:PRK08308 311 GRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErVKAKVIS--HEEIDPVQLREWCIQHLAPY----QV 384
|
90 100
....*....|....*....|....*.
gi 446729146 592 PKDIHVVEDLPKTRNSKVMRRVIKAA 617
Cdd:PRK08308 385 PHEIESVTEIPKNANGKVSRKLLELG 410
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
511-620 |
2.28e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 56.59 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 511 ITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVVLRDHVTFTGElkkELMSLVNSHIGKAL 590
Cdd:PRK07824 251 VLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLE---ALRAHVARTLDRTA 327
|
90 100 110
....*....|....*....|....*....|
gi 446729146 591 CPKDIHVVEDLPKTRNSKVMRRVIKAAYLG 620
Cdd:PRK07824 328 APRELHVVDELPRRGIGKVDRRALVRRFAG 357
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
116-281 |
1.66e-07 |
|
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: 54.14 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIItadg 195
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIF---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 196 fsrrgkivslkdevdkaCEHCPtvekvvivrhagndftphnydfswstlekekpfihaeemqsDDPLMLIYTSGTTGKPK 275
Cdd:cd17639 83 -----------------TDGKP-----------------------------------------DDLACIMYTSGSTGNPK 104
|
....*.
gi 446729146 276 GTVHTH 281
Cdd:cd17639 105 GVMLTH 110
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
116-282 |
2.02e-07 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 54.35 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVM-----TRVQA--AGSK 188
Cdd:PLN02387 108 TYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALChslneTEVTTviCDSK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 189 MIitadgfsrrGKIVSLKDEVDkacehcpTVEKVVIVRHAGNDFTPHNYD------FSWSTLEK---EKPfIHAEEMQSD 259
Cdd:PLN02387 188 QL---------KKLIDISSQLE-------TVKRVIYMDDEGVDSDSSLSGssnwtvSSFSEVEKlgkENP-VDPDLPSPN 250
|
170 180
....*....|....*....|...
gi 446729146 260 DPLMLIYTSGTTGKPKGTVHTHA 282
Cdd:PLN02387 251 DIAVIMYTSGSTGLPKGVMMTHG 273
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
116-281 |
2.09e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 54.05 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAV----------MTRVQAA 185
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVdyivdhaeidFVFVQDK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 186 GSKMIITAD--GFSRRGKIVSL----KDEVDKAcehcptvEKVVIVRHAGNDFTphnydfswsTLEKEKPfihaEEMQSD 259
Cdd:PLN02430 158 KIKELLEPDckSAKRLKAIVSFtsvtEEESDKA-------SQIGVKTYSWIDFL---------HMGKENP----SETNPP 217
|
170 180
....*....|....*....|....*
gi 446729146 260 DPL---MLIYTSGTTGKPKGTVHTH 281
Cdd:PLN02430 218 KPLdicTIMYTSGTSGDPKGVVLTH 242
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
116-282 |
9.07e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 52.15 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAV----------MTRVQAA 185
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVefiinhaevsIAFVQES 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 186 GSKMIITA--------DGFSRRGKIVS-LKDEVDKACEHCptvekvvivrhagndftphnydFSWS------TLEKEKPf 250
Cdd:PLN02861 159 KISSILSClpkcssnlKTIVSFGDVSSeQKEEAEELGVSC----------------------FSWEefslmgSLDCELP- 215
|
170 180 190
....*....|....*....|....*....|..
gi 446729146 251 ihaeEMQSDDPLMLIYTSGTTGKPKGTVHTHA 282
Cdd:PLN02861 216 ----PKQKTDICTIMYTSGTTGEPKGVILTNR 243
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
488-611 |
1.58e-06 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 51.15 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 488 YWSRFEN---KWVHGDWVIYDGEQY-IITGRSDDTLNIAGKRIGPAEYESILVKHNDVIEAAAIGVPDEVKGEVCHCFVV 563
Cdd:PRK07445 315 YYPQILDsqgIFETDDLGYLDAQGYlHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYV 394
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446729146 564 LRDHVTFTGELKkelmSLVNSHIGKALCPKDIHVVEDLPKTRNSKVMR 611
Cdd:PRK07445 395 PKDPSISLEELK----TAIKDQLSPFKQPKHWIPVPQLPRNPQGKINR 438
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
116-278 |
3.05e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 50.40 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVMTRVQAAGSKMIitadg 195
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIV----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 196 FSRRGKIVSLKDEVDKACEHCPTV--------------EKVVIVRHAGNDFTP----HNYDfswstLEKEKPfihaeemq 257
Cdd:PLN02614 156 FVEEKKISELFKTCPNSTEYMKTVvsfggvsreqkeeaETFGLVIYAWDEFLKlgegKQYD-----LPIKKK-------- 222
|
170 180
....*....|....*....|.
gi 446729146 258 sDDPLMLIYTSGTTGKPKGTV 278
Cdd:PLN02614 223 -SDICTIMYTSGTTGDPKGVM 242
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
112-169 |
1.11e-05 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 48.91 E-value: 1.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446729146 112 SKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPI 169
Cdd:TIGR03443 268 TRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVI 325
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
259-603 |
1.81e-05 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 48.00 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 259 DDPLMLIYTSGTTGKPKGTVHTHagFPLKAafdagfgmNIKQGDRVLWVTDMGWMMG--PFL--------LFGSLINGAT 328
Cdd:PRK08633 782 DDTATIIFSSGSEGEPKGVMLSH--HNILS--------NIEQISDVFNLRNDDVILSslPFFhsfgltvtLWLPLLEGIK 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 329 MVMyegVPDFPEADRLWETVDKYEITHLGISPTLIRAlmakgdeYVNKHSLKSLEvFAS-----TG-EPWNPDpwmwL-- 400
Cdd:PRK08633 852 VVY---HPDPTDALGIAKLVAKHRATILLGTPTFLRL-------YLRNKKLHPLM-FASlrlvvAGaEKLKPE----Vad 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 401 -FETvgKGNVPICNYSGGTEISGGIFGN---VLIKPIAPISFNAS------LPGMAAVVLD-DQGKPIRD-EVGELCLEK 468
Cdd:PRK08633 917 aFEE--KFGIRILEGYGATETSPVASVNlpdVLAADFKRQTGSKEgsvgmpLPGVAVRIVDpETFEELPPgEDGLILIGG 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 469 PWVgMtKSFWEDDERYVNTYWSRFENKW-VHGDWVIYDGEQYI-ITGRSDDTLNIAGKRI--GPAEYESILVKHNDVIEA 544
Cdd:PRK08633 995 PQV-M-KGYLGDPEKTAEVIKDIDGIGWyVTGDKGHLDEDGFLtITDRYSRFAKIGGEMVplGAVEEELAKALGGEEVVF 1072
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446729146 545 AAIGVPDEVKGEVchcFVVLRDHVTFTGELKKELMSlvNSHIGKALCPKDIHVVEDLPK 603
Cdd:PRK08633 1073 AVTAVPDEKKGEK---LVVLHTCGAEDVEELKRAIK--ESGLPNLWKPSRYFKVEALPL 1126
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
107-186 |
2.44e-05 |
|
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: 47.13 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 107 GENGTSKSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGA---IISP--------IFSGFAS 175
Cdd:cd17647 13 LNSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGAtfsVIDPaypparqnIYLGVAK 92
|
90
....*....|.
gi 446729146 176 DAVMTRVQAAG 186
Cdd:cd17647 93 PRGLIVIRAAG 103
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
116-281 |
4.92e-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: 46.58 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAIISPIFSGFASDAVmtRVQAAGSKM-IITAD 194
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEAC--QYVAETSEAnILVVE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 195 GFSRRGKIVSLKDEVdkacehcPTVEKVVIVRhagNDFTPH--NYdFSWSTLEkekpfihaeEMQSDDPL---------- 262
Cdd:cd05933 88 NQKQLQKILQIQDKL-------PHLKAIIQYK---EPLKEKepNL-YSWDEFM---------ELGRSIPDeqldaiissq 147
|
170 180
....*....|....*....|....*
gi 446729146 263 ------MLIYTSGTTGKPKGTVHTH 281
Cdd:cd05933 148 kpnqccTLIYTSGTTGMPKGVMLSH 172
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
86-318 |
2.40e-04 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 44.23 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 86 SALSRWLADEETRIQpALQY--EGENGTS---------KSFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVV 154
Cdd:PRK09192 11 SSLPRRYADFPTLVE-ALDYaaLGEAGMNfydrrgqleEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 155 AMLAVMKIGAIISPI-----FSGFASDAVMTRVQAAGSK--MIITADGFSrrgkivslkdevdkacehcPTVEKVVIVRH 227
Cdd:PRK09192 90 AFFACQYAGLVPVPLplpmgFGGRESYIAQLRGMLASAQpaAIITPDELL-------------------PWVNEATHGNP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 228 AGNDFTPHNYDfswstlEKEKPFIHAEEMQSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAGFGMNIKQGDRVL-- 305
Cdd:PRK09192 151 LLHVLSHAWFK------ALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGLKVRPGDRCVsw 224
|
250
....*....|....*
gi 446729146 306 --WVTDMGwMMGPFL 318
Cdd:PRK09192 225 lpFYHDMG-LVGFLL 238
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
88-426 |
7.47e-04 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 42.42 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 88 LSRWLADEETRIQPAlQYEGENGTSKsFTYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIG---A 164
Cdd:cd05921 1 LAHWARQAPDRTWLA-EREGNGGWRR-VTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGvpaA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 165 IISPIFSGFASD-----AVMTRVQAAgskMIITADGFSRRGKIVSLKDevdkacehcPTVEKVVIVRHAGNDFTphnydF 239
Cdd:cd05921 79 PVSPAYSLMSQDlaklkHLFELLKPG---LVFAQDAAPFARALAAIFP---------LGTPLVVSRNAVAGRGA-----I 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 240 SWSTLEKEKPFIHAEE----MQSDDPLMLIYTSGTTGKPKGTVHTHAGFPLKAAFDAG-FGMnikQGDRVLWVTDmgWM- 313
Cdd:cd05921 142 SFAELAATPPTAAVDAafaaVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQtYPF---FGEEPPVLVD--WLp 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 314 ----MGPFLLFG-SLINGATMVMYEGVpdfPEADRLWETVDK-YEithlgISPT-----------LIRALmaKGDEYVNK 376
Cdd:cd05921 217 wnhtFGGNHNFNlVLYNGGTLYIDDGK---PMPGGFEETLRNlRE-----ISPTvyfnvpagwemLVAAL--EKDEALRR 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 446729146 377 HSLKSLEVFASTGEPWNPDPWMWL----FETVGKgNVPICNYSGGTEISGGIFG 426
Cdd:cd05921 287 RFFKRLKLMFYAGAGLSQDVWDRLqalaVATVGE-RIPMMAGLGATETAPTATF 339
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
182-282 |
1.03e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 42.39 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446729146 182 VQAAGSKMIITADGFSRRGKIVSLKDEVDKAcehcptveKVVIVRHAGNDFTPHnyDFSWSTLEKEKPFIHAEEMQSDDP 261
Cdd:PRK08043 298 ITAAEIKTIFTSRQFLDKGKLWHLPEQLTQV--------RWVYLEDLKDDVTTA--DKLWIFAHLLMPRLAQVKQQPEDA 367
|
90 100
....*....|....*....|.
gi 446729146 262 LMLIYTSGTTGKPKGTVHTHA 282
Cdd:PRK08043 368 ALILFTSGSEGHPKGVVHSHK 388
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
116-165 |
5.60e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 40.09 E-value: 5.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446729146 116 TYEELDNWVSRVANGLKHAGIEKGDRVTIYMPMIPETVVAMLAVMKIGAI 165
Cdd:PRK07868 474 TYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAV 523
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