|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
1-651 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 1239.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 1 MFKLSNPFNYLNDFNYANSYPEAFWDEVAKKNVFWDKMYDKVYSGDEMYPDWFKGGELNTCYNVLDIQVQNPLKRDQDAL 80
Cdd:PTZ00237 1 MYKLSDPFDYENDSNYANSNPESFWDEVAKKYVHWDKMYDKVYSGDEIYPDWFKGGELNTCYNVLDIHVKNPLKRDQDAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 81 IYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRI 160
Cdd:PTZ00237 81 IYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 161 ETITPKLIITTNYGIFNDEIITFTPNLKDAIELSTFKPSNVITLFRNDITSESDLKKVKDIPTIPNTLSWYDEIKKFKEN 240
Cdd:PTZ00237 161 ETITPKLIITTNYGILNDEIITFTPNLKEAIELSTFKPSNVITLFRNDITSESDLKKIETIPTIPNTLSWYDEIKKIKEN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 241 NQSPFYEYVPVESSHPLYIIYSSGTTGNAKAVVRSNGPNLVCMNYFDRYISEKYECTTLLTTSSVGWVSFHGFLYGMLSF 320
Cdd:PTZ00237 241 NQSPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 321 GSTFVMYEGGIIKNKHIEVDFWNTIEKHKATHTLSLANTIRYFIKTDPEGTIIRSKYDLSNLKEIWVGGEVIEESIPEYI 400
Cdd:PTZ00237 321 GNTFVMFEGGIIKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDPEATIIRSKYDLSNLKEIWCGGEVIEESIPEYI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 401 EKKLKIKPTRGYGQTEIGIAYLYCFDHINIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLPMPPSFATTLYKND 480
Cdd:PTZ00237 401 ENKLKIKSSRGYGQTEIGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKLPMPPSFATTFYKND 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 481 EKFKQLFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIAl 560
Cdd:PTZ00237 481 EKFKQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIG- 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 561 lvlKQLQQQDQSIQQIDLNKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPIISKFLNDSNFQLPDNVNNVE 640
Cdd:PTZ00237 560 ---LLVLKQDQSNQSIDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLNDSNYQLPDNVNDSE 636
|
650
....*....|.
gi 60472587 641 IFYEIKELYMK 651
Cdd:PTZ00237 637 IFYKIKELYMK 647
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
10-645 |
1.72e-168 |
|
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: 495.30 E-value: 1.72e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 10 YLNDFNYANSYPEAFWDEVAKKnVFWDKMYDKVYSGDEM-YPDWFKGGELNTCYNVLDIQVQNPlKRDQDALIYECPYLK 88
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARL-IDWFKPPEKILDNSNPpFTRWFVGGRLNTCYNALDRHVEAG-RGDQIALIYDSPVTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 89 KTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLI 168
Cdd:cd05967 79 TERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 169 ITTNYGIFNDEIITFTPNLKDAIELSTFKPSNVITLFRNDITSESdLKKVKDiptipntLSWYDEIKkfkennQSPFYEY 248
Cdd:cd05967 159 VTASCGIEPGKVVPYKPLLDKALELSGHKPHHVLVLNRPQVPADL-TKPGRD-------LDWSELLA------KAEPVDC 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 249 VPVESSHPLYIIYSSGTTGNAKAVVRSNGPNLVCMNYFDRYISEKYECTTLLTTSSVGWVSFHGFL-YGMLSFGSTFVMY 327
Cdd:cd05967 225 VPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIvYGPLLHGATTVLY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 328 EGgiiknKHIEVD----FWNTIEKHKATHTLSLANTIRYFIKTDPEGTIIRsKYDLSNLKEIWVGGEVIEESIPEYIEKK 403
Cdd:cd05967 305 EG-----KPVGTPdpgaFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYIK-KYDLSSLRTLFLAGERLDPPTLEWAENT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 404 LKIKPTRGYGQTEIG---IAYLYCFDHINIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLPMPPSFATTLYKND 480
Cdd:cd05967 379 LGVPVIDHWWQTETGwpiTANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLPPGCLLTLWKND 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 481 EKFKQL-FSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIA 559
Cdd:cd05967 459 ERFKKLyLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLG 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 560 llvlkqlQQQDQSIQQIDLNKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPIISKFLNDSNFQLPDNVNNV 639
Cdd:cd05967 539 -------LVVLKEGVKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDYTIPSTIEDP 611
|
....*.
gi 60472587 640 EIFYEI 645
Cdd:cd05967 612 SVLDEI 617
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
52-618 |
2.54e-129 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 392.55 E-value: 2.54e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 52 WFKGGELNTCYNVLDIQVQNplKRDQDALIYECPyLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPL 131
Cdd:COG0365 2 WFVGGRLNIAYNCLDRHAEG--RGDKVALIWEGE-DGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 132 IAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGIFNDEIITFTPNLKDAIELSTfKPSNVITLFRNDits 211
Cdd:COG0365 79 IAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELP-SLEHVIVVGRTG--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 212 esdlkkvkDIPTIPNTLSWYDEIKkfkenNQSPFYEYVPVESSHPLYIIYSSGTTGNAKAVVRSNGPNLVCMNYFDRYIs 291
Cdd:COG0365 155 --------ADVPMEGDLDWDELLA-----AASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYV- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 292 ekYECT---TLLTTSSVGWVSFHG-FLYGMLSFGSTFVMYEGgiiKNKHIEVD-FWNTIEKHKATHTLSLANTIRYFIKT 366
Cdd:COG0365 221 --LDLKpgdVFWCTADIGWATGHSyIVYGPLLNGATVVLYEG---RPDFPDPGrLWELIEKYGVTVFFTAPTAIRALMKA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 367 DPEgtiIRSKYDLSNLKEIWVGGEVIEESIPEYIEKKLKIKPTRGYGQTEIGIAYLYCFDHINIPYYATGLPSIFIRPSI 446
Cdd:COG0365 296 GDE---PLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVKPGSMGKPVPGYDVAV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 447 FSDDGKELGVNEIGEIAFKLPMpPSFATTLYKNDEKFKQ-LFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGnkV 525
Cdd:COG0365 373 VDEDGNPVPPGEEGELVIKGPW-PGMFRGYWNDPERYREtYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSG--H 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 526 QLNT--IETSILKHPLVLECCSIGINDPTCYSVPIAllvlkqlqqqdqsiqQIDLNK-------LQNEINYIIKQDIESL 596
Cdd:COG0365 450 RIGTaeIESALVSHPAVAEAAVVGVPDEIRGQVVKA---------------FVVLKPgvepsdeLAKELQAHVREELGPY 514
|
570 580
....*....|....*....|..
gi 60472587 597 AVLRKIVIVNQLPKTKTGKIPR 618
Cdd:COG0365 515 AYPREIEFVDELPKTRSGKIMR 536
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
21-623 |
1.99e-110 |
|
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: 345.32 E-value: 1.99e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 21 PEAFWDEVAKKnVFWDKMYDKVYSGDEMYPD--WFKGGELNTCYNVLDIQVQNplKRDQDALIYECPYLKKTIKLTYYQL 98
Cdd:cd05966 14 PEEFWGEIAKE-LDWFKPWDKVLDWSKGPPFikWFEGGKLNISYNCLDRHLKE--RGDKVAIIWEGDEPDQSRTITYREL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 99 YEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGIFND 178
Cdd:cd05966 91 LREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLVITADGGYRGG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 179 EIITFTPNLKDAIELsTFKPSNVITLFRNDItsESDLKKVKDIptipntlsWYDEIKKfkenNQSPFYEYVPVESSHPLY 258
Cdd:cd05966 171 KVIPLKEIVDEALEK-CPSVEKVLVVKRTGG--EVPMTEGRDL--------WWHDLMA----KQSPECEPEWMDSEDPLF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 259 IIYSSGTTGNAKAVVRSNGPNLV----CMNY-FDRYISEKYECttlltTSSVGWVSFHGF-LYGMLSFGSTFVMYEG--- 329
Cdd:cd05966 236 ILYTSGSTGKPKGVVHTTGGYLLyaatTFKYvFDYHPDDIYWC-----TADIGWITGHSYiVYGPLANGATTVMFEGtpt 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 330 ----GIiknkhievdFWNTIEKHKATHtLSLANT-IRYFIKtdpEGTIIRSKYDLSNLKEIWVGGEVIEesiPE------ 398
Cdd:cd05966 311 ypdpGR---------YWDIVEKHKVTI-FYTAPTaIRALMK---FGDEWVKKHDLSSLRVLGSVGEPIN---PEawmwyy 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 399 -YI-EKKLKIKPTrgYGQTEIGiaylycfdHINI----------PYYATgLPSIFIRPSIFSDDGKELGVNEIGEIAFKL 466
Cdd:cd05966 375 eVIgKERCPIVDT--WWQTETG--------GIMItplpgatplkPGSAT-RPFFGIEPAILDEEGNEVEGEVEGYLVIKR 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 467 PMpPSFATTLYKNDEKFKQL-FSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCS 545
Cdd:cd05966 444 PW-PGMARTIYGDHERYEDTyFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAV 522
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60472587 546 IGINDPTCYSVPIALLVLKQLQQQDQsiqqidlnKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPIISK 623
Cdd:cd05966 523 VGRPHDIKGEAIYAFVTLKDGEEPSD--------ELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRK 592
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
21-634 |
2.81e-104 |
|
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: 329.59 E-value: 2.81e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 21 PEAFWDEVAKKNVFWDKMYDKVYSGD-EMYPDWFKGGELNTCYNVLDIQVQNplKRDQDALIYECPYLKKTIKLTYYQLY 99
Cdd:TIGR02188 18 PDKFWAKLARELLDWFKPFTKVLDWSfPPFYKWFVGGELNVSYNCVDRHLEA--RPDKVAIIWEGDEPGEVRKITYRELH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 100 EKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGIFNDE 179
Cdd:TIGR02188 96 REVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKLVITADEGLRGGK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 180 IITFTPNLKDAIELSTFKPSNVITLFRNDItsesdlkkvKDIPTIPNTLSWYDEIKKfkenNQSPFYEYVPVESSHPLYI 259
Cdd:TIGR02188 176 VIPLKAIVDEALEKCPVSVEHVLVVRRTGN---------PVVPWVEGRDVWWHDLMA----KASAYCEPEPMDSEDPLFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 260 IYSSGTTGNAKAVVRSNGPNLVC----MNY-FDRYISEKYECttlltTSSVGWVSFHGFL-YGMLSFGSTFVMYEGgiIK 333
Cdd:TIGR02188 243 LYTSGSTGKPKGVLHTTGGYLLYaamtMKYvFDIKDGDIFWC-----TADVGWITGHSYIvYGPLANGATTVMFEG--VP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 334 NKHIEVDFWNTIEKHKATHTLSLANTIRYFIKtdpEGTIIRSKYDLSNLKEIWVGGEVIEesiPE----YIEK----KLK 405
Cdd:TIGR02188 316 TYPDPGRFWEIIEKHKVTIFYTAPTAIRALMR---LGDEWVKKHDLSSLRLLGSVGEPIN---PEawmwYYKVvgkeRCP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 406 IKPTrgYGQTEIG---IAYLYCFDHINiPYYATgLPSIFIRPSIFSDDGKEL-GVNEIGEIAFKLPMpPSFATTLYKNDE 481
Cdd:TIGR02188 390 IVDT--WWQTETGgimITPLPGATPTK-PGSAT-LPFFGIEPAVVDEEGNPVeGPGEGGYLVIKQPW-PGMLRTIYGDHE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 482 KF-KQLFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIAL 560
Cdd:TIGR02188 465 RFvDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAF 544
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60472587 561 LVLKQLQQQDQsiqqidlnKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPIISKFLNDSNFQLPD 634
Cdd:TIGR02188 545 VTLKDGYEPDD--------ELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEILGD 610
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
21-618 |
5.14e-102 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 323.82 E-value: 5.14e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 21 PEAFWDEVAKKnVFWDKMYDKV--YSgDEMYPDWFKGGELNTCYNVLDIQVqnPLKRDQDALIYECPYLKKTIKLTYYQL 98
Cdd:PRK10524 15 PEAFWAEQARR-IDWQTPFTQVldYS-NPPFARWFVGGRTNLCHNAVDRHL--AKRPEQLALIAVSTETDEERTYTFRQL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 99 YEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGIFND 178
Cdd:PRK10524 91 HDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVSADAGSRGG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 179 EIITFTPNLKDAIELSTFKPSNVITLFRNditsesdLKKVKDIPtiPNTLSWYDEIKKFKENNqspfyeyVPV---ESSH 255
Cdd:PRK10524 171 KVVPYKPLLDEAIALAQHKPRHVLLVDRG-------LAPMARVA--GRDVDYATLRAQHLGAR-------VPVewlESNE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 256 PLYIIYSSGTTGNAKAVVRSNGPNLVCMNYFDRYISEKYECTTLLTTSSVGWVSFHGFL-YGMLSFGSTFVMYEG----- 329
Cdd:PRK10524 235 PSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIvYAPLLAGMATIMYEGlptrp 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 330 --GIiknkhievdFWNTIEKHKATHTLSLANTIRYFIKTDPEgtIIRsKYDLSNLKEIWVGGEVIEESIPEYIEKKLKIK 407
Cdd:PRK10524 315 daGI---------WWRIVEKYKVNRMFSAPTAIRVLKKQDPA--LLR-KHDLSSLRALFLAGEPLDEPTASWISEALGVP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 408 PTRGYGQTEIG---IAYLYCFDHINIPYYATGLPSIFIRPSIFSD-DGKELGVNEIGEIAFKLPMPPSFATTLYKNDEKF 483
Cdd:PRK10524 383 VIDNYWQTETGwpiLAIARGVEDRPTRLGSPGVPMYGYNVKLLNEvTGEPCGPNEKGVLVIEGPLPPGCMQTVWGDDDRF 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 484 -KQLFSKF-PGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALL 561
Cdd:PRK10524 463 vKTYWSLFgRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFV 542
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 60472587 562 VLKQLQQQDQSIQQIdlnKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:PRK10524 543 VPKDSDSLADREARL---ALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLR 596
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
21-616 |
6.31e-98 |
|
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: 312.20 E-value: 6.31e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 21 PEAFWDEvAKKNVFWDKMYDKVY-----SGDEMYPdWFKGGELNTCYNVLDIQVQNplKRDQDALIYECPYLKKTIKLTY 95
Cdd:cd17634 12 PDTFWGE-AGKILDWITPYQKVKntsfaPGAPSIK-WFEDATLNLAANALDRHLRE--NGDRTAIIYEGDDTSQSRTISY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 96 YQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGI 175
Cdd:cd17634 88 RELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 176 FNDEIITFTPNLKDAIELSTFKPSNVITLFRNDItsesdlkkvkDIPTIPNTLSWYDEIKKfkenNQSPFYEYVPVESSH 255
Cdd:cd17634 168 RAGRSVPLKKNVDDALNPNVTSVEHVIVLKRTGS----------DIDWQEGRDLWWRDLIA----KASPEHQPEAMNAED 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 256 PLYIIYSSGTTGNAKAVVRSNGPNLVCMNYFDRYISEKYECTTLLTTSSVGWVSFHGFL-YGMLSFGSTFVMYEGgiiKN 334
Cdd:cd17634 234 PLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLlYGPLACGATTLLYEG---VP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 335 KHIEVD-FWNTIEKHKATHTLSLANTIRYFIKTDPEGTiirSKYDLSNLKEIWVGGEVIEESIPEYIEKKLKIK--PTRG 411
Cdd:cd17634 311 NWPTPArMWQVVDKHGVNILYTAPTAIRALMAAGDDAI---EGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEkcPVVD 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 412 Y-GQTEIGIAYLYCFdHINIPYYA--TGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLPMPPSFATTLYKNDEKFKQLFS 488
Cdd:cd17634 388 TwWQTETGGFMITPL-PGAIELKAgsATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERFEQTYFS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 489 KFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALLVLKQLQQ 568
Cdd:cd17634 467 TFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVE 546
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 60472587 569 QDqsiqqidlNKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKI 616
Cdd:cd17634 547 PS--------PELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
21-623 |
3.88e-96 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 308.61 E-value: 3.88e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 21 PEAFWDEVAKKnVFWDKMYDKVYSGDEMYPDWFKGGELNTCYNVLDIQVQNplKRDQDALIYECPYLKKTIKLTYYQLYE 100
Cdd:PRK00174 30 PEGFWAEQAKR-LDWFKPFDTVLDWNAPFIKWFEDGELNVSYNCLDRHLKT--RGDKVAIIWEGDDPGDSRKITYRELHR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 101 KVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGIFNDEI 180
Cdd:PRK00174 107 EVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKLVITADEGVRGGKP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 181 ITFTPNLKDAIELStfkPS--NVITLFRNDitsesdlkkvKDIPTIPNTLSWYDEIKKfkenNQSPFYEYVPVESSHPLY 258
Cdd:PRK00174 187 IPLKANVDEALANC---PSveKVIVVRRTG----------GDVDWVEGRDLWWHELVA----GASDECEPEPMDAEDPLF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 259 IIYSSGTTGNAKAVVRSNGPNLV----CMNY-FDRYISEKYECttlltTSSVGWVSFHGFL-YGMLSFGSTFVMYEGgiI 332
Cdd:PRK00174 250 ILYTSGSTGKPKGVLHTTGGYLVyaamTMKYvFDYKDGDVYWC-----TADVGWVTGHSYIvYGPLANGATTLMFEG--V 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 333 KNKHIEVDFWNTIEKHKAThTLSLANT-IRYFIKtdpEGTIIRSKYDLSNLKEIWVGGEVIEesiPE----YIEK----K 403
Cdd:PRK00174 323 PNYPDPGRFWEVIDKHKVT-IFYTAPTaIRALMK---EGDEHPKKYDLSSLRLLGSVGEPIN---PEawewYYKVvggeR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 404 LKIKPTrgYGQTEIG---IAYLycfdhiniPyYAT-------GLPSIFIRPSIFSDDGKELGVNEIGEIAFKLPMpPSFA 473
Cdd:PRK00174 396 CPIVDT--WWQTETGgimITPL--------P-GATplkpgsaTRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPW-PGMM 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 474 TTLYKNDEKFKQ-LFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKvqLNT--IETSILKHPLVLECCSIGIND 550
Cdd:PRK00174 464 RTIYGDHERFVKtYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHR--LGTaeIESALVAHPKVAEAAVVGRPD 541
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60472587 551 PT------CYSVPIALLVLKQlqqqdqsiqqidlnKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPIISK 623
Cdd:PRK00174 542 DIkgqgiyAFVTLKGGEEPSD--------------ELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
255-616 |
1.59e-81 |
|
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: 261.07 E-value: 1.59e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 255 HPLYIIYSSGTTGNAKAVVRSNGPNLVCMNYFDRYISEKYEcTTLLTTSSVGWVSFHGFLYGMLSFGSTFVMYEggiikn 334
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEG-DVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 335 KHIEVDFWNTIEKHKATHTLSLANTIRYFIKTDPegtiiRSKYDLSNLKEIWVGGEVIEESIPEYIEKKLKIKPTRGYGQ 414
Cdd:cd04433 74 KFDPEAALELIEREKVTILLGVPTLLARLLKAPE-----SAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 415 TEIGIAYLYCFDHINI-PYYATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLPMPPSFAttlYKNDEKfkQLFSKFPGY 493
Cdd:cd04433 149 TETGGTVATGPPDDDArKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGY---WNNPEA--TAAVDEDGW 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 494 YNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALLVLKQLQqqdqsi 573
Cdd:cd04433 224 YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGA------ 297
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 60472587 574 qqidlNKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKI 616
Cdd:cd04433 298 -----DLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
15-621 |
8.60e-62 |
|
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: 216.59 E-value: 8.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 15 NYANSYPEAFWDEVAKKNVF-WDKMYDKV--YSGDEMYPDWFKGGELNTCYNVLDIQVQNplKRDQDALIYECPylKKTI 91
Cdd:cd05968 14 ERSAEDNAWFWGEFVKDVGIeWYEPPYQTldLSGGKPWAAWFVGGRMNIVEQLLDKWLAD--TRTRPALRWEGE--DGTS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 92 K-LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIIT 170
Cdd:cd05968 90 RtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 171 TNYGIFNDEIITFTPNLKDAIElSTFKPSNVITLFRNDitsesdlkkvKDIPTIPNTLSWYDEIKKfkennqSPFYEYVP 250
Cdd:cd05968 170 ADGFTRRGREVNLKEEADKACA-QCPTVEKVVVVRHLG----------NDFTPAKGRDLSYDEEKE------TAGDGAER 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 251 VESSHPLYIIYSSGTTGNAKAVVRSNGpNLVCMNYFDRYIS-EKYECTTLLTTSSVGWVSFHGFLYGMLSFGSTFVMYEG 329
Cdd:cd05968 233 TESEDPLMIIYTSGTTGKPKGTVHVHA-GFPLKAAQDMYFQfDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 330 GiikNKHIEVD-FWNTIEKHKATHtLSLANT-IRYFIktdPEGTIIRSKYDLSNLKEIWVGGEVIE-ESIPEYIEKKLK- 405
Cdd:cd05968 312 A---PDHPKADrLWRMVEDHEITH-LGLSPTlIRALK---PRGDAPVNAHDLSSLRVLGSTGEPWNpEPWNWLFETVGKg 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 406 IKPTRGY-GQTEI--GIAYLYCFDHINIPYYATGLPSIfiRPSIFSDDGKELgVNEIGEIAFKLPMPpSFATTLYKNDEK 482
Cdd:cd05968 385 RNPIINYsGGTEIsgGILGNVLIKPIKPSSFNGPVPGM--KADVLDESGKPA-RPEVGELVLLAPWP-GMTRGFWRDEDR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 483 F-KQLFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALL 561
Cdd:cd05968 461 YlETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFV 540
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 562 VLKQLQQQDQSIQQIDLNKLQNEINYIIKQDieslavlrKIVIVNQLPKTKTGKIPRPII 621
Cdd:cd05968 541 VLKPGVTPTEALAEELMERVADELGKPLSPE--------RILFVKDLPKTRNAKVMRRVI 592
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
4-623 |
5.69e-61 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 215.53 E-value: 5.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 4 LSNPFNYLNDFNYANSYPEAFWDEVAKKnVFWDKMY--DKVYSGD------EMYPDWFKGGELNTCYNVLDIQVQNPLKr 75
Cdd:PLN02654 26 VSSPQQYMEMYKRSVDDPAGFWSDIASQ-FYWKQKWegDEVCSENldvrkgPISIEWFKGGKTNICYNCLDRNVEAGNG- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 76 DQDALIYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKS 155
Cdd:PLN02654 104 DKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAES 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 156 LIDRIETITPKLIITTNYGIFNDEIItftpNLKDAIELSTfkpsnvitlfrndITSESDLKKVKDIPTIPNTLSWYDEIK 235
Cdd:PLN02654 184 LAQRIVDCKPKVVITCNAVKRGPKTI----NLKDIVDAAL-------------DESAKNGVSVGICLTYENQLAMKREDT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 236 KFKENNQSPFYEYVP----------VESSHPLYIIYSSGTTGNAKAVVRSNGPNLV----CMNY-FDRYISEKYECttll 300
Cdd:PLN02654 247 KWQEGRDVWWQDVVPnyptkcevewVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVytatTFKYaFDYKPTDVYWC---- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 301 tTSSVGWVSFHGFL-YGMLSFGSTFVMYEGgiIKNKHIEVDFWNTIEKHKATHTLSLANTIRYFIKtdpEGTIIRSKYDL 379
Cdd:PLN02654 323 -TADCGWITGHSYVtYGPMLNGATVLVFEG--APNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMR---DGDEYVTRHSR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 380 SNLKEIWVGGEVIEESIPEYI-----EKKLKIKPTrgYGQTEIG---IAYLY-CFDHinIPYYATgLPSIFIRPSIFSDD 450
Cdd:PLN02654 397 KSLRVLGSVGEPINPSAWRWFfnvvgDSRCPISDT--WWQTETGgfmITPLPgAWPQ--KPGSAT-FPFFGVQPVIVDEK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 451 GKELGVNEIGEIAFKLPMPPSFaTTLYKNDEKFK-QLFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNT 529
Cdd:PLN02654 472 GKEIEGECSGYLCVKKSWPGAF-RTLYGDHERYEtTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAE 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 530 IETSILKHPLVLECCSIGI---------------NDPTCYSvpiallvlkqlqqqdqsiqqidlNKLQNEINYIIKQDIE 594
Cdd:PLN02654 551 VESALVSHPQCAEAAVVGIehevkgqgiyafvtlVEGVPYS-----------------------EELRKSLILTVRNQIG 607
|
650 660
....*....|....*....|....*....
gi 60472587 595 SLAVLRKIVIVNQLPKTKTGKIPRPIISK 623
Cdd:PLN02654 608 AFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
91-521 |
4.00e-56 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 195.99 E-value: 4.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 91 IKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIIT 170
Cdd:pfam00501 20 RRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 171 tnygifnDEIITFTPNLKDAIELstFKPSNVITLFRNDItsesdlkkvkdiptipntlSWYDEIKKFKENNQSPFYEYVP 250
Cdd:pfam00501 100 -------DDALKLEELLEALGKL--EVVKLVLVLDRDPV-------------------LKEEPLPEEAKPADVPPPPPPP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 251 VESSHPLYIIYSSGTTGNAKAVVRSNGpNLVC----MNYFDRYISEKYECTTLLTTSSVGWV-SFHGFLYGMLSFGSTFV 325
Cdd:pfam00501 152 PDPDDLAYIIYTSGTTGKPKGVMLTHR-NLVAnvlsIKRVRPRGFGLGPDDRVLSTLPLFHDfGLSLGLLGPLLAGATVV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 326 MYEGGiikNKHIEVDFWNTIEKHKATHtLSLANTI-RYFIKTDPEgtiirSKYDLSNLKEIWVGGEVIEESIPEYIEKKL 404
Cdd:pfam00501 231 LPPGF---PALDPAALLELIERYKVTV-LYGVPTLlNMLLEAGAP-----KRALLSSLRLVLSGGAPLPPELARRFRELF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 405 KIKPTRGYGQTEIGIAYLYCFDHIN--IPYYATGLPSIFIRPSIFSDD-GKELGVNEIGEIAFKlpmPPSFATTLYKNDE 481
Cdd:pfam00501 302 GGALVNGYGLTETTGVVTTPLPLDEdlRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR---GPGVMKGYLNDPE 378
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 60472587 482 KFKQLFsKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKIS 521
Cdd:pfam00501 379 LTAEAF-DEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
76-616 |
1.19e-51 |
|
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: 185.01 E-value: 1.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 76 DQDALIYEcpylkkTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKS 155
Cdd:COG0318 14 DRPALVFG------GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 156 LIDRIETITPKLIITtnygifndeiitftpnlkdaielstfkpsnvitlfrnditsesdlkkvkdiptipntlswydeik 235
Cdd:COG0318 88 LAYILEDSGARALVT----------------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 236 kfkennqspfyeyvpvesshpLYIIYSSGTTGNAKAVVRSNGpNLV--CMNYFDRY-ISEKyecTTLLTTSSVgwvsFHG 312
Cdd:COG0318 103 ---------------------ALILYTSGTTGRPKGVMLTHR-NLLanAAAIAAALgLTPG---DVVLVALPL----FHV 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 313 F-----LYGMLSFGSTFVMYEggiikNKHIEvDFWNTIEKHKATHtLSLANTIRYFIKTDPEgtiiRSKYDLSNLKEIWV 387
Cdd:COG0318 154 FgltvgLLAPLLAGATLVLLP-----RFDPE-RVLELIERERVTV-LFGVPTMLARLLRHPE----FARYDLSSLRLVVS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 388 GGEVIEESIPEYIEKKLKIKPTRGYGQTEIGIAYLYCFDHINIPYYAT-GLPSIFIRPSIFSDDGKELGVNEIGEIAFKl 466
Cdd:COG0318 223 GGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERRPGSvGRPLPGVEVRIVDEDGRELPPGEVGEIVVR- 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 467 pmPPSFATTLYKNDEKFKQLFSkfPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSI 546
Cdd:COG0318 302 --GPNVMKGYWNDPEATAEAFR--DGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVV 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 547 GINDPTCYSVPIAllvlkqlqqqdqsiqqidlnklqneinYIIKQDIESL----------------AVLRKIVIVNQLPK 610
Cdd:COG0318 378 GVPDEKWGERVVA---------------------------FVVLRPGAELdaeelraflrerlaryKVPRRVEFVDELPR 430
|
....*.
gi 60472587 611 TKTGKI 616
Cdd:COG0318 431 TASGKI 436
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
93-618 |
1.12e-49 |
|
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: 179.24 E-value: 1.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTn 172
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 173 ygifndeiitftPNLKDAIELSTfkpsnvitlfrnditsesdlkkvkdiptipntlswydeikkfkennqspfyeyvpve 252
Cdd:cd05969 80 ------------EELYERTDPED--------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 253 sshPLYIIYSSGTTGNAKAVVRSNgpNLVCMNY------FDRYISEKYECTtllttSSVGWVSfhGFLYGMLS---FGST 323
Cdd:cd05969 91 ---PTLLHYTSGTTGTPKGVLHVH--DAMIFYYftgkyvLDLHPDDIYWCT-----ADPGWVT--GTVYGIWApwlNGVT 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 324 FVMYEGGIIKNKhievdFWNTIEKHKATHTLSLANTIRYFIKtdpEGTIIRSKYDLSNLKEIWVGGEVIEESIPEYIEKK 403
Cdd:cd05969 159 NVVYEGRFDAES-----WYGIIERVKVTVWYTAPTAIRMLMK---EGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEV 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 404 LKIKPTRGYGQTEIG---IAYLYCFDhinIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKlPMPPSFATTLYKND 480
Cdd:cd05969 231 FGVPIHDTWWQTETGsimIANYPCMP---IKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALK-PGWPSMFRGIWNDE 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 481 EKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIAL 560
Cdd:cd05969 307 ERYKNSFID--GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAF 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 60472587 561 LVLKQLQQQDqsiqqidlNKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:cd05969 385 ISLKEGFEPS--------DELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMR 434
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
92-616 |
1.25e-48 |
|
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: 177.40 E-value: 1.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 92 KLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITT 171
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 172 NYGIfndeiitftPNLKDAIELSTFKPsNVITLfrnditsESDLKKVKDIPTIPNTLSWYDEIKKFKENNQSPfyeyvpv 251
Cdd:cd05911 90 PDGL---------EKVKEAAKELGPKD-KIIVL-------DDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGK------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 252 esSHPLYIIYSSGTTGNAKAVVRSNGpNLVCMNYFDRYISEKYEC--TTLLTTSSVGWVSfhGFLYGMLS--FGSTfvmy 327
Cdd:cd05911 146 --DDTAAILYSSGTTGLPKGVCLSHR-NLIANLSQVQTFLYGNDGsnDVILGFLPLYHIY--GLFTTLASllNGAT---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 328 egGIIKNKHIEVDFWNTIEKHKATHTLsLANTIRYFIKTDPegtiIRSKYDLSNLKEIWVGGEVIEESIPEYIEKKLKIK 407
Cdd:cd05911 217 --VIIMPKFDSELFLDLIEKYKITFLY-LVPPIAAALAKSP----LLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 408 P-TRGYGQTEIGIAYLYCFDHINIPYyATG--LPSIFIRpsIFSDDGKE-LGVNEIGEIAFKLPMPpsfatTL--YKNDE 481
Cdd:cd05911 290 TiKQGYGMTETGGILTVNPDGDDKPG-SVGrlLPNVEAK--IVDDDGKDsLGPNEPGEICVRGPQV-----MKgyYNNPE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 482 KFKQLFSKfPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIAll 561
Cdd:cd05911 362 ATKETFDE-DGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRA-- 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60472587 562 vlkqlqqqdqsiqqidlnklqneinYIIKQDIESLAV----------------LRK-IVIVNQLPKTKTGKI 616
Cdd:cd05911 439 -------------------------YVVRKPGEKLTEkevkdyvakkvasykqLRGgVVFVDEIPKSASGKI 485
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
93-618 |
7.04e-43 |
|
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: 160.20 E-value: 7.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITtn 172
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 173 ygifndeiitftpnlkdaielstfkpsnvitlfrnditsesdlkkvkdiptipntlswydeikkfkennqspfyeyvpvE 252
Cdd:cd05972 79 -------------------------------------------------------------------------------D 79
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 253 SSHPLYIIYSSGTTGNAKAVVRSNGPNLVCMNYFdRYISEKYECTTLLTTSSVGWVSFHGF-LYGMLSFGSTFVMYEGGI 331
Cdd:cd05972 80 AEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTA-AYWLGLRPDDIHWNIADPGWAKGAWSsFFGPWLLGATVFVYEGPR 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 332 IKNKHIevdfWNTIEKHKAThTLSLANT-IRYFIKTDPEGtiirskYDLSNLKEIWVGGEVIEESIPEYIEKKLKIKPTR 410
Cdd:cd05972 159 FDAERI----LELLERYGVT-SFCGPPTaYRMLIKQDLSS------YKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRD 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 411 GYGQTEIGiayLYCFDHINIPYY--ATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLPmPPSFATTLYKNDEKFKQLFS 488
Cdd:cd05972 228 GYGQTETG---LTVGNFPDMPVKpgSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLP-PPGLFLGYVGDPEKTEASIR 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 489 KfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIAllvlkqlqQ 568
Cdd:cd05972 304 G--DYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKA--------F 373
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 60472587 569 QDQSIQQIDLNKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:cd05972 374 VVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRR 423
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
12-618 |
7.47e-41 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 156.98 E-value: 7.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 12 NDFNYANSYPEAFWDEVAKknVFwdkmydkvysgdemypDWFKGGELNTCYNVLDIQVQNPLKrDQDALIYECPYLKKTI 91
Cdd:PRK04319 14 NLKDYEETYATFSWEEVEK--EF----------------SWLETGKVNIAYEAIDRHADGGRK-DKVALRYLDASRKEKY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 92 klTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITT 171
Cdd:PRK04319 75 --TYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 172 NygifndeiitftpnlkdaiELSTFKPsnvitlfRNDITSesdLKKV----KDIPTIPNTLSWYDEIkkfkeNNQSPFYE 247
Cdd:PRK04319 153 P-------------------ALLERKP-------ADDLPS---LKHVllvgEDVEEGPGTLDFNALM-----EQASDEFD 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 248 YVPVESSHPLYIIYSSGTTGNAKAVVRSNgpNLVCMNYFD-RYI-----SEKYECTtllttSSVGWVSfhGFLYGM---L 318
Cdd:PRK04319 199 IEWTDREDGAILHYTSGSTGKPKGVLHVH--NAMLQHYQTgKYVldlheDDVYWCT-----ADPGWVT--GTSYGIfapW 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 319 SFGSTFVMYEGgiiknkHIEVDFW-NTIEKHKATHTLSLANTIRYFIKTDPEgtiIRSKYDLSNLKEIWVGGEVIEesiP 397
Cdd:PRK04319 270 LNGATNVIDGG------RFSPERWyRILEDYKVTVWYTAPTAIRMLMGAGDD---LVKKYDLSSLRHILSVGEPLN---P 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 398 EYI---EKKLKIKPTRGYGQTEIG---IAYLYCFDhinIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLPMPPS 471
Cdd:PRK04319 338 EVVrwgMKVFGLPIHDNWWMTETGgimIANYPAMD---IKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSM 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 472 FATTLyKNDEKFKQLFSkfPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDP 551
Cdd:PRK04319 415 MRGIW-NNPEKYESYFA--GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDP 491
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60472587 552 TCYSVPIAllvlkqlqqqdqsiqQIDLN-------KLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:PRK04319 492 VRGEIIKA---------------FVALRpgyepseELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMR 550
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
21-616 |
1.22e-38 |
|
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: 151.27 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 21 PEAFWDEVAK-KNVFWDKMYDKVY-SGDEM-YPDWFKGGELNTCYNVLDIQVQnplkrDQDALIYEcpYLKKTI-KLTYY 96
Cdd:cd05943 30 PGAFWAAVWDfSGVRGSKPYDVVVvSGRIMpGARWFPGARLNYAENLLRHADA-----DDPAAIYA--AEDGERtEVTWA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 97 QLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGIF 176
Cdd:cd05943 103 ELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAYTY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 177 NDEIITFTPNLKdaiELSTFKPSNVITLFRNDITSESDLkkvkDIPTIPNTLSWYDeikkFKENNQSPFYEYVPVESSHP 256
Cdd:cd05943 183 NGKRHDVREKVA---ELVKGLPSLLAVVVVPYTVAAGQP----DLSKIAKALTLED----FLATGAAGELEFEPLPFDHP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 257 LYIIYSSGTTGNAKAVVRSNGPNLVcmnyfdRYISEKYECT------TLLTTSSVGWVSFHgFLYGMLSFGSTFVMYEGG 330
Cdd:cd05943 252 LYILYSSGTTGLPKCIVHGAGGTLL------QHLKEHILHCdlrpgdRLFYYTTCGWMMWN-WLVSGLAVGATIVLYDGS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 331 -IIKNKHIevdFWNTIEKHKATHtlsLANTIRYFIKTDPEGTIIRSKYDLSNLKEIWVGGEVIEESIPEYIEKKLK--IK 407
Cdd:cd05943 325 pFYPDTNA---LWDLADEEGITV---FGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHIKpdVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 408 PTRGYGQTEIgiayLYCF--DHINIPYYATGL--PSIFIRPSIFSDDGKELgVNEIGEIAFKLPMP--PSFattlYKNDE 481
Cdd:cd05943 399 LASISGGTDI----ISCFvgGNPLLPVYRGEIqcRGLGMAVEAFDEEGKPV-WGEKGELVCTKPFPsmPVG----FWNDP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 482 ---KFKQ-LFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGnkVQLNTIE--TSILKHPLVLECCSIGI-NDPTCY 554
Cdd:cd05943 470 dgsRYRAaYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGG--VRIGTAEiyRVVEKIPEVEDSLVVGQeWKDGDE 547
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60472587 555 SVPIallvlkqlqQQDQSIQQIDLNKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKI 616
Cdd:cd05943 548 RVIL---------FVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKK 600
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
91-621 |
1.90e-36 |
|
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: 143.82 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 91 IKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIIT 170
Cdd:cd17642 43 VNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 171 TNYGIfnDEIITFTPNLKdaielstFKPSNVItlfrndITSESDLKKvkdiptipntlswYDEIKKFKENNQSP---FYE 247
Cdd:cd17642 123 SKKGL--QKVLNVQKKLK-------IIKTIII------LDSKEDYKG-------------YQCLYTFITQNLPPgfnEYD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 248 YVPVESSHP---LYIIYSSGTTGNAKAVvrsngpNLVCMNYFDR--------YISEKYECTTLLTTssVGWvsFHGFlyG 316
Cdd:cd17642 175 FKPPSFDRDeqvALIMNSSGSTGLPKGV------QLTHKNIVARfshardpiFGNQIIPDTAILTV--IPF--HHGF--G 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 317 MLSFGSTFVMYEGGIIKNKHIEVDFWNTIEKHKATHTLSLANTIRYFIKTDpegtiIRSKYDLSNLKEIWVGGEVIEESI 396
Cdd:cd17642 243 MFTTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKST-----LVDKYDLSNLHEIASGGAPLSKEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 397 PEYIEKKLKIKPTR-GYGQTEIGIAYLYCFDHINIPYyATGLPSIFIRPSIFS-DDGKELGVNEIGEIAFKLPMppsFAT 474
Cdd:cd17642 318 GEAVAKRFKLPGIRqGYGLTETTSAILITPEGDDKPG-AVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPM---IMK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 475 TLYKNDEKFKQLFSKfPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCY 554
Cdd:cd17642 394 GYVNNPEATKALIDK-DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAG 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 555 SVPIALLVLKQlqqqdqsiqqidlNKLQNE---INYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPII 621
Cdd:cd17642 473 ELPAAVVVLEA-------------GKTMTEkevMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
112-621 |
2.17e-34 |
|
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: 137.63 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 112 LNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNYGIFNDEIitftpnlKDAI 191
Cdd:cd05970 67 MGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEEI-------EKAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 192 ElstfkpsnvitlfrndiTSESDLKKVKDIPTIPNtlSWYDEIKKFKenNQSPFYEYVPVESSH----PLYIIYSSGTTG 267
Cdd:cd05970 140 P-----------------ECPSKPKLVWVGDPVPE--GWIDFRKLIK--NASPDFERPTANSYPcgedILLVYFSSGTTG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 268 NAKAVVRSNGPNLvcmnyfDRYISEKY-----ECTTLLTTSSVGWV-SFHGFLYGMLSFGSTFVMYEGGIIKNKHIevdf 341
Cdd:cd05970 199 MPKMVEHDFTYPL------GHIVTAKYwqnvrEGGLHLTVADTGWGkAVWGKIYGQWIAGAAVFVYDYDKFDPKAL---- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 342 WNTIEKHKAThTLSLANTI-RYFIKTDpegtiiRSKYDLSNLKEIWVGGEVIEESIPEYIEKKLKIKPTRGYGQTE--IG 418
Cdd:cd05970 269 LEKLSKYGVT-TFCAPPTIyRFLIRED------LSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTEttLT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 419 IAYLYCFDhinIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLP--MPPSFATTLYKNDEKFKQLFskFPGYYNP 496
Cdd:cd05970 342 IATFPWME---PKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgKPVGLFGGYYKDAEKTAEVW--HDGYYHT 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 497 GDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIAllvlkqlqqqdqsiqQI 576
Cdd:cd05970 417 GDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKA---------------TI 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 60472587 577 DLNK-------LQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPII 621
Cdd:cd05970 482 VLAKgyepseeLKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
93-618 |
1.44e-33 |
|
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: 133.50 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLfdgysvkslidrietitpkliittN 172
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL------------------------N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 173 YGIFNDEIitftpnlkdaielstfkpsnvitlfrNDITSESDLKKVKDiptipntlswyDeikkfkennqspfyeyvpve 252
Cdd:cd17631 77 FRLTPPEV--------------------------AYILADSGAKVLFD-----------D-------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 253 sshPLYIIYSSGTTGNAKAVVRSNGpNLVcMNYFDRYISEKyecttlLTTSSVGWVS---FHGFLYGMLSFGstfVMYEG 329
Cdd:cd17631 100 ---LALLMYTSGTTGRPKGAMLTHR-NLL-WNAVNALAALD------LGPDDVLLVVaplFHIGGLGVFTLP---TLLRG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 330 G-IIKNKHIEVD-FWNTIEKHKATHtLSLANTIRYFIKTDPEgtiiRSKYDLSNLKEIWVGGE-VIEESIPEYIEKKLKI 406
Cdd:cd17631 166 GtVVILRKFDPEtVLDLIERHRVTS-FFLVPTMIQALLQHPR----FATTDLSSLRAVIYGGApMPERLLRALQARGVKF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 407 kpTRGYGQTEI--GIAYLYCFDHINIPYyATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLP--MPpsfatTLYKNDEK 482
Cdd:cd17631 241 --VQGYGMTETspGVTFLSPEDHRRKLG-SAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPhvMA-----GYWNRPEA 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 483 FKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALLV 562
Cdd:cd17631 313 TAAAFRD--GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVV 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60472587 563 lkqlqqqdqsiqqidlnkLQNEINYIIKQDIESLA-------VLRKIVIVNQLPKTKTGKIPR 618
Cdd:cd17631 391 ------------------PRPGAELDEDELIAHCRerlarykIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
92-616 |
7.26e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 121.06 E-value: 7.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 92 KLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGA-THCV---LFDgysvksliDRIETIT--- 164
Cdd:PRK06187 31 RTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAvLHPInirLKP--------EEIAYILnda 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 165 -PKLIIttnygiFNDEIITFTPNLKDAIELSTFkpsnVItlfrndITSESDLKkvkdiPTIPNTLSwYDEIKkfkeNNQS 243
Cdd:PRK06187 103 eDRVVL------VDSEFVPLLAAILPQLPTVRT----VI------VEGDGPAA-----PLAPEVGE-YEELL----AAAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 244 PFYEYVPVESSHPLYIIYSSGTTGNAKAVVRSN----GPNLVCMNYFDryisekyecttlLTTSSVGWVS---FH----G 312
Cdd:PRK06187 157 DTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHrnlfLHSLAVCAWLK------------LSRDDVYLVIvpmFHvhawG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 313 FLYGMLSFGSTFVMyeggiikNKHIEVD-FWNTIEKHKATHTLsLANTIRYFIKTDPegtiIRSKYDLSNLKEIWVGGEV 391
Cdd:PRK06187 225 LPYLALMAGAKQVI-------PRRFDPEnLLDLIETERVTFFF-AVPTIWQMLLKAP----RAYFVDFSSLRLVIYGGAA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 392 IEESIPEYIEKKLKIKPTRGYGQTEIG--IAYLYCFDHI--NIPY-YATGLPSIFIRPSIFSDDGKELGVN--EIGEIAF 464
Cdd:PRK06187 293 LPPALLREFKEKFGIDLVQGYGMTETSpvVSVLPPEDQLpgQWTKrRSAGRPLPGVEARIVDDDGDELPPDggEVGEIIV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 465 KlpmPPSFATTLYKNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECC 544
Cdd:PRK06187 373 R---GPWLMQGYWNRPEATAETIDG--GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVA 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60472587 545 SIGINDPTCYSVPIAllvlkqlqqqdqsiqqidLNKLQNEINYIIKQDIESLA-------VLRKIVIVNQLPKTKTGKI 616
Cdd:PRK06187 448 VIGVPDEKWGERPVA------------------VVVLKPGATLDAKELRAFLRgrlakfkLPKRIAFVDELPRTSVGKI 508
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
252-618 |
2.61e-27 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 115.22 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 252 ESSHPLYIIYSSGTTGNAKAVVRS------NGPNL-VCMNYFDRYISEKYecttllTTSSVGWV-SFHGFLYGMLSFGST 323
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAhrvllgHLPGVqFPFNLFPRDGDLYW------TPADWAWIgGLLDVLLPSLYFGVP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 324 FVMYeggiiKNKHIEVD-FWNTIEKHKATHTLSLANTIRYFIKTDPEgtiiRSKYDLsNLKEIWVGGEVIEESIPEYIEK 402
Cdd:cd05971 160 VLAH-----RMTKFDPKaALDLMSRYGVTTAFLPPTALKMMRQQGEQ----LKHAQV-KLRAIATGGESLGEELLGWARE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 403 KLKIKPTRGYGQTEIGIAYLYCFDHINIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLPMPPSFaTTLYKNDEK 482
Cdd:cd05971 230 QFGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAF-LGYWNNPSA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 483 FKQlfsKFPG-YYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALL 561
Cdd:cd05971 309 TEK---KMAGdWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFV 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 60472587 562 VLKQLQQQDqsiqqidlNKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:cd05971 386 VLNPGETPS--------DALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRR 434
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-551 |
4.42e-26 |
|
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: 111.23 E-value: 4.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 256 PLYIIYSSGTTGNAKAVVrsngpnlvCMNYFDRYISEKYECTTLLTTSSVGWVS---FHG-----FLYGMLSFGSTFVMY 327
Cdd:cd05934 83 PASILYTSGTTGPPKGVV--------ITHANLTFAGYYSARRFGLGEDDVYLTVlplFHInaqavSVLAALSVGATLVLL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 328 EggiiknKHIEVDFWNTIEKHKATHTLSLANTIRYFIKTDPegtiirSKYDLSNLKEIWVGGEVIEESIPEyIEKKLKIK 407
Cdd:cd05934 155 P------RFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPP------SPDDRAHRLRAAYGAPNPPELHEE-FEERFGVR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 408 PTRGYGQTEIGIAYLYCFDHINIPYYAtGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLPMPPSFATTLYKNDEKFKQLF 487
Cdd:cd05934 222 LLEGYGMTETIVGVIGPRDEPRRPGSI-GRPAPGYEVRIVDDDGQELPAGEPGELVIRGLRGWGFFKGYYNMPEATAEAM 300
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60472587 488 SKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDP 551
Cdd:cd05934 301 RN--GWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDE 362
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
21-515 |
2.87e-24 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 107.96 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 21 PEAFWDEVakknvfWD-------KMYDKVYSGDEMyPD--WFKGGELNTCYNVLDIQvqnplKRDQDALIYECPyLKKTI 91
Cdd:PRK03584 47 LEAFWQSV------WDffgvigsTPYTVVLAGRRM-PGarWFPGARLNYAENLLRHR-----RDDRPAIIFRGE-DGPRR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 92 KLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITT 171
Cdd:PRK03584 114 ELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 172 N-YGiFNDEIITFTPNLKDAIE-LSTFKPSNVItlfrnditseSDLKKVKDIPTIPNTLSWYDEIKKFKEnnqSPFyEYV 249
Cdd:PRK03584 194 DgYR-YGGKAFDRRAKVAELRAaLPSLEHVVVV----------PYLGPAAAAAALPGALLWEDFLAPAEA---AEL-EFE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 250 PVESSHPLYIIYSSGTTGNAKAVVRSNG-----------------PNlvcmnyfDRYIsekYECTTllttssvGWVSFHg 312
Cdd:PRK03584 259 PVPFDHPLWILYSSGTTGLPKCIVHGHGgillehlkelglhcdlgPG-------DRFF---WYTTC-------GWMMWN- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 313 FLYGMLSFGSTFVMYEGGIIKNKHIevDFWNTIEKHKATHtlsLANTIRYFIKTDPEGTIIRSKYDLSNLKEIWVGGEVI 392
Cdd:PRK03584 321 WLVSGLLVGATLVLYDGSPFYPDPN--VLWDLAAEEGVTV---FGTSAKYLDACEKAGLVPGETHDLSALRTIGSTGSPL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 393 eesIPEyiekklkikptrgygqteigiAYLYCFDHI--NIPY------------YATGLPSIFIRP------------SI 446
Cdd:PRK03584 396 ---PPE---------------------GFDWVYEHVkaDVWLasisggtdicscFVGGNPLLPVYRgeiqcrglgmavEA 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60472587 447 FSDDGKELgVNEIGEIAFKLPMP--PSFattlYKNDEKFKQL----FSKFPGYYNPGDLGFKDENGFYTIVSRSD 515
Cdd:PRK03584 452 WDEDGRPV-VGEVGELVCTKPFPsmPLG----FWNDPDGSRYrdayFDTFPGVWRHGDWIEITEHGGVVIYGRSD 521
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
93-618 |
4.72e-24 |
|
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: 106.30 E-value: 4.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHC-------------VLFDGYSvkslidR 159
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVpvntlltpddyayYLEDSRA------R 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 160 IETITPKLiittnYGIFNDEIITFTPNLKDAIELSTFKPSNVITLFRNDITSESdlkkvkdiPTIPNTLSWYDEikkfke 239
Cdd:cd05959 104 VVVVSGEL-----APVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAEA--------EQLKPAATHADD------ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 240 nnqspfyeyvpvesshPLYIIYSSGTTGNAKAVV-RSNGPNLVCMNYFDR--YISEKYECttlLTTSSVgwvsFhgFLYG 316
Cdd:cd05959 165 ----------------PAFWLYSSGSTGRPKGVVhLHADIYWTAELYARNvlGIREDDVC---FSAAKL----F--FAYG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 317 M-------LSFGSTFVMYEGGIIKNKhievdFWNTIEKHKATHTLSLAnTIRYFIKTDPEGTiirsKYDLSNLKEIWVGG 389
Cdd:cd05959 220 LgnsltfpLSVGATTVLMPERPTPAA-----VFKRIRRYRPTVFFGVP-TLYAAMLAAPNLP----SRDLSSLRLCVSAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 390 EVIEESIPEYIEKKLKIKPTRGYGQTEIGIAYLYCFDHiNIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKlpmP 469
Cdd:cd05959 290 EALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPG-RVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVR---G 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 470 PSFATTLYKNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIN 549
Cdd:cd05959 366 PSSATMYWNNRDKTRDTFQG--EWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVE 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60472587 550 DPTCYSVPIALLVLKQLQQQDQsiqqidlnKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:cd05959 444 DEDGLTKPKAFVVLRPGYEDSE--------ALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQR 504
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
249-619 |
5.23e-23 |
|
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: 102.52 E-value: 5.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 249 VPVESSHPLYIIYSSGTTGNAKAVVRSNgPNLVcmnYFDRYISEKYECTT---LLTTSSVGWVsfHGF--LYGMLSFGST 323
Cdd:cd05922 112 HEVSHEDLALLLYTSGSTGSPKLVRLSH-QNLL---ANARSIAEYLGITAddrALTVLPLSYD--YGLsvLNTHLLRGAT 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 324 FVMYEGGIIknkhiEVDFWNTIEKHKAThtlSLANTIRYFIKTDpegTIIRSKYDLSNLKEIW-VGGEVIEESIPEYIEK 402
Cdd:cd05922 186 LVLTNDGVL-----DDAFWEDLREHGAT---GLAGVPSTYAMLT---RLGFDPAKLPSLRYLTqAGGRLPQETIARLREL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 403 KLKIKPTRGYGQTEI--GIAYLYCFDHINIPYyATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLPmppsFATTLYKND 480
Cdd:cd05922 255 LPGAQVYVMYGQTEAtrRMTYLPPERILEKPG-SIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGP----NVMKGYWND 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 481 EKFKQLFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIAl 560
Cdd:cd05922 330 PPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALF- 408
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60472587 561 lvlkqlqqqdqsiqqiDLNKLQNEINYIIKQDIESL---AVLRKIVIVNQLPKTKTGKIPRP 619
Cdd:cd05922 409 ----------------VTAPDKIDPKDVLRSLAERLppyKVPATVRVVDELPLTASGKVDYA 454
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
93-616 |
1.10e-22 |
|
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: 101.40 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGAThcvlfdgysvkslidrietitpkliittn 172
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAV----------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 173 ygifndeIITFTPNLKDAiELSTF-KPSNVITLFrndITSESDlkkvkDIPTIPntlswydeikkfkennqspfyeyvpv 251
Cdd:cd05935 53 -------VVPINPMLKER-ELEYIlNDSGAKVAV---VGSELD-----DLALIP-------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 252 esshplyiiYSSGTTGNAKAVVRSNG---PNLVCMnyfdryisekyECTTLLTTSSVGWVS---FH--GFLYGMLS---F 320
Cdd:cd05935 91 ---------YTSGTTGLPKGCMHTHFsaaANALQS-----------AVWTGLTPSDVILAClplFHvtGFVGSLNTavyV 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 321 GSTFVMYEggiIKNKHIEVDfwnTIEKHKATHTLSLANTIryfikTDPEGTIIRSKYDLSNLKEIWVGGEVIEESIPEYI 400
Cdd:cd05935 151 GGTYVLMA---RWDRETALE---LIEKYKVTFWTNIPTML-----VDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKL 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 401 EKKLKIKPTRGYGQTEIgIAYLYCFDHINIPYYATGLPSIFIRPSIFS-DDGKELGVNEIGEIAFKlpmPPSFATTLYKN 479
Cdd:cd05935 220 LKLTGLRFVEGYGLTET-MSQTHTNPPLRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVR---GPQIFKGYWNR 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 480 DEKFKQLFSKFPG--YYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVP 557
Cdd:cd05935 296 PEETEESFIEIKGrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEV 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 60472587 558 IALLVLKQLQQQDQSiqqidlnklQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKI 616
Cdd:cd05935 376 KAFIVLRPEYRGKVT---------EEDIIEWAREQMAAYKYPREVEFVDELPRSASGKI 425
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
93-628 |
4.58e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 99.93 E-value: 4.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 93 LTYYQLYEKVCEFSRVLLN-LNISKNDNVLIYMANTLEPLIAMLSCARIGathCVLfdgysvkslidrietiTPkliitt 171
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLIYeLNVKKGERIAILSQNSLEYIVLLFAIAKVE---CIA----------------VP------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 172 nygiFNdeiITFTPNlkdaiELS-TFKPSNVITLFRN---DITSESDLKKVKDIPTIpntlswydEIKKFKENNQSPFYE 247
Cdd:PRK06839 83 ----LN---IRLTEN-----ELIfQLKDSGTTVLFVEktfQNMALSMQKVSYVQRVI--------SITSLKEIEDRKIDN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 248 YVPVESSHPLYIIYSSGTTGNAKAVVRS------NGPNlvcmNYFDRYISEKYECTTLLTTSSVGWVsfhgflyGMLSFG 321
Cdd:PRK06839 143 FVEKNESASFIICYTSGTTGKPKGAVLTqenmfwNALN----NTFAIDLTMHDRSIVLLPLFHIGGI-------GLFAFP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 322 STFVmyeGG--IIKNKHIEVDFWNTIEKHKATHTLSLAnTIRYFIKTDPEgtiiRSKYDLSNLKEIWVGGE-VIEESIPE 398
Cdd:PRK06839 212 TLFA---GGviIVPRKFEPTKALSMIEKHKVTVVMGVP-TIHQALINCSK----FETTNLQSVRWFYNGGApCPEELMRE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 399 YIEKKLKIKptRGYGQTEIG-IAYLYCFDHINIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKlpmPPSFATTLY 477
Cdd:PRK06839 284 FIDRGFLFG--QGFGMTETSpTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIR---GPNVMKEYW 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 478 KNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVP 557
Cdd:PRK06839 359 NRPDATEETIQD--GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIP 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60472587 558 IALLVLKQLQQQdqsiqqidlnkLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPIISKFLNDS 628
Cdd:PRK06839 437 IAFIVKKSSSVL-----------IEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKSR 496
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
258-618 |
8.38e-22 |
|
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: 98.69 E-value: 8.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 258 YIIYSSGTTGNAKAVVRSNGPNLVCMNYFDRYISEKYECTTLLTTSSV--GWVSFHGfLYGMLSFGSTFVMYEGGIIKNK 335
Cdd:cd05919 95 YLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS-LWFPLAVGASAVLNPGWPTAER 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 336 HIEvdfwnTIEKHKAThtlSLANTIRYFIKTDPEGTIirSKYDLSNLKEIWVGGEVIEESIPEYIEKKLKIKPTRGYGQT 415
Cdd:cd05919 174 VLA-----TLARFRPT---VLYGVPTFYANLLDSCAG--SPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGAT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 416 EIGIAYLyCFDHINIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLPmppSFATTLYKNDEKFKQLFSKfpGYYN 495
Cdd:cd05919 244 EVGHIFL-SNRPGAWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGP---SAAVGYWNNPEKSRATFNG--GWYR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 496 PGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALLVLKQLQQQDQsiqq 575
Cdd:cd05919 318 TGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQE---- 393
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 60472587 576 idlnKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:cd05919 394 ----SLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
93-623 |
3.18e-21 |
|
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: 96.82 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITtn 172
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 173 ygifndeiitftpnlkDAIElstfkpsnvitlfRNDITSEsdlkkvkdiptipntlswydeikkfkennqspfyeyvpve 252
Cdd:cd05973 79 ----------------DAAN-------------RHKLDSD---------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 253 sshPLYIIYSSGTTGNAKAVVRSngpnLVCMNYFDRYISEKYEcttlLTTSSVGW-VSFHGFLYGM-------LSFGSTF 324
Cdd:cd05973 90 ---PFVMMFTSGTTGLPKGVPVP----LRALAAFGAYLRDAVD----LRPEDSFWnAADPGWAYGLyyaitgpLALGHPT 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 325 VMYEGGIiknkhiEVDF-WNTIEKHKAThTLSLANTIRYFIKTDPEGTIIRSKydlSNLKEIWVGGEVIEESIPEYIEKK 403
Cdd:cd05973 159 ILLEGGF------SVEStWRVIERLGVT-NLAGSPTAYRLLMAAGAEVPARPK---GRLRRVSSAGEPLTPEVIRWFDAA 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 404 LKIKPTRGYGQTEIGIaYLYCFDHINIPYYA--TGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLPMPPSFATTLYKNDE 481
Cdd:cd05973 229 LGVPIHDHYGQTELGM-VLANHHALEHPVHAgsAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPLMWFRGYQLPD 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 482 KfkqlfSKFPG-YYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIAL 560
Cdd:cd05973 308 T-----PAIDGgYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAF 382
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60472587 561 LVLKQLQQQDQsiqqidlnKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPIISK 623
Cdd:cd05973 383 VVLRGGHEGTP--------ALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
90-623 |
3.40e-21 |
|
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: 97.38 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 90 TIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLII 169
Cdd:cd05926 12 TPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 170 TTNYGifndeiitFTPNLKDAIELstfkpsnviTLFRNDITSEsdlKKVKDIPTIPNTLSwydeikkFKENNQSPFYEYV 249
Cdd:cd05926 92 TPKGE--------LGPASRAASKL---------GLAILELALD---VGVLIRAPSAESLS-------NLLADKKNAKSEG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 250 PVESSHPLYIIYSSGTTGNAKAVVRSNGPNLVCMnyfdRYISEKYECT----TLLTTSSvgwvsFH--GFLYGMLSfgst 323
Cdd:cd05926 145 VPLPDDLALILHTSGTTGRPKGVPLTHRNLAASA----TNITNTYKLTpddrTLVVMPL-----FHvhGLVASLLS---- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 324 fVMYEGG--IIKNKHIEVDFWNTIEKHKAT--------HTLSLANTIRYFIKTDPEGTIIRS-KYDLSnlkeiwvggEVI 392
Cdd:cd05926 212 -TLAAGGsvVLPPRFSASTFWPDVRDYNATwytavptiHQILLNRPEPNPESPPPKLRFIRScSASLP---------PAV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 393 EESIpeyiEKKLKIKPTRGYGQTEIGiaylycfdHiniPYYATGLPSIFIRP-----------SIFSDDGKELGVNEIGE 461
Cdd:cd05926 282 LEAL----EATFGAPVLEAYGMTEAA--------H---QMTSNPLPPGPRKPgsvgkpvgvevRILDEDGEILPPGVVGE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 462 IAFKLPMppsfATTLYKNDEKF-KQLFSKFpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLV 540
Cdd:cd05926 347 ICLRGPN----VTRGYLNNPEAnAEAAFKD-GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAV 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 541 LECCSIGINDPT------CYSVPIALLVlkqlqqqdqsiqqidlnKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTG 614
Cdd:cd05926 422 LEAVAFGVPDEKygeevaAAVVLREGAS-----------------VTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATG 484
|
....*....
gi 60472587 615 KIPRPIISK 623
Cdd:cd05926 485 KIQRRKVAE 493
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
92-618 |
3.68e-21 |
|
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: 96.86 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 92 KLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGAThcvlfdgysvkslidrietitpklIITT 171
Cdd:cd05936 24 KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV------------------------VVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 172 NygifndeiitftPNLKdAIEL-STFKPSNVITLFRnDITSESDLKKvkdiptipntlswydeikkfkennQSPFYEYVP 250
Cdd:cd05936 80 N------------PLYT-PRELeHILNDSGAKALIV-AVSFTDLLAA------------------------GAPLGERVA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 251 VESSHPLYIIYSSGTTGNAKAVVRSNGpNLVC-MNYFDRYISEKYE-CTTLLTTSSVgwvsFH--GFLYGMLSF---GST 323
Cdd:cd05936 122 LTPEDVAVLQYTSGTTGVPKGAMLTHR-NLVAnALQIKAWLEDLLEgDDVVLAALPL----FHvfGLTVALLLPlalGAT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 324 FVMYEGGIIKNkhievdFWNTIEKHKATHtLSLANTIRYFIKTDPEgtiiRSKYDLSNLKEIWVGGEVIEESIPEYIEKK 403
Cdd:cd05936 197 IVLIPRFRPIG------VLKEIRKHRVTI-FPGVPTMYIALLNAPE----FKKRDFSSLRLCISGGAPLPVEVAERFEEL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 404 LKIKPTRGYGQTEIgiAYLYCFDHINIPYYA----TGLPSIFIRpsIFSDDGKELGVNEIGEIAFKLPmppsfattlykn 479
Cdd:cd05936 266 TGVPIVEGYGLTET--SPVVAVNPLDGPRKPgsigIPLPGTEVK--IVDDDGEELPPGEVGELWVRGP------------ 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 480 dekfkqlfSKFPGYYN-P--------------GDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECC 544
Cdd:cd05936 330 --------QVMKGYWNrPeetaeafvdgwlrtGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAA 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 545 SIGINDPTCYSVPIAllvlkqlqqqdqsiqqidlnklqneinYIIKQDIESLA----------------VLRKIVIVNQL 608
Cdd:cd05936 402 VVGVPDPYSGEAVKA---------------------------FVVLKEGASLTeeeiiafcreqlagykVPRQVEFRDEL 454
|
570
....*....|
gi 60472587 609 PKTKTGKIPR 618
Cdd:cd05936 455 PKSAVGKILR 464
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
94-616 |
6.66e-21 |
|
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: 96.55 E-value: 6.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 94 TYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGAthcVLfdgysvkslidriETITPKL-----I 168
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGA---VL-------------HTINPRLfpeqiA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 169 ITTNYGifNDEIITFTPNLKDAIElsTFKPSnvITLFRNDITSESDLKKvkDIPTIPNTLSWYDEIkkfkeNNQSPFYEY 248
Cdd:cd12119 91 YIINHA--EDRVVFVDRDFLPLLE--AIAPR--LPTVEHVVVMTDDAAM--PEPAGVGVLAYEELL-----AAESPEYDW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 249 VPVESSHPLYIIYSSGTTGNAKAVV---RSNgpNLVCMnyfdryisekyectTLLTTSSVGwVS-----------FH--- 311
Cdd:cd12119 158 PDFDENTAAAICYTSGTTGNPKGVVyshRSL--VLHAM--------------AALLTDGLG-LSesdvvlpvvpmFHvna 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 312 -GFLYGMLSFGSTFVMyEGGIIKNKHIevdfWNTIEKHKATHTLSlANTIRYFIKTDPEGTiirsKYDLSNLKEIWVGGE 390
Cdd:cd12119 221 wGLPYAAAMVGAKLVL-PGPYLDPASL----AELIEREGVTFAAG-VPTVWQGLLDHLEAN----GRDLSSLRRVVIGGS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 391 VIEESIPEYIEKKLkIKPTRGYGQTE---IGIAYLYCFDHINIPYYA-------TGLPSIFIRPSIFSDDGKEL---GvN 457
Cdd:cd12119 291 AVPRSLIEAFEERG-VRVIHAWGMTEtspLGTVARPPSEHSNLSEDEqlalrakQGRPVPGVELRIVDDDGRELpwdG-K 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 458 EIGEIAFKlpmPPSFATTLYKNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISG---NKVQLntiETSI 534
Cdd:cd12119 369 AVGELQVR---GPWVTKSYYKNDEESEALTED--GWLRTGDVATIDEDGYLTITDRSKDVIKSGGewiSSVEL---ENAI 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 535 LKHPLVLECCSIGINDPTCYSVPIALLVLKQLQQQDqsiqqidlnklQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTG 614
Cdd:cd12119 441 MAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVT-----------AEELLEFLADKVAKWWLPDDVVFVDEIPKTSTG 509
|
..
gi 60472587 615 KI 616
Cdd:cd12119 510 KI 511
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
91-550 |
3.81e-20 |
|
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: 93.94 E-value: 3.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 91 IKLTYYQLYEKVCEFSRVLLNLNISkNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIIT 170
Cdd:cd05909 6 TSLTYRKLLTGAIALARKLAKMTKE-GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 171 TnygifndeiitftpnlKDAIELSTFKPSNVItLFRNDITSESDLKkvkdiptipNTLSWYDEIKKFKENNQSPFYEY-- 248
Cdd:cd05909 85 S----------------KQFIEKLKLHHLFDV-EYDARIVYLEDLR---------AKISKADKCKAFLAGKFPPKWLLri 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 249 ---VPVESSHPLYIIYSSGTTGNAKAVVRSNgPNLVCMNYfdrYISEKYECTTllttssvGWVSFhGFLYGMLSFGSTfv 325
Cdd:cd05909 139 fgvAPVQPDDPAVILFTSGSEGLPKGVVLSH-KNLLANVE---QITAIFDPNP-------EDVVF-GALPFFHSFGLT-- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 326 myeGGIIK--NKHIEVDFW----------NTIEKHKATHTLSLANTIRYFIKTdpegtiiRSKYDLSNLKEIWVGGEVIE 393
Cdd:cd05909 205 ---GCLWLplLSGIKVVFHpnpldykkipELIYDKKATILLGTPTFLRGYARA-------AHPEDFSSLRLVVAGAEKLK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 394 ESIPEYIEKKLKIKPTRGYGQTEIG--IAylycfdhINIPYYA-----TGLPSIFIRPSIFSDDGK-ELGVNEIGEIAFK 465
Cdd:cd05909 275 DTLRQEFQEKFGIRILEGYGTTECSpvIS-------VNTPQSPnkegtVGRPLPGMEVKIVSVETHeEVPIGEGGLLLVR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 466 lpmPPSFATTLYKNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKH-PLVLECC 544
Cdd:cd05909 348 ---GPNVMLGYLNEPELTSFAFGD--GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVA 422
|
....*.
gi 60472587 545 SIGIND 550
Cdd:cd05909 423 VVSVPD 428
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
237-618 |
3.92e-20 |
|
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: 94.45 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 237 FKENNQSPFYEYVPVESSH--PLYIIYSSGTTGNAKAVVRSNGPNLVCMNYFDRYISEKYECTTLLTTSSVGWVS----- 309
Cdd:cd05928 155 FKELLNEASTEHHCVETGSqePMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKsawss 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 310 -FHGFLYGMLSFGSTFVMYEGGIIknkhievdfWNTIEKHKATHTLSLANTIRYFIKTDpegtiiRSKYDLSNLKEIWVG 388
Cdd:cd05928 235 lFEPWIQGACVFVHHLPRFDPLVI---------LKTLSSYPITTFCGAPTVYRMLVQQD------LSSYKFPSLQHCVTG 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 389 GEVIEESIPEYIEKKLKIKPTRGYGQTEIGiayLYC--FDHINIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKL 466
Cdd:cd05928 300 GEPLNPEVLEKWKAQTGLDIYEGYGQTETG---LICanFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 467 -PMPP-SFATTLYKNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECC 544
Cdd:cd05928 377 kPIRPfGLFSGYVDNPEKTAATIRG--DFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESA 454
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60472587 545 SIGINDPTCYSVPIALLVLKQLQQQDQSiqqidlNKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:cd05928 455 VVSSPDPIRGEVVKAFVVLAPQFLSHDP------EQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQR 522
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
76-616 |
1.05e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 93.07 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 76 DQDALIYEcpylkkTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHC---VLFDGYS 152
Cdd:PRK08316 26 DKTALVFG------DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVpvnFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 153 VKSLIDRIETItpkliittnyGIFNDEiiTFTPNLKDAIELSTFKPSNVITLFRNDITSESDLkkvkdiptipNTLSWYD 232
Cdd:PRK08316 100 LAYILDHSGAR----------AFLVDP--ALAPTAEAALALLPVDTLILSLVLGGREAPGGWL----------DFADWAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 233 eikkfkenNQSPFYEYVPVESSHPLYIIYSSGTTGNAKAVVRSNGpNLV-----CMnyFDRYISEK---------YECTT 298
Cdd:PRK08316 158 --------AGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHR-ALIaeyvsCI--VAGDMSADdiplhalplYHCAQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 299 LlttssvgwvsfHGFLYGMLSFGSTFVmyeggIIKNKHIEVDFwNTIEKHKAThTLSLANTIryFIktdpegTIIRS--- 375
Cdd:PRK08316 227 L-----------DVFLGPYLYVGATNV-----ILDAPDPELIL-RTIEAERIT-SFFAPPTV--WI------SLLRHpdf 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 376 -KYDLSNLKEIWVG-----GEVIEEsipeyIEKKL-KIKPTRGYGQTEIG-IA-YLYCFDHINIPYYAtGLPSIFIRPSI 446
Cdd:PRK08316 281 dTRDLSSLRKGYYGasimpVEVLKE-----LRERLpGLRFYNCYGQTEIApLAtVLGPEEHLRRPGSA-GRPVLNVETRV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 447 FSDDGKELGVNEIGEIAFKLPMppsfATTLY-KNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKV 525
Cdd:PRK08316 355 VDDDGNDVAPGEVGEIVHRSPQ----LMLGYwDDPEKTAEAFRG--GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENV 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 526 QLNTIETSILKHPLVLECCSIGINDP------TCYSVPiallvlkqlqqqdqsiqqidlnKLQNEIN--YIIKQDIESLA 597
Cdd:PRK08316 429 ASREVEEALYTHPAVAEVAVIGLPDPkwieavTAVVVP----------------------KAGATVTedELIAHCRARLA 486
|
570 580
....*....|....*....|..
gi 60472587 598 ---VLRKIVIVNQLPKTKTGKI 616
Cdd:PRK08316 487 gfkVPKRVIFVDELPRNPSGKI 508
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
76-618 |
1.17e-19 |
|
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: 92.21 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 76 DQDALIYEcpylkkTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGAThCVLFDgysVKS 155
Cdd:cd05930 2 DAVAVVDG------DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAA-YVPLD---PSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 156 LIDRIETItpkliittnygifndeiitftpnLKDAielstfKPSNVITlfrnditsesdlkkvkdiptipntlswydeik 235
Cdd:cd05930 72 PAERLAYI-----------------------LEDS------GAKLVLT-------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 236 kfkennqspfyeyvpvESSHPLYIIYSSGTTGNAKAVVRSNGpNLVcmNYFdRYISEKY---ECTTLLTTSSVGWVSFHG 312
Cdd:cd05930 91 ----------------DPDDLAYVIYTSGSTGKPKGVMVEHR-GLV--NLL-LWMQEAYpltPGDRVLQFTSFSFDVSVW 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 313 FLYGMLSFGSTFVMYEGGIIKNkhiEVDFWNTIEKHKATH---TLSLANTIryfiktDPEGtiirSKYDLSNLKEIWVGG 389
Cdd:cd05930 151 EIFGALLAGATLVVLPEEVRKD---PEALADLLAEEGITVlhlTPSLLRLL------LQEL----ELAALPSLRLVLVGG 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 390 EVIEesiPEYIEKKLKIKPTR----GYGQTEIGIAYLYCfdHINIPYYATGLPSIFiRP------SIFSDDGKELGVNEI 459
Cdd:cd05930 218 EALP---PDLVRRWRELLPGArlvnLYGPTEATVDATYY--RVPPDDEEDGRVPIG-RPipntrvYVLDENLRPVPPGVP 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 460 GEIA----------FKLPmppsfATTlyknDEKFKQLFSkFPG--YYNPGDLGFKDENGfyTIV--SRSDDQIKISGNKV 525
Cdd:cd05930 292 GELYiggaglargyLNRP-----ELT----AERFVPNPF-GPGerMYRTGDLVRWLPDG--NLEflGRIDDQVKIRGYRI 359
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 526 QLNTIETSILKHPLVLECCSIGINDPT------CYSVPIALLvlkqlqqqdqsiqqidlnklQNEINYIIKQDIESL--- 596
Cdd:cd05930 360 ELGEIEAALLAHPGVREAAVVAREDGDgekrlvAYVVPDEGG--------------------ELDEEELRAHLAERLpdy 419
|
570 580
....*....|....*....|..
gi 60472587 597 AVLRKIVIVNQLPKTKTGKIPR 618
Cdd:cd05930 420 MVPSAFVVLDALPLTPNGKVDR 441
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
255-618 |
2.37e-19 |
|
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: 89.39 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 255 HPLYIIYSSGTTGNAKAVVRSNGPNLVCMNYFDRYISEKYECTTLLTtssvGWVSFHGFLYGMLSfgstfVMYEGG--II 332
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAP----GPLSHSLFLYGAIS-----ALYLGGtfIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 333 KNKHIEVDFWNTIEKHKATHTLSLANTIRYFIKTD-PEGTIirskydlsnlKEIWVGGEVIEESIPEYIEKKL-KIKPTR 410
Cdd:cd17633 72 QRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLePESKI----------KSIFSSGQKLFESTKKKLKNIFpKANLIE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 411 GYGQTEIG-IAYLycFDHINIPYYATGLPSIFIRPSIFSDDGkelgvNEIGEIAFKLPMppSFATTLYKNdekfkqlFSK 489
Cdd:cd17633 142 FYGTSELSfITYN--FNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEM--VFSGYVRGG-------FSN 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 490 FPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALLVLkqlqqq 569
Cdd:cd17633 206 PDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSG------ 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 60472587 570 dqsiqqidlnklqNEINY-----IIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:cd17633 280 -------------DKLTYkqlkrFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
92-619 |
2.87e-19 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 92.00 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 92 KLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTlePLIAMLSCArIGATHCVL------FDGYSVKSLIDRIEtitP 165
Cdd:PLN03102 39 RFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNT--PAMYEMHFA-VPMAGAVLnpintrLDATSIAAILRHAK---P 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 166 KLIittnygiFNDEiiTFTPNLKDAIELSTFKPSN----VITLFRNDITSESDLKKVKdiptipntlswYDEIKKFKENN 241
Cdd:PLN03102 113 KIL-------FVDR--SFEPLAREVLHLLSSEDSNlnlpVIFIHEIDFPKRPSSEELD-----------YECLIQRGEPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 242 QSPFYEYVPVESSH-PLYIIYSSGTTGNAKAVVRSNGPNLVC---------MNYFDRYIsekyecTTLLTTSSVGWVsfh 311
Cdd:PLN03102 173 PSLVARMFRIQDEHdPISLNYTSGTTADPKGVVISHRGAYLStlsaiigweMGTCPVYL------WTLPMFHCNGWT--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 312 gFLYGMLSFGSTFVMYeggiiknKHIEV-DFWNTIEKHKATHTLSLANTIRYFIKTDpegtiirsKYDLSNLK---EIWV 387
Cdd:PLN03102 244 -FTWGTAARGGTSVCM-------RHVTApEIYKNIEMHNVTHMCCVPTVFNILLKGN--------SLDLSPRSgpvHVLT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 388 GGEvieeSIPEYIEKK---LKIKPTRGYGQTEIGIAYLYC--FDHIN-IPYYAT------------GLPSIFIRPSIFSD 449
Cdd:PLN03102 308 GGS----PPPAALVKKvqrLGFQVMHAYGLTEATGPVLFCewQDEWNrLPENQQmelkarqgvsilGLADVDVKNKETQE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 450 ----DGKELGvneigEIAFKlpmPPSFATTLYKNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKV 525
Cdd:PLN03102 384 svprDGKTMG-----EIVIK---GSSIMKGYLKNPKATSEAFKH--GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 526 QLNTIETSILKHPLVLECCSIGINDPTCYSVPIALLVLKQLQQQDQSIQQIDLNKLQNEINYiIKQDIESLAVLRKIVIV 605
Cdd:PLN03102 454 SSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLVTRERDLIEY-CRENLPHFMCPRKVVFL 532
|
570
....*....|....
gi 60472587 606 NQLPKTKTGKIPRP 619
Cdd:PLN03102 533 QELPKNGNGKILKP 546
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
93-618 |
5.07e-19 |
|
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: 90.76 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTN 172
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 173 ygifndeiiTFTPNLKDAIelstfkpSNVITLFRNDITS--ESDLKKVKDIPTIPNtlswydeikkfkennqspfyeyVP 250
Cdd:cd05904 113 ---------ELAEKLASLA-------LPVVLLDSAEFDSlsFSDLLFEADEAEPPV----------------------VV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 251 VESSHPLYIIYSSGTTGNAKAVVRSNGpNL---VCMNYFDRYISEKYECTTLLTTSsvgwvSFH-----GFLYGMLSFGS 322
Cdd:cd05904 155 IKQDDVAALLYSSGTTGRSKGVMLTHR-NLiamVAQFVAGEGSNSDSEDVFLCVLP-----MFHiyglsSFALGLLRLGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 323 TFV---MYEGGiiknkhievDFWNTIEKHKATHtLSLANTIRYFIKTDPEGtiirSKYDLSNLKEIWVGG-----EVIEe 394
Cdd:cd05904 229 TVVvmpRFDLE---------ELLAAIERYKVTH-LPVVPPIVLALVKSPIV----DKYDLSSLRQIMSGAaplgkELIE- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 395 sipEYIEKKLKIKPTRGYGQTEIG--IAYLYCFDHINIPYYATG--LPSI---FIRPsifsDDGKELGVNEIGEIAFKLP 467
Cdd:cd05904 294 ---AFRAKFPNVDLGQGYGMTESTgvVAMCFAPEKDRAKYGSVGrlVPNVeakIVDP----ETGESLPPNQTGELWIRGP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 468 --MppsfatTLYKNDEKFKQLFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCS 545
Cdd:cd05904 367 siM------KGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAV 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60472587 546 IGINDPTCYSVPIALLVLKQLQQQDqsiqqidlnklQNEI-NYIIKQdieslaV-----LRKIVIVNQLPKTKTGKIPR 618
Cdd:cd05904 441 IPYPDEEAGEVPMAFVVRKPGSSLT-----------EDEImDFVAKQ------VapykkVRKVAFVDAIPKSPSGKILR 502
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
93-628 |
8.84e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 89.84 E-value: 8.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 93 LTYYQLYEKVCEfSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGAThCVLFD-GYSVKSLIDRIETITPKLIITT 171
Cdd:PRK07638 27 LTYKDWFESVCK-VANWLNEKESKNKTIAILLENRIEFLQLFAGAAMAGWT-CVPLDiKWKQDELKERLAISNADMIVTE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 172 NYgifndeiitftpnlkdaielstfkpsnvitlFRNDITSESdlKKVKDIptipntlswyDEIKKFKENNQSpfyEYVPV 251
Cdd:PRK07638 105 RY-------------------------------KLNDLPDEE--GRVIEI----------DEWKRMIEKYLP---TYAPI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 252 ESSH--PLYIIYSSGTTGNAKAVVRSNgpnlvcmnyfdRYISEKYECT-TLLTTSSVGWVSFHG------FLYGMLSfgs 322
Cdd:PRK07638 139 ENVQnaPFYMGFTSGSTGKPKAFLRAQ-----------QSWLHSFDCNvHDFHMKREDSVLIAGtlvhslFLYGAIS--- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 323 tfVMYEGG--IIKNKHIEVDFWNTIEKHKathtlslaNTIRYFIKTDPEGTIIRSKYDLSNLKEIWVGGEVIEESIPEYI 400
Cdd:PRK07638 205 --TLYVGQtvHLMRKFIPNQVLDKLETEN--------ISVMYTVPTMLESLYKENRVIENKMKIISSGAKWEAEAKEKIK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 401 EKKLKIKPTRGYGQTEIG-IAYLYCFDHINIPYyATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLPMppSFATtlYKN 479
Cdd:PRK07638 275 NIFPYAKLYEFYGASELSfVTALVDEESERRPN-SVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQ--FFMG--YII 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 480 DEKFKQLFSKfPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIA 559
Cdd:PRK07638 350 GGVLARELNA-DGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVA 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60472587 560 LLVLkqlqqqdqsiqqidlNKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPIISKFLNDS 628
Cdd:PRK07638 429 IIKG---------------SATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQ 482
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
261-551 |
2.01e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 88.86 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 261 YSSGTTGNAKAVV---RSNGPNLVCMNYFDRyisekyecttlLTTSSVGWVS---FH--GFLYGMLS---FGSTFVMyeg 329
Cdd:PRK08314 197 YTSGTTGVPKGCMhthRTVMANAVGSVLWSN-----------STPESVVLAVlplFHvtGMVHSMNApiyAGATVVL--- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 330 giiknkhieVDFWN------TIEKHKATHTLSLANTIRYFIKTdpeGTIirSKYDLSNLKEIWVGGEvieeSIPEYIEKK 403
Cdd:PRK08314 263 ---------MPRWDreaaarLIERYRVTHWTNIPTMVVDFLAS---PGL--AERDLSSLRYIGGGGA----AMPEAVAER 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 404 LK----IKPTRGYGQTEIgIAylycFDHIN-----------IPYYatGLPSIFIRPsifsDDGKELGVNEIGEIAFKlpm 468
Cdd:PRK08314 325 LKeltgLDYVEGYGLTET-MA----QTHSNppdrpklqclgIPTF--GVDARVIDP----ETLEELPPGEVGEIVVH--- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 469 PPSFATTLYKNDEKFKQLFSKFPG--YYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSI 546
Cdd:PRK08314 391 GPQVFKGYWNRPEATAEAFIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVI 470
|
....*
gi 60472587 547 GINDP 551
Cdd:PRK08314 471 ATPDP 475
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
93-550 |
3.64e-18 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 88.40 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 93 LTYYQLYEKVCEFSRVLLN-LNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDR-IETITPKLIIT 170
Cdd:PRK08751 51 ITYREADQLVEQFAAYLLGeLQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQlIDSGASVLVVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 171 TNYGIFNDEIITFTPnLKDAI-----ELSTFKPSNVITLFRNDItsesdlKKVKDIPTIPNTLSWYDEIKKFKENNQSPf 245
Cdd:PRK08751 131 DNFGTTVQQVIADTP-VKQVIttglgDMLGFPKAALVNFVVKYV------KKLVPEYRINGAIRFREALALGRKHSMPT- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 246 yeyVPVESSHPLYIIYSSGTTGNAKAVVRSNgPNLVC-MNYFDRYI--SEKYE--CTTLLTTSSVgwvsFHGFlygMLSF 320
Cdd:PRK08751 203 ---LQIEPDDIAFLQYTGGTTGVAKGAMLTH-RNLVAnMQQAHQWLagTGKLEegCEVVITALPL----YHIF---ALTA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 321 GSTFVMYEGG---IIKNKHIEVDFWNTIEKHKAThTLSLANTIRYFIKTDPEgtiiRSKYDLSNLKEIWVGGEVIEESIP 397
Cdd:PRK08751 272 NGLVFMKIGGcnhLISNPRDMPGFVKELKKTRFT-AFTGVNTLFNGLLNTPG----FDQIDFSSLKMTLGGGMAVQRSVA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 398 EYIEKKLKIKPTRGYGQTEIGIAYlyCFDHINIPYY--ATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKlpMPPSFATT 475
Cdd:PRK08751 347 ERWKQVTGLTLVEAYGLTETSPAA--CINPLTLKEYngSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK--GPQVMKGY 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60472587 476 LYKNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIND 550
Cdd:PRK08751 423 WKRPEETAKVMDAD--GWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPD 495
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
76-551 |
6.88e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 87.05 E-value: 6.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 76 DQDALIYEcPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKS 155
Cdd:PRK08008 22 HKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 156 ---LIDRIETitpKLIITTNygifndeiiTFTPnLKDAIELSTFKPSNVITLFRnditsesdlkkvKDIPTIPNTLSwYD 232
Cdd:PRK08008 101 sawILQNSQA---SLLVTSA---------QFYP-MYRQIQQEDATPLRHICLTR------------VALPADDGVSS-FT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 233 EIKkfkenNQSP--FYEYVPVESSHPLYIIYSSGTTGNAKAVVRSNGpNL----------VCMNYFDRYISE------KY 294
Cdd:PRK08008 155 QLK-----AQQPatLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHY-NLrfagyysawqCALRDDDVYLTVmpafhiDC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 295 ECTTLLTtssvgwvsfhgflygMLSFGSTFVMYEggiiknKHIEVDFWNTIEKHKATHTLSLANTIRYFIKTDPegtiir 374
Cdd:PRK08008 229 QCTAAMA---------------AFSAGATFVLLE------KYSARAFWGQVCKYRATITECIPMMIRTLMVQPP------ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 375 SKYDLSN-LKEIWVGGEVIEESiPEYIEKKLKIKPTRGYGQTE-----IGiaylycfdhiNIPYYATGLPSIFiRPS--- 445
Cdd:PRK08008 282 SANDRQHcLREVMFYLNLSDQE-KDAFEERFGVRLLTSYGMTEtivgiIG----------DRPGDKRRWPSIG-RPGfcy 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 446 ---IFSDDGKELGVNEIGEIAFK-LPmppsfATTLYK---NDEKFKQLFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQI 518
Cdd:PRK08008 350 eaeIRDDHNRPLPAGEIGEICIKgVP-----GKTIFKeyyLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMI 424
|
490 500 510
....*....|....*....|....*....|...
gi 60472587 519 KISGNKVQLNTIETSILKHPLVLECCSIGINDP 551
Cdd:PRK08008 425 KRGGENVSCVELENIIATHPKIQDIVVVGIKDS 457
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
242-618 |
1.30e-17 |
|
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: 86.43 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 242 QSPFYEYVPVESSHPLYIIYSSGTTGNAKAVVRSNGPNLVCMNYFDRYISEKYECTTLLTTSSVgwvsFhgFLYGM---- 317
Cdd:TIGR02262 149 ESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKL----F--FAYGLgnal 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 318 ---LSFGSTFVMYeggiiKNKHIEVDFWNTIEKHKAThTLSLANTIRYFIKTDPEgtiIRSKYDLSnLKEIWVGGEVIEE 394
Cdd:TIGR02262 223 tfpMSVGATTVLM-----GERPTPDAVFDRLRRHQPT-IFYGVPTLYAAMLADPN---LPSEDQVR-LRLCTSAGEALPA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 395 SIPEYIEKKLKIKPTRGYGQTEIGIAYLYCFDHiNIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIafkLPMPPSFAT 474
Cdd:TIGR02262 293 EVGQRWQARFGVDIVDGIGSTEMLHIFLSNLPG-DVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGEL---LISGPSSAT 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 475 TLYKNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCY 554
Cdd:TIGR02262 369 MYWNNRAKSRDTFQG--EWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGL 446
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60472587 555 SVPIALLVLKQLQQQdqsiqqidlnkLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:TIGR02262 447 IKPKAFVVLRPGQTA-----------LETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
261-618 |
2.36e-17 |
|
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: 84.84 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 261 YSSGTTGNAKAVV----------RSNGPNLVCMNYFDRYISekyeCTTLLTTSSVGwvsfhGFLYGMLSFGSTFVMYEGG 330
Cdd:cd05958 104 FTSGTTGAPKATMhfhrdplasaDRYAVNVLRLREDDRFVG----SPPLAFTFGLG-----GVLLFPFGVGASGVLLEEA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 331 IIKNkhievdFWNTIEKHKATHTLSLANTIRYFIKTDPEGtiirsKYDLSNLKEIWVGGEVIEESIPEYIEKKLKIKPTR 410
Cdd:cd05958 175 TPDL------LLSAIARYKPTVLFTAPTAYRAMLAHPDAA-----GPDLSSLRKCVSAGEALPAALHRAWKEATGIPIID 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 411 GYGQTEIgiayLYCF-----DHINIPyyATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLPmppsfaTTLYKNDEKFKQ 485
Cdd:cd05958 244 GIGSTEM----FHIFisarpGDARPG--ATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP------TGCRYLADKRQR 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 486 lfSKFPGYYN-PGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALLVLK 564
Cdd:cd05958 312 --TYVQGGWNiTGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLR 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 60472587 565 QLQQQDQSiqqidlnkLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:cd05958 390 PGVIPGPV--------LARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQR 435
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
376-551 |
7.35e-17 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 84.30 E-value: 7.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 376 KYDLSNLKEIWVGGEVIEESIPEYIEKKLKIKPTRGYGQTEIG-IAYLYCFD------HINIPyyatgLPSIFIrpSIFS 448
Cdd:PRK07059 323 KLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSpVATCNPVDatefsgTIGLP-----LPSTEV--SIRD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 449 DDGKELGVNEIGEIAFKLP--MPPsfattlYKN--DEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNK 524
Cdd:PRK07059 396 DDGNDLPLGEPGEICIRGPqvMAG------YWNrpDETAKVMTAD--GFFRTGDVGVMDERGYTKIVDRKKDMILVSGFN 467
|
170 180
....*....|....*....|....*..
gi 60472587 525 VQLNTIETSILKHPLVLECCSIGINDP 551
Cdd:PRK07059 468 VYPNEIEEVVASHPGVLEVAAVGVPDE 494
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
10-64 |
1.70e-16 |
|
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: 73.66 E-value: 1.70e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 60472587 10 YLNDFNYANSYPEAFWDEVAKKnVFWDKMYDKVYSGDEM-YPDWFKGGELNTCYNV 64
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKE-LDWFKPFDKVLDGSNGpFAKWFVGGKLNVCYNC 55
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
92-619 |
1.79e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 82.64 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 92 KLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITT 171
Cdd:PRK07656 30 RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 172 nyGIF---NDEIITFTPNLKDAIELSTfkpsnvitlfrnditsesdlkkVKDIPTIPNTLSWYDEIKkfkenNQSPFYEY 248
Cdd:PRK07656 110 --GLFlgvDYSATTRLPALEHVVICET----------------------EEDDPHTEKMKTFTDFLA-----AGDPAERA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 249 VPVESSHPLYIIYSSGTTGNAKAVVRSNGPNL-----VC----MNYFDRYIsekyeCTTLLttssvgwvsFHGFLY--GM 317
Cdd:PRK07656 161 PEVDPDDVADILFTSGTTGRPKGAMLTHRQLLsnaadWAeylgLTEGDRYL-----AANPF---------FHVFGYkaGV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 318 ---LSFGSTfvmyeggIIKNKHIEVD-FWNTIEKHKAThTLSLANTIRYFIKTDPEgtiiRSKYDLSNLKEIWVGGEVIE 393
Cdd:PRK07656 227 napLMRGAT-------ILPLPVFDPDeVFRLIETERIT-VLPGPPTMYNSLLQHPD----RSAEDLSSLRLAVTGAASMP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 394 ESIPEYIEKKLKIKP-TRGYGQTE-IGIAylyCF-----DHINIPYYA-TGLPSIFIRpsIFSDDGKELGVNEIGEIAFK 465
Cdd:PRK07656 295 VALLERFESELGVDIvLTGYGLSEaSGVT---TFnrlddDRKTVAGTIgTAIAGVENK--IVNELGEEVPVGEVGELLVR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 466 LP--------MPPSFATTLyKNDekfkqlfskfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKH 537
Cdd:PRK07656 370 GPnvmkgyydDPEATAAAI-DAD-----------GWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEH 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 538 PLVLECCSIGINDPT------CYSVPiallvlkqlqqqdqsiqqidlnKLQNEINyiiKQDI-----ESLA---VLRKIV 603
Cdd:PRK07656 438 PAVAEAAVIGVPDERlgevgkAYVVL----------------------KPGAELT---EEELiaycrEHLAkykVPRSIE 492
|
570
....*....|....*.
gi 60472587 604 IVNQLPKTKTGKIPRP 619
Cdd:PRK07656 493 FLDELPKNATGKVLKR 508
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
259-618 |
1.99e-16 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 82.97 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 259 IIYSSGTTGNAKAVVRSNGPNLVCMNYFDRYISEKYECTTLLTTSSVGWVSFHG-----FLYGMLSFGSTFVmyeggiIK 333
Cdd:PLN02574 203 IMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEYPGSDNVYLAALPMFHIyglslFVVGLLSLGSTIV------VM 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 334 NKHIEVDFWNTIEKHKATHTLSLANTIRYFIK-TDPEGTIIrskydLSNLKEIWVGGE-VIEESIPEYIEKKLKIKPTRG 411
Cdd:PLN02574 277 RRFDASDMVKVIDRFKVTHFPVVPPILMALTKkAKGVCGEV-----LKSLKQVSCGAApLSGKFIQDFVQTLPHVDFIQG 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 412 YGQTEIGIAYLYCFDHINIPYYAT-GLPSIFIRPSIFS-DDGKELGVNEIGEIAFKLPMppsfATTLYKNDEKFKQLFSK 489
Cdd:PLN02574 352 YGMTESTAVGTRGFNTEKLSKYSSvGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPG----VMKGYLNNPKATQSTID 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 490 FPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALLVLKQLQQQ 569
Cdd:PLN02574 428 KDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTL 507
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 60472587 570 DQSIQqidlnklqneINYIIKQdIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:PLN02574 508 SQEAV----------INYVAKQ-VAPYKKVRKVVFVQSIPKSPAGKILR 545
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
259-618 |
5.45e-16 |
|
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: 80.47 E-value: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 259 IIYSSGTTGNAKAVVRSNGpnlvcmNYFDRYISEKyecTTLLTTSSVGWVS----FHgflYGMLSFGSTFVMYEGGIIKN 334
Cdd:cd05912 82 IMYTSGTTGKPKGVQQTFG------NHWWSAIGSA---LNLGLTEDDNWLCalplFH---ISGLSILMRSVIYGMTVYLV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 335 KHIEVDFWNT-IEKHKATHTLSLANTIRYFIKTDPEGtiirskYDlSNLKEIWVGGEVIEESIPEYIEKKlKIKPTRGYG 413
Cdd:cd05912 150 DKFDAEQVLHlINSGKVTIISVVPTMLQRLLEILGEG------YP-NNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 414 QTE-----IGIAYLYCFDHINipyyATGLPSIFIRPSIFSDDGKElgvNEIGEIAFKLPM-PPSFattlYKNDEKFKQLF 487
Cdd:cd05912 222 MTEtcsqiVTLSPEDALNKIG----SAGKPLFPVELKIEDDGQPP---YEVGEILLKGPNvTKGY----LNRPDATEESF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 488 SKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALLVLKQLQ 567
Cdd:cd05912 291 EN--GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 60472587 568 QqdqsiqqidlnklQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:cd05912 369 S-------------EEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLR 406
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
94-544 |
6.45e-16 |
|
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: 80.39 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 94 TYYQLYEKVCEFSRVLLNL-NISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVksliDRIETI----TPKLI 168
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPA----ERLAFIledaGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 169 ITTnygifndeiitfTPNLKDAIELsTFKPSNVITLFRNDITSESDLKKVKdiptipntlswydeikkfkennqspfyey 248
Cdd:TIGR01733 77 LTD------------SALASRLAGL-VLPVILLDPLELAALDDAPAPPPPD----------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 249 VPVESSHPLYIIYSSGTTGNAKAVVRSNGpNLVcmNYFDRYISEkyecttLLTTSSVGWVSFHGF--------LYGMLSF 320
Cdd:TIGR01733 115 APSGPDDLAYVIYTSGSTGRPKGVVVTHR-SLV--NLLAWLARR------YGLDPDDRVLQFASLsfdasveeIFGALLA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 321 GSTFVMYEGGIIKNKHIEVDFWntIEKHKATHTLSLANTIRYFIKTDPEgtiirskyDLSNLKEIWVGGEVIEesiPEYI 400
Cdd:TIGR01733 186 GATLVVPPEDEERDDAALLAAL--IAEHPVTVLNLTPSLLALLAAALPP--------ALASLRLVILGGEALT---PALV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 401 EKKLKIKPTR----GYGQTEIGI---AYLYCFDHI----NIPYyatGLPSIFIRPSIFSDDGKELGVNEIGEIAFKlpmp 469
Cdd:TIGR01733 253 DRWRARGPGArlinLYGPTETTVwstATLVDPDDApresPVPI---GRPLANTRLYVLDDDLRPVPVGVVGELYIG---- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 470 psfATTL---YKND-EKFKQLFSKFPGY-------YNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHP 538
Cdd:TIGR01733 326 ---GPGVargYLNRpELTAERFVPDPFAggdgarlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHP 402
|
....*.
gi 60472587 539 LVLECC 544
Cdd:TIGR01733 403 GVREAV 408
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
261-619 |
9.27e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 79.45 E-value: 9.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 261 YSSGTTGNAKAVVRSNGpNLVCMNYFDRYISEKYECTTLLttssVGWVSFHGF-----LYGMLSFGSTFVMYEGGIIKNK 335
Cdd:cd05944 9 HTGGTTGTPKLAQHTHS-NEVYNAWMLALNSLFDPDDVLL----CGLPLFHVNgsvvtLLTPLASGAHVVLAGPAGYRNP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 336 HIEVDFWNTIEKHKAThTLSLANTIRYFIKTDPEGTiirskyDLSNLKEIWVGGEVIEESIPEYIEKKLKIKPTRGYGQT 415
Cdd:cd05944 84 GLFDNFWKLVERYRIT-SLSTVPTVYAALLQVPVNA------DISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 416 EIGIAYLYCFDHINIPYYATGLPSIFIRPSIFSDDG-----KELGVNEIGEIAFKLPMppsfATTLYKNDEKFKQLFSKf 490
Cdd:cd05944 157 EATCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGvgrllRDCAPDEVGEICVAGPG----VFGGYLYTEGNKNAFVA- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 491 PGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALLVLKQLQQQD 570
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVE 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 60472587 571 qsiqqidlnklQNEINYIIKQDI-ESLAVLRKIVIVNQLPKTKTGKIPRP 619
Cdd:cd05944 312 -----------EEELLAWARDHVpERAAVPKHIEVLEELPVTAVGKVFKP 350
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
92-618 |
1.01e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 80.39 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 92 KLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGAThcVLFdgysvkslidrietITPKLIItt 171
Cdd:PRK03640 27 KVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAV--AVL--------------LNTRLSR-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 172 nygifndEIITFtpNLKDAielstfkpsNVITLfrndITSESDLKKVKdiptiPNTLSWYDEIKKFKENNQSPfYEYVPV 251
Cdd:PRK03640 89 -------EELLW--QLDDA---------EVKCL----ITDDDFEAKLI-----PGISVKFAELMNGPKEEAEI-QEEFDL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 252 ESShpLYIIYSSGTTGNAKAVVRSNGpnlvcmNYFdryisekyecttlltTSSVG------------WVS----FH--GF 313
Cdd:PRK03640 141 DEV--ATIMYTSGTTGKPKGVIQTYG------NHW---------------WSAVGsalnlglteddcWLAavpiFHisGL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 314 -------LYGMlsfgsTFVMYEggiiknkHIEVDFWN-TIEKHKAThTLSLANT-IRYFIKTDPEGTiirskYDlSNLKE 384
Cdd:PRK03640 198 silmrsvIYGM-----RVVLVE-------KFDAEKINkLLQTGGVT-IISVVSTmLQRLLERLGEGT-----YP-SSFRC 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 385 IWVGGEVIEESIPEYIEKKlKIKPTRGYGQTEIG--IAYLYcfdhiniPYYA------TGLP----SIFIRpsifsDDGK 452
Cdd:PRK03640 259 MLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETAsqIVTLS-------PEDAltklgsAGKPlfpcELKIE-----KDGV 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 453 ELGVNEIGEIAFKlpmPPSFATTLYKNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIkISGNK-VQLNTIE 531
Cdd:PRK03640 326 VVPPFEEGEIVVK---GPNVTKGYLNREDATRETFQD--GWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGEnIYPAEIE 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 532 TSILKHPLVLECCSIGINDPTCYSVPIALLVLKQLQQqdqsiqqidlnklQNEINYIIKQDIESLAVLRKIVIVNQLPKT 611
Cdd:PRK03640 400 EVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVT-------------EEELRHFCEEKLAKYKVPKRFYFVEELPRN 466
|
....*..
gi 60472587 612 KTGKIPR 618
Cdd:PRK03640 467 ASGKLLR 473
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
254-618 |
1.59e-15 |
|
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: 78.46 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 254 SHPLYIIYSSGTTGNAKAVVRSNGPNLVCMnyfDRYISEKYECTTLLTTSSVGWVSFHGFLYGMLsfgsTFVMYEGGII- 332
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVP---DILQKEGLNWVVGDVTYLPLPATHIGGLWWIL----TCLIHGGLCVt 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 333 -KNKHIEVDFWNTIEKHKAThTLSLANTIRYFIKTDPEGTIIRSKydlsNLKEIWVGGEVIEESIPEYIEKKLKIKPTRG 411
Cdd:cd17635 74 gGENTTYKSLFKILTTNAVT-TTCLVPTLLSKLVSELKSANATVP----SLRLIGYGGSRAIAADVRFIEATGLTNTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 412 YGQTEIGIAYLYCFDHINIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKlpmPPSFATTLYKNDEKFKQLFSKfp 491
Cdd:cd17635 149 YGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIK---SPANMLGYWNNPERTAEVLID-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 492 GYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALLVLKQLQQQdq 571
Cdd:cd17635 224 GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDE-- 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 60472587 572 siqqidlNKLQNEINYIIKQdIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:cd17635 302 -------NAIRALKHTIRRE-LEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
256-550 |
9.75e-15 |
|
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: 77.04 E-value: 9.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 256 PLYIIYSSGTTGNAKAVVRSNGpNLVCMnyfDRYISEKYECT---TLLTTSSVGwvSFHGFLYGMLS---FGSTFVMyeg 329
Cdd:cd05903 95 VALLLFTSGTTGEPKGVMHSHN-TLSAS---IRQYAERLGLGpgdVFLVASPMA--HQTGFVYGFTLpllLGAPVVL--- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 330 giiknkhieVDFWN------TIEKHKATHTLSLAntirYFIkTDPEGTIIRSKYDLSNLKEIWVGGEVIEESIPEYIEKK 403
Cdd:cd05903 166 ---------QDIWDpdkalaLMREHGVTFMMGAT----PFL-TDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAEL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 404 LKIKPTRGYGQTEIGIAYLYCFDHINIPYYAT-GLPSIFIRPSIFSDDGKELGVNEIGEIAFKlpMPPSFATTLYKNDEK 482
Cdd:cd05903 232 LGAKVCSAYGSTECPGAVTSITPAPEDRRLYTdGRPLPGVEIKVVDDTGATLAPGVEGELLSR--GPSVFLGYLDRPDLT 309
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60472587 483 FKQLFSkfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIND 550
Cdd:cd05903 310 ADAAPE---GWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPD 374
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
93-551 |
1.05e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 77.27 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIIttn 172
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALV--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 173 ygiFNDEiitFTPNLKDAielstfkPSNVITLFRNDITSESDLKKVKDIPTIpntlswyDEIKKFKENnqspfyEYVPVE 252
Cdd:PRK07788 152 ---YDDE---FTDLLSAL-------PPDLGRLRAWGGNPDDDEPSGSTDETL-------DDLIAGSST------APLPKP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 253 SSHPLYIIYSSGTTGNAKAVVRSNGPNLVCMNYFDRYISEKYECTTLLTTSsvgwvSFH--GFLYGMLSF--GSTFVMye 328
Cdd:PRK07788 206 PKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAP-----MFHatGWAHLTLAMalGSTVVL-- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 329 ggiiknkHIEVDFWNT---IEKHKATHTLSLANTIRYFIKTDPEgtiIRSKYDLSNLKEIWVGGEVIEesiPEYIEKKLK 405
Cdd:PRK07788 279 -------RRRFDPEATledIAKHKATALVVVPVMLSRILDLGPE---VLAKYDTSSLKIIFVSGSALS---PELATRALE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 406 ikpTRG------YGQTEIGIAYLYCFDHINIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLPMPpsfattlykn 479
Cdd:PRK07788 346 ---AFGpvlynlYGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFP---------- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 480 dekfkqlfskFPGYYNP------------GDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIG 547
Cdd:PRK07788 413 ----------FEGYTDGrdkqiidgllssGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIG 482
|
....
gi 60472587 548 INDP 551
Cdd:PRK07788 483 VDDE 486
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
412-623 |
1.69e-14 |
|
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: 76.17 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 412 YGQTEIGIAylycfdhINIPYYA--------TGLPSIFIRpsIFSDD-GKELGVNEIGEIAFKlpmPPSFATTLYKNDEK 482
Cdd:cd05941 244 YGMTEIGMA-------LSNPLDGerrpgtvgMPLPGVQAR--IVDEEtGEPLPRGEVGEIQVR---GPSVFKEYWNKPEA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 483 FKQLFSKfPGYYNPGDLGFKDENGFYTIVSR-SDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALL 561
Cdd:cd05941 312 TKEEFTD-DGWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVV 390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60472587 562 VLKQLQQQDQsiqqidlnkLQNEINYiIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPIISK 623
Cdd:cd05941 391 VLRAGAAALS---------LEELKEW-AKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
256-551 |
1.80e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 76.56 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 256 PLYIIYSSGTTGNAKAVVRSNGpNLVCMN---YFDRYISE--KYECTTLLttSSVGWVsfhgFLYGMLSFGSTFVMYEGg 330
Cdd:PRK06188 170 IAGLAYTGGTTGKPKGVMGTHR-SIATMAqiqLAEWEWPAdpRFLMCTPL--SHAGGA----FFLPTLLRGGTVIVLAK- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 331 iiknkhIEVD-FWNTIEKHKATHTLsLANTIRYFIKTDPEgtiiRSKYDLSNLKEIWVGGEVIEES-IPEYIEKklkIKP 408
Cdd:PRK06188 242 ------FDPAeVLRAIEEQRITATF-LVPTMIYALLDHPD----LRTRDLSSLETVYYGASPMSPVrLAEAIER---FGP 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 409 TRG--YGQTEIG--IAYLYCFDHI-NIPYYAT--GLPSIFIRPSIFSDDGKELGVNEIGEIAFKLP--------MPPSFA 473
Cdd:PRK06188 308 IFAqyYGQTEAPmvITYLRKRDHDpDDPKRLTscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPlvmdgywnRPEETA 387
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60472587 474 TTLyKNdekfkqlfskfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDP 551
Cdd:PRK06188 388 EAF-RD------------GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDE 452
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
250-626 |
4.40e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 75.31 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 250 PVESSHPLYIIYSSGTTGNAKAVVRSNGPnlVCMNYFDRYISEKYECTTLLTTSsvgwvsfhGFLY--GMLSFGSTFVMY 327
Cdd:PRK06145 145 AVAPTDLVRLMYTSGTTDRPKGVMHSYGN--LHWKSIDHVIALGLTASERLLVV--------GPLYhvGAFDLPGIAVLW 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 328 EGGIIKnkhIEVDF-----WNTIEKHKATHTLsLANTIRYFIKTDPEgtiiRSKYDLSNLKEIWVGGEVIEES-IPEYIE 401
Cdd:PRK06145 215 VGGTLR---IHREFdpeavLAAIERHRLTCAW-MAPVMLSRVLTVPD----RDRFDLDSLAWCIGGGEKTPESrIRDFTR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 402 KKLKIKPTRGYGQTEI--GIAYLYCFDHIN-IPYYATGLPSIFIRpsIFSDDGKELGVNEIGEIAFKlpmPPSFATTLYK 478
Cdd:PRK06145 287 VFTRARYIDAYGLTETcsGDTLMEAGREIEkIGSTGRALAHVEIR--IADGAGRWLPPNMKGEICMR---GPKVTKGYWK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 479 NDEKFKQLFskFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPI 558
Cdd:PRK06145 362 DPEKTAEAF--YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERIT 439
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60472587 559 ALLVlkqlqqqdqsiqqidLNKLQN----EINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPIISKFLN 626
Cdd:PRK06145 440 AVVV---------------LNPGATltleALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELN 496
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
76-619 |
4.51e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 75.19 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 76 DQDALIYecpyLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKS 155
Cdd:PRK12583 33 DREALVV----RHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 156 LIDRIETITPKLII------TTNYGIFNDEIItftPNLKDA--IELSTFK-P--SNVITLfrnditsesdlkkvkDIPTI 224
Cdd:PRK12583 109 LEYALGQSGVRWVIcadafkTSDYHAMLQELL---PGLAEGqpGALACERlPelRGVVSL---------------APAPP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 225 PNTLSWyDEIKKFKE--NNQSPFYEYVPVESSHPLYIIYSSGTTGNAKAVVRSNGpNLVCMNYFdryISEKYEcttlLTT 302
Cdd:PRK12583 171 PGFLAW-HELQARGEtvSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHH-NILNNGYF---VAESLG----LTE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 303 SSVGWVS---FHGFlyGM-------LSFGSTFvmyeggIIKNKHIEVDF-WNTIEKHKAThtlSLANTIRYFIK--TDPE 369
Cdd:PRK12583 242 HDRLCVPvplYHCF--GMvlanlgcMTVGACL------VYPNEAFDPLAtLQAVEEERCT---ALYGVPTMFIAelDHPQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 370 gtiiRSKYDLSNLKEIWVGG-----EVIEESIPEYIEKKLKIkptrGYGQTEIG-IAYLYCF-DHINIPYYATGLPSIFI 442
Cdd:PRK12583 311 ----RGNFDLSSLRTGIMAGapcpiEVMRRVMDEMHMAEVQI----AYGMTETSpVSLQTTAaDDLERRVETVGRTQPHL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 443 RPSIFSDDGKELGVNEIGEIAFKlpmPPSFATTLYKNDEKFKQLFSKfPGYYNPGDLGFKDENGFYTIVSRSDDQIKISG 522
Cdd:PRK12583 383 EVKVVDPDGATVPRGEIGELCTR---GYSVMKGYWNNPEATAESIDE-DGWMHTGDLATMDEQGYVRIVGRSKDMIIRGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 523 NKVQLNTIETSILKHPLVLECCSIGINDPTcYSVPIALLVLKQLQQQDQsiqqidlnklQNEINYIIKQDIESLAVLRKI 602
Cdd:PRK12583 459 ENIYPREIEEFLFTHPAVADVQVFGVPDEK-YGEEIVAWVRLHPGHAAS----------EEELREFCKARIAHFKVPRYF 527
|
570
....*....|....*..
gi 60472587 603 VIVNQLPKTKTGKIPRP 619
Cdd:PRK12583 528 RFVDEFPMTVTGKVQKF 544
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
376-550 |
6.60e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 74.80 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 376 KYDLSNLKEIWVGGEVIEESIPEYIEKKLKIKPTRGYGQTEIG-IAYLYCFDHINIPYYATGLPSIFIRpsIFSDDGKEL 454
Cdd:PRK05677 322 KLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSpVVSVNPSQAIQVGTIGIPVPSTLCK--VIDDDGNEL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 455 GVNEIGEIAFKlpmPPSFATTLYKNDEKFKQLFSKfPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSI 534
Cdd:PRK05677 400 PLGEVGELCVK---GPQVMKGYWQRPEATDEILDS-DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVL 475
|
170
....*....|....*.
gi 60472587 535 LKHPLVLECCSIGIND 550
Cdd:PRK05677 476 AALPGVLQCAAIGVPD 491
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
376-548 |
8.28e-14 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 74.32 E-value: 8.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 376 KYDLSNLKEIWVGGEVIEESIPEYIEKKLKIKPTRGYGQTEIgiAYLYCFDHINIPYY--ATGLP--SIFIRpsIFSDDG 451
Cdd:PRK08974 321 ELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTEC--SPLVSVNPYDLDYYsgSIGLPvpSTEIK--LVDDDG 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 452 KELGVNEIGEIAFKLP--MP-----PSfATtlyknDEKFKQlfskfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNK 524
Cdd:PRK08974 397 NEVPPGEPGELWVKGPqvMLgywqrPE-AT-----DEVIKD------GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFN 464
|
170 180
....*....|....*....|....
gi 60472587 525 VQLNTIETSILKHPLVLECCSIGI 548
Cdd:PRK08974 465 VYPNEIEDVVMLHPKVLEVAAVGV 488
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
84-618 |
1.64e-13 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 73.64 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 84 CPYLKKTIK----LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGAtHCVLFD-GYSVKSLID 158
Cdd:PRK13382 56 CPDRPGLIDelgtLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGA-DILLLNtSFAGPALAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 159 RIETitPKLIIttnygIFNDEiiTFTPNLKDAielstfkpsnvitlfrnditsesdlkkVKDIPTIPNTLSWYDEIKKF- 237
Cdd:PRK13382 135 VVTR--EGVDT-----VIYDE--EFSATVDRA---------------------------LADCPQATRIVAWTDEDHDLt 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 238 ------KENNQSPfyeyvPVESSHPLYIIYSSGTTGNAKAVVRS-NGPNLVCMNYFDRyISEKYECTTLLTTSSvgwvsF 310
Cdd:PRK13382 179 vevliaAHAGQRP-----EPTGRKGRVILLTSGTTGTPKGARRSgPGGIGTLKAILDR-TPWRAEEPTVIVAPM-----F 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 311 H--GF--LYGMLSFGSTFVMyeggiiKNKHIEVDFWNTIEKHKATHTLSLANTIRYFIKTDPEgtiIRSKYDLSNLKEIW 386
Cdd:PRK13382 248 HawGFsqLVLAASLACTIVT------RRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAE---VRNRYSGRSLRFAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 387 VGGEVIEESIPEYIEKKLKIKPTRGYGQTEIGIAYLYCFDHINIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIafkl 466
Cdd:PRK13382 319 ASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTI---- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 467 pmppsfattLYKNDEKFKQLFSK-----FPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVL 541
Cdd:PRK13382 395 ---------FVRNDTQFDGYTSGstkdfHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 542 ECCSIGINDP------TCYSVPIAllvlkqlqqqdqsiqqiDLNKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGK 615
Cdd:PRK13382 466 EAAVIGVDDEqygqrlAAFVVLKP-----------------GASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGK 528
|
...
gi 60472587 616 IPR 618
Cdd:PRK13382 529 ILR 531
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
92-619 |
2.58e-13 |
|
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: 72.28 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 92 KLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHcVLFDGYSVkslIDRIETIT----PKL 167
Cdd:cd05945 16 TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAY-VPLDASSP---AERIREILdaakPAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 168 IITTNygifndeiitftpnlkdaielstfkpsnvitlfrnditsesdlkkvkdiptipntlswyDEikkfkennqspfye 247
Cdd:cd05945 92 LIADG-----------------------------------------------------------DD-------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 248 yvpvesshPLYIIYSSGTTGNAKAVVRSNGpNLVCmnyFDRYISEKYecttLLTTSSV--GWVSFHgF------LYGMLS 319
Cdd:cd05945 99 --------NAYIIFTSGSTGRPKGVQISHD-NLVS---FTNWMLSDF----PLGPGDVflNQAPFS-FdlsvmdLYPALA 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 320 FGSTFVMYEGGIIKNkhiEVDFWNTIEKHKATHTLSLANTIRYFIKT---DPEGtiirskydLSNLKEIWVGGEVIEESI 396
Cdd:cd05945 162 SGATLVPVPRDATAD---PKQLFRFLAEHGITVWVSTPSFAAMCLLSptfTPES--------LPSLRHFLFCGEVLPHKT 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 397 PEYIEKKLkikPTR----GYGQTEIGIAYLYcfDHINiPYYATGLPSIFI-------RPSIFSDDGKELGVNEIGEIafk 465
Cdd:cd05945 231 ARALQQRF---PDAriynTYGPTEATVAVTY--IEVT-PEVLDGYDRLPIgyakpgaKLVILDEDGRPVPPGEKGEL--- 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 466 LPMPPSFATTLYKNDEKFKQLFSKFPGY--YNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLEC 543
Cdd:cd05945 302 VISGPSVSKGYLNNPEKTAAAFFPDEGQraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEA 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60472587 544 CSIGINDPTCYSVPIALLVLKQLQQQdqsiqqidlnKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRP 619
Cdd:cd05945 382 VVVPKYKGEKVTELIAFVVPKPGAEA----------GLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRK 447
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
253-618 |
3.08e-13 |
|
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: 72.22 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 253 SSHPLYIIYSSGTTGNAKAVVRSNgpnlvcMNYFDRYISEKY-----ECTTLLTTSSVGWVSfHGF--LYGMLSFGSTFV 325
Cdd:cd05974 84 ADDPMLLYFTSGTTSKPKLVEHTH------RSYPVGHLSTMYwiglkPGDVHWNISSPGWAK-HAWscFFAPWNAGATVF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 326 MYEGGIIKNKHIevdfWNTIEKHKAThTLSLANTI-RYFIKTDPEGTIIRskydlsnLKEIWVGGEVIEESIPEYIEKKL 404
Cdd:cd05974 157 LFNYARFDAKRV----LAALVRYGVT-TLCAPPTVwRMLIQQDLASFDVK-------LREVVGAGEPLNPEVIEQVRRAW 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 405 KIKPTRGYGQTEIgIAYLYCFDHINIPYYATGLPSIFIRPSIFSDDGKElgVNEiGEIAFKLPMP-PSFATTLYKNDEKf 483
Cdd:cd05974 225 GLTIRDGYGQTET-TALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAP--ATE-GEVALDLGDTrPVGLMKGYAGDPD- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 484 KQLFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALLVL 563
Cdd:cd05974 300 KTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVL 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 60472587 564 KQLQQQDQSIQQIdlnklqneinyIIKQDIESLAVLRKI--VIVNQLPKTKTGKIPR 618
Cdd:cd05974 380 RAGYEPSPETALE-----------IFRFSRERLAPYKRIrrLEFAELPKTISGKIRR 425
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
94-623 |
4.41e-13 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 72.09 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 94 TYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIET------ITPKL 167
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKcqakmfFAPTL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 168 IITTNYGIFNDEIITFTPNLKDAIELSTFKPSnvitlfrndiTSESDLKKVKDiptipntlswydeikkfkenNQSPFYE 247
Cdd:PRK06087 131 FKQTRPVDLILPLQNQLPQLQQIVGVDKLAPA----------TSSLSLSQIIA--------------------DYEPLTT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 248 YVPVESSHPLYIIYSSGTTGNAKAVVRSNGpNLVcmnyfdryISEKYECTTL-LTTSSVGWVS---------FHGFLYGM 317
Cdd:PRK06087 181 AITTHGDELAAVLFTSGTEGLPKGVMLTHN-NIL--------ASERAYCARLnLTWQDVFMMPaplghatgfLHGVTAPF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 318 LsFGSTFVMYEggIIKNKH-IEVdfwntIEKHKAThtLSLANTIryFIkTDPEGTIIRSKYDLSNLKEIWVGGEVIEESI 396
Cdd:PRK06087 252 L-IGARSVLLD--IFTPDAcLAL-----LEQQRCT--CMLGATP--FI-YDLLNLLEKQPADLSALRFFLCGGTTIPKKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 397 PEYIEKKlKIKPTRGYGQTE-IGIAYLYCFDHINIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKlpMPPSFATT 475
Cdd:PRK06087 319 ARECQQR-GIKLLSVYGSTEsSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASR--GPNVFMGY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 476 LYKNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDP---- 551
Cdd:PRK06087 396 LDEPELTARALDEE--GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDErlge 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60472587 552 -TC-YSVPIALLVLKqlqqqdqsiqqidlnKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPIISK 623
Cdd:PRK06087 474 rSCaYVVLKAPHHSL---------------TLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
249-544 |
8.70e-13 |
|
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: 71.08 E-value: 8.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 249 VPVESSHPLYIIYSSGTTGNAKAV-VRSNGPNLVCMNyfDRYISEKyECTTLLTTSSVGWVSFHGFLYGMLSFGSTFVMY 327
Cdd:cd12117 131 VPVSPDDLAYVMYTSGSTGRPKGVaVTHRGVVRLVKN--TNYVTLG-PDDRVLQTSPLAFDASTFEIWGALLNGARLVLA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 328 EGGIIKNKHievDFWNTIEKHKATH---TLSLANTIryfIKTDPEGtiirskydLSNLKEIWVGGEVIEesiPEYIEKKL 404
Cdd:cd12117 208 PKGTLLDPD---ALGALIAEEGVTVlwlTAALFNQL---ADEDPEC--------FAGLRELLTGGEVVS---PPHVRRVL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 405 KIKP----TRGYGQTEiGIAYLYCFdHINIPYYATGlpSIFI-RPS------IFSDDGKELGVNEIGEI-------AFKl 466
Cdd:cd12117 271 AACPglrlVNGYGPTE-NTTFTTSH-VVTELDEVAG--SIPIgRPIantrvyVLDEDGRPVPPGVPGELyvggdglALG- 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 467 pmppsfattlYKND-----EKFKQLfSKFPG--YYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPL 539
Cdd:cd12117 346 ----------YLNRpaltaERFVAD-PFGPGerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPG 414
|
....*
gi 60472587 540 VLECC 544
Cdd:cd12117 415 VREAV 419
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
242-551 |
9.18e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 70.88 E-value: 9.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 242 QSPFYEYVPVESshPLYIIYSSGTTGNAKAVVRSNGPNLVCMNYFDRYI---SEKYECTTLLTtssvgwvsfhGFLY--- 315
Cdd:PRK12406 142 QQEPYDGPPVPQ--PQSMIYTSGTTGHPKGVRRAAPTPEQAAAAEQMRAliyGLKPGIRALLT----------GPLYhsa 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 316 ----GMLS--FGSTFVMyeggiiKNKHIEVDFWNTIEKHKATHTLSLANTIRYFIKTDPEgtiIRSKYDLSNLKEIWVGG 389
Cdd:PRK12406 210 pnayGLRAgrLGGVLVL------QPRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEE---VRAKYDVSSLRHVIHAA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 390 ---------EVIE---ESIPEYiekklkikptrgYGQTEIG-IAYLYCFDHINIPYyATGLPSIFIRPSIFSDDGKELGV 456
Cdd:PRK12406 281 apcpadvkrAMIEwwgPVIYEY------------YGSTESGaVTFATSEDALSHPG-TVGKAAPGAELRFVDEDGRPLPQ 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 457 NEIGEIAFKLPMPPSFatTLYKNDEKFKQLfsKFPGYYNPGDLGFKDENGFYTIVSRSDDQIkISGNkvqLNT----IET 532
Cdd:PRK12406 348 GEIGEIYSRIAGNPDF--TYHNKPEKRAEI--DRGGFITSGDVGYLDADGYLFLCDRKRDMV-ISGG---VNIypaeIEA 419
|
330
....*....|....*....
gi 60472587 533 SILKHPLVLECCSIGINDP 551
Cdd:PRK12406 420 VLHAVPGVHDCAVFGIPDA 438
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
242-621 |
1.21e-12 |
|
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: 70.41 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 242 QSPFYEYVPVESSH-PLYIIYSSGTTGNAKAVVRSN-GPNLvcMNYFDRYISEKYECTTLLTT----SSVGWvsfhGFLY 315
Cdd:cd12118 120 GDPDFEWIPPADEWdPIALNYTSGTTGRPKGVVYHHrGAYL--NALANILEWEMKQHPVYLWTlpmfHCNGW----CFPW 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 316 GMLSFGSTFVMYeggiiknKHIEVD-FWNTIEKHKATHtLSLANTIRYFIKTDPEgtiiRSKYDLSNLKEIWVGGEVIEE 394
Cdd:cd12118 194 TVAAVGGTNVCL-------RKVDAKaIYDLIEKHKVTH-FCGAPTVLNMLANAPP----SDARPLPHRVHVMTAGAPPPA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 395 SIPEYIEKkLKIKPTRGYGQTEIGIAYLYC-----FDHINIPYYA-----TGLPSIFIRPSIFSD---------DGKElg 455
Cdd:cd12118 262 AVLAKMEE-LGFDVTHVYGLTETYGPATVCawkpeWDELPTEERArlkarQGVRYVGLEEVDVLDpetmkpvprDGKT-- 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 456 vneIGEIAFKLPMppsFATTLYKNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSIL 535
Cdd:cd12118 339 ---IGEIVFRGNI---VMKGYLKNPEATAEAFRG--GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLY 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 536 KHPLVLECCSIGINDPTCYSVPIALLvlkqlqqqdqsiqqidlnKLQNEINY----IIKQDIESLAVLR--KIVIVNQLP 609
Cdd:cd12118 411 KHPAVLEAAVVARPDEKWGEVPCAFV------------------ELKEGAKVteeeIIAFCREHLAGFMvpKTVVFGELP 472
|
410
....*....|..
gi 60472587 610 KTKTGKIPRPII 621
Cdd:cd12118 473 KTSTGKIQKFVL 484
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
376-618 |
1.96e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 70.24 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 376 KYDLSNLKEIWVGGEVIEESIPEYIEKKLKIKPTRGYGQTE---IGIAYLYC----FDHINIPYYATGLPSIfirpsifS 448
Cdd:PRK12492 329 DLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTEtspVASTNPYGelarLGTVGIPVPGTALKVI-------D 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 449 DDGKELGVNEIGEIAFKLPM--------PPSFATTLyknDEKfkqlfskfpGYYNPGDLGFKDENGFYTIVSRSDDQIKI 520
Cdd:PRK12492 402 DDGNELPLGERGELCIKGPQvmkgywqqPEATAEAL---DAE---------GWFKTGDIAVIDPDGFVRIVDRKKDLIIV 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 521 SGNKVQLNTIETSILKHPLVLECCSIGINDPTC------YSVPIALLVLkqlqqqdqsiqqidlnklQNEINYIIKQDIE 594
Cdd:PRK12492 470 SGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSgeavklFVVARDPGLS------------------VEELKAYCKENFT 531
|
250 260
....*....|....*....|....
gi 60472587 595 SLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:PRK12492 532 GYKVPKHIVLRDSLPMTPVGKILR 555
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
90-632 |
2.02e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 70.04 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 90 TIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGAThCVLFDGYSVKSLIDRIETITpklii 169
Cdd:PRK05857 39 TSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAI-AVMADGNLPIAAIERFCQIT----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 170 ttnygifndeiitftpnlkdaielstfKPSNVITLFRNDITSESDLKKVKDIPTIPntlswYDEIKKFKENNQSPFYEYV 249
Cdd:PRK05857 113 ---------------------------DPAAALVAPGSKMASSAVPEALHSIPVIA-----VDIAAVTRESEHSLDAASL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 250 PVE----SSHPLYIIYSSGTTGNAKAVVRSNG-----PNLV---CMNYFDRYISEkyecTTL--LTTSSVG--WVSFHGF 313
Cdd:PRK05857 161 AGNadqgSEDPLAMIFTSGTTGEPKAVLLANRtffavPDILqkeGLNWVTWVVGE----TTYspLPATHIGglWWILTCL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 314 LYGMLSFgstfvmyEGGIIKNKHIEVDFWNTIekhkATHTL--SLANTIRYFIKTdpegtiirSKYDLSNLKEIWVGGEV 391
Cdd:PRK05857 237 MHGGLCV-------TGGENTTSLLEILTTNAV----ATTCLvpTLLSKLVSELKS--------ANATVPSLRLVGYGGSR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 392 IEESIPEYIEKKlKIKPTRGYGQTEIGIAYLyCFDHIN-----IPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIAfkl 466
Cdd:PRK05857 298 AIAADVRFIEAT-GVRTAQVYGLSETGCTAL-CLPTDDgsivkIEAGAVGRPYPGVDVYLAATDGIGPTAPGAGPSA--- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 467 pmppSFATTLYK----------NDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIkISGNkvqLNTIETSILK 536
Cdd:PRK05857 373 ----SFGTLWIKspanmlgywnNPERTAEVLID--GWVNTGDLLERREDGFFYIKGRSSEMI-ICGG---VNIAPDEVDR 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 537 hplVLECCSiGINDPTCYSVPIAL--LVLKQLQQQDQSIQQIDLNKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTG 614
Cdd:PRK05857 443 ---IAEGVS-GVREAACYEIPDEEfgALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSG 518
|
570
....*....|....*...
gi 60472587 615 KIPRPIISKFLNDSNFQL 632
Cdd:PRK05857 519 KVMRASLAAAATADKARV 536
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
378-625 |
2.20e-12 |
|
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: 68.51 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 378 DLSNLKEIWVGGEVIEESIPEYIEKkLKIKPTRGYGQTEIGiaylycfDHInipyyATGLPSIFIRPSIFSD-DGKELGV 456
Cdd:cd17630 109 ALKSLRAVLLGGAPIPPELLERAAD-RGIPLYTTYGMTETA-------SQV-----ATKRPDGFGRGGVGVLlPGRELRI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 457 NEIGEIAFKlpmPPSFATTLYKNDEKfkQLFSKfPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILK 536
Cdd:cd17630 176 VEDGEIWVG---GASLAMGYLRGQLV--PEFNE-DGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 537 HPLVLECCSIGINDPTCYSVPIALLVLKQLqqqdqsiqqidlnKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKI 616
Cdd:cd17630 250 HPAVRDAFVVGVPDEELGQRPVAVIVGRGP-------------ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKV 316
|
....*....
gi 60472587 617 PRPIISKFL 625
Cdd:cd17630 317 DRRALRAWL 325
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
310-552 |
3.37e-12 |
|
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: 68.10 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 310 FH-GFLYGMLSfgsTFVMyeGGiiKNKHI----EVDFWNTIEKHKATHTLSLANTIRYFIKTDPEGtiirsKYDLSNL-- 382
Cdd:cd17636 51 FHiGTLMFTLA---TFHA--GG--TNVFVrrvdAEEVLELIEAERCTHAFLLPPTIDQIVELNADG-----LYDLSSLrs 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 383 ---KEIWVGGEVIEESIPEYiekklkiKPtRGYGQTEIGiaYLYCFDHINIPYYAT-GLPSIFIRPSIFSDDGKELGVNE 458
Cdd:cd17636 119 spaAPEWNDMATVDTSPWGR-------KP-GGYGQTEVM--GLATFAALGGGAIGGaGRPSPLVQVRILDEDGREVPDGE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 459 IGEIAFKLPMppsfATTLYKNDEKFKQLFSKFpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHP 538
Cdd:cd17636 189 VGEIVARGPT----VMAGYWNRPEVNARRTRG-GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHP 263
|
250
....*....|....
gi 60472587 539 LVLECCSIGINDPT 552
Cdd:cd17636 264 AVADAAVIGVPDPR 277
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
261-551 |
3.79e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 69.16 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 261 YSSGTTGNAKAVVR---------SNGPNLVCMNyFDRYISEkyECTTLLTTSSvgwvsFHG--FLYGM--LSFGSTFVMY 327
Cdd:PRK08276 147 YSSGTTGRPKGIKRplpgldpdeAPGMMLALLG-FGMYGGP--DSVYLSPAPL-----YHTapLRFGMsaLALGGTVVVM 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 328 EggiiknKHIEVDFWNTIEKHKATHTlslantirYFIKTD-------PEGtiIRSKYDLSNLK----------------- 383
Cdd:PRK08276 219 E------KFDAEEALALIERYRVTHS--------QLVPTMfvrmlklPEE--VRARYDVSSLRvaihaaapcpvevkram 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 384 -EIWvgGEVIEESipeyiekklkikptrgYGQTE-IGIAYLYCFDHINIPYYAtGLPSI-FIRpsIFSDDGKELGVNEIG 460
Cdd:PRK08276 283 iDWW--GPIIHEY----------------YASSEgGGVTVITSEDWLAHPGSV-GKAVLgEVR--ILDEDGNELPPGEIG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 461 EIAFKLPMPPsFAttlYKND-EKFKQLFSKfPGYYNPGDLGFKDENGFYTIVSRSDDQIkISGNkvqLNT----IETSIL 535
Cdd:PRK08276 342 TVYFEMDGYP-FE---YHNDpEKTAAARNP-HGWVTVGDVGYLDEDGYLYLTDRKSDMI-ISGG---VNIypqeIENLLV 412
|
330
....*....|....*.
gi 60472587 536 KHPLVLECCSIGINDP 551
Cdd:PRK08276 413 THPKVADVAVFGVPDE 428
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
91-623 |
3.96e-12 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 69.00 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 91 IKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIit 170
Cdd:cd05915 23 HRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVL-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 171 tnygifndeiitftpnlkdaielstFKPSNVITLfrnditSESDLKKVKDIPTIPNTLSWYDEIKKFKENNQSPFYEYVP 250
Cdd:cd05915 101 -------------------------LFDPNLLPL------VEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 251 VESSHPLYIIYSSGTTGNAKAVVRS------NGPNLVCMNYFDRYISEKYECTTLLTTSSvGWVsfhgFLYGMLSFGSTF 324
Cdd:cd05915 150 VPERAACGMAYTTGTTGLPKGVVYShralvlHSLAASLVDGTALSEKDVVLPVVPMFHVN-AWC----LPYAATLVGAKQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 325 VMYEGgiIKNKHIevdFWNTIEKHKATHtlslantiryFIKTDPEGTIIRSKYDLSNLKEIWVGGEVIEESIPEYIEKKL 404
Cdd:cd05915 225 VLPGP--RLDPAS---LVELFDGEGVTF----------TAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAPRSLIAR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 405 K----IKPTRGYGQTEI---GIAYLYCFDHINIP--------------YYATGLPsiFIRPSIFS--DDGKELGVneige 461
Cdd:cd05915 290 FermgVEVRQGYGLTETspvVVQNFVKSHLESLSeeekltlkaktglpIPLVRLR--VADEEGRPvpKDGKALGE----- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 462 iafkLPMPPSFATTLYKNDEKFKQLFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVL 541
Cdd:cd05915 363 ----VQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVK 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 542 ECCSIGINDPTCYSVPIALLVLKQLQQQdqsiqqidlnklQNEINYIIKQDIESLAVLRKIVIVNQ-LPKTKTGKIPRPI 620
Cdd:cd05915 439 EAAVVAIPHPKWQERPLAVVVPRGEKPT------------PEELNEHLLKAGFAKWQLPDAYVFAEeIPRTSAGKFLKRA 506
|
...
gi 60472587 621 ISK 623
Cdd:cd05915 507 LRE 509
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
530-615 |
5.11e-12 |
|
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: 61.79 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 530 IETSILKHPLVLECCSIGINDPTCYSVPIALLVLKQLQQQdqsiqqidlnkLQNEINYIIKQDIESLAVLRKIVIVNQLP 609
Cdd:pfam13193 2 VESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVEL-----------LEEELVAHVREELGPYAVPKEVVFVDELP 70
|
....*.
gi 60472587 610 KTKTGK 615
Cdd:pfam13193 71 KTRSGK 76
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
264-619 |
5.90e-12 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 68.83 E-value: 5.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 264 GTTGNAKAVVRSNGpNLVCMNYF-DRYISEKYECTTLlttssVGWVSFHGF-LYG----MLSFGSTFVM-----YEG-GI 331
Cdd:PRK07529 223 GTTGMPKLAQHTHG-NEVANAWLgALLLGLGPGDTVF-----CGLPLFHVNaLLVtglaPLARGAHVVLatpqgYRGpGV 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 332 IKNkhievdFWNTIEKHKAThtlslantiryFIKTDPegTIIRSK-------YDLSNLKEIWVGGEVIEESIPEYIEKKL 404
Cdd:PRK07529 297 IAN------FWKIVERYRIN-----------FLSGVP--TVYAALlqvpvdgHDISSLRYALCGAAPLPVEVFRRFEAAT 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 405 KIKPTRGYGQTEIGiaylyCFDHINIPYYATGLPSIFIR-P------SIFSDDG---KELGVNEIGEIAFKlpMPPSFAT 474
Cdd:PRK07529 358 GVRIVEGYGLTEAT-----CVSSVNPPDGERRIGSVGLRlPyqrvrvVILDDAGrylRDCAVDEVGVLCIA--GPNVFSG 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 475 tlYKNDEKFKQLFSkFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCY 554
Cdd:PRK07529 431 --YLEAAHNKGLWL-EDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAG 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 555 SVPIAllvlkqlqqqdqsiqqidlnklqneinYI----------------IKQDI-ESLAVLRKIVIVNQLPKTKTGKIP 617
Cdd:PRK07529 508 ELPVA---------------------------YVqlkpgasateaellafARDHIaERAAVPKHVRILDALPKTAVGKIF 560
|
..
gi 60472587 618 RP 619
Cdd:PRK07529 561 KP 562
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
93-621 |
1.44e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 67.37 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTN 172
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 173 YGIFNDEIITFTPNLKDAI--ELSTFKP--SNVITLFRNDITSESDLKKVKDiptipNTLSWYDEIKKFKENNQSpfyey 248
Cdd:PRK06710 130 LVFPRVTNVQSATKIEHVIvtRIADFLPfpKNLLYPFVQKKQSNLVVKVSES-----ETIHLWNSVEKEVNTGVE----- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 249 VPVESSHPLYII-YSSGTTGNAKAVVRSNgPNLVCMNYFDryISEKYECTTLLTTSSVGWVSFHgfLYGMLSFGSTFVM- 326
Cdd:PRK06710 200 VPCDPENDLALLqYTGGTTGFPKGVMLTH-KNLVSNTLMG--VQWLYNCKEGEEVVLGVLPFFH--VYGMTAVMNLSIMq 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 327 -YEGGIIKNKHIEVDFwNTIEKHKAThTLSLANTIRYFIKTDPegtiIRSKYDLSNLKEIWVGGEVIEESIPEYIEKKLK 405
Cdd:PRK06710 275 gYKMVLIPKFDMKMVF-EAIKKHKVT-LFPGAPTIYIALLNSP----LLKEYDISSIRACISGSAPLPVEVQEKFETVTG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 406 IKPTRGYGQTEIGIAylycfDHINIPYY-----ATGLPSIFIRPSIFS-DDGKELGVNEIGEIAFKlpmPPSFATTLYKN 479
Cdd:PRK06710 349 GKLVEGYGLTESSPV-----THSNFLWEkrvpgSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVK---GPQIMKGYWNK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 480 DEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIA 559
Cdd:PRK06710 421 PEETAAVLQD--GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKA 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60472587 560 LLVLKQLQQQDqsiqqidlnklQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPII 621
Cdd:PRK06710 499 FVVLKEGTECS-----------EEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
445-559 |
1.60e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 66.99 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 445 SIFSDDGKELGVNEIGEIAFKlpMPPSFATtLYKNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDqIKIS-GN 523
Cdd:PRK07470 352 QIQDDEGRELPPGETGEICVI--GPAVFAG-YYNNPEANAKAFRD--GWFRTGDLGHLDARGFLYITGRASD-MYISgGS 425
|
90 100 110
....*....|....*....|....*....|....*.
gi 60472587 524 KVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIA 559
Cdd:PRK07470 426 NVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVA 461
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-618 |
1.65e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 66.15 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 256 PLYIIYSSGTTGNAKAV------VRSNGPNL-VCMNY--FDRYIsekyeCTTLLttssvgwvsFHGF-----LYGMLSFG 321
Cdd:cd05917 4 VINIQFTSGTTGSPKGAtlthhnIVNNGYFIgERLGLteQDRLC-----IPVPL---------FHCFgsvlgVLACLTHG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 322 STFVMYEGGIiknkHIEVDFwNTIEKHKAThtlSLANTIRYFIK--TDPEgtiiRSKYDLSNLKEIWVGGEVIEESIPEY 399
Cdd:cd05917 70 ATMVFPSPSF----DPLAVL-EAIEKEKCT---ALHGVPTMFIAelEHPD----FDKFDLSSLRTGIMAGAPCPPELMKR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 400 IEKKLKIKP-TRGYGQTEigiAYLYCF-----DHINIPYYATG--LPSIFIRpSIFSDDGKELGVNEIGEIAFKlpmppS 471
Cdd:cd05917 138 VIEVMNMKDvTIAYGMTE---TSPVSTqtrtdDSIEKRVNTVGriMPHTEAK-IVDPEGGIVPPVGVPGELCIR-----G 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 472 FATTL--YKNDEKFKQLFSKfPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIN 549
Cdd:cd05917 209 YSVMKgyWNDPEKTAEAIDG-DGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVP 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60472587 550 DPTCYSVPIALLvlkqlqqqdqsiqqidlnKLQN-------EINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:cd05917 288 DERYGEEVCAWI------------------RLKEgaelteeDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
92-542 |
1.82e-11 |
|
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: 66.73 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 92 KLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGAThCVLFD-GYSVKSLIDRIETITPKLIIT 170
Cdd:cd17656 13 KLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGA-FVPIDpEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 171 TNYgifndeiitftpnLKDAIELStfkpsNVITLFRNDITSESDLKKVKDIptipntlswydeikkfkennqspfyeyvp 250
Cdd:cd17656 92 QRH-------------LKSKLSFN-----KSTILLEDPSISQEDTSNIDYI----------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 251 VESSHPLYIIYSSGTTGNAKAVV--RSNGPNLVCMNYfdRYISEKYECTTLLTTSSVGWVSFHGFLYGMLSFGSTFVmye 328
Cdd:cd17656 125 NNSDDLLYIIYTSGTTGKPKGVQleHKNMVNLLHFER--EKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYI--- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 329 ggIIKNKHIEVDFWNTIEKHKATHTLSLANTiryFIKtdpegtIIRSKYDLSN-----LKEIWVGGE--VIEESIPEYIE 401
Cdd:cd17656 200 --IREETKRDVEQLFDLVKRHNIEVVFLPVA---FLK------FIFSEREFINrfptcVKHIITAGEqlVITNEFKEMLH 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 402 KKlKIKPTRGYGQTEIGIAYLYCFDH-INIPYYA-TGLPSIFIRPSIFSDDGKELGVNEIGEIAFKlpmPPSFATTLYKN 479
Cdd:cd17656 269 EH-NVHLHNHYGPSETHVVTTYTINPeAEIPELPpIGKPISNTWIYILDQEQQLQPQGIVGELYIS---GASVARGYLNR 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60472587 480 DEKFKQLFSKFP-----GYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLE 542
Cdd:cd17656 345 QELTAEKFFPDPfdpneRMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSE 412
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
257-618 |
2.23e-11 |
|
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: 66.30 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 257 LYIIYSSGTTGNAKAVVRSNgPNLVcmNYfDRYISEKYECTTLLTTSSVGWVSFHGF---LYGMLSFGSTFVMYEGGIIK 333
Cdd:cd17644 109 AYVIYTSGSTGKPKGVMIEH-QSLV--NL-SHGLIKEYGITSSDRVLQFASIAFDVAaeeIYVTLLSGATLVLRPEEMRS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 334 NKHievDFWNTIEKHKAThTLSLANTIRYFIKTDpegtIIRSKYDL-SNLKEIWVGGEVIEESIPEYIEKKLKIKPT--R 410
Cdd:cd17644 185 SLE---DFVQYIQQWQLT-VLSLPPAYWHLLVLE----LLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVGNFIQliN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 411 GYGQTEIGIAYLYCfdHINIPYYATGLpsifiRPSIfsddGKELGvNEIGEI--AFKLPMPPSFATTL----------YK 478
Cdd:cd17644 257 VYGPTEATIAATVC--RLTQLTERNIT-----SVPI----GRPIA-NTQVYIldENLQPVPVGVPGELhiggvglargYL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 479 N-----DEKFKQ---LFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIND 550
Cdd:cd17644 325 NrpeltAEKFIShpfNSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVRED 404
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60472587 551 PT------CYSVPiallvlkqlqqqdqsiqQIDLNKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:cd17644 405 QPgnkrlvAYIVP-----------------HYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDR 461
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
93-551 |
2.88e-11 |
|
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: 66.08 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDgysvkslidrietitpkliittn 172
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYP----------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 173 ygifndeiitftpnlkdaielsTFKPSNVITLFRNditSESDLKKVkdiptipntlSWYDEIKKfkennqspfyeyvpve 252
Cdd:cd05907 63 ----------------------TSSAEQIAYILND---SEAKALFV----------EDPDDLAT---------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 253 sshplyIIYSSGTTGNAKAVVRSNGPnlvcmnyfdrYISEKYECTTLLTTSSVGW-VSF----HGF-----LYGMLSFGS 322
Cdd:cd05907 92 ------IIYTSGTTGRPKGVMLSHRN----------ILSNALALAERLPATEGDRhLSFlplaHVFerragLYVPLLAGA 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 323 TFVMYEGgiiknkhIEV------DFWNTI--------EKHKATHTLSLANTIRYFIktdpegtiirskYDL---SNLKEI 385
Cdd:cd05907 156 RIYFASS-------AETllddlsEVRPTVflavprvwEKVYAAIKVKAVPGLKRKL------------FDLavgGRLRFA 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 386 WVGGEVIEESIPEYIEKkLKIKPTRGYGQTEIGIAYlycfdHINIP-YYATGLPSIFIRPSifsddgkELGVNEIGEIAF 464
Cdd:cd05907 217 ASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVV-----TLNPPgDNRIGTVGKPLPGV-------EVRIADDGEILV 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 465 KlpmPPSFATTLYKNDEKFKQLFSKfPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNK-VQLNTIETSILKHPLVLEC 543
Cdd:cd05907 284 R---GPNVMLGYYKNPEATAEALDA-DGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKnISPEPIENALKASPLISQA 359
|
....*...
gi 60472587 544 CSIGINDP 551
Cdd:cd05907 360 VVIGDGRP 367
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
259-551 |
5.16e-11 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 65.46 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 259 IIYSSGTTGNAKAVVRSNgpNLVCMNYfdRYISEKYECTT---LLTTSSVGwvsfH--GFLYGM---LSFGSTFVMYegg 330
Cdd:PRK13295 202 LIYTSGTTGEPKGVMHTA--NTLMANI--VPYAERLGLGAddvILMASPMA----HqtGFMYGLmmpVMLGATAVLQ--- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 331 iiknkhievDFWNT------IEKHKATHTLslANTIryFIkTDPEGTIIRSKYDLSNLKEIWVGGEVIEESIPEYIEKKL 404
Cdd:PRK13295 271 ---------DIWDParaaelIRTEGVTFTM--ASTP--FL-TDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAAL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 405 KIKPTRGYGQTEIGIAYLYCFDHINIPYYAT-GLPSIFIRPSIFSDDGKELGVNEIGEIafKLPMPPSFATTLykndeKF 483
Cdd:PRK13295 337 GAKIVSAWGMTENGAVTLTKLDDPDERASTTdGCPLPGVEVRVVDADGAPLPAGQIGRL--QVRGCSNFGGYL-----KR 409
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60472587 484 KQLFS-KFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDP 551
Cdd:PRK13295 410 PQLNGtDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDE 478
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
91-550 |
6.66e-11 |
|
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: 65.22 E-value: 6.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 91 IKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGAThcvlfdgysvkslidrietitPKLIit 170
Cdd:cd05923 27 LRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAV---------------------PALI-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 171 tnygifndeiitfTPNLKDAiELSTF-KPSNVITLFRNDI---TSESDLKKVKDIptipnTLSwyDEIKKFKENNQSPFY 246
Cdd:cd05923 84 -------------NPRLKAA-ELAELiERGEMTAAVIAVDaqvMDAIFQSGVRVL-----ALS--DLVGLGEPESAGPLI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 247 EYVPVESSHPLYIIYSSGTTGNAKAVV---RSNGPNLVCMNYFDRYISEKYECTT-LLTTSSVgwVSFHGFLYGMLSFGS 322
Cdd:cd05923 143 EDPPREPEQPAFVFYTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRHGRHNVVLgLMPLYHV--IGFFAVLVAALALDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 323 TFVMYEggiiKNKHIEVDFWntIEKHKAThtlSLANTIRYFikTDPEGTIIRSKYDLSNLKEIWVGGEVIEESIPEYIEK 402
Cdd:cd05923 221 TYVVVE----EFDPADALKL--IEQERVT---SLFATPTHL--DALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 403 KLKIKPTRGYGQTEIgiaylycfdhINIPYYATGLPSIFIRPSIFSD---------DGKELGVNEIGEIAFKLPMPPSFA 473
Cdd:cd05923 290 HLPGEKVNIYGTTEA----------MNSLYMRDARTGTEMRPGFFSEvrivriggsPDEALANGEEGELIVAAAADAAFT 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60472587 474 TTLYKNDEKFKQLFSkfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIND 550
Cdd:cd05923 360 GYLNQPEATAKKLQD---GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVAD 433
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
345-616 |
1.57e-10 |
|
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: 63.89 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 345 IEKHKATHTLSLANTIRYFIktdpeGTIIRSKYDLSNLKEIWVGGEVIEESIPEYIEKKLKIKPTRGYGQTEIGIAYLYC 424
Cdd:cd05920 225 IEREGVTVTALVPALVSLWL-----DAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTRL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 425 FDHINIPYYATGLPsifIRPS----IFSDDGKELGVNEIGEIAFKLPMPPSfatTLYKNDEKFKQLFSKfPGYYNPGDLG 500
Cdd:cd05920 300 DDPDEVIIHTQGRP---MSPDdeirVVDEEGNPVPPGEEGELLTRGPYTIR---GYYRAPEHNARAFTP-DGFYRTGDLV 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 501 FKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDP-----TCYsvpiallvlkqlqqqdqsiqq 575
Cdd:cd05920 373 RRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDEllgerSCA--------------------- 431
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 60472587 576 idlnklqneinYIIKQDIE-SLAVLRK---------------IVIVNQLPKTKTGKI 616
Cdd:cd05920 432 -----------FVVLRDPPpSAAQLRRflrerglaayklpdrIEFVDSLPLTAVGKI 477
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
254-618 |
2.41e-10 |
|
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: 63.17 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 254 SHPLYIIYSSGTTGNAKaVVRSNGPNLVCMNYFDRYISEKYECTTLLTTSSVGWVSF---HGFLYGMLSFGSTFVMYEgg 330
Cdd:cd05929 125 AAGWKMLYSGGTTGRPK-GIKRGLPGGPPDNDTLMAAALGFGPGADSVYLSPAPLYHaapFRWSMTALFMGGTLVLME-- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 331 iiknKHIEVDFWNTIEKHKATHTlSLANTIRYFIKTDPEgtIIRSKYDLSNL--------------KEIWV--GGEVIEE 394
Cdd:cd05929 202 ----KFDPEEFLRLIERYRVTFA-QFVPTMFVRLLKLPE--AVRNAYDLSSLkrvihaaapcppwvKEQWIdwGGPIIWE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 395 SipeyiekklkikptrgYGQTEiGIAYlyCFdhINIPYYATGLPSIFiRP-----SIFSDDGKELGVNEIGEIAFKlpMP 469
Cdd:cd05929 275 Y----------------YGGTE-GQGL--TI--INGEEWLTHPGSVG-RAvlgkvHILDEDGNEVPPGEIGEVYFA--NG 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 470 PSFATTLYKNDEKFKqlfSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIN 549
Cdd:cd05929 331 PGFEYTNDPEKTAAA---RNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVP 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60472587 550 DPTCYSVPIALLVLKQLQQQDQSiqqidlnkLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:cd05929 408 DEELGQRVHAVVQPAPGADAGTA--------LAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYR 468
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
249-544 |
4.57e-10 |
|
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: 62.95 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 249 VPVESSHPLYIIYSSGTTGNAKAVVRSNGpNLVcmNYFdRYISEKYECT----TLLTTSsvgwVSFHGF---LYGMLSFG 321
Cdd:COG1020 612 VPVTPDDLAYVIYTSGSTGRPKGVMVEHR-ALV--NLL-AWMQRRYGLGpgdrVLQFAS----LSFDASvweIFGALLSG 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 322 STFVMYEGGIIKNKHievDFWNTIEKHKATHTLSLANTIRYFIKTDPEgtiirskyDLSNLKEIWVGGEVIEesiPEYIE 401
Cdd:COG1020 684 ATLVLAPPEARRDPA---ALAELLARHRVTVLNLTPSLLRALLDAAPE--------ALPSLRLVLVGGEALP---PELVR 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 402 KKLKIKPTR----GYGQTE--IGIAYLYCFDHI----NIPYyatG--LPSIFIRpsIFSDDGKELGVNEIGEiafklpmp 469
Cdd:COG1020 750 RWRARLPGArlvnLYGPTEttVDSTYYEVTPPDadggSVPI---GrpIANTRVY--VLDAHLQPVPVGVPGE-------- 816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 470 psfattLY---------------KNDEKFKQLFSKFPG--YYNPGDLGFKDENGfyTI--VSRSDDQIKISGNKVQLNTI 530
Cdd:COG1020 817 ------LYiggaglargylnrpeLTAERFVADPFGFPGarLYRTGDLARWLPDG--NLefLGRADDQVKIRGFRIELGEI 888
|
330
....*....|....
gi 60472587 531 ETSILKHPLVLECC 544
Cdd:COG1020 889 EAALLQHPGVREAV 902
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
92-551 |
5.71e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 62.21 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 92 KLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHcV-------------LFDGYSVKSLI- 157
Cdd:PRK07798 28 RLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVP-VnvnyryvedelryLLDDSDAVALVy 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 158 -----DRIETITPKLiittnygifndeiitftPNLKDAIElstfkpsnvitlfrndITSESDLkkvkdiPTIPNTLSWYD 232
Cdd:PRK07798 107 erefaPRVAEVLPRL-----------------PKLRTLVV----------------VEDGSGN------DLLPGAVDYED 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 233 EIKkfkenNQSPfyEYVPVE-SSHPLYIIYSSGTTGNAKAVV-------RS--NGPNLVCMNyfdrYISEKYECTTLLTT 302
Cdd:PRK07798 148 ALA-----AGSP--ERDFGErSPDDLYLLYTGGTTGMPKGVMwrqedifRVllGGRDFATGE----PIEDEEELAKRAAA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 303 SSVG--------------WVSFHGFLygmlsFGSTFVMYEggiiKNKHIEVDFWNTIEKHKAThtlslantiRYFIKTD- 367
Cdd:PRK07798 217 GPGMrrfpapplmhgagqWAAFAALF-----SGQTVVLLP----DVRFDADEVWRTIEREKVN---------VITIVGDa 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 368 ---P--EGTIIRSKYDLSNLKEIWVGGEVIEesiPEYIEKKLKIKPTR----GYGQTEIGIAYLYCFDHINIPyyaTGLP 438
Cdd:PRK07798 279 marPllDALEARGPYDLSSLFAIASGGALFS---PSVKEALLELLPNVvltdSIGSSETGFGGSGTVAKGAVH---TGGP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 439 SIFIRPS--IFSDDGKEL--GVNEIGEIAFKLPMPpsfatTLYKND-EKFKQLFSKFPG--YYNPGDLGFKDENGFYTIV 511
Cdd:PRK07798 353 RFTIGPRtvVLDEDGNPVepGSGEIGWIARRGHIP-----LGYYKDpEKTAETFPTIDGvrYAIPGDRARVEADGTITLL 427
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 60472587 512 SRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDP 551
Cdd:PRK07798 428 GRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDE 467
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
221-618 |
5.76e-10 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 62.14 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 221 IPTIPNTLSWYDEIKKFKENNQSPFYEYVPV--ESSHPLYIIYSSGTTGNAKAVVRSNGPNLVCMN----YFDRYISEKY 294
Cdd:PLN03051 84 VPLREQDLSWCDFLGVAAAQGSVGGNEYSPVyaPVESVTNILFSSGTTGEPKAIPWTHLSPLRCASdgwaHMDIQPGDVV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 295 ECTTllttsSVGWVSFHGFLYGMLSFGSTFVMYEGGIIKNkhievDFWNTIEKHKATHTLSLANTIRYFIKTdpeGTIIR 374
Cdd:PLN03051 164 CWPT-----NLGWMMGPWLLYSAFLNGATLALYGGAPLGR-----GFGKFVQDAGVTVLGLVPSIVKAWRHT---GAFAM 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 375 SKYDLSNLKEIWVGGEVieesipEYIEKKLKIKPTRGY--------GQTEIGIAYLY-CFDHINIPyYATGLPSIFIRPS 445
Cdd:PLN03051 231 EGLDWSKLRVFASTGEA------SAVDDVLWLSSVRGYykpvieycGGTELASGYISsTLLQPQAP-GAFSTASLGTRFV 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 446 IFSDDGKELG--VNEIGEIAfkLPMPPSFATTLYKNDEKFKQLFSKFPGYYNP-------GDLGFKDENGFYTIVSRSDD 516
Cdd:PLN03051 304 LLNDNGVPYPddQPCVGEVA--LAPPMLGASDRLLNADHDKVYYKGMPMYGSKgmplrrhGDIMKRTPGGYFCVQGRADD 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 517 QIKISGNKVQLNTIETSILK-HPLVLECCSIGINDPTcySVPIALLVLKQLQQQDQSIQQIDLNKLQNEINYIIKQDIES 595
Cdd:PLN03051 382 TMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPD--GGPELLVIFLVLGEEKKGFDQARPEALQKKFQEAIQTNLNP 459
|
410 420
....*....|....*....|...
gi 60472587 596 LAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:PLN03051 460 LFKVSRVKIVPELPRNASNKLLR 482
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
88-536 |
7.14e-10 |
|
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: 61.56 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 88 KKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLfDGysvKSLIDRIETI---- 163
Cdd:cd17653 18 SLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPL-DA---KLPSARIQAIlrts 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 164 TPKLIITTNygifndeiitftpnlkdaielstfkpsnvitlfrnditSESDLKkvkdiptipntlswydeikkfkennqs 243
Cdd:cd17653 94 GATLLLTTD--------------------------------------SPDDLA--------------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 244 pfyeyvpvesshplYIIYSSGTTGNAKAVV--RSNGPNLVCMNYFDRYISEKyecTTLLTTSSVGWVSFHGFLYGMLSFG 321
Cdd:cd17653 109 --------------YIIFTSGSTGIPKGVMvpHRGVLNYVSQPPARLDVGPG---SRVAQVLSIAFDACIGEIFSTLCNG 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 322 STFVMyeggiiknKHIEVDFWNTIEKHKATH-TLSLANTIRyfiktdPEgtiirskyDLSNLKEIWVGGEVIEESIPEyi 400
Cdd:cd17653 172 GTLVL--------ADPSDPFAHVARTVDALMsTPSILSTLS------PQ--------DFPNLKTIFLGGEAVPPSLLD-- 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 401 ekklKIKPTR----GYGQTEIGIAYLYC------FDHINIPyyatgLPSIFIRpsIFSDDGKELGVNEIGEIAFklpMPP 470
Cdd:cd17653 228 ----RWSPGRrlynAYGPTECTISSTMTellpgqPVTIGKP-----IPNSTCY--ILDADLQPVPEGVVGEICI---SGV 293
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60472587 471 SFATTLYKNDEK--FKQLFSKF-PG--YYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILK 536
Cdd:cd17653 294 QVARGYLGNPALtaSKFVPDPFwPGsrMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQ 364
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
372-551 |
8.48e-10 |
|
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: 60.75 E-value: 8.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 372 IIRSKYDLSNLKEiwVGGevIEesIPEYIEKKLKIKPTR---GYGQTEI-GIAYLYcfdhiniPYY----ATGLPSIFIR 443
Cdd:cd17637 106 AEKSGVDLSSLRH--VLG--LD--APETIQRFEETTGATfwsLYGQTETsGLVTLS-------PYRerpgSAGRPGPLVR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 444 PSIFSDDGKELGVNEIGEIAFKLPMppSFATtLYKNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRS--DDQIKIS 521
Cdd:cd17637 173 VRIVDDNDRPVPAGETGEIVVRGPL--VFQG-YWNLPELTAYTFRN--GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPG 247
|
170 180 190
....*....|....*....|....*....|
gi 60472587 522 GNKVQLNTIETSILKHPLVLECCSIGINDP 551
Cdd:cd17637 248 GENVYPAEVEKVILEHPAIAEVCVIGVPDP 277
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
259-616 |
8.52e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 259 IIYSSGTTGNAKAV--------VRSNGPNLVCM--NYFDryISEK---YECTTLLTTSSVGWVSFhgflygMLSFGSTFV 325
Cdd:PRK13390 153 MLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIarAFYD--ISESdiyYSSAPIYHAAPLRWCSM------VHALGGTVV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 326 MyeggiiKNKHIEVDFWNTIEKHKATHTLSLANTIRYFIKTDPEgtiIRSKYDLSNLKEiwvggeVIEESIPEYIEKKLK 405
Cdd:PRK13390 225 L------AKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDAD---VRTRYDVSSLRA------VIHAAAPCPVDVKHA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 406 IKPTRG------YGQTEI-GIAYLYCFDHINIPyyATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLPMPPsFAttlYK 478
Cdd:PRK13390 290 MIDWLGpivyeyYSSTEAhGMTFIDSPDWLAHP--GSVGRSVLGDLHICDDDGNELPAGRIGTVYFERDRLP-FR---YL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 479 ND-EKFKQL-FSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSV 556
Cdd:PRK13390 364 NDpEKTAAAqHPAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQ 443
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 557 PIALLVLKQLQQQDqsiqqidlNKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKI 616
Cdd:PRK13390 444 VKAVIQLVEGIRGS--------DELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
259-550 |
9.72e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 61.55 E-value: 9.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 259 IIYSSGTTGNAKAVVRSngPNL-----VCMNYFDRyisekyecTTLLTTS--SVGWVSFHGFLYGMLSFGstfVMYEGGI 331
Cdd:PRK13383 179 VLLTSGTTGKPKGVPRA--PQLrsavgVWVTILDR--------TRLRTGSriSVAMPMFHGLGLGMLMLT---IALGGTV 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 332 IKNKHIEVDfwNTIEK---HKATHTLSLANTIRYFIKTDPEgtiIRSKYDLSNLKEIWVGGEVIEESIPEYIEKKLKIKP 408
Cdd:PRK13383 246 LTHRHFDAE--AALAQaslHRADAFTAVPVVLARILELPPR---VRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDIL 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 409 TRGYGQTEIGIAYLYCFDHINIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIAfklpMPPSFATTLYkNDEKFKQLFS 488
Cdd:PRK13383 321 YNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIF----VGGELAGTRY-TDGGGKAVVD 395
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60472587 489 kfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIND 550
Cdd:PRK13383 396 ---GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPD 454
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
258-624 |
4.19e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 60.36 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 258 YIIYSSGTTGNAKAVVRSNGP--NLVCmnyfdrYISEKYECTT---LLTTSSVGWVSFHGFLYGMLSFGSTFVMYEGGIi 332
Cdd:PRK12316 4698 YVIYTSGSTGRPKGVAVSHGSlvNHLH------ATGERYELTPddrVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSL- 4770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 333 knkHIEVDFWNTIEKHKATHTLSLANTIRYFIKTDPEgtiirsKYDLSNLKEIWVGGEVIEESipEYIEKKLKIKPTR-- 410
Cdd:PRK12316 4771 ---WDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAER------DGEPPSLRVYCFGGEAVAQA--SYDLAWRALKPVYlf 4839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 411 -GYGQTEIGIAYLyCFDhiNIPYYATGLPSIFIrpsifsddGKELGvneiGEIAFKL-----PMPPSFATTLYKNDEKFK 484
Cdd:PRK12316 4840 nGYGPTETTVTVL-LWK--ARDGDACGAAYMPI--------GTPLG----NRSGYVLdgqlnPLPVGVAGELYLGGEGVA 4904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 485 QLFSKFPGY-----------------YNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIG 547
Cdd:PRK12316 4905 RGYLERPALtaerfvpdpfgapggrlYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIA 4984
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 548 INDPT-----CYSVPIALLVLKQLQQQDqsiqqidlnKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPIIS 622
Cdd:PRK12316 4985 QEGAVgkqlvGYVVPQDPALADADEAQA---------ELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALP 5055
|
..
gi 60472587 623 KF 624
Cdd:PRK12316 5056 QP 5057
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
257-552 |
4.19e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 58.93 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 257 LYIIYSSGTTGNAKAVVRS---------NGPNLVCMNYFDRYISEKYECTTLLTTS---------SVGWVSFHGFLygml 318
Cdd:cd05924 6 LYILYTGGTTGMPKGVMWRqedifrmlmGGADFGTGEFTPSEDAHKAAAAAAGTVMfpapplmhgTGSWTAFGGLL---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 319 sFGSTFVmyeggIIKNKHIEVDFWNTIEKHKAThTLSLANTI--RYFIKT-DPEGTiirskYDLSNLKEIWVGGEVIEES 395
Cdd:cd05924 82 -GGQTVV-----LPDDRFDPEEVWRTIEKHKVT-SMTIVGDAmaRPLIDAlRDAGP-----YDLSSLFAISSGGALLSPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 396 IPEYIekkLKIKP----TRGYGQTEIGIAYLycfdHINIPYYATGLPSIFIRPS--IFSDDGKEL--GVNEIGEIAFKLP 467
Cdd:cd05924 150 VKQGL---LELVPnitlVDAFGSSETGFTGS----GHSAGSGPETGPFTRANPDtvVLDDDGRVVppGSGGVGWIARRGH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 468 MPPSFattlYKNDEKFKQLFSKFPG--YYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCS 545
Cdd:cd05924 223 IPLGY----YGDEAKTAETFPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLV 298
|
....*..
gi 60472587 546 IGINDPT 552
Cdd:cd05924 299 VGRPDER 305
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
251-540 |
5.18e-09 |
|
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: 58.86 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 251 VESSHPLYIIYSSGTTGNAKAVVRSNGpNLvcmnyfdryisekyecTTLL--TTSSVG------WVSFHGF--------L 314
Cdd:cd17643 90 TDPDDLAYVIYTSGSTGRPKGVVVSHA-NV----------------LALFaaTQRWFGfneddvWTLFHSYafdfsvweI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 315 YGMLSFGSTFVMYEGGIIKNkhiEVDFWNTIEKHKAT---HTLSlanTIRYFIKTDPEGTIirskyDLSNLKEIWVGGEV 391
Cdd:cd17643 153 WGALLHGGRLVVVPYEVARS---PEDFARLLRDEGVTvlnQTPS---AFYQLVEAADRDGR-----DPLALRYVIFGGEA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 392 IE-ESIPEYIEKKLKIKP--TRGYGQTEIGI---------AYLYCFDHINIpyyATGLPSIFIRpsIFSDDGKELGVNEI 459
Cdd:cd17643 222 LEaAMLRPWAGRFGLDRPqlVNMYGITETTVhvtfrpldaADLPAAAASPI---GRPLPGLRVY--VLDADGRPVPPGVV 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 460 GEIAFKLPMppsfATTLYKN-----DEKFKQLFSKFPG--YYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIET 532
Cdd:cd17643 297 GELYVSGAG----VARGYLGrpeltAERFVANPFGGPGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEA 372
|
....*...
gi 60472587 533 SILKHPLV 540
Cdd:cd17643 373 ALATHPSV 380
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
92-542 |
5.55e-09 |
|
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: 58.88 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 92 KLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVksliDRIEtitpkliitt 171
Cdd:cd17655 22 TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPE----ERIQ---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 172 nYgIFNDEIITFtpnlkdaieLSTFKPSNVITLFRNDITSESDlkkvkdiptipntlswyDEIKKFKENNQSPfyeyvPV 251
Cdd:cd17655 88 -Y-ILEDSGADI---------LLTQSHLQPPIAFIGLIDLLDE-----------------DTIYHEESENLEP-----VS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 252 ESSHPLYIIYSSGTTGNAKAVV--RSNGPNLVcmNYFDRYISeKYECTTLLTTSSVGWVSFHGFLYGMLSFGSTFVMYEG 329
Cdd:cd17655 135 KSDDLAYVIYTSGSTGKPKGVMieHRGVVNLV--EWANKVIY-QGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRK 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 330 GIIKNKHIEVDFwntIEKHKATHT------LSLANTIRyfiktDPEGtiirskydlSNLKEIWVGGEVIEESIPEYIEKK 403
Cdd:cd17655 212 ETVLDGQALTQY---IRQNRITIIdltpahLKLLDAAD-----DSEG---------LSLKHLIVGGEALSTELAKKIIEL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 404 LKIKP--TRGYGQTEIGI---AYLYCFDHINIPYYATGLPSIFIRPSIFSDDGKELGVNEIGE--IA--------FKLPm 468
Cdd:cd17655 275 FGTNPtiTNAYGPTETTVdasIYQYEPETDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGElyIGgegvargyLNRP- 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60472587 469 ppsfatTLykNDEKFKQlfSKF-PG--YYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLE 542
Cdd:cd17655 354 ------EL--TAEKFVD--DPFvPGerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKE 420
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
94-551 |
6.15e-09 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 58.60 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 94 TYYQLYEKVCEFSRVLL-NLNISKNDNVLIYMANTLEPLIAMLSCARIGAThcvlfdgysvkslidrietitPKLIittN 172
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA---------------------PAFI---N 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 173 YgifndeiitftpNLKDAIELSTFKPSNVITLFRNDitsesdlkkvkDIPTIpntlswydeikkfkennqspfyeyvpve 252
Cdd:cd05937 63 Y------------NLSGDPLIHCLKLSGSRFVIVDP-----------DDPAI---------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 253 sshplyIIYSSGTTGNAKAVVRSNGPNLVCMNYFDRYISEK-----YECTTLlttssvgwvsFHG--FLYGM---LSFGS 322
Cdd:cd05937 92 ------LIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKngdrtYTCMPL----------YHGtaAFLGAcncLMSGG 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 323 TFvmyeggIIKNKHIEVDFWNTIEKHKATHTLSLANTIRYFIKTDPegtiirSKYDlSNLKEIWVGGEVIEESIPEYIEK 402
Cdd:cd05937 156 TL------ALSRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPP------SPYD-RDHKVRVAWGNGLRPDIWERFRE 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 403 KLKIkPTRG--YGQTEiGIAYLycFDHINIPYyatGLPSI----FIRPSIFSDD---------------------GKELG 455
Cdd:cd05937 223 RFNV-PEIGefYAATE-GVFAL--TNHNVGDF---GAGAIghhgLIRRWKFENQvvlvkmdpetddpirdpktgfCVRAP 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 456 VNEIGEIAFKLPMPPSFATTLYKNDEKFKQ------LFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNT 529
Cdd:cd05937 296 VGEPGEMLGRVPFKNREAFQGYLHNEDATEsklvrdVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTE 375
|
490 500
....*....|....*....|..
gi 60472587 530 IETSILKHPLVLECCSIGINDP 551
Cdd:cd05937 376 VADVLGAHPDIAEANVYGVKVP 397
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
259-551 |
6.26e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 58.93 E-value: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 259 IIYSSGTTGNAKAVVR--SNGPNLVCMNYFD------RYISE-KYECTT-LLTTSSVGWVSFhgflygMLSFGSTFVMYE 328
Cdd:PRK13391 159 MLYSSGTTGRPKGIKRplPEQPPDTPLPLTAflqrlwGFRSDmVYLSPApLYHSAPQRAVML------VIRLGGTVIVME 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 329 ggiiknkHIEVD-FWNTIEKHKATHTLSLANTIRYFIKTdPEGtiIRSKYDLSNLK------------------EIWvgG 389
Cdd:PRK13391 233 -------HFDAEqYLALIEEYGVTHTQLVPTMFSRMLKL-PEE--VRDKYDLSSLEvaihaaapcppqvkeqmiDWW--G 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 390 EVIEEsipeYiekklkikptrgYGQTEiGIAYLYCFDHINIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIAFKLPMP 469
Cdd:PRK13391 301 PIIHE----Y------------YAATE-GLGFTACDSEEWLAHPGTVGRAMFGDLHILDDDGAELPPGEPGTIWFEGGRP 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 470 PSfattlYKND-EKFKQLFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIkISGN-KVQLNTIETSILKHPLVLECCSIG 547
Cdd:PRK13391 364 FE-----YLNDpAKTAEARHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMI-ISGGvNIYPQEAENLLITHPKVADAAVFG 437
|
....
gi 60472587 548 INDP 551
Cdd:PRK13391 438 VPNE 441
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
411-621 |
1.21e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 57.89 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 411 GYGQTEIGIAYLYCFDH--INIPYYATGL--PSIFIRpsIFSDDGKELGVNEIGEIAFKlpmPPSFATTLYKNDEKFKQL 486
Cdd:PRK09088 282 GFGMSEAGTVFGMSVDCdvIRAKAGAAGIptPTVQTR--VVDDQGNDCPAGVPGELLLR---GPNLSPGYWRRPQATARA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 487 FSKfPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALLVLKQL 566
Cdd:PRK09088 357 FTG-DGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 60472587 567 QQQDQSiqqidlnklqnEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPII 621
Cdd:PRK09088 436 APLDLE-----------RIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
345-551 |
1.52e-08 |
|
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: 57.46 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 345 IEKHKATHTL---SLA----NTIRyfiktdpegtiiRSKYDLSNLKEIWVGGEVIEESIPEYIEKKLKIKPTRGYGQTEi 417
Cdd:COG1021 270 IERERVTVTAlvpPLAllwlDAAE------------RSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 418 GiayLYCF-------DHInipyYAT-GLPsifIRPS----IFSDDGKELGVNEIGEIAFKLPMppsfatTL---YKNDEK 482
Cdd:COG1021 337 G---LVNYtrlddpeEVI----LTTqGRP---ISPDdevrIVDEDGNPVPPGEVGELLTRGPY------TIrgyYRAPEH 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60472587 483 FKQLFSKfPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDP 551
Cdd:COG1021 401 NARAFTP-DGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDE 468
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
94-621 |
1.69e-08 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 57.68 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 94 TYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGAthcvLFDGYSVKSLIDRI----ETITPKLII 169
Cdd:PLN02330 57 TYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG----VFSGANPTALESEIkkqaEAAGAKLIV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 170 T--TNYGIFNdeiitftpnlkdAIELStfkpsnVITLFRNditsesdlkkvkdipTIPNTLSWYDEIKKFKENNQSPFYE 247
Cdd:PLN02330 133 TndTNYGKVK------------GLGLP------VIVLGEE---------------KIEGAVNWKELLEAADRAGDTSDNE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 248 yvPVESSHPLYIIYSSGTTGNAKAVVRSNgPNLVCmNYfdryisekyeCTTLLTTSS--VGWVS-------FHgfLYGML 318
Cdd:PLN02330 180 --EILQTDLCALPFSSGTTGISKGVMLTH-RNLVA-NL----------CSSLFSVGPemIGQVVtlglipfFH--IYGIT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 319 SFGSTFVMYEGGIIKNKHIEVD-FWNTIEKHKATHTLSLANTIRYFIKtDPegtiIRSKYDLSNLK--EIWVGGEVIEES 395
Cdd:PLN02330 244 GICCATLRNKGKVVVMSRFELRtFLNALITQEVSFAPIVPPIILNLVK-NP----IVEEFDLSKLKlqAIMTAAAPLAPE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 396 IPEYIEKKL-KIKPTRGYGQTEIGIAYLYCFDhiniPYYATG----------LPSI---FIRPsifsDDGKELGVNEIGE 461
Cdd:PLN02330 319 LLTAFEAKFpGVQVQEAYGLTEHSCITLTHGD----PEKGHGiakknsvgfiLPNLevkFIDP----DTGRSLPKNTPGE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 462 IAFKlpmPPSFATTLYKNDEKFKQLFSKfPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVL 541
Cdd:PLN02330 391 LCVR---SQCVMQGYYNNKEETDRTIDE-DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 542 ECCSIGINDPTCYSVPIALLVLKQLQQqdqsiqqidlNKLQNEINYiIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPII 621
Cdd:PLN02330 467 DAAVVPLPDEEAGEIPAACVVINPKAK----------ESEEDILNF-VAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
381-618 |
2.10e-08 |
|
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: 57.07 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 381 NLKEIWVGGEVIEESIPEYIeKKLKIKPTRGYGQTEIGIayLYCFDHIN-IPYYATGLPSIFIRPSIFSDDGKelgvNEI 459
Cdd:cd05914 235 NIKEFVIGGAKINPDVEEFL-RTIGFPYTIGYGMTETAP--IISYSPPNrIRLGSAGKVIDGVEVRIDSPDPA----TGE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 460 GEIAFKlpmPPSFATTLYKNDEKFKQLFSKfPGYYNPGDLGFKDENGFYTIVSRSDDQIKI-SGNKVQLNTIETSILKHP 538
Cdd:cd05914 308 GEIIVR---GPNVMKGYYKNPEATAEAFDK-DGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMP 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 539 LVLECCSIGINDPTCYSVPIALLVLKQLQQQDQSIQQIDLNKLQNEINyiikQDIESLAVLRKIVIVNQ-LPKTKTGKIP 617
Cdd:cd05914 384 FVLESLVVVQEKKLVALAYIDPDFLDVKALKQRNIIDAIKWEVRDKVN----QKVPNYKKISKVKIVKEeFEKTPKGKIK 459
|
.
gi 60472587 618 R 618
Cdd:cd05914 460 R 460
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
249-624 |
2.38e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 57.86 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 249 VPVESSHPLYIIYSSGTTGNAKAVVRSNGP--NLVCMnyfdryISEKYECTTLLTTSSVGWVSFHGF---LYGMLSFGST 323
Cdd:PRK12467 651 VALDPDNLAYVIYTSGSTGQPKGVAISHGAlaNYVCV------IAERLQLAADDSMLMVSTFAFDLGvteLFGALASGAT 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 324 FVMYEGGIIKNKHievDFWNTIEKHKATHTLSLANTIRYFIKtDPEGTIIRSkydlsnLKEIWVGGEVIEESIPEYI-EK 402
Cdd:PRK12467 725 LHLLPPDCARDAE---AFAALMADQGVTVLKIVPSHLQALLQ-ASRVALPRP------QRALVCGGEALQVDLLARVrAL 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 403 KLKIKPTRGYGQTE--IGIAYLYCFDHiNIPYYATGLPSIFIRPSIFSDDGkELGvneigeiafklPMPPSFATTLYKND 480
Cdd:PRK12467 795 GPGARLINHYGPTEttVGVSTYELSDE-ERDFGNVPIGQPLANLGLYILDH-YLN-----------PVPVGVVGELYIGG 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 481 EKFKQLFSKFPG-----------------YYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHP----- 538
Cdd:PRK12467 862 AGLARGYHRRPAltaerfvpdpfgadggrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPgvrea 941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 539 LVLECCSIGINDPTCYSVPIALLVLKQLQQqdqsiqqidlnkLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:PRK12467 942 VVLAQPGDAGLQLVAYLVPAAVADGAEHQA------------TRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDR 1009
|
....*.
gi 60472587 619 PIISKF 624
Cdd:PRK12467 1010 KALPKP 1015
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
494-619 |
2.48e-08 |
|
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: 56.76 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 494 YNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIND----PT--CYSVP----IALLVL 563
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDkdeePTlvSYIVPrfdkPDDESF 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60472587 564 KQLQQQDQSIQQIDLN------KLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRP 619
Cdd:cd17647 454 AQEDVPKEVSTDPIVKgligyrKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKP 515
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
220-542 |
3.24e-08 |
|
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: 56.58 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 220 DIPTIPNTLSWYDEIKKFKENNQSPFyeyVPVESSHPLYIIYSSGTTGNAKAVVRSNGP--NLVcmNYFDRYISEKYECT 297
Cdd:cd17651 105 ELAVELVAVTLLDQPGAAAGADAEPD---PALDADDLAYVIYTSGSTGRPKGVVMPHRSlaNLV--AWQARASSLGPGAR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 298 TLLTtSSVGW-VSFHGfLYGMLSFGSTFVmyeggiIKNKHIEVD---FWNTIEKHKATHTLSLANTIRYFIK-TDPEGTI 372
Cdd:cd17651 180 TLQF-AGLGFdVSVQE-IFSTLCAGATLV------LPPEEVRTDppaLAAWLDEQRISRVFLPTVALRALAEhGRPLGVR 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 373 irskydLSNLKEIWVGGE--VIEESIPEYIEKKLKIKPTRGYGQTEIGIAYLYCFDhiNIPYYATGLPSIFiRPSifsdD 450
Cdd:cd17651 252 ------LAALRYLLTGGEqlVLTEDLREFCAGLPGLRLHNHYGPTETHVVTALSLP--GDPAAWPAPPPIG-RPI----D 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 451 GKELGVNEigeiAFKLPMPPSFATTLY---------------KNDEKFKQL-FSKFPGYYNPGDLGFKDENGFYTIVSRS 514
Cdd:cd17651 319 NTRVYVLD----AALRPVPPGVPGELYiggaglargylnrpeLTAERFVPDpFVPGARMYRTGDLARWLPDGELEFLGRA 394
|
330 340
....*....|....*....|....*...
gi 60472587 515 DDQIKISGNKVQLNTIETSILKHPLVLE 542
Cdd:cd17651 395 DDQVKIRGFRIELGEIEAALARHPGVRE 422
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
256-542 |
4.09e-08 |
|
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: 55.94 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 256 PLYIIYSSGTTGNAKAVVRSNGpNLVCMNY-FDRYISEKYECTTLLTTSSVGWVSFHGFLYGMLSFGSTFVMYEGGIIKN 334
Cdd:cd17650 95 LAYVIYTSGTTGKPKGVMVEHR-NVAHAAHaWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLD 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 335 khiEVDFWNTIEKHKATHTLSLANTIRYFIKTdpegtIIRSKYDLSNLKEIWVGGEV--IEESIPEYIEKKLKIKPTRGY 412
Cdd:cd17650 174 ---PAALYDLILKSRITLMESTPALIRPVMAY-----VYRNGLDLSAMRLLIVGSDGckAQDFKTLAARFGQGMRIINSY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 413 GQTEIGIaylycfdhiNIPYYATGLPSIfiRPSIFSDDGKELGVNEIGEIAFKL-PMPPSFATTL----------YKND- 480
Cdd:cd17650 246 GVTEATI---------DSTYYEEGRDPL--GDSANVPIGRPLPNTAMYVLDERLqPQPVGVAGELyiggagvargYLNRp 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60472587 481 ----EKFKQL-FSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLE 542
Cdd:cd17650 315 eltaERFVENpFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE 381
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
76-547 |
4.17e-08 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 56.26 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 76 DQDALIYecPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFdgysvks 155
Cdd:COG1022 26 DRVALRE--KEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIY------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 156 lidriETITPKLIIttnYgIFNDeiitftpnlkdaielstfkpSNVITLF-------------RNDITSesdLKKV---- 218
Cdd:COG1022 97 -----PTSSAEEVA---Y-ILND--------------------SGAKVLFvedqeqldkllevRDELPS---LRHIvvld 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 219 -KDIPTIPNTLSWyDEIKKFKENNQSP-FYEYVP--VESSHPLYIIYSSGTTGNAKAVVRSNGpNLV--CMNYFDRY-IS 291
Cdd:COG1022 145 pRGLRDDPRLLSL-DELLALGREVADPaELEARRaaVKPDDLATIIYTSGTTGRPKGVMLTHR-NLLsnARALLERLpLG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 292 EKYECTTLLTTSSVG--WVSFHGFLYG---------------MLSFGSTFVM-----YEGgiIKNKhIEVdfwnTIEKHK 349
Cdd:COG1022 223 PGDRTLSFLPLAHVFerTVSYYALAAGatvafaespdtlaedLREVKPTFMLavprvWEK--VYAG-IQA----KAEEAG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 350 AT------HTLSLAntIRYFIKTD---PEGTIIRSKYDL------SNLKEIwVGGEVI-----EESIPEYIEK-----KL 404
Cdd:COG1022 296 GLkrklfrWALAVG--RRYARARLagkSPSLLLRLKHALadklvfSKLREA-LGGRLRfavsgGAALGPELARffralGI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 405 KIKptRGYGQTEI-GIAYLYCFDHINIpyyAT-GLPSifirpsifsdDGKELGVNEIGEIAFKLPMppsfaTTL--YKND 480
Cdd:COG1022 373 PVL--EGYGLTETsPVITVNRPGDNRI---GTvGPPL----------PGVEVKIAEDGEILVRGPN-----VMKgyYKNP 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 481 EKFKQLFSKfPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKV---QLntIETSILKHPLVLECCSIG 547
Cdd:COG1022 433 EATAEAFDA-DGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNvapQP--IENALKASPLIEQAVVVG 499
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
93-543 |
6.33e-08 |
|
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: 55.38 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVksliDRIETI----TPKLI 168
Cdd:cd12116 13 LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPA----DRLRYIledaEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 169 ITTnygifndeiitftPNLKDaielstfkpsnviTLFRNDITSESDLKKVKDIPTIPNTlswydeikkfkennqspfyey 248
Cdd:cd12116 89 LTD-------------DALPD-------------RLPAGLPVLLLALAAAAAAPAAPRT--------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 249 vPVESSHPLYIIYSSGTTGNAKAVVRSNGpNLVC----MNyfdRYISEKYECTTL-LTTssvgwvsfHGF------LYGM 317
Cdd:cd12116 122 -PVSPDDLAYVIYTSGSTGRPKGVVVSHR-NLVNflhsMR---ERLGLGPGDRLLaVTT--------YAFdislleLLLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 318 LSFGSTFVMYEGGIIKNKHIEVDfwnTIEKHKATHTLSLANTIRYFIKTDPEGtiirskydLSNLKeIWVGGEVIEESIP 397
Cdd:cd12116 189 LLAGARVVIAPRETQRDPEALAR---LIEAHSITVMQATPATWRMLLDAGWQG--------RAGLT-ALCGGEALPPDLA 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 398 EYIekklkIKPTRG----YGQTEIGIAYLYCF-----DHINIpyyatGLPSIFIRPSIFSDDGKELGVNEIGEIAFKlpm 468
Cdd:cd12116 257 ARL-----LSRVGSlwnlYGPTETTIWSTAARvtaaaGPIPI-----GRPLANTQVYVLDAALRPVPPGVPGELYIG--- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 469 PPSFATTLYKN----DEKFKQLFSKFPG--YYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLE 542
Cdd:cd12116 324 GDGVAQGYLGRpaltAERFVPDPFAGPGsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQ 403
|
.
gi 60472587 543 C 543
Cdd:cd12116 404 A 404
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
6-618 |
9.99e-08 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 55.09 E-value: 9.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 6 NPFNYLNDF-NYANSYPEAFWDEVakknvfWDKMYDK--------VYSGDEMYP--DWFKGGELNTCYNVLdiqVQNPLK 74
Cdd:PLN03052 117 DPISSFSEFqRFSVENPEVYWSIV------LDELSLVfsvpprciLDTSDESNPggQWLPGAVLNVAECCL---TPKPSK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 75 RDQD-ALIY------ECPYLKKTIKltyyQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLScarigathcVL 147
Cdd:PLN03052 188 TDDSiAIIWrdegsdDLPVNRMTLS----ELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLA---------II 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 148 FDGYSVKSLIDRI--ETITPKLIITTNYGIFNDEIItftpnLKDAIELSTF------KPSNVITLfrNDITSESDLK-KV 218
Cdd:PLN03052 255 LAGCVVVSIADSFapSEIATRLKISKAKAIFTQDVI-----VRGGKSIPLYsrvveaKAPKAIVL--PADGKSVRVKlRE 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 219 KDiptipntLSWYDEIKKfkENNQSPFYEYVPVESSHPLY--IIYSSGTTGNAKAVVRSNGPNLVCMNyfDRYI-SEKYE 295
Cdd:PLN03052 328 GD-------MSWDDFLAR--ANGLRRPDEYKAVEQPVEAFtnILFSSGTTGEPKAIPWTQLTPLRAAA--DAWAhLDIRK 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 296 CTTLLTTSSVGWVSFHGFLYGMLSFGSTFVMYEGGIIKNkhievDFWNTIEKHKATHTLSLANTIRYFIKTDpegtiIRS 375
Cdd:PLN03052 397 GDIVCWPTNLGWMMGPWLVYASLLNGATLALYNGSPLGR-----GFAKFVQDAKVTMLGTVPSIVKTWKNTN-----CMA 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 376 KYDLSNLKEIWVGGEVieESIPEYI--EKKLKIKPTRGY-GQTEIGIAYLycfdhinipyyaTG------------LPSI 440
Cdd:PLN03052 467 GLDWSSIRCFGSTGEA--SSVDDYLwlMSRAGYKPIIEYcGGTELGGGFV------------TGsllqpqafaafsTPAM 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 441 FIRPSIFSDDGKELGVNE--IGEIAFklpMPPSF-ATTLYKNDEKFKQLFSKFPGYYNP-----GDLGFKDENGFYTIVS 512
Cdd:PLN03052 533 GCKLFILDDSGNPYPDDApcTGELAL---FPLMFgASSTLLNADHYKVYFKGMPVFNGKilrrhGDIFERTSGGYYRAHG 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 513 RSDDQIKISGNKVQLNTIETSILK-HPLVLECCSIGINDPTcySVP----IAllvlkqLQQQDQSIQQIDLNKLQNEINY 587
Cdd:PLN03052 610 RADDTMNLGGIKVSSVEIERVCNAaDESVLETAAIGVPPPG--GGPeqlvIA------AVLKDPPGSNPDLNELKKIFNS 681
|
650 660 670
....*....|....*....|....*....|.
gi 60472587 588 IIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:PLN03052 682 AIQKKLNPLFKVSAVVIVPSFPRTASNKVMR 712
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
249-618 |
2.43e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 54.58 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 249 VPVESSHPLYIIYSSGTTGNAKAVVRSNGPnlvcMNYFDRYISEKYECTTLLTTSSVGWVSFHGF---LYGMLSFGSTFV 325
Cdd:PRK12316 3191 IRTMPENLAYVIYTSGSTGKPKGVGIRHSA----LSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFveeLFWPLMSGARVV 3266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 326 MYEGGIiknkhievdfWNTIEKHKATHTLSLANTIRYFIKTDPEGTIIRSKYDLSNLKEIWVGGEVIEESIPEYIEKKLK 405
Cdd:PRK12316 3267 LAGPED----------WRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP 3336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 406 IKPTRGYGQTEIGIAYLYCFDHiNIPYYATGLPSIFIRPSIFSDDGKELGVNEIGE--IAFKLPMPPSFATTLYKNDEKF 483
Cdd:PRK12316 3337 LYNLYGPTEATITVTHWQCVEE-GKDAVPIGRPIANRACYILDGSLEPVPVGALGElyLGGEGLARGYHNRPGLTAERFV 3415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 484 KQLFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDP--TCYSVPIALL 561
Cdd:PRK12316 3416 PDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRqlVAYVVPEDEA 3495
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 60472587 562 VlkqlqqqdqsiqqidlnKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:PRK12316 3496 G-----------------DLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDR 3535
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
344-616 |
4.58e-07 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 53.39 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 344 TIEKHKATHTLSLANTIRYFI---KTDPEgtiirskyDLSNLKEIWVGGEVIEESIPEYIEKKLKIKPTRGYGQTEIG-- 418
Cdd:PRK08633 867 LVAKHRATILLGTPTFLRLYLrnkKLHPL--------MFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSpv 938
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 419 IAylycfdhINIP-------YYATG---------LPSIFIR---PsifsDDGKELGVNEIGEIAFKLP--MppsfaTTLY 477
Cdd:PRK08633 939 AS-------VNLPdvlaadfKRQTGskegsvgmpLPGVAVRivdP----ETFEELPPGEDGLILIGGPqvM-----KGYL 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 478 KNDEKFKQLF--SKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILK--HPLVLECCSIGINDP-- 551
Cdd:PRK08633 1003 GDPEKTAEVIkdIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEkk 1082
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60472587 552 --------TCYSVPIAllvlkqlqqqdqsiqqidlnKLQNEinyIIKQDIESLAVLRKIVIVNQLPKTKTGKI 616
Cdd:PRK08633 1083 geklvvlhTCGAEDVE--------------------ELKRA---IKESGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
255-542 |
5.10e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.42 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 255 HPLYIIYSSGTTGNAKAVVRSNGP--NLVCmnyfdrYISEKYEC---TTLLTTSSVGWVSFHGFLYGMLSFGSTFVMYEG 329
Cdd:PRK12316 656 NLAYVIYTSGSTGKPKGAGNRHRAlsNRLC------WMQQAYGLgvgDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAP 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 330 GIIKNKhieVDFWNTIEKHKATHTLSLANTIRYFIktdPEGTIIrskyDLSNLKEIWVGGEVIEESIPEYIEKKLkikPT 409
Cdd:PRK12316 730 GDHRDP---AKLVELINREGVDTLHFVPSMLQAFL---QDEDVA----SCTSLRRIVCSGEALPADAQEQVFAKL---PQ 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 410 RG----YGQTE--IGIAYLYCFDHI--NIPyyaTGLPSIFIRPSIFSDDGKelgvneigeiafklPMPPSFATTLYKNDE 481
Cdd:PRK12316 797 AGlynlYGPTEaaIDVTHWTCVEEGgdSVP---IGRPIANLACYILDANLE--------------PVPVGVLGELYLAGR 859
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 60472587 482 KFKQLFSKFPGY----------------YNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLE 542
Cdd:PRK12316 860 GLARGYHGRPGLtaerfvpspfvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVRE 936
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
259-550 |
9.50e-07 |
|
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: 51.35 E-value: 9.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 259 IIYSSGTTGNAKAVVRSNGPNLvcmnyfdRYISEKYECTTLLTTSSVGWVS--FH------GFLYGMLSfGSTfvMYEGG 330
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTL-------RAAAAWADCADLTEDDRYLIINpfFHtfgykaGIVACLLT-GAT--VVPVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 331 IIKNKHIevdfWNTIEKHKAThTLSLANTIRYFIKTDPEgtiiRSKYDLSNLKEIWVGGEVIEESIPEYIEKKLKIKP-T 409
Cdd:cd17638 75 VFDVDAI----LEAIERERIT-VLPGPPTLFQSLLDHPG----RKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETvL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 410 RGYGQTEIGIAYLyCFDHINIPYYATGLPSIFirpsifsdDGKELGVNEIGEIAFKLPMppsfATTLYKNDEKFKQLFSK 489
Cdd:cd17638 146 TAYGLTEAGVATM-CRPGDDAETVATTCGRAC--------PGFEVRIADDGEVLVRGYN----VMQGYLDDPEATAEAID 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60472587 490 FPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIND 550
Cdd:cd17638 213 ADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPD 273
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
437-616 |
1.42e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 51.32 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 437 LPSIFIRpsIFSDDGKELGVNEIGEIAFKlpmPPSFATTLYKNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDD 516
Cdd:PRK07786 351 IPTVAAR--VVDENMNDVPVGEVGEIVYR---APTLMSGYWNNPEATAEAFAG--GWFHSGDLVRQDEEGYVWVVDRKKD 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 517 QIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALLVlkqlqqqdqsiqqidlnkLQNEINYIIKQDIES- 595
Cdd:PRK07786 424 MIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAA------------------VRNDDAALTLEDLAEf 485
|
170 180
....*....|....*....|....*...
gi 60472587 596 ----LAVLRK---IVIVNQLPKTKTGKI 616
Cdd:PRK07786 486 ltdrLARYKHpkaLEIVDALPRNPAGKV 513
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
246-618 |
1.50e-06 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 51.13 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 246 YEYVPVESSHPLYIIYSSGTTGNAKAVVRSNgPNLVCMnyfdryiSEKYECTTLLTTSSVG--WVSFHGFlyGMLSFGST 323
Cdd:cd05906 159 HDLPQSRPDDLALLMLTSGSTGFPKAVPLTH-RNILAR-------SAGKIQHNGLTPQDVFlnWVPLDHV--GGLVELHL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 324 FVMYEGGIIKNKHIE------VDFWNTIEKHKATHT------LSLantIRYFIKTDPEGTiirskYDLSNLKEIWVGGEV 391
Cdd:cd05906 229 RAVYLGCQQVHVPTEeiladpLRWLDLIDRYRVTITwapnfaFAL---LNDLLEEIEDGT-----WDLSSLRYLVNAGEA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 392 IEESIPEYIEKKLK--------IKPtrGYGQTEI--GIAY---LYCFDHIN-IPYYATGLPSIFIRPSIFSDDGKELGVN 457
Cdd:cd05906 301 VVAKTIRRLLRLLEpyglppdaIRP--AFGMTETcsGVIYsrsFPTYDHSQaLEFVSLGRPIPGVSMRIVDDEGQLLPEG 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 458 EIGEIAFKLPMPPSfatTLYKNDEKFKQLFSKfPGYYNPGDLGFKDeNGFYTIVSRSDDQIKISGNKVQLNTIETSILKH 537
Cdd:cd05906 379 EVGRLQVRGPVVTK---GYYNNPEANAEAFTE-DGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEV 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 538 PLVLE--CCSIGINDPTC--------YSVPIALLVLKQlqqqdqsiqqidlnklqnEINYIIKQdieslAVLRKIVIV-- 605
Cdd:cd05906 454 PGVEPsfTAAFAVRDPGAeteelaifFVPEYDLQDALS------------------ETLRAIRS-----VVSREVGVSpa 510
|
410 420
....*....|....*....|
gi 60472587 606 -------NQLPKTKTGKIPR 618
Cdd:cd05906 511 yliplpkEEIPKTSLGKIQR 530
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
253-618 |
1.58e-06 |
|
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: 51.00 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 253 SSHPLYIIYSSGTTGNAKAVVRSNGpNLV-CMNYFDRYIseKYECTT-LLTTSSVGW-VSFHGFLYGMLSFGSTFVMYEG 329
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHR-ALStSALAHGRAL--GLTSESrVLQFASYTFdVSILEIFTTLAAGGCLCIPSEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 330 GIIknkhieVDFWNTIEKHKATH---TLSLANTIryfiktDPEgtiirskyDLSNLKEIWVGGEVIEESIpeyIEK-KLK 405
Cdd:cd05918 182 DRL------NDLAGFINRLRVTWaflTPSVARLL------DPE--------DVPSLRTLVLGGEALTQSD---VDTwADR 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 406 IKPTRGYGQTEIGIAYLYCFDHINIPYYATGLP---SIFI-RPSifsDDGKELGVNEIGEI------------------A 463
Cdd:cd05918 239 VRLINAYGPAECTIAATVSPVVPSTDPRNIGRPlgaTCWVvDPD---NHDRLVPIGAVGELliegpilargylndpektA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 464 FKLPMPPSFAttlykndekfKQLFSKFPGY-YNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKH-PLVL 541
Cdd:cd05918 316 AAFIEDPAWL----------KQEGSGRGRRlYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAK 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 542 ECCSIGINDPTCYSVP-----IALLVLKQLQQQDQSIQQIDLNKLQNEINYIIKQDIESLA---VLRKIVIVNQLPKTKT 613
Cdd:cd05918 386 EVVVEVVKPKDGSSSPqlvafVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKLRQRLPsymVPSVFLPLSHLPLTAS 465
|
....*
gi 60472587 614 GKIPR 618
Cdd:cd05918 466 GKIDR 470
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
258-623 |
2.16e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 51.50 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 258 YIIYSSGTTGNAKAVVRSNGPnlvcMNYFDRYISEKYECTT---LLTTSSVGWVSFHGFLYGMLSFGSTFVMYEGGIIKN 334
Cdd:PRK12316 2150 YVIYTSGSTGLPKGVAVSHGA----LVAHCQAAGERYELSPadcELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDP 2225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 335 KHIevdfWNTIEKHKATHTLSLANTIRYFIK-TDPEGTIIrskydlsNLKEIWVGGEVIEESIPEYIEKKLKikPTR--- 410
Cdd:PRK12316 2226 EQL----YDEMERHGVTILDFPPVYLQQLAEhAERDGRPP-------AVRVYCFGGEAVPAASLRLAWEALR--PVYlfn 2292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 411 GYGQTEIGIAYLYCFDHINIPYYATGLPSifirpsifsddGKELGvneiGEIAFKL-----PMPPSFATTLYKNDEKFKQ 485
Cdd:PRK12316 2293 GYGPTEAVVTPLLWKCRPQDPCGAAYVPI-----------GRALG----NRRAYILdadlnLLAPGMAGELYLGGEGLAR 2357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 486 LFSKFPG-----------------YYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGI 548
Cdd:PRK12316 2358 GYLNRPGltaerfvpdpfsasgerLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ 2437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 549 NDPT-----CYSVPIALLVLkqlqqqdqsiqqidlnkLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRPIISK 623
Cdd:PRK12316 2438 DGASgkqlvAYVVPDDAAED-----------------LLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
449-551 |
2.29e-06 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 50.64 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 449 DDGKELGVNEIGEIAFKLP--------MPpsfattlykndEKFKQLFSKfPGYYNPGDLGFKDENGFYTIVSRSDDQIkI 520
Cdd:PRK07514 338 ETGAELPPGEIGMIEVKGPnvfkgywrMP-----------EKTAEEFRA-DGFFITGDLGKIDERGYVHIVGRGKDLI-I 404
|
90 100 110
....*....|....*....|....*....|...
gi 60472587 521 SG--NkVQLNTIETSILKHPLVLECCSIGINDP 551
Cdd:PRK07514 405 SGgyN-VYPKEVEGEIDELPGVVESAVIGVPHP 436
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
375-551 |
2.97e-06 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 50.37 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 375 SKYDLSNLKEIWVGGEVIEESIPEYIEKKLKIKPTRGYGQTEIGIAYLYCFDHINIPYYATGLPsifIRPS----IFSDD 450
Cdd:PRK10946 295 SRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTRLDDSDERIFTTQGRP---MSPDdevwVADAD 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 451 GKELGVNEIGEIAFKLPMppsfatTL---YKNDEKFKQLFSKfPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQL 527
Cdd:PRK10946 372 GNPLPQGEVGRLMTRGPY------TFrgyYKSPQHNASAFDA-NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAA 444
|
170 180
....*....|....*....|....
gi 60472587 528 NTIETSILKHPLVLECCSIGINDP 551
Cdd:PRK10946 445 EEIENLLLRHPAVIHAALVSMEDE 468
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
492-551 |
3.01e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 49.99 E-value: 3.01e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60472587 492 GYYNPGDLGFKDENGFYTIVSR-SDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDP 551
Cdd:PRK07787 350 GWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDD 410
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
248-551 |
3.93e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 50.03 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 248 YVPVESSHPLYIIYSSGTTGNAKAVVRSNGPNLVCmnyfDRYISEKYEcttlLTTSSVGWVS---FH------------- 311
Cdd:PRK13388 144 HREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFA----GRALTERFG----LTRDDVCYVSmplFHsnavmagwapava 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 312 --------------GFLYGMLSFGSTFVMYEGgiiknkhievdfwntiekhKAthtlslantIRYFIKTdPEgtiirSKY 377
Cdd:PRK13388 216 sgaavalpakfsasGFLDDVRRYGATYFNYVG-------------------KP---------LAYILAT-PE-----RPD 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 378 DLSNLKEIWVGGEVIEESIPEYiEKKLKIKPTRGYGQTEIGIAylycfdhI----NIPYYATGLPSIFIR---------- 443
Cdd:PRK13388 262 DADNPLRVAFGNEASPRDIAEF-SRRFGCQVEDGYGSSEGAVI-------VvrepGTPPGSIGRGAPGVAiynpetltec 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 444 -PSIFSDDGKELGVNE-IGEIAFKlpMPPSFATTLYKND----EKFKQlfskfpGYYNPGDLGFKDENGFYTIVSRSDDQ 517
Cdd:PRK13388 334 aVARFDAHGALLNADEaIGELVNT--AGAGFFEGYYNNPeataERMRH------GMYWSGDLAYRDADGWIYFAGRTADW 405
|
330 340 350
....*....|....*....|....*....|....
gi 60472587 518 IKISGNKVQLNTIETSILKHPLVLECCSIGINDP 551
Cdd:PRK13388 406 MRVDGENLSAAPIERILLRHPAINRVAVYAVPDE 439
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
412-553 |
5.37e-06 |
|
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: 49.34 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 412 YGQTEIGIAYLYCFDHiNIPYYATGLPSifirpsifsdDGKELGVNEIGEIAFKlpmPPSFATTLYKNDEKFKQLFSKfP 491
Cdd:cd17641 355 YGQTELAGAYTVHRDG-DVDPDTVGVPF----------PGTEVRIDEVGEILVR---SPGVFVGYYKNPEATAEDFDE-D 419
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60472587 492 GYYNPGDLGFKDENGFYTIVSRSDDQIKIS-GNKVQLNTIETSILKHPLVLECCSIGINDPTC 553
Cdd:cd17641 420 GWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKLKFSPYIAEAVVLGAGRPYL 482
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
437-618 |
6.83e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 49.12 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 437 LPSIFIRP----SIFSDDGKELGVNEIGEIAFKlpmPPSFATTLYKNDEKFKQLFSKFPGY--YNPGDLGFKDeNGFYTI 510
Cdd:PRK04813 318 LPIGYAKPdsplLIIDEEGTKLPDGEQGEIVIS---GPSVSKGYLNNPEKTAEAFFTFDGQpaYHTGDAGYLE-DGLLFY 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 511 VSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPtcysvpiallvlkqlqqqdqsiqqidlNKLQNEINYII- 589
Cdd:PRK04813 394 QGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKD---------------------------HKVQYLIAYVVp 446
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 60472587 590 -KQDIESLAVL------------------RKIVIVNQLPKTKTGKIPR 618
Cdd:PRK04813 447 kEEDFEREFELtkaikkelkerlmeymipRKFIYRDSLPLTPNGKIDR 494
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
92-558 |
8.66e-06 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 48.50 E-value: 8.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 92 KLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITT 171
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 172 nygifndeiitftpnlkdaielstfkpsnvitlfrnditsesdlkkvkdiptipntlswydeikkfkennqspfyeyvpv 251
Cdd:cd05940 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 252 esshPLYIIYSSGTTGNAKAVVRSNGPNLVCMNYF---------DRYisekYECTTLL--TTSSVGWVSfhgflygMLSF 320
Cdd:cd05940 83 ----AALYIYTSGTTGLPKAAIISHRRAWRGGAFFagsggalpsDVL----YTCLPLYhsTALIVGWSA-------CLAS 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 321 GSTFVmyeggiIKNKHIEVDFWNTIEKHKATHTLSLANTIRYFIKTDPEGTIIRSKYDL---SNLK-EIWvgGEVIEE-S 395
Cdd:cd05940 148 GATLV------IRKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMifgNGLRpDIW--EEFKERfG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 396 IPEYIEKklkikptrgYGQTEIGIAYLYCFDHIN----IPYY-ATGLPSIFIRPSIFSD------DG--KELGVNEIGEI 462
Cdd:cd05940 220 VPRIAEF---------YAATEGNSGFINFFGKPGaigrNPSLlRKVAPLALVKYDLESGepirdaEGrcIKVPRGEPGLL 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 463 AFKL-PMPP--SFATTLYKNDEKFKQLFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPL 539
Cdd:cd05940 291 ISRInPLEPfdGYTDPAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPG 370
|
490
....*....|....*....
gi 60472587 540 VLECcsigindpTCYSVPI 558
Cdd:cd05940 371 VEEA--------NVYGVQV 381
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
494-619 |
1.22e-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: 48.52 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 494 YNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIND----PT--CYSVPIALLVLKQLQ 567
Cdd:TIGR03443 680 YRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDkdeePTlvSYIVPQDKSDELEEF 759
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60472587 568 QQDQSIQQ---------IDLNKLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTGKIPRP 619
Cdd:TIGR03443 760 KSEVDDEEssdpvvkglIKYRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKP 820
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
379-551 |
1.23e-05 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 48.07 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 379 LSNLKEIWVGGEvieESIPEYIEK----KLKIKPTrgYGQTEIG--IAYLycfdhinipyyatgLPSIFIRPSIFSddGK 452
Cdd:PRK07445 229 LAQFRTILLGGA---PAWPSLLEQarqlQLRLAPT--YGMTETAsqIATL--------------KPDDFLAGNNSS--GQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 453 -------ELGVNEIGEIAFKlpmppsfATTLYKNdekFKQLFSKFPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKV 525
Cdd:PRK07445 288 vlphaqiTIPANQTGNITIQ-------AQSLALG---YYPQILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENV 357
|
170 180
....*....|....*....|....*.
gi 60472587 526 QLNTIETSILKHPLVLECCSIGINDP 551
Cdd:PRK07445 358 YPAEVEAAILATGLVQDVCVLGLPDP 383
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
248-542 |
1.27e-05 |
|
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: 48.13 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 248 YVPVESSHPL------------------------YIIYSSGTTGNAKAVVRSNGPnlvcMNYFDRYISEKYECTT---LL 300
Cdd:cd17649 64 YVPLDPEYPAerlrymledsgaglllthhprqlaYVIYTSGSTGTPKGVAVSHGP----LAAHCQATAERYGLTPgdrEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 301 TTSSVGWVSFHGFLYGMLSFGSTFVMYEGGIiknkhievdfWNT-------IEKHKAThTLSLANTIRYFIKTDPEGTII 373
Cdd:cd17649 140 QFASFNFDGAHEQLLPPLICGACVVLRPDEL----------WASadelaemVRELGVT-VLDLPPAYLQQLAEEADRTGD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 374 RSKydlSNLKEIWVGGEVIEesiPEYIEKKLKIKPT--RGYGQTEIGIAYLYCfdHINiPYYATGLPSIFI-------RP 444
Cdd:cd17649 209 GRP---PSLRLYIFGGEALS---PELLRRWLKAPVRlfNAYGPTEATVTPLVW--KCE-AGAARAGASMPIgrplggrSA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 445 SIFSDDGKELGVNEIGEIAFK--------LPMPPSFAttlykndEKFKQLFSKFPG--YYNPGDLGFKDENGFYTIVSRS 514
Cdd:cd17649 280 YILDADLNPVPVGVTGELYIGgeglargyLGRPELTA-------ERFVPDPFGAPGsrLYRTGDLARWRDDGVIEYLGRV 352
|
330 340
....*....|....*....|....*...
gi 60472587 515 DDQIKISGNKVQLNTIETSILKHPLVLE 542
Cdd:cd17649 353 DHQVKIRGFRIELGEIEAALLEHPGVRE 380
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
93-281 |
1.78e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 47.80 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRI-ETitpklIITT 171
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLnET-----EVTT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 172 nygifndeIITFTPNLKDAIELS----TFKpsNVITLFRNDITSESDLKKVKDIptipnTLSWYDEIKKFKENNqspfye 247
Cdd:PLN02387 182 --------VICDSKQLKKLIDISsqleTVK--RVIYMDDEGVDSDSSLSGSSNW-----TVSSFSEVEKLGKEN------ 240
|
170 180 190
....*....|....*....|....*....|....*....
gi 60472587 248 yvPVESSHPL-----YIIYSSGTTGNAKAVVRSNGpNLV 281
Cdd:PLN02387 241 --PVDPDLPSpndiaVIMYTSGSTGLPKGVMMTHG-NIV 276
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
492-559 |
2.92e-05 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 47.08 E-value: 2.92e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60472587 492 GYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIA 559
Cdd:PRK05620 430 GWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLA 497
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
85-540 |
3.17e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 47.12 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 85 PYLKKTikltYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGAThCV-LFDGY---SVKSLIDRI 160
Cdd:PLN02430 73 PYMWKT----YKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLI-CVpLYDTLgpgAVDYIVDHA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 161 EtitpkliitTNYGIFNDEIIT--FTPNLKDAIELSTfkpsnvITLFRNDITSESDlkKVKDIPTIPntLSWYDEIKKFK 238
Cdd:PLN02430 148 E---------IDFVFVQDKKIKelLEPDCKSAKRLKA------IVSFTSVTEEESD--KASQIGVKT--YSWIDFLHMGK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 239 ENNQSPFyeyvPVESSHPLYIIYSSGTTGNAKAVVRSN--------GPNLvCMNYF--------------------DRYI 290
Cdd:PLN02430 209 ENPSETN----PPKPLDICTIMYTSGTSGDPKGVVLTHeavatfvrGVDL-FMEQFedkmthddvylsflplahilDRMI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 291 SEKYecttLLTTSSVGWvsFHGFLYGM----LSFGSTFV---------MYEGgiIKNKHIEVD-----FWNTIEKHKath 352
Cdd:PLN02430 284 EEYF----FRKGASVGY--YHGDLNALrddlMELKPTLLagvprvferIHEG--IQKALQELNprrrlIFNALYKYK--- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 353 tLSLANTIRYFIKTDPEGTII---RSKYDL-SNLKEIWVGGEVIEESIPEYIEKKLKIKPTRGYGQTEIGIAYLYCFDHI 428
Cdd:PLN02430 353 -LAWMNRGYSHKKASPMADFLafrKVKAKLgGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 429 NIPYYATGLPSIF--IRPSIFSDDGKE-LGVNEIGEIAFKlpmPPSFATTLYKNDEKFKQLFSKfpGYYNPGDLGFKDEN 505
Cdd:PLN02430 432 MCMLGTVGAPAVYneLRLEEVPEMGYDpLGEPPRGEICVR---GKCLFSGYYKNPELTEEVMKD--GWFHTGDIGEILPN 506
|
490 500 510
....*....|....*....|....*....|....*.
gi 60472587 506 GFYTIVSRSDDQIKIS-GNKVQLNTIETSILKHPLV 540
Cdd:PLN02430 507 GVLKIIDRKKNLIKLSqGEYVALEYLENVYGQNPIV 542
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
258-542 |
3.39e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 47.46 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 258 YIIYSSGTTGNAKAVVRSNGP--NLVCmnyfdrYISEKYEC----TTLLTTSsvgwVSFHGF---LYGMLSFGSTFVmye 328
Cdd:PRK12467 3241 YVIYTSGSTGKPKGVGVRHGAlaNHLC------WIAEAYELdandRVLLFMS----FSFDGAqerFLWTLICGGCLV--- 3307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 329 ggIIKNKHIEVD-FWNTIEKHKAThTLSLANTIRYFIKTDPEGTiirskyDLSNLKEIWVGGEVIEESIPEYIEKKLK-I 406
Cdd:PRK12467 3308 --VRDNDLWDPEeLWQAIHAHRIS-IACFPPAYLQQFAEDAGGA------DCASLDIYVFGGEAVPPAAFEQVKRKLKpR 3378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 407 KPTRGYGQTEIGIAYLYCFDHINIPYYATGLPsiFIRP----SIFSDDGK----ELGVneIGE-------IAFKLPMPPS 471
Cdd:PRK12467 3379 GLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAP--IGRPvagrSIYVLDGQlnpvPVGV--AGElyiggvgLARGYHQRPS 3454
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60472587 472 FATtlykndEKFkqLFSKFPG----YYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLE 542
Cdd:PRK12467 3455 LTA------ERF--VADPFSGsggrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVRE 3521
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
449-559 |
3.41e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 46.96 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 449 DDGKELGVNEIGEIAFKlpmPPSFATTLYKNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLN 528
Cdd:PRK06178 404 ETGELLPLGAEGEIVVR---TPSLLKGYWNKPEATAEALRD--GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPS 478
|
90 100 110
....*....|....*....|....*....|.
gi 60472587 529 TIETSILKHPLVLECCSIGINDPTCYSVPIA 559
Cdd:PRK06178 479 EVEALLGQHPAVLGSAVVGRPDPDKGQVPVA 509
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
249-552 |
4.34e-05 |
|
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: 46.50 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 249 VPVESSHPLYIIYSSGTTGNAKAVVRSNGPnlvCMNYFDRyISEKYECTT---LLTTSSVGwvsfhgF------LYGMLS 319
Cdd:cd12114 121 VDVAPDDLAYVIFTSGSTGTPKGVMISHRA---ALNTILD-INRRFAVGPddrVLALSSLS------FdlsvydIFGALS 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 320 FGSTFVMYEGgiikNKHIEVDFWN-TIEKHKATH----------TLSLAntiryfikTDPEGtiirskyDLSNLKEIWVG 388
Cdd:cd12114 191 AGATLVLPDE----ARRRDPAHWAeLIERHGVTLwnsvpallemLLDVL--------EAAQA-------LLPSLRLVLLS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 389 GEVIEESIPeyiekkLKIKPTRGY-------GQTEIGI-AYLYCFDHIN-----IPYyatGLP----SIFIrpsifsddg 451
Cdd:cd12114 252 GDWIPLDLP------ARLRALAPDarlislgGATEASIwSIYHPIDEVPpdwrsIPY---GRPlanqRYRV--------- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 452 kelgVNEIGEiafklPMPPSFATTL----------YKNDEKFKQlfSKFP------GYYNPGDLGFKDENGFYTIVSRSD 515
Cdd:cd12114 314 ----LDPRGR-----DCPDWVPGELwiggrgvalgYLGDPELTA--ARFVthpdgeRLYRTGDLGRYRPDGTLEFLGRRD 382
|
330 340 350
....*....|....*....|....*....|....*..
gi 60472587 516 DQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPT 552
Cdd:cd12114 383 GQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPG 419
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
411-552 |
4.91e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 46.21 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 411 GYGQTEIGIAYLYC-----------FDHINIPYYATGLPsifIRPSIFSDDGKELGVNEIGEIAfKLPMPPSFATtLYKN 479
Cdd:PRK07867 296 GFGSTEGGVAITRTpdtppgalgplPPGVAIVDPDTGTE---CPPAEDADGRLLNADEAIGELV-NTAGPGGFEG-YYND 370
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60472587 480 DEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPT 552
Cdd:PRK07867 371 PEADAERMRG--GVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPV 441
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
261-551 |
5.53e-05 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 46.28 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 261 YSSGTTGNAKAVVRSNGPN----LVCMNYFDRYISEKyecTTLLTTSSVgwvsFHGFLYGML----SFGSTFVMyEGGII 332
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHRSNvlhaLMANNGDALGTSAA---DTMLPVVPL----FHANSWGIAfsapSMGTKLVM-PGAKL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 333 KNKHIevdfWNTIEKHKATHTLSLANT----IRYFIKTDPEgtiirskydLSNLKEIWVGGEVIEESIPEYIEKkLKIKP 408
Cdd:PRK06018 256 DGASV----YELLDTEKVTFTAGVPTVwlmlLQYMEKEGLK---------LPHLKMVVCGGSAMPRSMIKAFED-MGVEV 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 409 TRGYGQTE---IGIAYLYCFDHINIPYYA-------TGLPSIFIRPSIFSDDGKELGVNeiGEIAFKLPMP-PSFATTLY 477
Cdd:PRK06018 322 RHAWGMTEmspLGTLAALKPPFSKLPGDArldvlqkQGYPPFGVEMKITDDAGKELPWD--GKTFGRLKVRgPAVAAAYY 399
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60472587 478 KNDEKfkqLFSKfPGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDP 551
Cdd:PRK06018 400 RVDGE---ILDD-DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHP 469
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
249-540 |
6.88e-05 |
|
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: 45.73 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 249 VPVESSHPLYIIYSSGTTGNAKAVVRSNGPnLVcmNYFdRYISEKYECTT---LLTTSSVGW-VSFHGFLYGMLSfGSTF 324
Cdd:cd17646 133 VPPRPDNLAYVIYTSGSTGRPKGVMVTHAG-IV--NRL-LWMQDEYPLGPgdrVLQKTPLSFdVSVWELFWPLVA-GARL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 325 VMYE-GGiiknkHIEVDFW-NTIEKHKATHTLSLANTIRYFIKTDPEGtiirskyDLSNLKEIWVGGEVIEESIPEYIEK 402
Cdd:cd17646 208 VVARpGG-----HRDPAYLaALIREHGVTTCHFVPSMLRVFLAEPAAG-------SCASLRRVFCSGEALPPELAARFLA 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 403 KLKIKPTRGYGQTE--IGIAYLYCFDHINIPYYATGLPSIFIRPSIFSDDGKELGVNEIGEIafklpmppsFATTL---- 476
Cdd:cd17646 276 LPGAELHNLYGPTEaaIDVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGEL---------YLGGVqlar 346
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60472587 477 -YKND-----EKFkqLFSKF-PG--YYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLV 540
Cdd:cd17646 347 gYLGRpaltaERF--VPDPFgPGsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAV 417
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
491-551 |
7.82e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 45.42 E-value: 7.82e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60472587 491 PGYYNPGDLGFKDeNGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDP 551
Cdd:PRK07824 233 PGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDD 292
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
62-277 |
8.11e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 45.74 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 62 YNVLDIQVQNPLKrDQDAL--IYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSC-- 137
Cdd:PTZ00216 90 YRPVERVEKEVVK-DADGKerTMEVTHFNETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIws 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 138 ---------ARIG---------ATHC--VLFDGYSVKSLIDRIETI-TPKLIIttnygIFNDEIitftpnlkdaielstf 196
Cdd:PTZ00216 169 qsmvaatvyANLGedalayalrETECkaIVCNGKNVPNLLRLMKSGgMPNTTI-----IYLDSL---------------- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 197 kPSNVitlfrnditsesDLKKVKdiptipnTLSWYDEIKKFKEnnqspfyeyvpVESSHPL----------YIIYSSGTT 266
Cdd:PTZ00216 228 -PASV------------DTEGCR-------LVAWTDVVAKGHS-----------AGSHHPLnipennddlaLIMYTSGTT 276
|
250
....*....|.
gi 60472587 267 GNAKAVVRSNG 277
Cdd:PTZ00216 277 GDPKGVMHTHG 287
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
478-616 |
1.41e-04 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 44.84 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 478 KNDEKFKQLFSKfpGYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVP 557
Cdd:PLN02479 418 KNPKANEEAFAN--GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESP 495
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 60472587 558 IALLVLKQLQQQDQSiqqidlNKLQNEINYIIKQDIESLAVLRKIVIvNQLPKTKTGKI 616
Cdd:PLN02479 496 CAFVTLKPGVDKSDE------AALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKI 547
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
249-618 |
2.65e-04 |
|
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: 43.85 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 249 VPVESSHPLYIIYSSGTTGNAKAVV--RSNGPNLV--CMNYFdryiSEKYECTTLLTTS-----SVgwvsFHgfLYGMLS 319
Cdd:cd12115 100 VLTDPDDLAYVIYTSGSTGRPKGVAieHRNAAAFLqwAAAAF----SAEELAGVLASTSicfdlSV----FE--LFGPLA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 320 FGSTFVMyeggiiknkhieVDFWNTIEKHKATHTLSLANTIryfiktdPegTIIRSKYDL----SNLKEIWVGGEVIEES 395
Cdd:cd12115 170 TGGKVVL------------ADNVLALPDLPAAAEVTLINTV-------P--SAAAELLRHdalpASVRVVNLAGEPLPRD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 396 IPEYIEKKLKIKPTRG-YGQTEigiAYLYCFDHInIPYYATGLPSIFiRP------SIFSDDGKELGVNEIGEiafkLPM 468
Cdd:cd12115 229 LVQRLYARLQVERVVNlYGPSE---DTTYSTVAP-VPPGASGEVSIG-RPlantqaYVLDRALQPVPLGVPGE----LYI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 469 PPSFATTLYKND-----EKFkqLFSKF-PG--YYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLV 540
Cdd:cd12115 300 GGAGVARGYLGRpgltaERF--LPDPFgPGarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGV 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 541 LECCSIGINDPT------CYSVPIALLVLkqlqqqdqsiqqidlnkLQNEINYIIKQDIESLAVLRKIVIVNQLPKTKTG 614
Cdd:cd12115 378 REAVVVAIGDAAgerrlvAYIVAEPGAAG-----------------LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNG 440
|
....
gi 60472587 615 KIPR 618
Cdd:cd12115 441 KIDR 444
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
497-618 |
5.97e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 42.72 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 497 GDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPlvleccsiGINDPTCYSV--PIALLVLKQLQQQDQSIQ 574
Cdd:PRK08308 296 KDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLP--------GVQEAVVYRGkdPVAGERVKAKVISHEEID 367
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 60472587 575 QIDLNKlqneinYIIKQdIESLAVLRKIVIVNQLPKTKTGKIPR 618
Cdd:PRK08308 368 PVQLRE------WCIQH-LAPYQVPHEIESVTEIPKNANGKVSR 404
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
494-540 |
7.49e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 42.72 E-value: 7.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 60472587 494 YNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLV 540
Cdd:PRK10252 839 YRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDV 885
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
494-551 |
1.11e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.46 E-value: 1.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 60472587 494 YNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGINDP 551
Cdd:PRK05691 2570 YRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTP 2627
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
258-544 |
2.08e-03 |
|
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: 40.92 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 258 YIIYSSGTTGNAKAV---VRSNGPNLVcmnyfdrYISEKYECT---TLLTTSSVGWVSFHGFLYGMLSFGSTFVMYEGGI 331
Cdd:cd17654 122 YVIHTSGTTGTPKIVavpHKCILPNIQ-------HFRSLFNITsedILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 332 IKNKHI--EVDF-WNTIEKHKATHTLslantIRYFIKTDPEGTIIrSKydLSNLKEIWVGGE-----VIEESipeYIEKK 403
Cdd:cd17654 195 KVLPSKlaDILFkRHRITVLQATPTL-----FRRFGSQSIKSTVL-SA--TSSLRVLALGGEpfpslVILSS---WRGKG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 404 LKIKPTRGYGQTEIGI-AYLYCFDHINIPYYaTGLPSIFIRPSIFSDDGKEL-GVNEIGEIAFKLPMppsfattlyknDE 481
Cdd:cd17654 264 NRTRIFNIYGITEVSCwALAYKVPEEDSPVQ-LGSPLLGTVIEVRDQNGSEGtGQVFLGGLNRVCIL-----------DD 331
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 60472587 482 KFKQLFSKFpgyYNPGDLGFKDENGFYtIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECC 544
Cdd:cd17654 332 EVTVPKGTM---RATGDFVTVKDGELF-FLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCA 390
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
492-550 |
2.55e-03 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 40.94 E-value: 2.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 60472587 492 GYYNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIND 550
Cdd:PLN02860 414 GWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPD 472
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
449-618 |
2.86e-03 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 40.73 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 449 DDGKELGVNEIGEIAFKLP--M------PPSFATTLYKNdekfkqlfskfpGYYNPGDLGFKDENGFYTIVSRSDDQIKI 520
Cdd:PLN02246 373 ETGASLPRNQPGEICIRGPqiMkgylndPEATANTIDKD------------GWLHTGDIGYIDDDDELFIVDRLKELIKY 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 521 SGNKVQLNTIETSILKHPLVLECCSIGINDPTCYSVPIALLVLKQLQQQDqsiqqidlnklQNEI-NYIIKQDIeSLAVL 599
Cdd:PLN02246 441 KGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEIT-----------EDEIkQFVAKQVV-FYKRI 508
|
170
....*....|....*....
gi 60472587 600 RKIVIVNQLPKTKTGKIPR 618
Cdd:PLN02246 509 HKVFFVDSIPKAPSGKILR 527
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
255-618 |
3.65e-03 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 40.16 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 255 HPLYIIYSSGTTGNAKAVVRSNGpNLVcMNYFD-RYISEKYECTTLLT----TSSVGWVSFHgfLYGMLSFGSTFVMYEG 329
Cdd:cd05908 107 ELAFIQFSSGSTGDPKGVMLTHE-NLV-HNMFAiLNSTEWKTKDRILSwmplTHDMGLIAFH--LAPLIAGMNQYLMPTR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 330 GIIKNKhieVDFWNTIEKHKATHTLSLANTIRYFIKTDPEGTIirSKYDLSNLKEIWVGGEVIE-ESIPEYIE------- 401
Cdd:cd05908 183 LFIRRP---ILWLKKASEHKATIVSSPNFGYKYFLKTLKPEKA--NDWDLSSIRMILNGAEPIDyELCHEFLDhmskygl 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 402 KKLKIKPTRGYGQTEIGIAYLYCFDHINIPYY-------------------------ATGLPSIFIRPSIFSDDGKELGV 456
Cdd:cd05908 258 KRNAILPVYGLAEASVGASLPKAQSPFKTITLgrrhvthgepepevdkkdsecltfvEVGKPIDETDIRICDEDNKILPD 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 457 NEIGEIAFK-LPMPPSFattlYKNDEKFKQLFSKfPGYYNPGDLGFKdENGFYTIVSRSDDQIKISGNKVQLNTIE-TSI 534
Cdd:cd05908 338 GYIGHIQIRgKNVTPGY----YNNPEATAKVFTD-DGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIErIAE 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 535 LKHPLVL-ECCSIGINDPTCYSVPIALLVLKQLQQQDQSIQQidlNKLQNEINYIIKQDIeslavlRKIVIVNQLPKTKT 613
Cdd:cd05908 412 ELEGVELgRVVACGVNNSNTRNEEIFCFIEHRKSEDDFYPLG---KKIKKHLNKRGGWQI------NEVLPIRRIPKTTS 482
|
....*
gi 60472587 614 GKIPR 618
Cdd:cd05908 483 GKVKR 487
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
494-542 |
6.13e-03 |
|
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: 39.54 E-value: 6.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 60472587 494 YNPGDLGFKDENGFYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLE 542
Cdd:cd17652 319 YRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAE 367
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
93-368 |
8.66e-03 |
|
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: 39.20 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 93 LTYYQLYEKVCEFSRVLLN-LNISKNDNVLIYMANTLEPLIAMLSCARIG-ATHCVLFDGYSvKSLIDRIETITPKLIIT 170
Cdd:cd05938 6 YTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGcPVAFLNTNIRS-KSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 171 TnygifndeiitftPNLKDAIE--LSTFKPSNVITLF--RNDITS--ESDLKKVKDIPTIPNTLSWYDEIkkfkeNNQSP 244
Cdd:cd05938 85 A-------------PELQEAVEevLPALRADGVSVWYlsHTSNTEgvISLLDKVDAASDEPVPASLRAHV-----TIKSP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60472587 245 FyeyvpvesshpLYIiYSSGTTGNAKAVVRSNGPNLVCMNYF-------DRYIsekYECTTLLTTSsvgwvsfhGFLYGM 317
Cdd:cd05938 147 A-----------LYI-YTSGTTGLPKAARISHLRVLQCSGFLslcgvtaDDVI---YITLPLYHSS--------GFLLGI 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 60472587 318 ---LSFGSTFVMyeggiiKNKHIEVDFWNTIEKHKATHTLSLANTIRYFIKTDP 368
Cdd:cd05938 204 ggcIELGATCVL------KPKFSASQFWDDCRKHNVTVIQYIGELLRYLCNQPQ 251
|
|
| |
