|
Name |
Accession |
Description |
Interval |
E-value |
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
62-678 |
0e+00 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 1167.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 62 YKTHFAASVTDPERFWGKAAEQISWYKPWTKTLENKHSPSTR-FVEGMLNICYNAVDRHIENGKGDKIAIIYDSPVTNTK 140
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPPEKILDNSNPPFTRwFVGGRLNTCYNALDRHVEAGRGDQIALIYDSPVTGTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 141 ATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT 220
Cdd:cd05967 81 RTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 221 ASFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRPNMEAVPLAPGRDLDWDEEMAKAQSHDCVPVLSEHPLYILYTSG 300
Cdd:cd05967 161 ASCGIEPGKVVPYKPLLDKALELSGHKPHHVLVLNRPQVPADLTKPGRDLDWSELLAKAEPVDCVPVAATDPLYILYTSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 301 TTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVGTPDAGAYFRV 380
Cdd:cd05967 241 TTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEGKPVGTPDPGAFWRV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 381 LAEHGVAALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITASC 460
Cdd:cd05967 321 IEKYQVNALFTAPTAIRAIRKEDPDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITANP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 461 VGLGNsKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAG 540
Cdd:cd05967 401 VGLEP-LPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 541 YMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVK 620
Cdd:cd05967 480 YKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKELVA 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 32258701 621 HVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYKITSTIEDPSIFGHV 678
Cdd:cd05967 560 LVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGEDYTIPSTIEDPSVLDEI 617
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
104-680 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 709.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 104 FVEGMLNICYNAVDRHIEnGKGDKIAIIYDSpVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYT 183
Cdd:COG0365 3 FVGGRLNIAYNCLDRHAE-GRGDKVALIWEG-EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 184 MLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASFGIEPGRRVEYVPLVEEALKiGQHKPDKILIYNRPNMEAvp 263
Cdd:COG0365 81 MLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALE-ELPSLEHVIVVGRTGADV-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 264 lAPGRDLDWDEEMAKA-QSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLG 342
Cdd:COG0365 158 -PMEGDLDWDELLAAAsAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 343 WVVGHSYICYGPLLHGNTTVLYEGKPVgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaALGKQYSLTRFKTLFV 422
Cdd:COG0365 237 WATGHSYIVYGPLLNGATVVLYEGRPD-FPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGD--EPLKKYDLSSLRLLGS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 423 AGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITASCVGlgnskTPP-PGQAGKSVPGYNVMILDDNMQKLKARCLGNI 501
Cdd:COG0365 314 AGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPG-----LPVkPGSMGKPVPGYDVAVVDEDGNPVPPGEEGEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 502 VVKLPLpPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVA 581
Cdd:COG0365 389 VIKGPW-PGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVA 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 582 DCAVVGKEDPLKGHVPLALCVLRKDINATEEQVlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGK 661
Cdd:COG0365 468 EAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELA-KELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR 546
|
570
....*....|....*....
gi 32258701 662 PYKITSTIEDPSIFGHVEE 680
Cdd:COG0365 547 PLGDTSTLEDPEALDEIKE 565
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
62-684 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 665.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 62 YKTHFAASVTDPERFWGKAAEQISWYKPWTKTLENKHSPSTR-FVEGMLNICYNAVDRHIEnGKGDKIAIIYDSPVTNTK 140
Cdd:PRK10524 4 YSEFYQRSIDDPEAFWAEQARRIDWQTPFTQVLDYSNPPFARwFVGGRTNLCHNAVDRHLA-KRPEQLALIAVSTETDEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 141 ATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT 220
Cdd:PRK10524 83 RTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 221 ASFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRpNMEAVPLAPGRDLDWDEEMAKAQSHDcVPVL---SEHPLYILY 297
Cdd:PRK10524 163 ADAGSRGGKVVPYKPLLDEAIALAQHKPRHVLLVDR-GLAPMARVAGRDVDYATLRAQHLGAR-VPVEwleSNEPSYILY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 298 TSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgTPDAGAY 377
Cdd:PRK10524 241 TSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGMATIMYEGLPT-RPDAGIW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 378 FRVLAEHGVAALFTAPTAIRAIRQQDPgaALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPIT 457
Cdd:PRK10524 320 WRIVEKYKVNRMFSAPTAIRVLKKQDP--ALLRKHDLSSLRALFLAGEPLDEPTASWISEALGVPVIDNYWQTETGWPIL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 458 ASCVGLGnSKTPPPGQAGKSVPGYNVMILDDNM-QKLKARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEKF-PGYYD 535
Cdd:PRK10524 398 AIARGVE-DRPTRLGSPGVPMYGYNVKLLNEVTgEPCGPNEKGVLVIEGPLPPGCMQTVWGDDDRFVKTYWSLFgRQVYS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 536 TMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRK-DINATEEQV 614
Cdd:PRK10524 477 TFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDsDSLADREAR 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32258701 615 LE---EIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYKITSTIEDPSIFGHVEEMLKQ 684
Cdd:PRK10524 557 LAlekEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGRDPGDLTTIEDPAALQQIRQALEE 629
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
61-671 |
0e+00 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 631.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 61 EYKTHFAASVTDPERFWGKAAEQISWYKPWTKTLE-NKHSPSTR-FVEGMLNICYNAVDRHIENgKGDKIAIIYDSPVTN 138
Cdd:cd05966 2 QYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVLDwSKGPPFIKwFEGGKLNISYNCLDRHLKE-RGDKVAIIWEGDEPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 139 TKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVV 218
Cdd:cd05966 81 QSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 219 VTASFGIEPGRRVEYVPLVEEALKIGqHKPDKILIYNRPNMEaVPLAPGRDLDWDEEMAKA-QSHDCVPVLSEHPLYILY 297
Cdd:cd05966 161 ITADGGYRGGKVIPLKEIVDEALEKC-PSVEKVLVVKRTGGE-VPMTEGRDLWWHDLMAKQsPECEPEWMDSEDPLFILY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 298 TSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgTPDAGAY 377
Cdd:cd05966 239 TSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMFEGTPT-YPDPGRY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 378 FRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNV---FRVPVLDHWWQTETGS 454
Cdd:cd05966 318 WDIVEKHKVTIFYTAPTAIRALMKF--GDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVigkERCPIVDTWWQTETGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 455 PITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLpPGAFSGLWKNQEAFKHLYFEKFPGYY 534
Cdd:cd05966 396 IMITPLPGATPLK---PGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPW-PGMARTIYGDHERYEDTYFSKFPGYY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 535 DTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqV 614
Cdd:cd05966 472 FTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDE-L 550
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 32258701 615 LEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNG-KPYKITSTIED 671
Cdd:cd05966 551 RKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGeEELGDTSTLAD 608
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
61-680 |
0e+00 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 612.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 61 EYKTHFAASVTDPERFWGK-AAEQISWYKPWTKTLENKHSPSTR-FVEGMLNICYNAVDRHIENgKGDKIAIIYDSPVTN 138
Cdd:TIGR02188 6 QYKELYEESIEDPDKFWAKlARELLDWFKPFTKVLDWSFPPFYKwFVGGELNVSYNCVDRHLEA-RPDKVAIIWEGDEPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 139 TKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVV 218
Cdd:TIGR02188 85 EVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 219 VTASFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRPNMEAVPLAPGRDLDWDEEMAKaQSHDCVP--VLSEHPLYIL 296
Cdd:TIGR02188 165 ITADEGLRGGKVIPLKAIVDEALEKCPVSVEHVLVVRRTGNPVVPWVEGRDVWWHDLMAK-ASAYCEPepMDSEDPLFIL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 297 YTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgTPDAGA 376
Cdd:TIGR02188 244 YTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFEGVPT-YPDPGR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 377 YFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF---RVPVLDHWWQTETG 453
Cdd:TIGR02188 323 FWEIIEKHKVTIFYTAPTAIRALMRL--GDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVgkeRCPIVDTWWQTETG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 454 SPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNI-VVKLPLpPGAFSGLWKNQEAFKHLYFEKFPG 532
Cdd:TIGR02188 401 GIMITPLPGATPTK---PGSATLPFFGIEPAVVDEEGNPVEGPGEGGYlVIKQPW-PGMLRTIYGDHERFVDTYFSPFPG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 533 YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEE 612
Cdd:TIGR02188 477 YYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDE 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 613 qVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKP--YKITSTIEDPSIFGHVEE 680
Cdd:TIGR02188 557 -LRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAeiLGDTSTLEDPSVVEELIE 625
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
61-685 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 610.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 61 EYKTHFAASVTDPERFWGKAAEQISWYKPWTKTLeNKHSPSTR-FVEGMLNICYNAVDRHIENGkGDKIAIIY--DSPVT 137
Cdd:PRK00174 18 QYKALYQESVEDPEGFWAEQAKRLDWFKPFDTVL-DWNAPFIKwFEDGELNVSYNCLDRHLKTR-GDKVAIIWegDDPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 138 NTKatFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKV 217
Cdd:PRK00174 96 SRK--ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEALADRIIDAGAKL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 218 VVTASFGIEPGRRVEYVPLVEEALKIGqHKPDKILIYNRPNmEAVPLAPGRDLDWDEEMAKAQS-HDCVPVLSEHPLYIL 296
Cdd:PRK00174 174 VITADEGVRGGKPIPLKANVDEALANC-PSVEKVIVVRRTG-GDVDWVEGRDLWWHELVAGASDeCEPEPMDAEDPLFIL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 297 YTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgTPDAGA 376
Cdd:PRK00174 252 YTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPN-YPDPGR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 377 YFRVLAEHGVAALFTAPTAIRA-IRQqdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF---RVPVLDHWWQTET 452
Cdd:PRK00174 331 FWEVIDKHKVTIFYTAPTAIRAlMKE---GDEHPKKYDLSSLRLLGSVGEPINPEAWEWYYKVVggeRCPIVDTWWQTET 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 453 GSPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLpPGAFSGLWKNQEAFKHLYFEKFPG 532
Cdd:PRK00174 408 GGIMITPLPGATPLK---PGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPW-PGMMRTIYGDHERFVKTYFSTFKG 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 533 YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEE 612
Cdd:PRK00174 484 MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDE 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32258701 613 qVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPykI---TSTIEDPSIfghVEEMLKQA 685
Cdd:PRK00174 564 -LRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEE--IlgdTSTLADPSV---VEKLIEAR 633
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
62-649 |
0e+00 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 594.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 62 YKTHFAASVTDPERFWGKAAEQISWYKPWTK---TLENKHSPSTR-FVEGMLNICYNAVDRHIENGkGDKIAIIYDSPVT 137
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQKvknTSFAPGAPSIKwFEDATLNLAANALDRHLREN-GDRTAIIYEGDDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 138 NTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKV 217
Cdd:cd17634 80 SQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 218 VVTASFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRPNMeAVPLAPGRDLDWDEEMAKAQ-SHDCVPVLSEHPLYIL 296
Cdd:cd17634 160 LITADGGVRAGRSVPLKKNVDDALNPNVTSVEHVIVLKRTGS-DIDWQEGRDLWWRDLIAKASpEHQPEAMNAEDPLFIL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 297 YTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVGtPDAGA 376
Cdd:cd17634 239 YTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEGVPNW-PTPAR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 377 YFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGkqYSLTRFKTLFVAGERCDVETLEWSKNVF---RVPVLDHWWQTETG 453
Cdd:cd17634 318 MWQVVDKHGVNILYTAPTAIRALMAAGDDAIEG--TDRSSLRILGSVGEPINPEAYEWYWKKIgkeKCPVVDTWWQTETG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 454 SPITASCVGLGNSKTpppGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEaFKHLYFEKFPGY 533
Cdd:cd17634 396 GFMITPLPGAIELKA---GSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHER-FEQTYFSTFKGM 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 534 YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEq 613
Cdd:cd17634 472 YFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPE- 550
|
570 580 590
....*....|....*....|....*....|....*.
gi 32258701 614 VLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKI 649
Cdd:cd17634 551 LYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
52-685 |
3.28e-134 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 410.06 E-value: 3.28e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 52 RALSSgSGSEYKTHFAASVTDPERFWGKAAEQISWYKPW------TKTLENKHSPST--RFVEGMLNICYNAVDRHIENG 123
Cdd:PLN02654 23 QALVS-SPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKWegdevcSENLDVRKGPISieWFKGGKTNICYNCLDRNVEAG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 124 KGDKIAIIYDSPVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFAS 203
Cdd:PLN02654 102 NGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 204 KELSSRIDHVKPKVVVTASfGIEPGRRVEYVP-LVEEALKIGQHKP---DKILIY-NRPNM--EAVPLAPGRDLDWDEEM 276
Cdd:PLN02654 182 ESLAQRIVDCKPKVVITCN-AVKRGPKTINLKdIVDAALDESAKNGvsvGICLTYeNQLAMkrEDTKWQEGRDVWWQDVV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 277 AK-AQSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPL 355
Cdd:PLN02654 261 PNyPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPM 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 356 LHGNTTVLYEGKPvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEWS 435
Cdd:PLN02654 341 LNGATVLVFEGAP-NYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRD--GDEYVTRHSRKSLRVLGSVGEPINPSAWRWF 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 436 KNVF---RVPVLDHWWQTETGSPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLpPGAF 512
Cdd:PLN02654 418 FNVVgdsRCPISDTWWQTETGGFMITPLPGAWPQK---PGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKSW-PGAF 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 513 SGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPL 592
Cdd:PLN02654 494 RTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEV 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 593 KGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYKI--TSTIE 670
Cdd:PLN02654 574 KGQGIYAFVTLVEGVPYSEE-LRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDELgdTSTLA 652
|
650
....*....|....*
gi 32258701 671 DPSIfghVEEMLKQA 685
Cdd:PLN02654 653 DPGV---VDQLIALA 664
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
62-684 |
6.64e-126 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 387.56 E-value: 6.64e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 62 YKTHFAASVTDPERFWGKAAEQ-ISWYKPWTKTLENKHSPSTRFVEGMLNICYNAVDRHIENG-KGDKIAIIYDSPVTNT 139
Cdd:PTZ00237 10 YENDSNYANSNPESFWDEVAKKyVHWDKMYDKVYSGDEIYPDWFKGGELNTCYNVLDIHVKNPlKRDQDALIYECPYLKK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 140 KATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVV 219
Cdd:PTZ00237 90 TIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLII 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 220 TASFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRPN---------MEAVPLAPGrDLDWDEEMAK----AQS--HDC 284
Cdd:PTZ00237 170 TTNYGILNDEIITFTPNLKEAIELSTFKPSNVITLFRNDitsesdlkkIETIPTIPN-TLSWYDEIKKikenNQSpfYEY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 285 VPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVLY 364
Cdd:PTZ00237 249 VPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFL-YGSLSLGNTFVMF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 365 EGKPVGTPDAGAYF-RVLAEHGVAALFTAPTAIRAIRQQDPGAA-LGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVP 442
Cdd:PTZ00237 328 EGGIIKNKHIEDDLwNTIEKHKVTHTLTLPKTIRYLIKTDPEATiIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIK 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 443 VLDHWWQTETGspiTASCVGLGNSKTpPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEAF 522
Cdd:PTZ00237 408 SSRGYGQTEIG---ITYLYCYGHINI-PYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKLPMPPSFATTFYKNDEKF 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 523 KHLyFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCV 602
Cdd:PTZ00237 484 KQL-FSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLV 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 603 LRKDINATE---EQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYKITSTIEDPSIFGHVE 679
Cdd:PTZ00237 563 LKQDQSNQSidlNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLNDSNYQLPDNVNDSEIFYKIK 642
|
....*
gi 32258701 680 EMLKQ 684
Cdd:PTZ00237 643 ELYMK 647
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
77-671 |
1.75e-120 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 371.15 E-value: 1.75e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 77 WGKAAEQISWYKpwtktlenkhspstrfvEGMLNICYNAVDRHIENGKGDKIAIIYDSPvtNTKATFTYKEVLEQVSKLA 156
Cdd:PRK04319 27 WEEVEKEFSWLE-----------------TGKVNIAYEAIDRHADGGRKDKVALRYLDA--SRKEKYTYKELKELSNKFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 157 GVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTAsfgiepgrrveyvpl 236
Cdd:PRK04319 88 NVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITT--------------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 237 veEALKigQHKPDKILiynrPNMEAVPL------APGRDLDWDEEMAKAQSH-DCVPVLSEHPLYILYTSGTTGLPKGVI 309
Cdd:PRK04319 153 --PALL--ERKPADDL----PSLKHVLLvgedveEGPGTLDFNALMEQASDEfDIEWTDREDGAILHYTSGSTGKPKGVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 310 RPTGgyAVMLHWsMSSIYGL--QPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPvgtpDAGAYFRVLAEHGVA 387
Cdd:PRK04319 225 HVHN--AMLQHY-QTGKYVLdlHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGGRF----SPERWYRILEDYKVT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 388 ALFTAPTAIRAIRQQdpGAALGKQYSLTRFKtlFVA--GERCDVETLEWSKNVFRVPVLDHWWQTETGSPITAscvglgN 465
Cdd:PRK04319 298 VWYTAPTAIRMLMGA--GDDLVKKYDLSSLR--HILsvGEPLNPEVVRWGMKVFGLPIHDNWWMTETGGIMIA------N 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 466 SKTPP--PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPpGAFSGLWKNQEAFKHlYFEkfPGYYDTMDAGYMD 543
Cdd:PRK04319 368 YPAMDikPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWP-SMMRGIWNNPEKYES-YFA--GDWYVSGDSAYMD 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 544 EEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVR 623
Cdd:PRK04319 444 EDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEE-LKEEIRGFVK 522
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 32258701 624 QNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYKITSTIED 671
Cdd:PRK04319 523 KGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWELGLPEGDLSTMED 570
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
61-672 |
7.99e-108 |
|
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: 339.47 E-value: 7.99e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 61 EYKTHFAASVTDPERFWGKAAEQ--ISWYKPWTKTLE-NKHSPSTR-FVEGMLNICYNAVDRHIENGKgDKIAIIYDSPV 136
Cdd:cd05968 8 DLEAFLERSAEDNAWFWGEFVKDvgIEWYEPPYQTLDlSGGKPWAAwFVGGRMNIVEQLLDKWLADTR-TRPALRWEGED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 137 TNTKaTFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPK 216
Cdd:cd05968 87 GTSR-TLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 217 VVVTASFGIEPGRRVEyvpLVEEALKIGQHKP--DKILIYNRPNMeAVPLAPGRDLDWDEEMAKAQSHdCVPVLSEHPLY 294
Cdd:cd05968 166 ALITADGFTRRGREVN---LKEEADKACAQCPtvEKVVVVRHLGN-DFTPAKGRDLSYDEEKETAGDG-AERTESEDPLM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 295 ILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGhSYICYGPLLHGNTTVLYEGKPvGTPDA 374
Cdd:cd05968 241 IIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMG-PWLIFGGLILGATMVLYDGAP-DHPKA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 375 GAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF---RVPVLDHWWQTE 451
Cdd:cd05968 319 DRLWRMVEDHEITHLGLSPTLIRALKPR--GDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVgkgRNPIINYSGGTE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 452 TGSPItascvgLGNSKTPP--PGQAGKSVPGYNVMILDDNMQKLKARcLGNIVVKLPLPpGAFSGLWKNQEAFKHLYFEK 529
Cdd:cd05968 397 ISGGI------LGNVLIKPikPSSFNGPVPGMKADVLDESGKPARPE-VGELVLLAPWP-GMTRGFWRDEDRYLETYWSR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 530 FPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINA 609
Cdd:cd05968 469 FDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTP 548
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32258701 610 TEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYKITSTIEDP 672
Cdd:cd05968 549 TEA-LAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGKELGDLSSLENP 610
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
143-656 |
9.58e-107 |
|
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: 330.84 E-value: 9.58e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 143 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTAS 222
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 223 fgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrdldwdeemakaqshdcvpvlsEHPLYILYTSGTT 302
Cdd:cd05972 81 -------------------------------------------------------------------EDPALIYFTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 303 GLPKGVIRPTGgyAVMLHWS-MSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgtpDAGAYFRVL 381
Cdd:cd05972 94 GLPKGVLHTHS--YPLGHIPtAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRF---DAERILELL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 382 AEHGVAALFTAPTAIRAIRQQDPgaalgKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGspitascV 461
Cdd:cd05972 169 ERYGVTSFCGPPTAYRMLIKQDL-----SSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETG-------L 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 462 GLGNSKTPP--PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDA 539
Cdd:cd05972 237 TVGNFPDMPvkPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLP-PPGLFLGYVGDPEKTEASIRG---DYYLTGDR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 540 GYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVlEEIV 619
Cdd:cd05972 313 AYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELA-EELQ 391
|
490 500 510
....*....|....*....|....*....|....*..
gi 32258701 620 KHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 656
Cdd:cd05972 392 GHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
143-657 |
1.74e-105 |
|
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: 327.92 E-value: 1.74e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 143 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTAs 222
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 223 fgiepgrrveyvplvEEalkigqhkpdkilIYNRPNMEavplapgrdldwdeemakaqshdcvpvlseHPLYILYTSGTT 302
Cdd:cd05969 80 ---------------EE-------------LYERTDPE------------------------------DPTLLHYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 303 GLPKGVIRPTGgyAVMLHW-SMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPvgtpDAGAYFRVL 381
Cdd:cd05969 102 GTPKGVLHVHD--AMIFYYfTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF----DAESWYGII 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 382 AEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITASCV 461
Cdd:cd05969 176 ERVKVTVWYTAPTAIRMLMKE--GDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 462 GLgnskTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlPLPPGAFSGLWKNQEAFKhLYFEKfpGYYDTMDAGY 541
Cdd:cd05969 254 CM----PIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALK-PGWPSMFRGIWNDEERYK-NSFID--GWYLTGDLAY 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 542 MDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKH 621
Cdd:cd05969 326 RDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDE-LKEEIINF 404
|
490 500 510
....*....|....*....|....*....|....*.
gi 32258701 622 VRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAI 657
Cdd:cd05969 405 VRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAK 440
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
125-654 |
9.47e-90 |
|
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: 287.09 E-value: 9.47e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 125 GDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 204
Cdd:COG0318 13 PDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 205 ELSSRIDHVKPKVVVTAsfgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrdldwdeemakaqshdc 284
Cdd:COG0318 87 ELAYILEDSGARALVTA--------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 285 vpvlsehplYILYTSGTTGLPKGVIRPTGGYAVMLhWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLY 364
Cdd:COG0318 104 ---------LILYTSGTTGRPKGVMLTHRNLLANA-AAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 365 EGkpvgtPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAAlgkQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVL 444
Cdd:COG0318 174 PR-----FDPERVLELIERERVTVLFGVPTMLARLLRH-PEFA---RYDLSSLRLVVSGGAPLPPELLERFEERFGVRIV 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 445 DHWWQTETGSPITascVGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKh 524
Cdd:COG0318 245 EGYGLTETSPVVT---VNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVR---GPNVMKGYWNDPEATA- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 525 lyfEKFP-GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVL 603
Cdd:COG0318 318 ---EAFRdGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVL 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 32258701 604 RKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:COG0318 395 RPGAELDAEELRA----FLRERLARYKVPRRVEFVDELPRTASGKIDRRAL 441
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
122-561 |
6.42e-88 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 281.51 E-value: 6.42e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 122 NGKGDKIAIIYDSPVTntkatFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGF 201
Cdd:pfam00501 6 ARTPDKTALEVGEGRR-----LTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 202 ASKELSSRIDHVKPKVVVTASFGIepgrrveyVPLVEEALKIGQHKPDKILIYnrpnmeAVPLAPGRDLDWDEEMAKAQS 281
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALK--------LEELLEALGKLEVVKLVLVLD------RDPVLKEEPLPEEAKPADVPP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 282 HDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGG--YAVMLHWSMS-SIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHG 358
Cdd:pfam00501 147 PPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNlvANVLSIKRVRpRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 359 NTTVLYEGKPvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaalGKQYSLTRFKTLFVAGERCDVETLEWSKNV 438
Cdd:pfam00501 227 ATVVLPPGFP--ALDPAALLELIERYKVTVLYGVPTLLNMLLEAGA----PKRALLSSLRLVLSGGAPLPPELARRFREL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 439 FRVPVLDHWWQTETGSPITasCVGLGNSKTPPPGQAGKSVPGYNVMILDDN-MQKLKARCLGNIVVKlplPPGAFSGLWK 517
Cdd:pfam00501 301 FGGALVNGYGLTETTGVVT--TPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR---GPGVMKGYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 32258701 518 NQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVA 561
Cdd:pfam00501 376 DPELTAEAFDED--GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
291-649 |
1.12e-82 |
|
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: 264.92 E-value: 1.12e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 291 HPLYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVvGHSYICYGPLLHGNTTVLYEGkpvg 370
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAA-LAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 371 tPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQT 450
Cdd:cd04433 75 -FDPEAALELIEREKVTILLGVPTLLARLLKAPESAG----YDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 451 ETGSPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPpgaFSGLWKNQEAFkhlYFEKF 530
Cdd:cd04433 150 ETGGTVATGPPDDDARK---PGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSV---MKGYWNNPEAT---AAVDE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 531 PGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINAT 610
Cdd:cd04433 221 DGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLD 300
|
330 340 350
....*....|....*....|....*....|....*....
gi 32258701 611 EeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKI 649
Cdd:cd04433 301 A----EELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
143-654 |
2.53e-74 |
|
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: 246.28 E-value: 2.53e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 143 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTas 222
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 223 fgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrDLDwdeemakaQSHDcvpvLSEHPLYILYTSGTT 302
Cdd:cd05973 79 ----------------------------------------------DAA--------NRHK----LDSDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 303 GLPKGVIRPTGgYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKpvGTPDAgaYFRVLA 382
Cdd:cd05973 101 GLPKGVPVPLR-ALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGG--FSVES--TWRVIE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 383 EHGVAALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTlfvAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPItasCVG 462
Cdd:cd05973 176 RLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRRVSS---AGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVL---ANH 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 463 LGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPP-GAFSGLWK-NQEAFKHlyfekfpGYYDTMDAG 540
Cdd:cd05973 250 HALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPlMWFRGYQLpDTPAIDG-------GYYLTGDTV 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 541 YMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVK 620
Cdd:cd05973 323 EFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPA-LADELQL 401
|
490 500 510
....*....|....*....|....*....|....
gi 32258701 621 HVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05973 402 HVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLL 435
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
138-656 |
1.67e-71 |
|
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: 238.87 E-value: 1.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 138 NTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKV 217
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 218 VVTasfgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrdldwDEemakaqshdcvpvlSEHPLYILY 297
Cdd:cd05971 82 LVT----------------------------------------------------DG--------------SDDPALIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 298 TSGTTGLPKGVIRptgGYAVML-H---WSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVgtpD 373
Cdd:cd05971 96 TSGTTGPPKGALH---AHRVLLgHlpgVQFPFNLFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKF---D 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 374 AGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaalGKQYSLT--RFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTE 451
Cdd:cd05971 170 PKAALDLMSRYGVTTAFLPPTALKMMRQQ------GEQLKHAqvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 452 tGSPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlPPGAFSGLWKNQEAFKhlyfEKFP 531
Cdd:cd05971 244 -CNLVIGNCSALFPIK---PGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELP-DPVAFLGYWNNPSATE----KKMA 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 532 G-YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDInAT 610
Cdd:cd05971 315 GdWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGE-TP 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 32258701 611 EEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 656
Cdd:cd05971 394 SDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
139-649 |
7.63e-67 |
|
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: 227.87 E-value: 7.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 139 TKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVV 218
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 219 VTASFGIEPgrrveyvplVEEALKIGQHKPDKILIYNRP----NMEAVPLAPGRDLDWDEEMAKAQSHDcvpvlseHPLY 294
Cdd:cd05911 87 FTDPDGLEK---------VKEAAKELGPKDKIIVLDDKPdgvlSIEDLLSPTLGEEDEDLPPPLKDGKD-------DTAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 295 ILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYG-LQPGEVWWAASDLGWVVG-HSYICYgpLLHGNTTVLYEGkpvgtP 372
Cdd:cd05911 151 ILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGnDGSNDVILGFLPLYHIYGlFTTLAS--LLNGATVIIMPK-----F 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 373 DAGAYFRVLAEHGVAALFTAPtAIRAIRQQDPgaaLGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWW-QTE 451
Cdd:cd05911 224 DSELFLDLIEKYKITFLYLVP-PIAAALAKSP---LLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYgMTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 452 TGSPITascvglgnsKTPP----PGQAGKSVPGYNVMILDDN-MQKLKARCLGNIVVKLPLppgAFSGLWKNQEAFKHLY 526
Cdd:cd05911 300 TGGILT---------VNPDgddkPGSVGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQ---VMKGYYNNPEATKETF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 527 FEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKD 606
Cdd:cd05911 368 DED--GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPG 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 32258701 607 INATEeqvlEEIVKHVRQNIGPVAAFRNAV-FVKQLPKTRSGKI 649
Cdd:cd05911 446 EKLTE----KEVKDYVAKKVASYKQLRGGVvFVDEIPKSASGKI 485
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
110-654 |
4.89e-65 |
|
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: 224.30 E-value: 4.89e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 110 NICYNAVDRHIENgKGDKIAIIYDSPVTNTKaTFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACAR 189
Cdd:cd05970 17 NFAYDVVDAMAKE-YPDKLALVWCDDAGEER-IFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 190 IGAIHSLIFGGFASKELSSRIDHVKPKVVVTASFGIEPGR---RVEYVPLVEEALKIGQHKPDKILIYNRPNMEAVPLAP 266
Cdd:cd05970 95 LGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEEiekAAPECPSKPKLVWVGDPVPEGWIDFRKLIKNASPDFE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 267 GRdldwdeemakaqsHDCVPVLSEHPLYILYTSGTTGLPKGV----IRPTGGYAVMLHWsmssiYGLQPGEVWWAASDLG 342
Cdd:cd05970 175 RP-------------TANSYPCGEDILLVYFSSGTTGMPKMVehdfTYPLGHIVTAKYW-----QNVREGGLHLTVADTG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 343 WVVGHSYICYGPLLHGNTTVLYEgkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaalgKQYSLTRFKTLFV 422
Cdd:cd05970 237 WGKAVWGKIYGQWIAGAAVFVYD---YDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDL-----SRYDLSSLRYCTT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 423 AGERCDVETLEWSKNVFRVPVLDHWWQTETGSPI-TASCVglgnskTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNI 501
Cdd:cd05970 309 AGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIaTFPWM------EPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 502 VVKLP--LPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGT 579
Cdd:cd05970 383 VIRTSkgKPVGLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPA 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32258701 580 VADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05970 460 VLECAVTGVPDPIRGQVVKATIVLAKGYEPSEE-LKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
125-651 |
5.15e-62 |
|
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: 213.24 E-value: 5.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 125 GDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 204
Cdd:cd17631 9 PDRTALVFGG------RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 205 ELSSRIDHVKPKVVVtasfgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrdldwdeemakaqsHDc 284
Cdd:cd17631 83 EVAYILADSGAKVLF--------------------------------------------------------------DD- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 285 vpvlsehPLYILYTSGTTGLPKGVIRPtggYAVMLHWSMSSIY--GLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTV 362
Cdd:cd17631 100 -------LALLMYTSGTTGRPKGAMLT---HRNLLWNAVNALAalDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 363 LYEGkpvgtPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAAlgkQYSLTRFKTLFVAGERCDVETLE-WSknVFRV 441
Cdd:cd17631 170 ILRK-----FDPETVLDLIERHRVTSFFLVPTMIQALLQH-PRFA---TTDLSSLRAVIYGGAPMPERLLRaLQ--ARGV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 442 PVLDHWWQTETGSPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEA 521
Cdd:cd17631 239 KFVQGYGMTETSPGVTFLSPEDHRRK---LGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVR---GPHVMAGYWNRPEA 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 522 ----FKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVP 597
Cdd:cd17631 313 taaaFRD-------GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAV 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 32258701 598 LALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 651
Cdd:cd17631 386 VAVVVPRPGAELDE----DELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
125-654 |
8.19e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 215.05 E-value: 8.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 125 GDKIAiiydspVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAI-HSL-IFggFA 202
Cdd:PRK06187 20 PDKEA------VYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVlHPInIR--LK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 203 SKELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKIGQHKPDKILIYNRPNMEAVPLAPgrdlDWDEEMAKAQSH 282
Cdd:PRK06187 92 PEEIAYILNDAEDRVVLVDS---------EFVPLLAAILPQLPTVRTVIVEGDGPAAPLAPEVG----EYEELLAAASDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 283 DCVPVLSEHPLY-ILYTSGTTGLPKGVIrptggYA---VMLHwSMSSIYGLQpgevwWAASDLGWVV---GHSY---ICY 352
Cdd:PRK06187 159 FDFPDIDENDAAaMLYTSGTTGHPKGVV-----LShrnLFLH-SLAVCAWLK-----LSRDDVYLVIvpmFHVHawgLPY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 353 GPLLHGNTTVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVETL 432
Cdd:PRK06187 228 LALMAGAKQVI-----PRRFDPENLLDLIETERVTFFFAVPTIWQMLLK----APRAYFVDFSSLRLVIYGGAALPPALL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 433 EWSKNVFRVPVLDHWWQTETGSPITAScvglgnsktPPPGQ----------AGKSVPGYNVMILDDNMQKLKARC--LGN 500
Cdd:PRK06187 299 REFKEKFGIDLVQGYGMTETSPVVSVL---------PPEDQlpgqwtkrrsAGRPLPGVEARIVDDDGDELPPDGgeVGE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 501 IVVKlplPPGAFSGLWKNQEAFKhlyfEKFP-GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGT 579
Cdd:PRK06187 370 IIVR---GPWLMQGYWNRPEATA----ETIDgGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPA 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32258701 580 VADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:PRK06187 443 VAEVAVIGVPDEKWGERPVAVVVLKPGATLDA----KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
69-672 |
1.39e-59 |
|
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: 211.36 E-value: 1.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 69 SVTDPERFWGKAAE--QISWYKPWTKTLENKH-SPSTRFVEGM-LNICYNAVdRHIENGkgDKIAIIYDSpvTNTKATFT 144
Cdd:cd05943 26 SVDDPGAFWAAVWDfsGVRGSKPYDVVVVSGRiMPGARWFPGArLNYAENLL-RHADAD--DPAAIYAAE--DGERTEVT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 145 YKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASFG 224
Cdd:cd05943 101 WAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 225 IEPGRRveyVPLVEEALKIGQHKPDKI------LIYNRPNMEAVPLAPGRDLDWDEEMAKAQSHDCVPVLSEHPLYILYT 298
Cdd:cd05943 181 TYNGKR---HDVREKVAELVKGLPSLLavvvvpYTVAAGQPDLSKIAKALTLEDFLATGAAGELEFEPLPFDHPLYILYS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 299 SGTTGLPKGVIRPTGGY------AVMLHWSMssiyglQPGEVWWAASDLGWVVGHSYIcyGPLLHGNTTVLYEGKPvGTP 372
Cdd:cd05943 258 SGTTGLPKCIVHGAGGTllqhlkEHILHCDL------RPGDRLFYYTTCGWMMWNWLV--SGLAVGATIVLYDGSP-FYP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 373 DAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEW-SKNVFRvpvlDHWWQTE 451
Cdd:cd05943 329 DTNALWDLADEEGITVFGTSAKYLDALEKA--GLKPAETHDLSSLRTILSTGSPLKPESFDYvYDHIKP----DVLLASI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 452 TGSPITASCVGLGNSKTPP-PGQAGKSVPGYNVMILDDNMQKLKARcLGNIVVKLPLP--PGAFsglWKNQEA--FKHLY 526
Cdd:cd05943 403 SGGTDIISCFVGGNPLLPVyRGEIQCRGLGMAVEAFDEEGKPVWGE-KGELVCTKPFPsmPVGF---WNDPDGsrYRAAY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 527 FEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDP-LKGHVPLALcVLRK 605
Cdd:cd05943 479 FAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKdGDERVILFV-KLRE 557
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32258701 606 DINATEEqVLEEIVKHVRQNIGPvaafR---NAVF-VKQLPKTRSGKIPRSALSAIVNGKPYKITSTIEDP 672
Cdd:cd05943 558 GVELDDE-LRKRIRSTIRSALSP----RhvpAKIIaVPDIPRTLSGKKVEVAVKKIIAGRPVKNAGALANP 623
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
122-654 |
3.55e-59 |
|
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: 208.09 E-value: 3.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 122 NGKGDKIaiiydspvtntkaTFTYKEVLEQVSKLAGVLVKH-GIKKGDTVVIYMPMIPQAMYTMLACARIGAIhsLIFGG 200
Cdd:cd05928 34 NGKGDEV-------------KWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLV--FIPGT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 201 --FASKELSSRIDHVKPKVVVTASfgiEPGRRVEYVPLVEEALKIgqhkpdKILIYNRPnmeavplapgRD--LDWDEEM 276
Cdd:cd05928 99 iqLTAKDILYRLQASKAKCIVTSD---ELAPEVDSVASECPSLKT------KLLVSEKS----------RDgwLNFKELL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 277 AKA-QSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPL 355
Cdd:cd05928 160 NEAsTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 356 LHGNTTVLYEGKPVgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaalgKQYSLTRFKTLFVAGERCDVETLEWS 435
Cdd:cd05928 240 IQGACVFVHHLPRF---DPLVILKTLSSYPITTFCGAPTVYRMLVQQDL-----SSYKFPSLQHCVTGGEPLNPEVLEKW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 436 KNVFRVPVLDHWWQTETGspitascVGLGNSKTP--PPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKL-PLPP-GA 511
Cdd:cd05928 312 KAQTGLDIYEGYGQTETG-------LICANFKGMkiKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVkPIRPfGL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 512 FSGLWKNQEAFKHLYFEKFpgyYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDP 591
Cdd:cd05928 385 FSGYVDNPEKTAATIRGDF---YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32258701 592 LKGHVPLALCVLRKDINATE-EQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05928 462 IRGEVVKAFVVLAPQFLSHDpEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
69-662 |
1.56e-58 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 209.27 E-value: 1.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 69 SVTDPERFWGKAAE--QISWYKPWTKTLENKHSPSTR-FVEGMLNICYNAVdRHienGKGDKIAIIYDSPvTNTKATFTY 145
Cdd:PRK03584 43 SVEDLEAFWQSVWDffGVIGSTPYTVVLAGRRMPGARwFPGARLNYAENLL-RH---RRDDRPAIIFRGE-DGPRRELSW 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 146 KEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA---S 222
Cdd:PRK03584 118 AELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVdgyR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 223 FGiepGRRVEYVPLVEE---ALKIGQHkpdkILIYNRPNMEAVPLAPGRDLDWDE--EMAKAQSHDCVPVLSEHPLYILY 297
Cdd:PRK03584 198 YG---GKAFDRRAKVAElraALPSLEH----VVVVPYLGPAAAAAALPGALLWEDflAPAEAAELEFEPVPFDHPLWILY 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 298 TSGTTGLPKGVIRPTGG------YAVMLHWsmssiyGLQPGE-VWWAASdLGW------VVGhsyicygpLLHGNTTVLY 364
Cdd:PRK03584 271 SSGTTGLPKCIVHGHGGillehlKELGLHC------DLGPGDrFFWYTT-CGWmmwnwlVSG--------LLVGATLVLY 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 365 EGKPvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEW-SKNVFRvpv 443
Cdd:PRK03584 336 DGSP-FYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKA--GLVPGETHDLSALRTIGSTGSPLPPEGFDWvYEHVKA--- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 444 lDHWWQTETGSPITASCVGLGNSKTPP-PGQAGKSVPGYNVMILDDNMQKLKARcLGNIVVKLPLP--PgafSGLW--KN 518
Cdd:PRK03584 410 -DVWLASISGGTDICSCFVGGNPLLPVyRGEIQCRGLGMAVEAWDEDGRPVVGE-VGELVCTKPFPsmP---LGFWndPD 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 519 QEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAG-------AIEEsilshgtVADCAVVGKEDP 591
Cdd:PRK03584 485 GSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAeiyrqveALPE-------VLDSLVIGQEWP 557
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32258701 592 LKG-HVPLaLCVLRKDINATEEqVLEEIVKHVRQNIGP--VAAfrNAVFVKQLPKTRSGKIPRSALSAIVNGKP 662
Cdd:PRK03584 558 DGDvRMPL-FVVLAEGVTLDDA-LRARIRTTIRTNLSPrhVPD--KIIAVPDIPRTLSGKKVELPVKKLLHGRP 627
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
124-654 |
4.08e-50 |
|
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: 181.61 E-value: 4.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 124 KGDKIAIIydspvtNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAI---HSLIFGG 200
Cdd:cd05936 12 FPDKTALI------FMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVvvpLNPLYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 201 fasKELSSRIDHVKPKVVVTA-SFgiepgrrveyvplvEEALKIGqhkpdkiliynrpnmEAVPLAPGRDLDwdeemaka 279
Cdd:cd05936 86 ---RELEHILNDSGAKALIVAvSF--------------TDLLAAG---------------APLGERVALTPE-------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 280 qshD-CVpvlsehplyILYTSGTTGLPKGVirptggyavML-HWSMSSIygLQPGEVWWAASDLGwvvGHSYICYGPLLH 357
Cdd:cd05936 126 ---DvAV---------LQYTSGTTGVPKGA---------MLtHRNLVAN--ALQIKAWLEDLLEG---DDVVLAALPLFH 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 358 --------------GNTTVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGaalgKQYSLTRFKTLFVA 423
Cdd:cd05936 180 vfgltvalllplalGATIVL-----IPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEF----KKRDFSSLRLCISG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 424 GERCDVETLEWSKNVFRVPVLDHWWQTETgSPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVV 503
Cdd:cd05936 251 GAPLPVEVAERFEELTGVPIVEGYGLTET-SPVVAVNPLDGPRK---PGSIGIPLPGTEVKIVDDDGEELPPGEVGELWV 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 504 KlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADC 583
Cdd:cd05936 327 R---GPQVMKGYWNRPEETAEAFVD---GWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEA 400
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32258701 584 AVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05936 401 AVVGVPDPYSGEAVKAFVVLKEGASLTE----EEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
143-654 |
8.58e-50 |
|
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: 179.41 E-value: 8.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 143 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTAs 222
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 223 fgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrdldwdeemakaqshdcvpvlsehPLYILYTSGTT 302
Cdd:cd05934 83 ---------------------------------------------------------------------PASILYTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 303 GLPKGVIRPtggYAVMLHW--SMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEgkpvgTPDAGAYFRV 380
Cdd:cd05934 94 GPPKGVVIT---HANLTFAgyYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLP-----RFSASRFWSD 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 381 LAEHGVAALFTAPTAIRAIRQQDPGAalgkQYSLTRFKTLFVAGERCDVETlEWSKNvFRVPVLDHWWQTETGSPITASC 460
Cdd:cd05934 166 VRRYGATVTNYLGAMLSYLLAQPPSP----DDRAHRLRAAYGAPNPPELHE-EFEER-FGVRLLEGYGMTETIVGVIGPR 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 461 VGlgnskTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEA----FKHlyfekfpGYYDT 536
Cdd:cd05934 240 DE-----PRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGLRGWGFFKGYYNMPEAtaeaMRN-------GWFHT 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 537 MDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlE 616
Cdd:cd05934 308 GDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDP----E 383
|
490 500 510
....*....|....*....|....*....|....*...
gi 32258701 617 EIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05934 384 ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
113-654 |
1.08e-48 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 178.72 E-value: 1.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 113 YNA---VDRHIENGKGDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACAR 189
Cdd:cd05959 3 YNAatlVDLNLNEGRGDKTAFIDDA------GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 190 IGAIHSLIFGGFASKELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKIGQHKpDKILIYNRPNMEAVPLAPGRD 269
Cdd:cd05959 77 AGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG---------ELAPVLAAALTKSEHT-LVVLIVSGGAGPEAGALLLAE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 270 L--DWDEEMAKAQSHdcvpvlSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGH 347
Cdd:cd05959 147 LvaAEAEQLKPAATH------ADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 348 SYICYGPLLHGNTTVLYEGKPvgTPDAgaYFRVLAEHGVAALFTAPTaIRAIRQQDPGAalgKQYSLTRFKTLFVAGERC 427
Cdd:cd05959 221 GNSLTFPLSVGATTVLMPERP--TPAA--VFKRIRRYRPTVFFGVPT-LYAAMLAAPNL---PSRDLSSLRLCVSAGEAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 428 DVETLEWSKNVFRVPVLDHWWQTETGSpitascVGLGNskTP---PPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVK 504
Cdd:cd05959 293 PAEVGERWKARFGLDILDGIGSTEMLH------IFLSN--RPgrvRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 505 lplPPGAFSGLWKNQEAFKhlyfEKFPGY-YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADC 583
Cdd:cd05959 365 ---GPSSATMYWNNRDKTR----DTFQGEwTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEA 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32258701 584 AVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05959 438 AVVGVEDEDGLTKPKAFVVLRPGYEDSEA-LEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
126-649 |
4.87e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 174.35 E-value: 4.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PRK08316 26 DKTALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 LSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKigQHKPDKILiynRPNMEAVPLAPGRDLDWDEeMAKAQS--HD 283
Cdd:PRK08316 100 LAYILDHSGARAFLVDP---------ALAPTAEAALA--LLPVDTLI---LSLVLGGREAPGGWLDFAD-WAEAGSvaEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 284 CVPVLSEHPLYILYTSGTTGLPKGvirptggyAVMLHWS-----MSSIYGLQpgevwWAASDlgwVVGHS---YIC---- 351
Cdd:PRK08316 165 DVELADDDLAQILYTSGTESLPKG--------AMLTHRAliaeyVSCIVAGD-----MSADD---IPLHAlplYHCaqld 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 352 --YGPLLH-GNTTVLYEGkpvgtPDAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDPGaalgkQYSLTRFKTLFVAGERC 427
Cdd:PRK08316 229 vfLGPYLYvGATNVILDA-----PDPELILRTIEAERITSFFAPPTVwISLLRHPDFD-----TRDLSSLRKGYYGASIM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 428 DVETLEWSKNvfRVPVLDHW---WQTETGSPITAscvgLGnsktpP------PGQAGKsvPGYNV--MILDDNMQKLKAR 496
Cdd:PRK08316 299 PVEVLKELRE--RLPGLRFYncyGQTEIAPLATV----LG-----PeehlrrPGSAGR--PVLNVetRVVDDDGNDVAPG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 497 CLGNIVVKlplPPGAFSGLWKN----QEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:PRK08316 366 EVGEIVHR---SPQLMLGYWDDpektAEAFRG-------GWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEE 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32258701 573 SILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKI 649
Cdd:PRK08316 436 ALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTE----DELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
136-655 |
5.33e-47 |
|
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: 173.65 E-value: 5.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 136 VTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKP 215
Cdd:cd05926 8 VPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 216 KVVVTASFGIEP---GRRVEYVPLVEEALkigqhkpDKILIYNRPNMEAVPLAPGrDLDWDEEMAKAQSHDcvPVLsehp 292
Cdd:cd05926 88 KLVLTPKGELGPasrAASKLGLAILELAL-------DVGVLIRAPSAESLSNLLA-DKKNAKSEGVPLPDD--LAL---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 293 lyILYTSGTTGLPKGV-IRPTggyavMLHWSMSSI---YGLQPgevwwaaSDLGWVVGhsyicygPLLHGN-------TT 361
Cdd:cd05926 154 --ILHTSGTTGRPKGVpLTHR-----NLAASATNItntYKLTP-------DDRTLVVM-------PLFHVHglvasllST 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 362 VLYEGKPVGTP--DAGAYFRVLAEHGvAALFTA-PTaIRAIRQQDPGAALGKQYSLTRFktLFVAGERCDVETLEWSKNV 438
Cdd:cd05926 213 LAAGGSVVLPPrfSASTFWPDVRDYN-ATWYTAvPT-IHQILLNRPEPNPESPPPKLRF--IRSCSASLPPAVLEALEAT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 439 FRVPVLDHWWQTETGSPITASCVglgNSKTPPPGQAGKSVpGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKN 518
Cdd:cd05926 289 FGAPVLEAYGMTEAAHQMTSNPL---PPGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLR---GPNVTRGYLNN 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 519 QEAFKHlYFEKFpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPL 598
Cdd:cd05926 362 PEANAE-AAFKD-GWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVA 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 599 ALCVLRKDINATEeqvlEEIVKHVRQNIgpvAAF---RNAVFVKQLPKTRSGKIPRSALS 655
Cdd:cd05926 440 AAVVLREGASVTE----EELRAFCRKHL---AAFkvpKKVYFVDELPKTATGKIQRRKVA 492
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
126-654 |
9.67e-47 |
|
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: 171.56 E-value: 9.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIhslifggfaske 205
Cdd:cd05930 2 DAVAVVDGD------QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAA------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 lssridhvkpkvvvtasfgiepgrrveYVPLveealkigqhkpdkiliynrpnmeavplapgrDLDWDEEMAKAQSHDCV 285
Cdd:cd05930 64 ---------------------------YVPL--------------------------------DPSYPAERLAYILEDSG 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 286 PVL----SEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTT 361
Cdd:cd05930 85 AKLvltdPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW-MQEAYPLTPGDRVLQFTSFSFDVSVWEI-FGALLAGATL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 362 VLYEGKPVGTPDAgaYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqyslTRFKTLFVAGERCDVETLE-WSKNVFR 440
Cdd:cd05930 163 VVLPEEVRKDPEA--LADLLAEEGITVLHLTPSLLRLLLQELELAAL------PSLRLVLVGGEALPPDLVRrWRELLPG 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 441 VPVLDHWWQTETGSPITASCVGLGN-SKTPPPgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLW--- 516
Cdd:cd05930 235 ARLVNLYGPTEATVDATYYRVPPDDeEDGRVP--IGRPIPNTRVYVLDENLR--------------PVPPGVPGELYigg 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 517 ------------KNQEAFKHLYFekFPG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVAD 582
Cdd:cd05930 299 aglargylnrpeLTAERFVPNPF--GPGerMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVRE 376
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32258701 583 CAVVGKEDPLKGHVPLALCVLRKDinatEEQVLEEIVKHVRQNIGPV---AAFrnaVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05930 377 AAVVAREDGDGEKRLVAYVVPDEG----GELDEEELRAHLAERLPDYmvpSAF---VVLDALPLTPNGKVDRKAL 444
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
142-654 |
1.60e-45 |
|
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: 168.04 E-value: 1.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 142 TFTYKEVLEQVSKLAGVLV-KHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT 220
Cdd:cd05958 10 EWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVALC 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 221 AsfgiepgrrveyvplveEALKigqhKPDKILIYNrpnmeavplapgrdldwdeemakaqshdcvpvlsehplyilYTSG 300
Cdd:cd05958 90 A-----------------HALT----ASDDICILA-----------------------------------------FTSG 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 301 TTGLPKGVIRPTGGY-AVMLHWSMSsIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKpvgTPDAgaYFR 379
Cdd:cd05958 108 TTGAPKATMHFHRDPlASADRYAVN-VLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA---TPDL--LLS 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 380 VLAEHGVAALFTAPTAIRAIRQQDPGAalgkQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETgspitas 459
Cdd:cd05958 182 AIARYKPTVLFTAPTAYRAMLAHPDAA----GPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEM------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 460 cVGLGNSKTPP---PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlppgafSGLWKNQEAFKHLYFEKfpGYYDT 536
Cdd:cd05958 251 -FHIFISARPGdarPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP------TGCRYLADKRQRTYVQG--GWNIT 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 537 MDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDInATEEQVLE 616
Cdd:cd05958 322 GDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGV-IPGPVLAR 400
|
490 500 510
....*....|....*....|....*....|....*...
gi 32258701 617 EIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05958 401 ELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
126-661 |
1.92e-43 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 163.21 E-value: 1.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDspvtNTKATFtyKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PRK03640 17 DRTAIEFE----EKKVTF--MELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 LSSRIDHVKPKVVVTASfGIEPGRRVEYVPLVEEAlkigqhkpdkiliynrPNMEAVPLAPGRDLDWDEEMAkaqshdcv 285
Cdd:PRK03640 91 LLWQLDDAEVKCLITDD-DFEAKLIPGISVKFAEL----------------MNGPKEEAEIQEEFDLDEVAT-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 286 pvlsehplyILYTSGTTGLPKGVIRPTGGyavmlHW--SMSSI--YGLQPGEVWWAASDLGWVVGHSyICYGPLLHGNTT 361
Cdd:PRK03640 146 ---------IMYTSGTTGKPKGVIQTYGN-----HWwsAVGSAlnLGLTEDDCWLAAVPIFHISGLS-ILMRSVIYGMRV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 362 VLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkQYSLTrFKTLFVAGERCDVETLEWSKNvFRV 441
Cdd:PRK03640 211 VLVE-----KFDAEKINKLLQTGGVTIISVVSTMLQRLLERLGEG----TYPSS-FRCMLLGGGPAPKPLLEQCKE-KGI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 442 PVLDHWWQTETGSPITascvglgnskTPPP-------GQAGKSVPGYNVMILDDNmQKLKARCLGNIVVKLP-LPPGAFS 513
Cdd:PRK03640 280 PVYQSYGMTETASQIV----------TLSPedaltklGSAGKPLFPCELKIEKDG-VVVPPFEEGEIVVKGPnVTKGYLN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 514 GLWKNQEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLK 593
Cdd:PRK03640 349 REDATRETFQD-------GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKW 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32258701 594 GHVPLALCVLRKDINateeqvLEEIVKHVRQNIG----PVAAFrnavFVKQLPKTRSGKIPRSALSAIVNGK 661
Cdd:PRK03640 422 GQVPVAFVVKSGEVT------EEELRHFCEEKLAkykvPKRFY----FVEELPRNASGKLLRHELKQLVEEM 483
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
125-654 |
5.68e-43 |
|
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: 162.40 E-value: 5.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 125 GDKIAIIyDSPvtnTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 204
Cdd:cd05904 19 PSRPALI-DAA---TGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 205 ELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKigqhkpdKILIYNRPnmEAVPLAPGRDLDWDEEMAKAQshdc 284
Cdd:cd05904 95 EIAKQVKDSGAKLAFTTA---------ELAEKLASLAL-------PVVLLDSA--EFDSLSFSDLLFEADEAEPPV---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 285 VPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVM---LHWSMSSiyGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTT 361
Cdd:cd05904 153 VVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMvaqFVAGEGS--NSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 362 VLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF-R 440
Cdd:cd05904 231 VV-----MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKS----PIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFpN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 441 VPVLDHWWQTETgSPITASCVGLGNSKTPPpGQAGKSVPGYNVMILDdnmqklkarclgnIVVKLPLPPGaFSG-LW--- 516
Cdd:cd05904 302 VDLGQGYGMTES-TGVVAMCFAPEKDRAKY-GSVGRLVPNVEAKIVD-------------PETGESLPPN-QTGeLWirg 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 517 --------KNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGK 588
Cdd:cd05904 366 psimkgylNNPEATAATIDKE--GWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPY 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32258701 589 EDPLKGHVPLALCVLRKDINATEEQVLEEIVKHVrqniGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05904 444 PDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQV----APYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
142-654 |
4.39e-42 |
|
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: 158.39 E-value: 4.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 142 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 221
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 222 sfgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrdldwDEEMAkaqshdcvpvlsehplYILYTSGT 301
Cdd:cd05919 90 ---------------------------------------------------ADDIA----------------YLLYSSGT 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 302 TGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDL--GWVVGHSYIcyGPLLHGNTTVLYEGKPvgtpDAGAYFR 379
Cdd:cd05919 103 TGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNSLW--FPLAVGASAVLNPGWP----TAERVLA 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 380 VLAEHGVAALFTAPTAIRAIRQQdpgaALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITAS 459
Cdd:cd05919 177 TLARFRPTVLYGVPTFYANLLDS----CAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSN 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 460 CVGLGNsktppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlppGAFSGLWKNQEAFKHLYFEkfpGYYDTMDA 539
Cdd:cd05919 253 RPGAWR-----LGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGP---SAAVGYWNNPEKSRATFNG---GWYRTGDK 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 540 GYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDpLKGHVPLALCVLRKDINATEEQVLEEIV 619
Cdd:cd05919 322 FCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPE-STGLSRLTAFVVLKSPAAPQESLARDIH 400
|
490 500 510
....*....|....*....|....*....|....*
gi 32258701 620 KHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05919 401 RHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
144-585 |
4.77e-41 |
|
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: 154.73 E-value: 4.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 144 TYKEVLEQVSKLAGVLVK-HGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASkelsSRIDHV----KPKVV 218
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPA----ERLAFIledaGARLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 219 VTASfgiepgrrvEYVPLVEEalkigqhkpdkiliynrpnMEAVPLAPGRDLDWDEEMAKAQSHDCVPVLSEHPLYILYT 298
Cdd:TIGR01733 77 LTDS---------ALASRLAG-------------------LVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 299 SGTTGLPKGVIRPTGGyAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVLYEGKPVGtPDAGAYF 378
Cdd:TIGR01733 129 SGSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEI-FGALLAGATLVVPPEDEER-DDAALLA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 379 RVLAEHGVAALFTAPTAIRAIRQQDPGAalgkqysLTRFKTLFVAGERCDVETLE-WSKNVFRVPVLDHWWQTET--GSP 455
Cdd:TIGR01733 206 ALIAEHPVTVLNLTPSLLALLAAALPPA-------LASLRLVILGGEALTPALVDrWRARGPGARLINLYGPTETtvWST 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 456 ITASCVGLGNSKTPPPgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVklpLPPGAFSGLW----KNQEAFK-HLYF-EK 529
Cdd:TIGR01733 279 ATLVDPDDAPRESPVP--IGRPLANTRLYVLDDDLRPVPVGVVGELYI---GGPGVARGYLnrpeLTAERFVpDPFAgGD 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 32258701 530 FPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAV 585
Cdd:TIGR01733 354 GARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
142-649 |
7.81e-41 |
|
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: 154.85 E-value: 7.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 142 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTa 221
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 222 sfgiePGRrveyvplveealkIGQHKPdkiliynrpnmEAVPLAPGrdldwdeemakaqshdcvpvlsehplYILYTSGT 301
Cdd:cd05903 80 -----PER-------------FRQFDP-----------AAMPDAVA--------------------------LLLFTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 302 TGLPKGVIRPtggyAVMLHWSMSSI---YGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEgkpVGTPDAGAyf 378
Cdd:cd05903 105 TGEPKGVMHS----HNTLSASIRQYaerLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD---IWDPDKAL-- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 379 RVLAEHGVAALFTAPT----AIRAIRQQDPgaalgkqySLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGS 454
Cdd:cd05903 176 ALMREHGVTFMMGATPfltdLLNAVEEAGE--------PLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 455 pitascvGLGNSKTPPPGQA----GKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQeafkHLYFEKF 530
Cdd:cd05903 248 -------AVTSITPAPEDRRlytdGRPLPGVEIKVVDDTGATLAPGVEGELLSR---GPSVFLGYLDRP----DLTADAA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 531 P-GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINA 609
Cdd:cd05903 314 PeGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALL 393
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 32258701 610 TeeqvLEEIVKHV-RQNIGPVAAFRNAVFVKQLPKTRSGKI 649
Cdd:cd05903 394 T----FDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
141-654 |
4.59e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 151.85 E-value: 4.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 141 ATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT 220
Cdd:PRK07786 41 NTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 221 ASF--GIEPGRRvEYVPLVEEALKIGQHKPDKILIYNRPNMEAVPLAPGRDLDWDEemakaqshdcvpvlsehPLYILYT 298
Cdd:PRK07786 121 EAAlaPVATAVR-DIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDS-----------------PALIMYT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 299 SGTTGLPKGvirptggyAVMLHWSMSS-----IYGLQ---PGEVWWAASDLGWVVGHSYICYGPLLhGNTTVLYegkPVG 370
Cdd:PRK07786 183 SGTTGRPKG--------AVLTHANLTGqamtcLRTNGadiNSDVGFVGVPLFHIAGIGSMLPGLLL-GAPTVIY---PLG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 371 TPDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPGAAlGKQYSLtRFKTlFVAGERCDVETLEWSKNVFRVPVLDHWWQT 450
Cdd:PRK07786 251 AFDPGQLLDVLEAEKVTGIFLVPAQWQAV-CAEQQAR-PRDLAL-RVLS-WGAAPASDTLLRQMAATFPEAQILAAFGQT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 451 ETgSPITasCVGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKhlyfEKF 530
Cdd:PRK07786 327 EM-SPVT--CMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYR---APTLMSGYWNNPEATA----EAF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 531 PG-YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRkdiNA 609
Cdd:PRK07786 397 AGgWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVR---ND 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 32258701 610 TEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:PRK07786 474 DAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
143-656 |
5.36e-39 |
|
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: 149.64 E-value: 5.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 143 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHvkpkvvvtas 222
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDR---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 223 fgiepGRRVeyVPLVEEAlkigQHKPDKILIYnrpnmeavplapgrdldwdeemakaqshdcvpvlsehplyilYTSGTT 302
Cdd:cd05974 71 -----GGAV--YAAVDEN----THADDPMLLY------------------------------------------FTSGTT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 303 GLPKGVIRPTGGYAVMlHWSMSSIYGLQPGEVWWAASDLGWVvGHSYIC-YGPLLHGNTTVLYEGKPVgtpDAGAYFRVL 381
Cdd:cd05974 98 SKPKLVEHTHRSYPVG-HLSTMYWIGLKPGDVHWNISSPGWA-KHAWSCfFAPWNAGATVFLFNYARF---DAKRVLAAL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 382 AEHGVAALFTAPTAIRAIRQQDpgaalgkqysLTRFKT----LFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPIt 457
Cdd:cd05974 173 VRYGVTTLCAPPTVWRMLIQQD----------LASFDVklreVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALV- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 458 ascvglGNSKTPP--PGQAGKSVPGYNVMILDDNMQKLKArclGNIVVKL--PLPPGAFSGLWKNQEAFKHLYFEkfpGY 533
Cdd:cd05974 242 ------GNSPGQPvkAGSMGRPLPGYRVALLDPDGAPATE---GEVALDLgdTRPVGLMKGYAGDPDKTAHAMRG---GY 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 534 YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQ 613
Cdd:cd05974 310 YRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPET 389
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 32258701 614 VLeEIVKHVRQNIGPVAAFRNAVFVkQLPKTRSGKIPRSALSA 656
Cdd:cd05974 390 AL-EIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRR 430
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
114-656 |
4.53e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 148.60 E-value: 4.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 114 NAVDRHiengkGDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQA----MYTMLACAR 189
Cdd:PRK06188 20 SALKRY-----PDRPALVLGD------TRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVlmaiGAAQLAGLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 190 IGAIHSLifggfaskelSSRIDHVkpkvVVTASFGIEpGRRVEYVPLVEEALKIGQHKPdkiliyNRPNMEAV-PLAPGR 268
Cdd:PRK06188 89 RTALHPL----------GSLDDHA----YVLEDAGIS-TLIVDPAPFVERALALLARVP------SLKHVLTLgPVPDGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 269 DLdwdeeMAKAQSHDCVPVLSEH----PLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSsiyglqpgevwwaasDLGWV 344
Cdd:PRK06188 148 DL-----LAAAAKFGPAPLVAAAlppdIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLA---------------EWEWP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 345 VGHSYICYGPLLH------------GNTTVLYEGKpvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqY 412
Cdd:PRK06188 208 ADPRFLMCTPLSHaggafflptllrGGTVIVLAKF-----DPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRT----R 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 413 SLTRFKTLFVAGERCD----VETLEWSKNVFrvpvLDHWWQTETGSPIT---------------ASCvglgnsktpppgq 473
Cdd:PRK06188 279 DLSSLETVYYGASPMSpvrlAEAIERFGPIF----AQYYGQTEAPMVITylrkrdhdpddpkrlTSC------------- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 474 aGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGafsGLWK----NQEAFKHlyfekfpGYYDTMDAGYMDEEGYLY 549
Cdd:PRK06188 342 -GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMD---GYWNrpeeTAEAFRD-------GWLHTGDVAREDEDGFYY 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 550 VMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPV 629
Cdd:PRK06188 411 IVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA----AELQAHVKERKGSV 486
|
570 580
....*....|....*....|....*..
gi 32258701 630 AAFRNAVFVKQLPKTRSGKIPRSALSA 656
Cdd:PRK06188 487 HAPKQVDFVDSLPLTALGKPDKKALRA 513
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
125-654 |
1.07e-37 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 148.95 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 125 GDKIAIIY--DSPVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIG---AIHSLIFG 199
Cdd:PRK07529 39 PDAPALSFllDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGianPINPLLEP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 200 GfaskELSSRIDHVKPKVVVTAsfGIEPGRRV-EYVPLVEEALKIGQHkpdkILIYN------RPNMEAVPL----APGR 268
Cdd:PRK07529 119 E----QIAELLRAAGAKVLVTL--GPFPGTDIwQKVAEVLAALPELRT----VVEVDlarylpGPKRLAVPLirrkAHAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 269 DLDWDEEMAK--AQSHDCVPVLSEHPLYILY-TSGTTGLPKGVIRPTGGYAVMlHWSMSSIYGLQPGEVWWAASDLGWVV 345
Cdd:PRK07529 189 ILDFDAELARqpGDRLFSGRPIGPDDVAAYFhTGGTTGMPKLAQHTHGNEVAN-AWLGALLLGLGPGDTVFCGLPLFHVN 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 346 GHSYICYGPLLHGNTTVLyeGKPVGTPDAGAY---FRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqySLTRFKTLFV 422
Cdd:PRK07529 268 ALLVTGLAPLARGAHVVL--ATPQGYRGPGVIanfWKIVERYRINFLSGVPTVYAALLQVPVDGH-----DISSLRYALC 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 423 AGERCDVETLEWSKNVFRVPVLDHWWQTEtgspitASCVglgNSKTPP-----PGQAGKSVPGYNV--MILDDN---MQK 492
Cdd:PRK07529 341 GAAPLPVEVFRRFEAATGVRIVEGYGLTE------ATCV---SSVNPPdgerrIGSVGLRLPYQRVrvVILDDAgryLRD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 493 LKARCLGNIVVKlplPPGAFSGlWKNQEAFKHLYFEkfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEE 572
Cdd:PRK07529 412 CAVDEVGVLCIA---GPNVFSG-YLEAAHNKGLWLE--DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 573 SILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAV-FVKQLPKTRSGKIPR 651
Cdd:PRK07529 486 ALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLA----FARDHIAERAAVPKHVrILDALPKTAVGKIFK 561
|
...
gi 32258701 652 SAL 654
Cdd:PRK07529 562 PAL 564
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
143-657 |
2.33e-37 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 146.83 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 143 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTAS 222
Cdd:PRK06155 47 WTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 223 FGIEpgrRVEYVPLVEEALKigqhkpdKILIYNRPNMEAVPLAPgrdlDWDEEMAKAQSHDCVPVLSEHPLYILYTSGTT 302
Cdd:PRK06155 127 ALLA---ALEAADPGDLPLP-------AVWLLDAPASVSVPAGW----STAPLPPLDAPAPAAAVQPGDTAAILYTSGTT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 303 GLPKGVIRPTGGYavmlhwsmssiyglqpgeVWW---AASDLGWVVGHSYICYGPLLHGNT------TVLYEGKPVGTP- 372
Cdd:PRK06155 193 GPSKGVCCPHAQF------------------YWWgrnSAEDLEIGADDVLYTTLPLFHTNAlnaffqALLAGATYVLEPr 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 373 -DAGAYFRVLAEHGvAALFTAPTAIRAIRQQDPGAALGKQYSLT---------RFKTLFvaGERcdvetlewsknvFRVP 442
Cdd:PRK06155 255 fSASGFWPAVRRHG-ATVTYLLGAMVSILLSQPARESDRAHRVRvalgpgvpaALHAAF--RER------------FGVD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 443 VLDHWWQTETGSPITAScvglgnSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPlPPGAF-SGLW----K 517
Cdd:PRK06155 320 LLDGYGSTETNFVIAVT------HGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAD-EPFAFaTGYFgmpeK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 518 NQEAFKHLYFEkfpgyydTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVP 597
Cdd:PRK06155 393 TVEAWRNLWFH-------TGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEV 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32258701 598 LALCVLRkdinatEEQVLE--EIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAI 657
Cdd:PRK06155 466 MAAVVLR------DGTALEpvALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
118-654 |
1.51e-35 |
|
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: 141.23 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 118 RHIENGKGDKiAIIYDSPvTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAI-HSL 196
Cdd:cd12119 3 EHAARLHGDR-EIVSRTH-EGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVlHTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 197 IFGGFAsKELSSRIDHVKPKVVVtasfgIEPgrrvEYVPLVEEALkiGQHKPDKILIYNRPNMEAVPLAPGRDLDWDEEM 276
Cdd:cd12119 81 NPRLFP-EQIAYIINHAEDRVVF-----VDR----DFLPLLEAIA--PRLPTVEHVVVMTDDAAMPEPAGVGVLAYEELL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 277 AKAQSHDCVPVLSEH-PLYILYTSGTTGLPKGVIrptggY---AVMLHwSMSSiygLQPGEVWWAASDlgwvvghSYICY 352
Cdd:cd12119 149 AAESPEYDWPDFDENtAAAICYTSGTTGNPKGVV-----YshrSLVLH-AMAA---LLTDGLGLSESD-------VVLPV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 353 GPLLHGN------TTVLYEGK---PVGTPDAGAYFRVLAEHGVAalFTA--PTAIRAIRQQdPGAALGKQYSLTRfktLF 421
Cdd:cd12119 213 VPMFHVNawglpyAAAMVGAKlvlPGPYLDPASLAELIEREGVT--FAAgvPTVWQGLLDH-LEANGRDLSSLRR---VV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 422 VAGERCDVETLEWsknvFR---VPVLDHWWQTETgSPI-TASCVGLGNSKTPPPGQA------GKSVPGYNVMILDDNMQ 491
Cdd:cd12119 287 IGGSAVPRSLIEA----FEergVRVIHAWGMTET-SPLgTVARPPSEHSNLSEDEQLalrakqGRPVPGVELRIVDDDGR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 492 KLKA--RCLGNIVVKLP-LPPGAFsglwKNQEAfKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAG 568
Cdd:cd12119 362 ELPWdgKAVGELQVRGPwVTKSYY----KNDEE-SEALTED--GWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSV 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 569 AIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGK 648
Cdd:cd12119 435 ELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTA----EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGK 510
|
....*.
gi 32258701 649 IPRSAL 654
Cdd:cd12119 511 IDKKAL 516
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
144-654 |
3.65e-35 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 138.38 E-value: 3.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 144 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASf 223
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 224 giepgrrveyvplveealkigqhkpdkiliynrpNMEAVPLAPgrdldwdeemakaqshdcvpvlsehplyilYTSGTTG 303
Cdd:cd05935 82 ----------------------------------ELDDLALIP------------------------------YTSGTTG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 304 LPKGVIRpTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLyegkpVGTPDAGAYFRVLAE 383
Cdd:cd05935 98 LPKGCMH-THFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVL-----MARWDRETALELIEK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 384 HGVAALFTAPTAIRAIrQQDPGAalgKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITascvgl 463
Cdd:cd05935 172 YKVTFWTNIPTMLVDL-LATPEF---KTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTH------ 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 464 gnskTPPPGQAGKS---VPGYNV--MILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWK----NQEAFKHLYFEKFpgy 533
Cdd:cd05935 242 ----TNPPLRPKLQclgIP*FGVdaRVIDiETGRELPPNEVGEIVVR---GPQIFKGYWNrpeeTEESFIEIKGRRF--- 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 534 YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQ 613
Cdd:cd05935 312 FRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKVTE 391
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 32258701 614 vlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05935 392 --EDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
100-651 |
3.96e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 140.18 E-value: 3.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 100 PSTRFVEGMLNICYNAVDRHiengkGDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQ 179
Cdd:PRK07470 1 PMSRRVMNLAHFLRQAARRF-----PDRIALVWGD------RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 180 AMYTMLACARIGAihslifggfaskelssridhvkpkVVVTASFGIEPGrrveyvplveEALKIGQHKPDKILIYNRPNM 259
Cdd:PRK07470 70 MFESMFAAFRLGA------------------------VWVPTNFRQTPD----------EVAYLAEASGARAMICHADFP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 260 EAVPL---------------APGRDLDWDEEMAKAQSHDCVPVLSEH--PLYILYTSGTTGLPKGvirptggyAVMLHWS 322
Cdd:PRK07470 116 EHAAAvraaspdlthvvaigGARAGLDYEALVARHLGARVANAAVDHddPCWFFFTSGTTGRPKA--------AVLTHGQ 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 323 MSSIYG-----LQPGEvwwAASDLGWVVGhsyicygPLLHGN------------TTVLYEGKPVgtpDAGAYFRVLAEHG 385
Cdd:PRK07470 188 MAFVITnhladLMPGT---TEQDASLVVA-------PLSHGAgihqlcqvargaATVLLPSERF---DPAEVWALVERHR 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 386 VAALFTAPTaIRAIRQQDPGAALGKQYSLtrfKTLFVAGE---RCDvetlewSKNVFRV--PVLDHWWqtetgspitasc 460
Cdd:PRK07470 255 VTNLFTVPT-ILKMLVEHPAVDRYDHSSL---RYVIYAGApmyRAD------QKRALAKlgKVLVQYF------------ 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 461 vGL----GNSKTPPP-------------GQAGKSVPGYNVMILDDNMQKLKARCLGNIVVklpLPPGAFSGLWKNQEA-- 521
Cdd:PRK07470 313 -GLgevtGNITVLPPalhdaedgpdariGTCGFERTGMEVQIQDDEGRELPPGETGEICV---IGPAVFAGYYNNPEAna 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 522 --FKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLA 599
Cdd:PRK07470 389 kaFRD-------GWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVA 461
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 32258701 600 LCVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 651
Cdd:PRK07470 462 VCVARDGAPVDEAELLA----WLDGKVARYKLPKRFFFWDALPKSGYGKITK 509
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
126-656 |
4.87e-35 |
|
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: 143.07 E-value: 4.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMP----MIPqamyTMLACARIGAihslifggf 201
Cdd:COG1020 491 DAVAVVFGD------QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLErsleMVV----ALLAVLKAGA--------- 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 202 askelssridhvkpkvvvtAsfgiepgrrveYVPL------------VEEAlkigqhKPdKILIYNRPNMEAVPLAPGRD 269
Cdd:COG1020 552 -------------------A-----------YVPLdpaypaerlaymLEDA------GA-RLVLTQSALAARLPELGVPV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 270 LDWDEEMAKAQSHD--CVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGH 347
Cdd:COG1020 595 LALDALALAAEPATnpPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAW-MQRRYGLGPGDRVLQFASLSFDASV 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 348 SYIcYGPLLHGNTTVLYEgkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkqysLTRFKTLFVAGERC 427
Cdd:COG1020 674 WEI-FGALLSGATLVLAP--PEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEA-------LPSLRLVLVGGEAL 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 428 DVETLE-WSKNVFRVPVLDHWWQTETGspITASCvglgnSKTPPPGQAGKSVP------GYNVMILDDNMQklkarclgn 500
Cdd:COG1020 744 PPELVRrWRARLPGARLVNLYGPTETT--VDSTY-----YEVTPPDADGGSVPigrpiaNTRVYVLDAHLQ--------- 807
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 501 ivvklPLPPGAfSG-LW---------------KNQEAFKHLYFEkFPG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAG 562
Cdd:COG1020 808 -----PVPVGV-PGeLYiggaglargylnrpeLTAERFVADPFG-FPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRG 880
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 563 HRISAGAIEESILSHGTVADCAVVGKEDPLkGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFrnaVFVKQLP 642
Cdd:COG1020 881 FRIELGEIEAALLQHPGVREAVVVAREDAP-GDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAV---VLLLPLP 956
|
570
....*....|....
gi 32258701 643 KTRSGKIPRSALSA 656
Cdd:COG1020 957 LTGNGKLDRLALPA 970
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
142-654 |
2.92e-34 |
|
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: 135.55 E-value: 2.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 142 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 221
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKLDDIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 222 SfgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrdldwdeemakaqshdcvpvlsehplyILYTSGT 301
Cdd:cd05912 81 T------------------------------------------------------------------------IMYTSGT 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 302 TGLPKGVIRPTGGyavmlHW-----SMSSIyGLQPGEVWWAASDLGWVVGHSYICYGpLLHGNTTVLYEgkpvgTPDAGA 376
Cdd:cd05912 89 TGKPKGVQQTFGN-----HWwsaigSALNL-GLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVD-----KFDAEQ 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 377 YFRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkqYSLTrFKTLFVAGERCDVETLEWSKNvFRVPVLDHWWQTETGSPI 456
Cdd:cd05912 157 VLHLINSGKVTIISVVPTMLQRLLEILGEG-----YPNN-LRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETCSQI 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 457 TASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKarcLGNIVVKLP-LPPGAFSGLWKNQEAFKHlyfekfpGYYD 535
Cdd:cd05912 230 VTLSPEDALNK---IGSAGKPLFPVELKIEDDGQPPYE---VGEILLKGPnVTKGYLNRPDATEESFEN-------GWFK 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 536 TMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINAteeqvl 615
Cdd:cd05912 297 TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISE------ 370
|
490 500 510
....*....|....*....|....*....|....*....
gi 32258701 616 EEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05912 371 EELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
126-654 |
2.42e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 135.05 E-value: 2.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIyMPMIPQAM-YTMLACARIGAIHSLIFGGFASK 204
Cdd:PRK07788 64 DRAALIDE------RGTLTYAELDEQSNALARGLLALGVRAGDGVAV-LARNHRGFvLALYAAGKVGARIILLNTGFSGP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 205 ELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEAlkigqhKPD--KILIYNRPNMEAVPLAPG-RDLDwdeEMAKAQS 281
Cdd:PRK07788 137 QLAEVAAREGVKALVYDD---------EFTDLLSAL------PPDlgRLRAWGGNPDDDEPSGSTdETLD---DLIAGSS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 282 HDCVPVLSEHPLYILYTSGTTGLPKGVIRPTggyavmlhwsmssIYGLQPgevwwAASDLGWV---VGHSYICYGPLLH- 357
Cdd:PRK07788 199 TAPLPKPPKPGGIVILTSGTTGTPKGAPRPE-------------PSPLAP-----LAGLLSRVpfrAGETTLLPAPMFHa 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 358 ------------GNTTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIRaiRQQDPGAALGKQYSLTRFKTLFVAGE 425
Cdd:PRK07788 261 tgwahltlamalGSTVVLRR-----RFDPEATLEDIAKHKATALVVVPVMLS--RILDLGPEVLAKYDTSSLKIIFVSGS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 426 RCDVETLEWSKNVFRvPVLDHWW-QTETGSPITAscvglgnskTPP-----PGQAGKSVPGYNVMILDDNMQKLKARCLG 499
Cdd:PRK07788 334 ALSPELATRALEAFG-PVLYNLYgSTEVAFATIA---------TPEdlaeaPGTVGRPPKGVTVKILDENGNEVPRGVVG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 500 NIVVKLPLPpgaFSGlwknqeafkhlYF-----EKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESI 574
Cdd:PRK07788 404 RIFVGNGFP---FEG-----------YTdgrdkQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 575 LSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:PRK07788 470 AGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKD----YVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
117-662 |
1.64e-32 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 132.48 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 117 DRHIENgKGDKIAIIYDSPVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSL 196
Cdd:PRK13295 31 DACVAS-CPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 197 IFGGFASKELSSRIDHVKPKV-VVTASF----------GIEPGrrveyVPLVEEALKIGQHKPDkiliynrpNMEAVPLA 265
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVlVVPKTFrgfdhaamarRLRPE-----LPALRHVVVVGGDGAD--------SFEALLIT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 266 PgrdlDWDEEmakaqsHDCVPVLSEHPL------YILYTSGTTGLPKGVirptggyavmLHWS---MSSIY------GLQ 330
Cdd:PRK13295 177 P----AWEQE------PDAPAILARLRPgpddvtQLIYTSGTTGEPKGV----------MHTAntlMANIVpyaerlGLG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 331 PGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEgkpVGTPDAGAyfRVLAEHGVAalFT---APTAIRAIRQQDPGAa 407
Cdd:PRK13295 237 ADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD---IWDPARAA--ELIRTEGVT--FTmasTPFLTDLTRAVKESG- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 408 lgkqYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSpitASCVGLGNSKTPPPGQAGKSVPGYNVMILD 487
Cdd:PRK13295 309 ----RPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA---VTLTKLDDPDERASTTDGCPLPGVEVRVVD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 488 DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQeafkHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISA 567
Cdd:PRK13295 382 ADGAPLPAGQIGRLQVR---GCSNFGGYLKRP----QLNGTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 568 GAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRkdinATEEQVLEEIV-----KHVRQNIGPvaafRNAVFVKQLP 642
Cdd:PRK13295 455 VEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPR----PGQSLDFEEMVeflkaQKVAKQYIP----ERLVVRDALP 526
|
570 580
....*....|....*....|
gi 32258701 643 KTRSGKIPRSALSAIVNGKP 662
Cdd:PRK13295 527 RTPSGKIQKFRLREMLRGED 546
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
144-654 |
1.74e-32 |
|
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: 131.86 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 144 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASf 223
Cdd:cd05923 30 TYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAV- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 224 gIEPGRRVEYVPLVEEaLKIGQHKPDKILIYNRPNMEAVPLAPgrdldwdeemakaqshdcvpvlsEHPLYILYTSGTTG 303
Cdd:cd05923 109 -DAQVMDAIFQSGVRV-LALSDLVGLGEPESAGPLIEDPPREP-----------------------EQPAFVFYTSGTTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 304 LPKGVIRP----------TGGYAVMLHWSMSSIYGLQPgevwwaasdLGWVVGHSYICYGPLLHGNTTVlyegkPVGTPD 373
Cdd:cd05923 164 LPKGAVIPqraaesrvlfMSTQAGLRHGRHNVVLGLMP---------LYHVIGFFAVLVAALALDGTYV-----VVEEFD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 374 AGAYFRVLAEHGVAALFTAPTAIRAIrqqdPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETG 453
Cdd:cd05923 230 PADALKLIEQERVTSLFATPTHLDAL----AAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 454 SPITAscvglgnsKTPPPGQAGKsvPGYN-----VMILDDNMQKLKARCLGNIVVKLPlPPGAFSGLWKNQEA-FKHLYF 527
Cdd:cd05923 306 NSLYM--------RDARTGTEMR--PGFFsevriVRIGGSPDEALANGEEGELIVAAA-ADAAFTGYLNQPEAtAKKLQD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 528 ekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLAlCVLRKDI 607
Cdd:cd05923 375 ----GWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTA-CVVPREG 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 32258701 608 NATEEQvLEEIVKHvrqniGPVAAF---RNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05923 450 TLSADE-LDQFCRA-----SELADFkrpRRYFFLDELPKNAMNKVLRRQL 493
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
136-656 |
4.25e-32 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 131.06 E-value: 4.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 136 VTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKP 215
Cdd:TIGR03098 19 LVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 216 KVVVTASfgiepgrrvEYVPLVEEALKiGQHKPDKILIYNRPNMEAVPLAPGRDLDWDEEMAKAQSHDCVPVLSEHPLYI 295
Cdd:TIGR03098 99 RLLVTSS---------ERLDLLHPALP-GCHDLRTLIIVGDPAHASEGHPGEEPASWPKLLALGDADPPHPVIDSDMAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 296 LYTSGTTGLPKGVIRP-----TGGYAVmlhwsmSSIYGLQPGEVWWAASDLGWVVGHSYICYGpLLHGNTTVLYE---GK 367
Cdd:TIGR03098 169 LYTSGSTGRPKGVVLShrnlvAGAQSV------ATYLENRPDDRLLAVLPLSFDYGFNQLTTA-FYVGATVVLHDyllPR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 368 PVGT--------------------------PDAGAYFRVLAEHGVAalfTAPTAIRAIRQQDPGAALGKQYSLTR-FKTL 420
Cdd:TIGR03098 242 DVLKalekhgitglaavpplwaqlaqldwpESAAPSLRYLTNSGGA---MPRATLSRLRSFLPNARLFLMYGLTEaFRST 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 421 FVAGERCDVEtlewsknvfrvpvldhwwqtetgspitascvglgnsktppPGQAGKSVPGYNVMILDDnmqkLKARCL-- 498
Cdd:TIGR03098 319 YLPPEEVDRR----------------------------------------PDSIGKAIPNAEVLVLRE----DGSECApg 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 499 --GNIVVKLPLppgAFSGLWKNQEAFKHLyFEKFPGYYDTM----------DAGYMDEEGYLYVMSRVDDVINVAGHRIS 566
Cdd:TIGR03098 355 eeGELVHRGAL---VAMGYWNDPEKTAER-FRPLPPFPGELhlpelavwsgDTVRRDEEGFLYFVGRRDEMIKTSGYRVS 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 567 AGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPvaafRNAVFVKQLPKTRS 646
Cdd:TIGR03098 431 PTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDRAALLAECRARLPNYMVP----ALIHVRQALPRNAN 506
|
570
....*....|
gi 32258701 647 GKIPRSALSA 656
Cdd:TIGR03098 507 GKIDRKALAK 516
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
59-654 |
4.51e-32 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 132.90 E-value: 4.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 59 GSEYK---THFAA----SVTDPERFWGKAAEQ--ISWYKPWTKTLE--NKHSPSTRFVEG-MLNI---CYNAVDrhieNG 123
Cdd:PLN03052 112 GSKYKdpiSSFSEfqrfSVENPEVYWSIVLDElsLVFSVPPRCILDtsDESNPGGQWLPGaVLNVaecCLTPKP----SK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 124 KGDKIAIIY------DSPVTntkaTFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLI 197
Cdd:PLN03052 188 TDDSIAIIWrdegsdDLPVN----RMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSI 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 198 FGGFASKELSSRIDHVKPKVVVTASFGIEPGRRVEYVPLVEEAlkigqHKPDKILIYNRPNMEAVPLAPGrDLDWDEEMA 277
Cdd:PLN03052 264 ADSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLYSRVVEA-----KAPKAIVLPADGKSVRVKLREG-DMSWDDFLA 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 278 KAQSHDC----VPVlsEHPL----YILYTSGTTGLPKGV--IRPTGGYAVMLHWSMSSIyglQPGEVWWAASDLGWVVGH 347
Cdd:PLN03052 338 RANGLRRpdeyKAV--EQPVeaftNILFSSGTTGEPKAIpwTQLTPLRAAADAWAHLDI---RKGDIVCWPTNLGWMMGP 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 348 sYICYGPLLHGNTTVLYEGKPVGTpdagAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqySLTRFKTLFVAGERC 427
Cdd:PLN03052 413 -WLVYASLLNGATLALYNGSPLGR----GFAKFVQDAKVTMLGTVPSIVKTWKNTNCMAGL----DWSSIRCFGSTGEAS 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 428 DVETLEW--SKNVFRvPVLDHWWQTETGSP-ITASCVglgnsktPPPGQAGKSVP--GYNVMILDDNMQKL--KARCLGN 500
Cdd:PLN03052 484 SVDDYLWlmSRAGYK-PIIEYCGGTELGGGfVTGSLL-------QPQAFAAFSTPamGCKLFILDDSGNPYpdDAPCTGE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 501 IVVkLPLPPGAFSGLWkNQEAFKhLYFEKFPGYYDTMDAGYMDE-----EGYLYVMSRVDDVINVAGHRISAGAIEESI- 574
Cdd:PLN03052 556 LAL-FPLMFGASSTLL-NADHYK-VYFKGMPVFNGKILRRHGDIfertsGGYYRAHGRADDTMNLGGIKVSSVEIERVCn 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 575 LSHGTVADCAVVGKEDPLKGhvPLALC---VLRKDINATEEqvLEEIVK----HVRQNIGPVAAFRNAVFVKQLPKTRSG 647
Cdd:PLN03052 633 AADESVLETAAIGVPPPGGG--PEQLViaaVLKDPPGSNPD--LNELKKifnsAIQKKLNPLFKVSAVVIVPSFPRTASN 708
|
....*..
gi 32258701 648 KIPRSAL 654
Cdd:PLN03052 709 KVMRRVL 715
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
139-657 |
5.21e-32 |
|
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: 130.72 E-value: 5.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 139 TKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVV 218
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 219 VTASFGIEPgrrveyVPLVEEALKIGQhkpdKILIynrpnmeavpLAPGRDLDWDEEMAKAQSHDCVPVLSEHPL----- 293
Cdd:cd17642 121 FCSKKGLQK------VLNVQKKLKIIK----TIII----------LDSKEDYKGYQCLYTFITQNLPPGFNEYDFkppsf 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 294 -------YILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVvgHSYICY---GPLLHGNTTVL 363
Cdd:cd17642 181 drdeqvaLIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFH--HGFGMFttlGYLICGFRVVL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 364 yegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrqqdPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVP- 442
Cdd:cd17642 259 -----MYKFEEELFLRSLQDYKVQSALLVPTLFAFF----AKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPg 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 443 VLDHWWQTETGSPITAScvglgNSKTPPPGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEA 521
Cdd:cd17642 330 IRQGYGLTETTSAILIT-----PEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVK---GPMIMKGYVNNPEA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 522 FKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALC 601
Cdd:cd17642 402 TKALIDKD--GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVV 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 32258701 602 VLRKDINATEEqvleEIVKHVRQNIGPVAAFRNAV-FVKQLPKTRSGKIPRSALSAI 657
Cdd:cd17642 480 VLEAGKTMTEK----EVMDYVASQVSTAKRLRGGVkFVDEVPKGLTGKIDRRKIREI 532
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
125-654 |
1.80e-31 |
|
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: 128.18 E-value: 1.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 125 GDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfask 204
Cdd:cd12116 1 PDATAVRDDD------RSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAY---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 205 elssridhvkpkVVVTASFgiePGRRVEYVplVEEAlkigqhKPDKILIynRPNMEAVPLAPGRDLDWDEEMAKAQSHDC 284
Cdd:cd12116 65 ------------VPLDPDY---PADRLRYI--LEDA------EPALVLT--DDALPDRLPAGLPVLLLALAAAAAAPAAP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 285 -VPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHwSMSSIYGLQPGEVWWAASDlgwvvghsyIC--------YGPL 355
Cdd:cd12116 120 rTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH-SMRERLGLGPGDRLLAVTT---------YAfdisllelLLPL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 356 LHGNTTVLYEGKpvGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGKqysltrfkTLFVAGERCDVETLEws 435
Cdd:cd12116 190 LAGARVVIAPRE--TQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRAGL--------TALCGGEALPPDLAA-- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 436 KNVFRVPVLdhwWQ----TETgsPITASCVGLGNSKTPPPgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGA 511
Cdd:cd12116 258 RLLSRVGSL---WNlygpTET--TIWSTAARVTAAAGPIP--IGRPLANTQVYVLDAALR--------------PVPPGV 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 512 FSGLWKNQEAFKHLYF-------EKF-------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESIL 575
Cdd:cd12116 317 PGELYIGGDGVAQGYLgrpaltaERFvpdpfagPGsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALA 396
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32258701 576 SHGTVADCAVVGKEDPLKGHVpLALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFRnavfVKQLPKTRSGKIPRSAL 654
Cdd:cd12116 397 AHPGVAQAAVVVREDGGDRRL-VAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVR----LDALPLTANGKLDRKAL 470
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
125-654 |
1.94e-31 |
|
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: 129.11 E-value: 1.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 125 GDKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHslIFGGFA-- 202
Cdd:COG1021 39 PDRIAVVDG------ERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIP--VFALPAhr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 203 SKELSSRIDHVKPKVVVTAsfgiepgRRVE---YVPLVEEALKigQHkpdkiliynrPNMEAVPLA--PGRDLDWDEEMA 277
Cdd:COG1021 111 RAEISHFAEQSEAVAYIIP-------DRHRgfdYRALARELQA--EV----------PSLRHVLVVgdAGEFTSLDALLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 278 KAQSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLhWSMSSIYGLQPGEVWWAASDlgwvVGHSY--IC---Y 352
Cdd:COG1021 172 APADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSV-RASAEICGLDADTVYLAALP----AAHNFplSSpgvL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 353 GPLLHGNTTVLyegkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVETL 432
Cdd:COG1021 247 GVLYAGGTVVL-----APDPSPDTAFPLIERERVTVTALVPPLALLWLD----AAERSRYDLSSLRVLQVGGAKLSPELA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 433 EwsknvfRV-PVLDHWWQ------------TETGSP--ITASCVGLGNSktpppgqagksvPGYNVMILDDNmqklkarc 497
Cdd:COG1021 318 R------RVrPALGCTLQqvfgmaeglvnyTRLDDPeeVILTTQGRPIS------------PDDEVRIVDED-------- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 498 lGNivvklPLPPGA-----------FSGLWK----NQEAFKHlyfekfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAG 562
Cdd:COG1021 372 -GN-----PVPPGEvgelltrgpytIRGYYRapehNARAFTP------DGFYRTGDLVRRTPDGYLVVEGRAKDQINRGG 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 563 HRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRkdinaTEEQVLEEIVKHVRQnIGpVAAFR---NAVFVK 639
Cdd:COG1021 440 EKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-----GEPLTLAELRRFLRE-RG-LAAFKlpdRLEFVD 512
|
570
....*....|....*
gi 32258701 640 QLPKTRSGKIPRSAL 654
Cdd:COG1021 513 ALPLTAVGKIDKKAL 527
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
142-636 |
4.60e-31 |
|
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: 126.94 E-value: 4.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 142 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTa 221
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 222 sfgiepgrrveyvplveealkigqhkpdkiliynrpnmeavplapgrdlDWDEEMAKaqshdcvpvlsehplyILYTSGT 301
Cdd:cd05907 84 -------------------------------------------------EDPDDLAT----------------IIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 302 TGLPKGvirptggyaVMLHWS--MSSIYGLqpGEVWWAASD--------LGWVVGHSYICYGPLLHGNTTVLYEGKPVGT 371
Cdd:cd05907 99 TGRPKG---------VMLSHRniLSNALAL--AERLPATEGdrhlsflpLAHVFERRAGLYVPLLAGARIYFASSAETLL 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 372 PDagayfrvLAEHGVAALFTAPTAIR----AIRQQDPGAALGKQY---SLTRFKTLFVAGERCDVETLEWsknvFR---V 441
Cdd:cd05907 168 DD-------LSEVRPTVFLAVPRVWEkvyaAIKVKAVPGLKRKLFdlaVGGRLRFAASGGAPLPAELLHF----FRalgI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 442 PVLDHWWQTETGSPITASCVGlgnskTPPPGQAGKSVPGYNVMILDDnmqklkarclGNIVVKlplPPGAFSGLWKNQEA 521
Cdd:cd05907 237 PVYEGYGLTETSAVVTLNPPG-----DNRIGTVGKPLPGVEVRIADD----------GEILVR---GPNVMLGYYKNPEA 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 522 FKHLYFEkfPGYYDTMDAGYMDEEGYLYVMSRVDDVI-NVAGHRISAGAIEESILSHGTVADCAVVGKEDPlkghVPLAL 600
Cdd:cd05907 299 TAEALDA--DGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVAL 372
|
490 500 510
....*....|....*....|....*....|....*....
gi 32258701 601 CVLRKDIN---ATEEQVLEEIVKHVRQNIGPVAAFRNAV 636
Cdd:cd05907 373 IVPDPEALeawAEEHGIAYTDVAELAANPAVRAEIEAAV 411
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
124-654 |
1.09e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 126.56 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 124 KGDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFAS 203
Cdd:PRK07656 18 FGDKEAYVFGD------QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 204 KELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEAlkigQHKPDKILIYNRPNMEAVPLAPGRDLDWDEEMAKAQSHD 283
Cdd:PRK07656 92 DEAAYILARGDAKALFVLG---------LFLGVDYSA----TTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGDPAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 284 CVPVLS-EHPLYILYTSGTTGLPKGVirptggyaVMLHWSMSSIY-------GLQPGEVWWAASDLGWVVGHSYICYGPL 355
Cdd:PRK07656 159 RAPEVDpDDVADILFTSGTTGRPKGA--------MLTHRQLLSNAadwaeylGLTEGDRYLAANPFFHVFGYKAGVNAPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 356 LHGNTTVlyegkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqyslTRFKTLFVA---GERCDVETL 432
Cdd:PRK07656 231 MRGATIL-----PLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSA-------EDLSSLRLAvtgAASMPVALL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 433 EWSKNVFRVP-VLDHWWQTETgSPITASCvGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGA 511
Cdd:PRK07656 299 ERFESELGVDiVLTGYGLSEA-SGVTTFN-RLDDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR---GPNV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 512 FSGLWKNQEAFKHLYfeKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDP 591
Cdd:PRK07656 374 MKGYYDDPEATAAAI--DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDE 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32258701 592 LKGHVPLALCVLRKDINATEEQVLEeivkHVRQNIgpvAAF---RNAVFVKQLPKTRSGKIPRSAL 654
Cdd:PRK07656 452 RLGEVGKAYVVLKPGAELTEEELIA----YCREHL---AKYkvpRSIEFLDELPKNATGKVLKRAL 510
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
142-654 |
4.49e-30 |
|
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: 123.90 E-value: 4.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 142 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 221
Cdd:cd05945 16 TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 222 sfgiepgrrveyvplveealkigqhkPDkiliynrpnmeavPLApgrdldwdeemakaqshdcvpvlsehplYILYTSGT 301
Cdd:cd05945 96 --------------------------GD-------------DNA----------------------------YIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 302 TGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVlyegkPVG---TPDAGAYF 378
Cdd:cd05945 109 TGRPKGVQISHDNLVSFTNW-MLSDFPLGPGDVFLNQAPFSFDLSVMDL-YPALASGATLV-----PVPrdaTADPKQLF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 379 RVLAEHGVAALFTAPTAIRAIRQqDPGAALGKQYSLTRFktLFvAGERCDVETLEWSKNVF-RVPVLDHWWQTETgspiT 457
Cdd:cd05945 182 RFLAEHGITVWVSTPSFAAMCLL-SPTFTPESLPSLRHF--LF-CGEVLPHKTARALQQRFpDARIYNTYGPTEA----T 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 458 ASCVG-------LGNSKTPPPGQAgksVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEafKHLY-FEK 529
Cdd:cd05945 254 VAVTYievtpevLDGYDRLPIGYA---KPGAKLVILDEDGRPVPPGEKGELVIS---GPSVSKGYLNNPE--KTAAaFFP 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 530 FPGY--YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRkdi 607
Cdd:cd05945 326 DEGQraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPK--- 402
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 32258701 608 NATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05945 403 PGAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
125-649 |
5.20e-30 |
|
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: 124.33 E-value: 5.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 125 GDKIAIIYDSPVtntkatFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPqAMYTM-LACARIGAIHSLIFGGFAS 203
Cdd:cd12118 18 PDRTSIVYGDRR------YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTP-AMYELhFGVPMAGAVLNALNTRLDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 204 KELSSRIDHVKPKVV-VTASFgiepgrrvEYvplvEEALKIGqhKPDKILIynRPNMEavplapgrdldWDeemakaqsh 282
Cdd:cd12118 91 EEIAFILRHSEAKVLfVDREF--------EY----EDLLAEG--DPDFEWI--PPADE-----------WD--------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 283 dcvpvlsehPLYILYTSGTTGLPKGVIRPTGGYAVMlhwSMSSIY--GLQPGEVwwaasdlgwvvghsYICYGPLLHGN- 359
Cdd:cd12118 135 ---------PIALNYTSGTTGRPKGVVYHHRGAYLN---ALANILewEMKQHPV--------------YLWTLPMFHCNg 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 360 -----TTVLYEGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqySLTRFKTLFVAGERCDVETL 432
Cdd:cd12118 189 wcfpwTVAAVGGTNVCLRkvDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDAR----PLPHRVHVMTAGAPPPAAVL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 433 EWSKNV-FRVpvlDH-WWQTETGSPITAsCVGLGNSKT-PPPGQA------GKSVPGYN-VMILDDNMQKLKAR------ 496
Cdd:cd12118 265 AKMEELgFDV---THvYGLTETYGPATV-CAWKPEWDElPTEERArlkarqGVRYVGLEeVDVLDPETMKPVPRdgktig 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 497 ---CLGNIVVKlplppgafsGLWKN----QEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGA 569
Cdd:cd12118 341 eivFRGNIVMK---------GYLKNpeatAEAFRG-------GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVE 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 570 IEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIgpvAAF---RNAVFVkQLPKTRS 646
Cdd:cd12118 405 VEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTE----EEIIAFCREHL---AGFmvpKTVVFG-ELPKTST 476
|
...
gi 32258701 647 GKI 649
Cdd:cd12118 477 GKI 479
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
126-660 |
5.46e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 124.23 E-value: 5.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PRK06145 17 DRAALVYRD------QEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 LSSRIDHVKPKVV-VTASFGIEPGrrveyvpLVEEALKIGQHKPDKILIYNRPNMEAVPLAPGRDLDwdeemakaqshdc 284
Cdd:PRK06145 91 VAYILGDAGAKLLlVDEEFDAIVA-------LETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPTD------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 285 vpvlsehpLY-ILYTSGTTGLPKGVirptggyavMLHWsmssiyglqpGEVWWAASD----LGWVVGHSYICYGPLLH-- 357
Cdd:PRK06145 151 --------LVrLMYTSGTTDRPKGV---------MHSY----------GNLHWKSIDhviaLGLTASERLLVVGPLYHvg 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 358 ----GNTTVLYEGKPVGTP---DAGAYFRVLAEHGVAALFTAP---TAIRAIRQQDpgaalgkQYSLTRFKTLFVAGERC 427
Cdd:PRK06145 204 afdlPGIAVLWVGGTLRIHrefDPEAVLAAIERHRLTCAWMAPvmlSRVLTVPDRD-------RFDLDSLAWCIGGGEKT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 428 -DVETLEWSKNVFRVPVLDHWWQTETGSPITASCVGLGNSKTpppGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlp 506
Cdd:PRK06145 277 pESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEKI---GSTGRALAHVEIRIADGAGRWLPPNMKGEICMR-- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 507 lPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVV 586
Cdd:PRK06145 352 -GPKVTKGYWKDPEKTAEAFYG---DWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVI 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32258701 587 GKEDPLKGHVPLALCVLRKDINATeeqvLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNG 660
Cdd:PRK06145 428 GVHDDRWGERITAVVVLNPGATLT----LEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELNG 497
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
126-649 |
7.15e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 124.69 E-value: 7.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAII-YDSPVTntkatftYKEVLEQVSKLAGVLV-KHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFAS 203
Cdd:PRK08314 25 DKTAIVfYGRAIS-------YRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNRE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 204 KELSSRIDHVKPKVVVTAS---FGIEP---GRRVEYVPLVEEALKIGQHKPDKILIYNRPNMEAVPLAPGRDLDWDEEMA 277
Cdd:PRK08314 98 EELAHYVTDSGARVAIVGSelaPKVAPavgNLRLRHVIVAQYSDYLPAEPEIAVPAWLRAEPPLQALAPGGVVAWKEALA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 278 kaqSHDCVPVLSEHP--LYIL-YTSGTTGLPKGVIRPTGgyAVM------LHWSMSSiyglqPGEVWWAASDLGWVVGHS 348
Cdd:PRK08314 178 ---AGLAPPPHTAGPddLAVLpYTSGTTGVPKGCMHTHR--TVManavgsVLWSNST-----PESVVLAVLPLFHVTGMV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 349 YICYGPLLHGNTTVLYegkPVGTPDAGAyfRVLAEHGVAALFTAPT------AIRAIRQQD---------PGAALGK--- 410
Cdd:PRK08314 248 HSMNAPIYAGATVVLM---PRWDREAAA--RLIERYRVTHWTNIPTmvvdflASPGLAERDlsslryiggGGAAMPEava 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 411 QYSLTRFKTLFVAGercdvetlewsknvfrvpvldhWWQTETGSPITAScvglgnsktPP--PGQAGKSVPGYNV--MIL 486
Cdd:PRK08314 323 ERLKELTGLDYVEG----------------------YGLTETMAQTHSN---------PPdrPKLQCLGIPTFGVdaRVI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 487 D-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkFPG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGH 563
Cdd:PRK08314 372 DpETLEELPPGEVGEIVVH---GPQVFKGYWNRPEATAEAFIE-IDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGF 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 564 RISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQvlEEIVKHVRQNIGPVAAFRNAVFVKQLPK 643
Cdd:PRK08314 448 KVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTE--EEIIAWAREHMAAYKYPRIVEFVDSLPK 525
|
....*.
gi 32258701 644 TRSGKI 649
Cdd:PRK08314 526 SGSGKI 531
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
126-660 |
9.15e-30 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 124.75 E-value: 9.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPqAMYTM-LACARIGAIHSLIFGGFASK 204
Cdd:PLN03102 29 NRTSIIYG------KTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTP-AMYEMhFAVPMAGAVLNPINTRLDAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 205 ELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKI-----GQHKPDKILIYNrpnMEAVPLAPGRDLDWDEEMAKA 279
Cdd:PLN03102 102 SIAAILRHAKPKILFVDR---------SFEPLAREVLHLlssedSNLNLPVIFIHE---IDFPKRPSSEELDYECLIQRG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 280 QShdcVPVLS--------EH-PLYILYTSGTTGLPKGV-IRPTGGYAVMLhwsmSSIYGLQPG--EVW-WAASDL---GW 343
Cdd:PLN03102 170 EP---TPSLVarmfriqdEHdPISLNYTSGTTADPKGVvISHRGAYLSTL----SAIIGWEMGtcPVYlWTLPMFhcnGW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 344 VvghsyICYGPLLHGNTTVLYegKPVGTPDAgayFRVLAEHGVAALFTAPTAIRAIRQQD-------------------P 404
Cdd:PLN03102 243 T-----FTWGTAARGGTSVCM--RHVTAPEI---YKNIEMHNVTHMCCVPTVFNILLKGNsldlsprsgpvhvltggspP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 405 GAALGKQYSLTRFKTLFVAGER---CDVETLEWSKNVFRVPvlDHWW----QTETGSPITASCVGLGNSKTPppgqagKS 477
Cdd:PLN03102 313 PAALVKKVQRLGFQVMHAYGLTeatGPVLFCEWQDEWNRLP--ENQQmelkARQGVSILGLADVDVKNKETQ------ES 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 478 VPgynvmilddnmqkLKARCLGNIVVKlplPPGAFSGLWKN----QEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSR 553
Cdd:PLN03102 385 VP-------------RDGKTMGEIVIK---GSSIMKGYLKNpkatSEAFKH-------GWLNTGDVGVIHPDGHVEIKDR 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 554 VDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLE------EIVKHVRQNIG 627
Cdd:PLN03102 442 SKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKlvtrerDLIEYCRENLP 521
|
570 580 590
....*....|....*....|....*....|...
gi 32258701 628 PVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNG 660
Cdd:PLN03102 522 HFMCPRKVVFLQELPKNGNGKILKPKLRDIAKG 554
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
144-654 |
1.03e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 124.38 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 144 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMytmlacarIGAIHSLIFGG--------FASKELSSRIDHVKP 215
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAV--------IGYYGTLLAGGivvqtnplYTERELEYQLHDSGA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 216 KVVVTASFGIEPGRRVEYVPLVEEAL--KIGQHKP-DKILIY-----NRPNMeAVPLAPGRDLD-WDEEMAKAQSHDCVP 286
Cdd:PRK06710 123 KVILCLDLVFPRVTNVQSATKIEHVIvtRIADFLPfPKNLLYpfvqkKQSNL-VVKVSESETIHlWNSVEKEVNTGVEVP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 287 VLSEHPLYIL-YTSGTTGLPKGVIRP----TGGYAVMLHWsmssIYGLQPGEvwwaasDLGWVVGHSYICYGPLLHGNTT 361
Cdd:PRK06710 202 CDPENDLALLqYTGGTTGFPKGVMLThknlVSNTLMGVQW----LYNCKEGE------EVVLGVLPFFHVYGMTAVMNLS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 362 VLYEGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF 439
Cdd:PRK06710 272 IMQGYKMVLIPkfDMKMVFEAIKKHKVTLFPGAPTIYIALLN----SPLLKEYDISSIRACISGSAPLPVEVQEKFETVT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 440 RVPVLDHWWQTETgSPITASCVgLGNSKTPppGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKN 518
Cdd:PRK06710 348 GGKLVEGYGLTES-SPVTHSNF-LWEKRVP--GSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVK---GPQIMKGYWNK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 519 QEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPL 598
Cdd:PRK06710 421 PEETAAVLQD---GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVK 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 32258701 599 ALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:PRK06710 498 AFVVLKEGTECSE----EELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
125-587 |
1.08e-29 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 124.44 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 125 GDKIAIIYdsPVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 204
Cdd:COG1022 25 PDRVALRE--KEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 205 ELSSRIDHVKPKVVVtasfgiepgrrVEYVPLVEEALKIGQHKPD--KILIYNRPNMEAVP--------LAPGRDLDWDE 274
Cdd:COG1022 103 EVAYILNDSGAKVLF-----------VEDQEQLDKLLEVRDELPSlrHIVVLDPRGLRDDPrllsldelLALGREVADPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 275 EMAKAQSHdcvpVLSEHPLYILYTSGTTGLPKGvirptggyaVML-HWSMSS-------IYGLQPGEVW-----WAasdl 341
Cdd:COG1022 172 ELEARRAA----VKPDDLATIIYTSGTTGRPKG---------VMLtHRNLLSnaralleRLPLGPGDRTlsflpLA---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 342 gWVVGHSYICYgpLLHGNTTVLY------------EGKP---VGTPD------AGAYFRVLAEHGVA-ALFTA--PTAIR 397
Cdd:COG1022 235 -HVFERTVSYY--ALAAGATVAFaespdtlaedlrEVKPtfmLAVPRvwekvyAGIQAKAEEAGGLKrKLFRWalAVGRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 398 AIRQQD----PGAALGKQYSL--------------TRFKTLFVAGERCDVETLEWsknvFR---VPVLDHWWQTETGSPI 456
Cdd:COG1022 312 YARARLagksPSLLLRLKHALadklvfsklrealgGRLRFAVSGGAALGPELARF----FRalgIPVLEGYGLTETSPVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 457 TASCvgLGNSKtppPGQAGKSVPGYNVMILDDnmqklkarclGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDT 536
Cdd:COG1022 388 TVNR--PGDNR---IGTVGPPLPGVEVKIAED----------GEILVR---GPNVMKGYYKNPEATAEAFDAD--GWLHT 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 32258701 537 MDAGYMDEEGYLYVMSRVDDVINVA-GHRISAGAIEESILSHGTVADCAVVG 587
Cdd:COG1022 448 GDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
125-654 |
1.50e-29 |
|
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: 122.69 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 125 GDKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfask 204
Cdd:cd12117 11 PDAVAVVYG------DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAY---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 205 eLSSRIDHvkpkvvvtasfgiePGRRVEYvpLVEEAlkigqhkPDKILIYNRPNMEAVPLAPGRDLDWDEEMAKAQSHDC 284
Cdd:cd12117 75 -VPLDPEL--------------PAERLAF--MLADA-------GAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 285 VPVLSEHPLYILYTSGTTGLPKGVIRPtggyavmlHWSMSSIY------GLQPGEVWWAASDLGWVVGhSYICYGPLLHG 358
Cdd:cd12117 131 VPVSPDDLAYVMYTSGSTGRPKGVAVT--------HRGVVRLVkntnyvTLGPDDRVLQTSPLAFDAS-TFEIWGALLNG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 359 NTTVLYEGKPVGTPDAGAyfRVLAEHGVAALFTAPTAIRAIRQQDPGAalgkqysLTRFKTLFVAGERCDVetlewsKNV 438
Cdd:cd12117 202 ARLVLAPKGTLLDPDALG--ALIAEEGVTVLWLTAALFNQLADEDPEC-------FAGLRELLTGGEVVSP------PHV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 439 FRvpVLDHW-----WQ----TETGSPITASCVglgnskTPPPGQA-----GKSVPGYNVMILDDNMQklkarclgnivvk 504
Cdd:cd12117 267 RR--VLAACpglrlVNgygpTENTTFTTSHVV------TELDEVAgsipiGRPIANTRVYVLDEDGR------------- 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 505 lPLPPGAF-------SGLWK---NQEAfkhLYFEKF------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRIS 566
Cdd:cd12117 326 -PVPPGVPgelyvggDGLALgylNRPA---LTAERFvadpfgPGerLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIE 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 567 AGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINAteeqvlEEIVKHVRQNIGPV---AAFrnaVFVKQLPK 643
Cdd:cd12117 402 LGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDA------AELRAFLRERLPAYmvpAAF---VVLDELPL 472
|
570
....*....|.
gi 32258701 644 TRSGKIPRSAL 654
Cdd:cd12117 473 TANGKVDRRAL 483
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
126-654 |
1.80e-29 |
|
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: 122.03 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfaske 205
Cdd:cd17643 2 EAVAVVDED------RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGG------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 lssridhvkpkvvvtasfgiepgrrvEYVPLveealkigqhkpdkiliynrpnmeavplapgrDLDWDEEMAKAQSHDCV 285
Cdd:cd17643 63 --------------------------AYVPI--------------------------------DPAYPVERIAFILADSG 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 286 PVL----SEHPLYILYTSGTTGLPKGVIRPTGGyAVMLHWSMSSIYGLQPGEVWWAAsdlgwvvgHSYI-------CYGP 354
Cdd:cd17643 85 PSLlltdPDDLAYVIYTSGSTGRPKGVVVSHAN-VLALFAATQRWFGFNEDDVWTLF--------HSYAfdfsvweIWGA 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 355 LLHGNTTVLYEGKPVGTPDAgaYFRVLAEHGVAALFTAPTAIRAIRQ---QDPGAALGKQYsltrfktLFVAGERCDVET 431
Cdd:cd17643 156 LLHGGRLVVVPYEVARSPED--FARLLRDEGVTVLNQTPSAFYQLVEaadRDGRDPLALRY-------VIFGGEALEAAM 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 432 LE-WSKNVF--RVPVLDHWWQTETG-----SPITASCVGLGNSKTpppgqAGKSVPGYNVMILDDNMQklkarclgnivv 503
Cdd:cd17643 227 LRpWAGRFGldRPQLVNMYGITETTvhvtfRPLDAADLPAAAASP-----IGRPLPGLRVYVLDADGR------------ 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 504 klPLPPGAFSGLW----------KNQEAfkhLYFEKF-------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHR 564
Cdd:cd17643 290 --PVPPGVVGELYvsgagvargyLGRPE---LTAERFvanpfggPGsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFR 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 565 ISAGAIEESILSHGTVADCAVVGKEDPLKGHVpLALCVlrkDINATEEQVLEEIVKHVRQNIGPV---AAFrnaVFVKQL 641
Cdd:cd17643 365 IELGEIEAALATHPSVRDAAVIVREDEPGDTR-LVAYV---VADDGAAADIAELRALLKELLPDYmvpARY---VPLDAL 437
|
570
....*....|...
gi 32258701 642 PKTRSGKIPRSAL 654
Cdd:cd17643 438 PLTVNGKLDRAAL 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
141-654 |
2.05e-29 |
|
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: 122.45 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 141 ATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT 220
Cdd:cd17651 19 RRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 221 AsfgiepgrrveyvPLVEEALkigqhkpdkiliynrpnmeAVPLAPGRDLDWDEEMAKAQSHDCVPVLSEHPLYILYTSG 300
Cdd:cd17651 99 H-------------PALAGEL-------------------AVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 301 TTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVLyeGKPVGTPDAGAYFRV 380
Cdd:cd17651 147 STGRPKGVVMPHRSLANLVAW-QARASSLGPGARTLQFAGLGFDVSVQEI-FSTLCAGATLVL--PPEEVRTDPPALAAW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 381 LAEHGVAALFTAPTAIRAIRQQdpGAALGKQysLTRFKTLFVAGER--CDVETLEWSKNVFRVPVLDHWWQTETgSPITA 458
Cdd:cd17651 223 LDEQRISRVFLPTVALRALAEH--GRPLGVR--LAALRYLLTGGEQlvLTEDLREFCAGLPGLRLHNHYGPTET-HVVTA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 459 SCVGLGNSKTPPPGQAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPG-------AFSGLWKNQEAFKHLYFEKF- 530
Cdd:cd17651 298 LSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALR--------------PVPPGvpgelyiGGAGLARGYLNRPELTAERFv 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 531 -----PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVL 603
Cdd:cd17651 364 pdpfvPGarMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVG 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 32258701 604 RkdinATEEQVLEEIVKHVRQNIGP---VAAFrnaVFVKQLPKTRSGKIPRSAL 654
Cdd:cd17651 444 D----PEAPVDAAELRAALATHLPEymvPSAF---VLLDALPLTPNGKLDRRAL 490
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
174-654 |
2.83e-29 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 122.23 E-value: 2.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 174 MPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASFGIEPGRRveyVPLVEEALKIGQHKPDKILI 253
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRA---LPLYSKVVEAAPAKAIVLPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 254 YNRPNmeAVPLAPGrDLDWDEEMAKAQSHDCV------PVL--SEHPLYILYTSGTTGLPKGV-------IR-PTGGYAV 317
Cdd:PLN03051 78 AGEPV--AVPLREQ-DLSWCDFLGVAAAQGSVggneysPVYapVESVTNILFSSGTTGEPKAIpwthlspLRcASDGWAH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 318 MlhwsmssiyGLQPGEVWWAASDLGWVVGhSYICYGPLLHGNTTVLYEGKPVGtpdaGAYFRVLAEHGVAALFTAPTAIR 397
Cdd:PLN03051 155 M---------DIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLG----RGFGKFVQDAGVTVLGLVPSIVK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 398 AIRQQdpGAALGKQYSLTRFKTLFVAGERCDVETLEW--SKNVFRVPVLDHWWQTETGSPITASCVGLGNSktppPGQAG 475
Cdd:PLN03051 221 AWRHT--GAFAMEGLDWSKLRVFASTGEASAVDDVLWlsSVRGYYKPVIEYCGGTELASGYISSTLLQPQA----PGAFS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 476 KSVPGYNVMILDDNMQKL--KARCLGNIVVKLPLPPGAFSGLWKNQEAfkhLYFEKFPGYY----------DTMDAgymD 543
Cdd:PLN03051 295 TASLGTRFVLLNDNGVPYpdDQPCVGEVALAPPMLGASDRLLNADHDK---VYYKGMPMYGskgmplrrhgDIMKR---T 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 544 EEGYLYVMSRVDDVINVAGHRISAGAIEESIL-SHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKH- 621
Cdd:PLN03051 369 PGGYFCVQGRADDTMNLGGIKTSSVEIERACDrAVAGIAETAAVGVAPPDGGPELLVIFLVLGEEKKGFDQARPEALQKk 448
|
490 500 510
....*....|....*....|....*....|....*..
gi 32258701 622 ----VRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:PLN03051 449 fqeaIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVL 485
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
126-656 |
3.24e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 122.84 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDSPVTntkatfTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PRK06178 48 QRPAIIFYGHVI------TYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 LSSRIDHVKPKVVVTASFGIEPGRRVEYVPLVEEALKIGQHK--PDKILIYNRPNMEAVPLAPGrdlDWDEEMAkAQSHD 283
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLADvlPAEPTLPLPDSLRAPRLAAA---GAIDLLP-ALRAC 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 284 CVPVLSEHP----LYIL-YTSGTTGLPKGVIRPTG--------GYAVMLHWSMSSIY-GLQPgEVWWAASDLGWVVghsy 349
Cdd:PRK06178 198 TAPVPLPPPaldaLAALnYTGGTTGMPKGCEHTQRdmvytaaaAYAVAVVGGEDSVFlSFLP-EFWIAGENFGLLF---- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 350 icygPLLHGNTTVLyegkpVGTPDAGAYFRVLAEHGVAALF-TAPTAIRAIrqQDPGAAlgkQYSLTRFKTLFVAGErcd 428
Cdd:PRK06178 273 ----PLFSGATLVL-----LARWDAVAFMAAVERYRVTRTVmLVDNAVELM--DHPRFA---EYDLSSLRQVRVVSF--- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 429 VETLEwsknvfrvPVLDHWWQTETGSPITASCVGLGNSKT----------------PPPGQAGKSVPGYNVMILD-DNMQ 491
Cdd:PRK06178 336 VKKLN--------PDYRQRWRALTGSVLAEAAWGMTETHTcdtftagfqdddfdllSQPVFVGLPVPGTEFKICDfETGE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 492 KLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK06178 408 LLPLGAEGEIVVR---TPSLLKGYWNKPEATAEALRD---GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 572 ESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGP--VAAFRnavFVKQLPKTRSGKI 649
Cdd:PRK06178 482 ALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTA----AALQAWCRENMAVykVPEIR---IVDALPMTATGKV 554
|
....*..
gi 32258701 650 PRSALSA 656
Cdd:PRK06178 555 RKQDLQA 561
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
125-655 |
7.62e-29 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 120.94 E-value: 7.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 125 GDKIAIIYDSPVTNTKaTFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 204
Cdd:PRK08008 21 GHKTALIFESSGGVVR-RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 205 ELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKIGQHKPDKILIYNrpnmEAVPLAPGRdLDWDEEMAK--AQSH 282
Cdd:PRK08008 100 ESAWILQNSQASLLVTSA---------QFYPMYRQIQQEDATPLRHICLTR----VALPADDGV-SSFTQLKAQqpATLC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 283 DCVPVLSEHPLYILYTSGTTGLPKGVirptggyaVMLHWSM--SSIYGlqpgeVWWAA---SDLgwvvghsYICYGPLLH 357
Cdd:PRK08008 166 YAPPLSTDDTAEILFTSGTTSRPKGV--------VITHYNLrfAGYYS-----AWQCAlrdDDV-------YLTVMPAFH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 358 --------------GNTTVLYEGKpvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAALGKQYSLTRFktLFVA 423
Cdd:PRK08008 226 idcqctaamaafsaGATFVLLEKY-----SARAFWGQVCKYRATITECIPMMIRTLMVQ-PPSANDRQHCLREV--MFYL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 424 G----ERCDVETLewsknvFRVPVLDHWWQTETgspitasCVGLgnsKTPPPGQA------GKSVPGYNVMILDDNMQKL 493
Cdd:PRK08008 298 NlsdqEKDAFEER------FGVRLLTSYGMTET-------IVGI---IGDRPGDKrrwpsiGRPGFCYEAEIRDDHNRPL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 494 KARCLGNIVVKLPlpPGA--FSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK08008 362 PAGEIGEICIKGV--PGKtiFKEYYLDPKATAKVLEAD--GWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELE 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 572 ESILSHGTVADCAVVGKEDPLKGHVPLALCVLrkdiNATEEQVLEEIVKHVRQNIgpvAAFRNAVFV---KQLPKTRSGK 648
Cdd:PRK08008 438 NIIATHPKIQDIVVVGIKDSIRDEAIKAFVVL----NEGETLSEEEFFAFCEQNM---AKFKVPSYLeirKDLPRNCSGK 510
|
....*..
gi 32258701 649 IPRSALS 655
Cdd:PRK08008 511 IIKKNLK 517
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
291-651 |
1.27e-28 |
|
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: 116.74 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 291 HPLYILYTSGTTGLPKGVIRPtggyavmlHWSmssiyglqpgevwWAAS-----DLGWVVGHSYICY-GPLLH-----GN 359
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRS--------ERS-------------WIESfvcneDLFNISGEDAILApGPLSHslflyGA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 360 TTVLYEGKPV---GTPDAGAYFRVLAEHGVAALFTAPTAIRA-IRQQDPgaalgkqysLTRFKTLFVAGERCDVETLEWS 435
Cdd:cd17633 60 ISALYLGGTFigqRKFNPKSWIRKINQYNATVIYLVPTMLQAlARTLEP---------ESKIKSIFSSGQKLFESTKKKL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 436 KNVFRVPVLDHWWQTETGSPITASCvglgNSKTPPPGQAGKSVPGYNVMILDDNmqklkARCLGNIVVKLPLppgAFSGL 515
Cdd:cd17633 131 KNIFPKANLIEFYGTSELSFITYNF----NQESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEM---VFSGY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 516 WKNQEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGH 595
Cdd:cd17633 199 VRGGFSNPD-------GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 32258701 596 VPLALCVLRKdinATEEQVLEEIVKHVRQNIGPvaafRNAVFVKQLPKTRSGKIPR 651
Cdd:cd17633 272 IAVALYSGDK---LTYKQLKRFLKQKLSRYEIP----KKIIFVDSLPYTSSGKIAR 320
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
297-654 |
4.44e-28 |
|
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: 116.04 E-value: 4.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 297 YTSGTTGLPKgVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLgWVVGHSYICYGPLLHGNTTVLYEGkPVGTPDAGA 376
Cdd:cd05944 9 HTGGTTGTPK-LAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPL-FHVNGSVVTLLTPLASGAHVVLAG-PAGYRNPGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 377 Y---FRVLAEHGVAALFTAPTAIRAIRQQDPGAALGkqySLtrfKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTEtg 453
Cdd:cd05944 86 FdnfWKLVERYRITSLSTVPTVYAALLQVPVNADIS---SL---RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTE-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 454 spitASCVglgNSKTPP-----PGQAGKSVPGYNVMIL-DDNMQKLKARC----LGNIVVKlplPPGAFsGLWKNQEAFK 523
Cdd:cd05944 158 ----ATCL---VAVNPPdgpkrPGSVGLRLPYARVRIKvLDGVGRLLRDCapdeVGEICVA---GPGVF-GGYLYTEGNK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 524 HLYFEkfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVL 603
Cdd:cd05944 227 NAFVA--DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQL 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 32258701 604 RKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFV-KQLPKTRSGKIPRSAL 654
Cdd:cd05944 305 KPGAVVEEEELLA----WARDHVPERAAVPKHIEVlEELPVTAVGKVFKPAL 352
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
262-654 |
5.38e-28 |
|
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: 117.42 E-value: 5.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 262 VPLAPGRDLDWDEEMAkaQSHDCVPVL--SEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSiyglqpgevwWAAS 339
Cdd:cd12115 77 VPLDPAYPPERLRFIL--EDAQARLVLtdPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAA----------FSAE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 340 DLGWVVGHSYICY--------GPLLHGNTTVLYEgkpvgtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQD--PGAAlg 409
Cdd:cd12115 145 ELAGVLASTSICFdlsvfelfGPLATGGKVVLAD-------NVLALPDLPAAAEVTLINTVPSAAAELLRHDalPASV-- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 410 kqysltrfKTLFVAGE---RCDVETLEWSKNVFRVPVLdhWWQTETGSPITASCVGLGNSKTPPpgqAGKSVPGYNVMIL 486
Cdd:cd12115 216 --------RVVNLAGEplpRDLVQRLYARLQVERVVNL--YGPSEDTTYSTVAPVPPGASGEVS---IGRPLANTQAYVL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 487 DDNMQklkarclgnivvklPLPPGAFSGLWKNQEAFKHLYF-------EKF------PG--YYDTMDAGYMDEEGYLYVM 551
Cdd:cd12115 283 DRALQ--------------PVPLGVPGELYIGGAGVARGYLgrpgltaERFlpdpfgPGarLYRTGDLVRWRPDGLLEFL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 552 SRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRkdinATEEQVLEEIVKHVRQNIGPVAA 631
Cdd:cd12115 349 GRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAE----PGAAGLVEDLRRHLGTRLPAYMV 424
|
410 420
....*....|....*....|...
gi 32258701 632 FRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd12115 425 PSRFVRLDALPLTPNGKIDRSAL 447
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
295-658 |
9.14e-28 |
|
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: 114.35 E-value: 9.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 295 ILYTSGTTGLPKGVIRptgGYAVMLHWSMS--SIYGLQPGEVWWAASDLGWVVGhsyicYGPLLHGnttvLYEGKP--VG 370
Cdd:cd17630 5 VILTSGSTGTPKAVVH---TAANLLASAAGlhSRLGFGGGDSWLLSLPLYHVGG-----LAILVRS----LLAGAElvLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 371 TPDAGAYFRvLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqySLTRFKTLFVAGERCDVETLEWSKNVfRVPVLDHWWQT 450
Cdd:cd17630 73 ERNQALAED-LAPPGVTHVSLVPTQLQRLLDSGQGPA-----ALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 451 ETGSPITASCVGLgnsktPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWknqeafkhlyfekf 530
Cdd:cd17630 146 ETASQVATKRPDG-----FGRGGVGVLLPGRELRIVEDGEIWVGGASLAMGYLRGQLVPEFNEDGW-------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 531 pgyYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRkdinat 610
Cdd:cd17630 207 ---FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGR------ 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 32258701 611 EEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIV 658
Cdd:cd17630 278 GPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
145-649 |
1.27e-27 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 117.49 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 145 YKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASFG 224
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 225 IEPGRRV--EYVPLVEEAlkigqhKPDKILIYNRPNMEAVPLAPGrDLDWDEEMAKAQSHDCVPVlsEHPLYILYTSGTT 302
Cdd:PRK12406 94 LHGLASAlpAGVTVLSVP------TPPEIAAAYRISPALLTPPAG-AIDWEGWLAQQEPYDGPPV--PQPQSMIYTSGTT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 303 GLPKGVIR--PTGGYAVMLHWSMSSIYGLQPGEVwwaasdlgwvvghsYICYGPLLHG--NTTVLYEGKPVGT----P-- 372
Cdd:PRK12406 165 GHPKGVRRaaPTPEQAAAAEQMRALIYGLKPGIR--------------ALLTGPLYHSapNAYGLRAGRLGGVlvlqPrf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 373 DAGAYFRVLAEHGVAALFTAPTAIraIRQQDPGAALGKQYSLTRFKTLFVAGERCDVET----LEWSKNVfrvpVLDHWW 448
Cdd:PRK12406 231 DPEELLQLIERHRITHMHMVPTMF--IRLLKLPEEVRAKYDVSSLRHVIHAAAPCPADVkramIEWWGPV----IYEYYG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 449 QTETGSPITAScvglGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGaFSglWKNQEAfKHLYFE 528
Cdd:PRK12406 305 STESGAVTFAT----SEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPD-FT--YHNKPE-KRAEID 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 529 KfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHvplALC-VLRKDI 607
Cdd:PRK12406 377 R-GGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGE---ALMaVVEPQP 452
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 32258701 608 NATEEqvLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKI 649
Cdd:PRK12406 453 GATLD--EADIRAQLKARLAGYKVPKHIEIMAELPREDSGKI 492
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
152-654 |
1.36e-27 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 116.39 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 152 VSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIF----GGFASKELSSRIDHVKPKVVVTASfgiep 227
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFvplnPTLKESVLRYLVADAGGRIVLADA----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 228 grrveyvPLVEEALKIGQHKPDKILIYnrpnmeavplapgrdlDWDEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKG 307
Cdd:cd05922 78 -------GAADRLRDALPASPDPGTVL----------------DADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 308 VIRPTggYAVMLHW-SMSSIYGLQPGEVWWAASDLGWvvghsyiCYG------PLLHGNTTVLYEGkpvGTPDAGaYFRV 380
Cdd:cd05922 135 VRLSH--QNLLANArSIAEYLGITADDRALTVLPLSY-------DYGlsvlntHLLRGATLVLTND---GVLDDA-FWED 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 381 LAEHGVAALFTAPT--AI--RAIRQQDPGAAL-------GK--QYSLTRFKTLFVAGercdvetlewsknvfRVPVLdhW 447
Cdd:cd05922 202 LREHGATGLAGVPStyAMltRLGFDPAKLPSLryltqagGRlpQETIARLRELLPGA---------------QVYVM--Y 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 448 WQTETGSPITAscvglgnskTPP------PGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLppgAFSGLWkNQEA 521
Cdd:cd05922 265 GQTEATRRMTY---------LPPerilekPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPN---VMKGYW-NDPP 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 522 FKhLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVplALC 601
Cdd:cd05922 332 YR-RKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKL--ALF 408
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 32258701 602 VLRKDinateEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05922 409 VTAPD-----KIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
139-649 |
1.41e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 116.93 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 139 TKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVV 218
Cdd:PRK08276 8 SGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 219 VTaSFGiepgrrveyvpLVEEALKIGQHKPDKIliynrPNMEAVPLAPGRDLDWDEEMAkAQSHDcvPVLSEHPLY-ILY 297
Cdd:PRK08276 88 IV-SAA-----------LADTAAELAAELPAGV-----PLLLVVAGPVPGFRSYEEALA-AQPDT--PIADETAGAdMLY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 298 TSGTTGLPKGVIRPtggyavmlhwsmssIYGLQPGEV-----WWAASDLGWVVGHSYICYGPLLH-------------GN 359
Cdd:PRK08276 148 SSGTTGRPKGIKRP--------------LPGLDPDEApgmmlALLGFGMYGGPDSVYLSPAPLYHtaplrfgmsalalGG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 360 TTVLYEG-KPVGTPDAGAYFRVLAEHGVAALFTA----PTAIRAirqqdpgaalgkQYSLTRFKTLFVAGERCDVET--- 431
Cdd:PRK08276 214 TVVVMEKfDAEEALALIERYRVTHSQLVPTMFVRmlklPEEVRA------------RYDVSSLRVAIHAAAPCPVEVkra 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 432 -LEWSKnvfrvPVLDHWWQTETGSPITAScvglgNSKT--PPPGQAGKSVPGyNVMILDDNMQKLKARCLGNIVVKLPLP 508
Cdd:PRK08276 282 mIDWWG-----PIIHEYYASSEGGGVTVI-----TSEDwlAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGY 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 509 PgaFSGLwKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVInvaghrISAGA------IEESILSHGTVAD 582
Cdd:PRK08276 351 P--FEYH-NDPEKTAAARNPH--GWVTVGDVGYLDEDGYLYLTDRKSDMI------ISGGVniypqeIENLLVTHPKVAD 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32258701 583 CAVVGKEDPLKGHVPLALCVLRKDINATEEQVlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKI 649
Cdd:PRK08276 420 VAVFGVPDEEMGERVKAVVQPADGADAGDALA-AELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
125-654 |
1.59e-27 |
|
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: 116.66 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 125 GDKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 204
Cdd:cd05920 29 PDRIAVVDG------DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 205 ELSSRIDHVKPKVVVTAsfgiEPGRRVEYVPLVEEalkigqhkpdkiliynrpnmeavplapgrdldwdeemakaqshdc 284
Cdd:cd05920 103 ELSAFCAHAEAVAYIVP----DRHAGFDHRALARE--------------------------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 285 vpVLSEHP--LYILYTSGTTGLPKGVIRPTGGYAVMLHWSmSSIYGLQPGEVWWAASDlgwvVGHSYICYGP-----LLH 357
Cdd:cd05920 134 --LAESIPevALFLLSGGTTGTPKLIPRTHNDYAYNVRAS-AEVCGLDQDTVYLAVLP----AAHNFPLACPgvlgtLLA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 358 GNTTVLyegkpVGTPDAGAYFRVLAEHGVaalfTAPTAIRAIRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEwskn 437
Cdd:cd05920 207 GGRVVL-----APDPSPDAAFPLIEREGV----TVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALAR---- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 438 vfRV-PVLDHWWQTETGspiTAScvGLGNSKTP--PP----GQAGKSV-PGYNVMILDDNmqklkarclGNivvklPLPP 509
Cdd:cd05920 274 --RVpPVLGCTLQQVFG---MAE--GLLNYTRLddPDeviiHTQGRPMsPDDEIRVVDEE---------GN-----PVPP 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 510 GA-----------FSGLWK----NQEAFKHlyfekfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESI 574
Cdd:cd05920 333 GEegelltrgpytIRGYYRapehNARAFTP------DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLL 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 575 LSHGTVADCAVVGKEDPLKGHVPLALCVLRkdinatEEQVLEEIVKHVRQNIGpVAAFR---NAVFVKQLPKTRSGKIPR 651
Cdd:cd05920 407 LRHPAVHDAAVVAMPDELLGERSCAFVVLR------DPPPSAAQLRRFLRERG-LAAYKlpdRIEFVDSLPLTAVGKIDK 479
|
...
gi 32258701 652 SAL 654
Cdd:cd05920 480 KAL 482
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
295-654 |
2.65e-27 |
|
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: 115.46 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 295 ILYTSGTTGLPKGVirptggyaVMLHWSMSS-IYGLQpgEVW-WAASD-----LGWVVGHSYI--CYGPLLHGNTTVLye 365
Cdd:cd05941 94 ILYTSGTTGRPKGV--------VLTHANLAAnVRALV--DAWrWTEDDvllhvLPLHHVHGLVnaLLCPLFAGASVEF-- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 366 gkpVGTPDAGAYFRVLAEHGVAALFTAPTA----IRAIRQQDPGAALGKQYSLTRFKtLFVAGERC-DVETLEWSKNVFR 440
Cdd:cd05941 162 ---LPKFDPKEVAISRLMPSITVFMGVPTIytrlLQYYEAHFTDPQFARAAAAERLR-LMVSGSAAlPVPTLEEWEAITG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 441 VPVLDHWWQTETGspITASCvGLGNSKTPppGQAGKSVPGYNVMILDDNMQK-LKARCLGNIVVKlplPPGAFSGLWKNQ 519
Cdd:cd05941 238 HTLLERYGMTEIG--MALSN-PLDGERRP--GTVGMPLPGVQARIVDEETGEpLPRGEVGEIQVR---GPSVFKEYWNKP 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 520 EAFKhlyfEKFP--GYYDTMDAGYMDEEGYLYVMSRV-DDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHV 596
Cdd:cd05941 310 EATK----EEFTddGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGER 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 32258701 597 PLALCVLRKDINATEeqvLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05941 386 VVAVVVLRAGAAALS---LEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
126-654 |
2.84e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 116.26 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIydspVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PRK13390 12 DRPAVI----VAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 LSSRIDHVKPKVVVTASfgiepgrrveyvPLVEEALKIGQHKPDKILIYNRPNMEAvplapgrdlDWDEEMAKAQshdcv 285
Cdd:PRK13390 88 ADYIVGDSGARVLVASA------------ALDGLAAKVGADLPLRLSFGGEIDGFG---------SFEAALAGAG----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 286 PVLSEHPL--YILYTSGTTGLPKGvIRPT---------GGYAVMLhwsMSSIYGLQPGEVWWA------ASDLGWvvghs 348
Cdd:PRK13390 142 PRLTEQPCgaVMLYSSGTTGFPKG-IQPDlpgrdvdapGDPIVAI---ARAFYDISESDIYYSsapiyhAAPLRW----- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 349 yiCygPLLH--GNTTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIraIRQQDPGAALGKQYSLTRFKTLFVAGER 426
Cdd:PRK13390 213 --C--SMVHalGGTVVLAK-----RFDAQATLGHVERYRITVTQMVPTMF--VRLLKLDADVRTRYDVSSLRAVIHAAAP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 427 CDVET----LEWSKNVfrvpVLDHWWQTET-GSPITASCVGLGNsktppPGQAGKSVPGyNVMILDDNMQKLKARCLGNI 501
Cdd:PRK13390 282 CPVDVkhamIDWLGPI----VYEYYSSTEAhGMTFIDSPDWLAH-----PGSVGRSVLG-DLHICDDDGNELPAGRIGTV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 502 VVKLPLPPGAFSGLWKNQEAFKHlyfEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVA 581
Cdd:PRK13390 352 YFERDRLPFRYLNDPEKTAAAQH---PAHPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVH 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32258701 582 DCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:PRK13390 429 DVAVIGVPDPEMGEQVKAVIQLVEGIRGSDE-LARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
143-649 |
5.92e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 115.64 E-value: 5.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 143 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA- 221
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICAd 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 222 SFgiepgRRVEYVPLVEEALKIGQHKPDKILIYNR-PNMEAV----PLAPGRDLDWDEEMAKA------------QSHDC 284
Cdd:PRK12583 126 AF-----KTSDYHAMLQELLPGLAEGQPGALACERlPELRGVvslaPAPPPGFLAWHELQARGetvsrealaerqASLDR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 285 vpvlsEHPLYILYTSGTTGLPKGvirptggyAVMLHWSMssiyglqpgevwwaaSDLGWVVGHS---------------Y 349
Cdd:PRK12583 201 -----DDPINIQYTSGTTGFPKG--------ATLSHHNI---------------LNNGYFVAESlgltehdrlcvpvplY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 350 ICYGPLL-------HGNTTVLyegkPVGTPDAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDPGAalgkqYSLTRFKTLF 421
Cdd:PRK12583 253 HCFGMVLanlgcmtVGACLVY----PNEAFDPLATLQAVEEERCTALYGVPTMfIAELDHPQRGN-----FDLSSLRTGI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 422 VAGERCDVETLEWSKNVFRVP-VLDHWWQTETgSPIT------------ASCVG-------------LGNskTPPPGQAG 475
Cdd:PRK12583 324 MAGAPCPIEVMRRVMDEMHMAeVQIAYGMTET-SPVSlqttaaddlerrVETVGrtqphlevkvvdpDGA--TVPRGEIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 476 K-SVPGYNVMIlddnmqklkarclgnivvklplppgafsGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRV 554
Cdd:PRK12583 401 ElCTRGYSVMK----------------------------GYWNNPEATAESIDED--GWMHTGDLATMDEQGYVRIVGRS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 555 DDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRN 634
Cdd:PRK12583 451 KDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASE----EELREFCKARIAHFKVPRY 526
|
570
....*....|....*
gi 32258701 635 AVFVKQLPKTRSGKI 649
Cdd:PRK12583 527 FRFVDEFPMTVTGKV 541
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
126-657 |
6.25e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 114.96 E-value: 6.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIydspvtNTKATFTYKEVLEQVSKLAGVLVKH-GIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASK 204
Cdd:PRK06839 17 DRIAII------TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 205 ELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKIgqhkpdkilIYNRPNMEAVPLApgrdldwdeEMAKAQSHDC 284
Cdd:PRK06839 91 ELIFQLKDSGTTVLFVEK---------TFQNMALSMQKV---------SYVQRVISITSLK---------EIEDRKIDNF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 285 VPVLSEHPLYILYTSGTTGLPKGvirptggyAVMLHWSM--SSIYGLqpgevwwAASDLgwVVGHSYICYGPLLH-GNTT 361
Cdd:PRK06839 144 VEKNESASFIICYTSGTTGKPKG--------AVLTQENMfwNALNNT-------FAIDL--TMHDRSIVLLPLFHiGGIG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 362 V-----LYEGKPVGTP---DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVetle 433
Cdd:PRK06839 207 LfafptLFAGGVIIVPrkfEPTKALSMIEKHKVTVVMGVPTIHQALIN----CSKFETTNLQSVRWFYNGGAPCPE---- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 434 wsknvfrvPVLDHWwqTETGSPITAscvGLGNSKTPP-------------PGQAGKSVPGYNVMILDDNMQKLKARCLGN 500
Cdd:PRK06839 279 --------ELMREF--IDRGFLFGQ---GFGMTETSPtvfmlseedarrkVGSIGKPVLFCDYELIDENKNKVEVGEVGE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 501 IVVKlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTV 580
Cdd:PRK06839 346 LLIR---GPNVMKEYWNRPDATEETIQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDV 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32258701 581 ADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAI 657
Cdd:PRK06839 420 YEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIE----HCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
126-654 |
1.70e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 110.94 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDSpvtnTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIfggfaske 205
Cdd:PRK13391 12 DKPAVIMAS----TGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 lSSRIdhvkpkvvvtasfgiepgrrveyvpLVEEALKIGQHKPDKILIYNRPNMEAVPLAPGR--------DLDWDEEMA 277
Cdd:PRK13391 80 -NSHL-------------------------TPAEAAYIVDDSGARALITSAAKLDVARALLKQcpgvrhrlVLDGDGELE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 278 KAQSH-DCVPVLSEHPL-------YILYTSGTTGLPKGVIRP--------TGGYAVMLHwsmsSIYGLQPGEVwwaasdl 341
Cdd:PRK13391 134 GFVGYaEAVAGLPATPIadeslgtDMLYSSGTTGRPKGIKRPlpeqppdtPLPLTAFLQ----RLWGFRSDMV------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 342 gwvvghsYICYGPLLH-------------GNTTVLYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDpgaA 407
Cdd:PRK13391 203 -------YLSPAPLYHsapqravmlvirlGGTVIVME-----HFDAEQYLALIEEYGVTHTQLVPTMfSRMLKLPE---E 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 408 LGKQYSLTRFKTLFVAGERCDVETLEwsknvfrvPVLDhWWqtetgSPIT----ASCVGLGNSKTPP------PGQAGKS 477
Cdd:PRK13391 268 VRDKYDLSSLEVAIHAAAPCPPQVKE--------QMID-WW-----GPIIheyyAATEGLGFTACDSeewlahPGTVGRA 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 478 VPGyNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEAfKHlyfeKFPGYYDTMDAGYMDEEGYLYVMSRVDDV 557
Cdd:PRK13391 334 MFG-DLHILDDDGAELPPGEPGTIWFEGGRPFEYLNDPAKTAEA-RH----PDGTWSTVGDIGYVDEDGYLYLTDRAAFM 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 558 INVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEqVLEEIVKHVRQNIGPVAAFRNAVF 637
Cdd:PRK13391 408 IISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPA-LAAELIAFCRQRLSRQKCPRSIDF 486
|
570
....*....|....*..
gi 32258701 638 VKQLPKTRSGKIPRSAL 654
Cdd:PRK13391 487 EDELPRLPTGKLYKRLL 503
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
125-649 |
1.87e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 111.19 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 125 GDKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPqAMYTM-LACARIGAIHSLIFGGFAS 203
Cdd:PRK08162 32 PDRPAVIHG------DRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIP-AMVEAhFGVPMAGAVLNTLNTRLDA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 204 KELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKIGQHkpDKILIYNRPNMEAVPLAPGRDLDW-------DEEM 276
Cdd:PRK08162 105 ASIAFMLRHGEAKVLIVDT---------EFAEVAREALALLPG--PKPLVIDVDDPEYPGGRFIGALDYeaflasgDPDF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 277 AKAQSHDCVPVLSehplyILYTSGTTGLPKGVIRPTGGYAVM-----LHWSMS--SIYglqpgevwwaasdLgWVVghsy 349
Cdd:PRK08162 174 AWTLPADEWDAIA-----LNYTSGTTGNPKGVVYHHRGAYLNalsniLAWGMPkhPVY-------------L-WTL---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 350 icygPLLHGN------TTVLYEGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLF 421
Cdd:PRK08162 231 ----PMFHCNgwcfpwTVAARAGTNVCLRkvDPKLIFDLIREHGVTHYCGAPIVLSALIN----APAEWRAGIDHPVHAM 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 422 VAGERCDVETLEWSKNV-FRVpvlDHWWQ-TETGSPITASCVGLGNSKTPPPGQAG-KSVPGYN------VMILD-DNMQ 491
Cdd:PRK08162 303 VAGAAPPAAVIAKMEEIgFDL---THVYGlTETYGPATVCAWQPEWDALPLDERAQlKARQGVRyplqegVTVLDpDTMQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 492 KLKA----------RclGNIVVKlplppgafsGLWKNQEAFKhlyfEKFP-GYYDTMDAGYMDEEGYLYVMSRVDDVINV 560
Cdd:PRK08162 380 PVPAdgetigeimfR--GNIVMK---------GYLKNPKATE----EAFAgGWFHTGDLAVLHPDGYIKIKDRSKDIIIS 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 561 AGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIgpvAAFR--NAVFV 638
Cdd:PRK08162 445 GGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATE----EEIIAHCREHL---AGFKvpKAVVF 517
|
570
....*....|.
gi 32258701 639 KQLPKTRSGKI 649
Cdd:PRK08162 518 GELPKTSTGKI 528
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
142-656 |
4.77e-25 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 109.85 E-value: 4.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 142 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 221
Cdd:PRK13382 68 TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 222 SfgiepgrrvEYVPLVEEALKigqHKPDKILIynrpnmEAVPLAPGRDLDwdEEMAKAQSHDCVPVLSEHPLYILYTSGT 301
Cdd:PRK13382 148 E---------EFSATVDRALA---DCPQATRI------VAWTDEDHDLTV--EVLIAAHAGQRPEPTGRKGRVILLTSGT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 302 TGLPKGVIRP-TGGYAVMlhwsmSSIYGLQPgevwWAASDLGWVVGhsyicygPLLH--GNTTVLYEGKPVGTP------ 372
Cdd:PRK13382 208 TGTPKGARRSgPGGIGTL-----KAILDRTP----WRAEEPTVIVA-------PMFHawGFSQLVLAASLACTIvtrrrf 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 373 DAGAYFRVLAEHGVAALFTAPTAIRaiRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTET 452
Cdd:PRK13382 272 DPEATLDLIDRHRATGLAVVPVMFD--RIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 453 GSPITASCVGLGNSktppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVK-LPLPPGAFSGLWKNQEAfkhlyfekfp 531
Cdd:PRK13382 350 GMIATATPADLRAA----PDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRnDTQFDGYTSGSTKDFHD---------- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 532 GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATE 611
Cdd:PRK13382 416 GFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATP 495
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 32258701 612 eqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 656
Cdd:PRK13382 496 ----ETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
136-654 |
4.99e-25 |
|
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: 109.29 E-value: 4.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 136 VTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKP 215
Cdd:cd17646 17 VVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 216 KVVVTASFGIEPGRRVEYVPLVEEalkigqhkpdkiliynrpnmEAVPLAPGRDLDwdeemakaqshdcVPVLSEHPLYI 295
Cdd:cd17646 97 AVVLTTADLAARLPAGGDVALLGD--------------------EALAAPPATPPL-------------VPPRPDNLAYV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 296 LYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVLYEgkPVGTPDAG 375
Cdd:cd17646 144 IYTSGSTGRPKGVMVTHAGIVNRLLW-MQDEYPLGPGDRVLQKTPLSFDVSVWEL-FWPLVAGARLVVAR--PGGHRDPA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 376 AYFRVLAEHGVAALFTAPTAIRA-IRQQDPGAALgkqySLTRfktLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGS 454
Cdd:cd17646 220 YLAALIREHGVTTCHFVPSMLRVfLAEPAAGSCA----SLRR---VFCSGEALPPELAARFLALPGAELHNLYGPTEAAI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 455 PITA-SCVGlgnSKTPPPGQAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGL----------WKNQEAfk 523
Cdd:cd17646 293 DVTHwPVRG---PAETPSVPIGRPVPNTRLYVLDDALR--------------PVPVGVPGELylggvqlargYLGRPA-- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 524 hLYFEKF------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGH 595
Cdd:cd17646 354 -LTAERFvpdpfgPGsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAA 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32258701 596 VPLALCVLRKDINATEEQVLEEivkHVRQNIGPV---AAFrnaVFVKQLPKTRSGKIPRSAL 654
Cdd:cd17646 433 RLVGYVVPAAGAAGPDTAALRA---HLAERLPEYmvpAAF---VVLDALPLTANGKLDRAAL 488
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
227-654 |
5.01e-25 |
|
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: 109.00 E-value: 5.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 227 PGRRVEYVPLVEEALKIGQHKPDKILiynrPNMEAVPLAPGRDLDWDEEMAkAQSHDCVPVLSEhPLYILYTSGTTGLPK 306
Cdd:cd05929 68 CPAYKSSRAPRAEACAIIEIKAAALV----CGLFTGGGALDGLEDYEAAEG-GSPETPIEDEAA-GWKMLYSGGTTGRPK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 307 GVIRPTGGyavmlhwsmssiyGLQPGEVWWAASDL-GWVVGHSYICYGPLLHG------NTTVLYEGKPVGTP--DAGAY 377
Cdd:cd05929 142 GIKRGLPG-------------GPPDNDTLMAAALGfGPGADSVYLSPAPLYHAapfrwsMTALFMGGTLVLMEkfDPEEF 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 378 FRVLAEHGVAALFTAPTAIRAIRQQdPGAALGKqYSLTRFKTLFVAGERCDVET----LEWSKnvfrvPVLdhwWQTETG 453
Cdd:cd05929 209 LRLIERYRVTFAQFVPTMFVRLLKL-PEAVRNA-YDLSSLKRVIHAAAPCPPWVkeqwIDWGG-----PII---WEYYGG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 454 SPITASCVGLGNSKTPPPGQAGKSVPGyNVMILDDNMQklkarclgnivvklPLPPGAFSGLW-KNQEAFK-HLYFEKFP 531
Cdd:cd05929 279 TEGQGLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGN--------------EVPPGEIGEVYfANGPGFEyTNDPEKTA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 532 -----GYYDTM-DAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALcVLRK 605
Cdd:cd05929 344 aarneGGWSTLgDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAV-VQPA 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 32258701 606 DINATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05929 423 PGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
143-654 |
8.21e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 108.36 E-value: 8.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 143 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTas 222
Cdd:PRK09088 23 WTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 223 fgiepgrrveyvplveealkigqhkpDKILIYNRPNMEAVplapgrdldwDEEMAKAQSHDCVPVLS---EHPLYILYTS 299
Cdd:PRK09088 101 --------------------------DDAVAAGRTDVEDL----------AAFIASADALEPADTPSippERVSLILFTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 300 GTTGLPKGVirptggyavmlhwsMSSIYGLQPGEVWWaaSDLGWVVGHS-YICYGPLLH--GNTT----VLYEGKPVGTP 372
Cdd:PRK09088 145 GTSGQPKGV--------------MLSERNLQQTAHNF--GVLGRVDAHSsFLCDAPMFHiiGLITsvrpVLAVGGSILVS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 373 D---AGAYFRVLAEH--GVAALFTAPTAIRAIRQQdPGAALGkqySLTRFKTLFVAGERCDVETLEWSKNVfRVPVLDHW 447
Cdd:PRK09088 209 NgfePKRTLGRLGDPalGITHYFCVPQMAQAFRAQ-PGFDAA---ALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 448 WQTETGS--PITASCvGLGNSKTpppGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHL 525
Cdd:PRK09088 284 GMSEAGTvfGMSVDC-DVIRAKA---GAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLR---GPNLSPGYWRRPQATARA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 526 YFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLaLCVLRK 605
Cdd:PRK09088 357 FTGD--GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGY-LAIVPA 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 32258701 606 DINATEeqvLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:PRK09088 434 DGAPLD---LERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
570-648 |
8.79e-25 |
|
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: 98.00 E-value: 8.79e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32258701 570 IEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGK 648
Cdd:pfam13193 2 VESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLE----EELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
126-654 |
1.04e-24 |
|
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: 107.72 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIhslifggfaske 205
Cdd:cd17652 2 DAPAVVFGD------ETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAA------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 lssridhvkpkvvvtasfgiepgrrveYVPLveealkigqhkpdkiliynrpnmeavplapgrDLDWDEEMAKAQSHDCV 285
Cdd:cd17652 64 ---------------------------YLPL--------------------------------DPAYPAERIAYMLADAR 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 286 PVL----SEHPLYILYTSGTTGLPKGVirptggyaVMLHWSMSSI-------YGLQPGEVWWAASDLGWVVGHSYICyGP 354
Cdd:cd17652 85 PALllttPDNLAYVIYTSGSTGRPKGV--------VVTHRGLANLaaaqiaaFDVGPGSRVLQFASPSFDASVWELL-MA 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 355 LLHGNTTVLyegKPVGTPDAGAYF-RVLAEHGVAALFTAPTAIRAIrqqDPGAALGkqysltrFKTLFVAGERCDVETLE 433
Cdd:cd17652 156 LLAGATLVL---APAEELLPGEPLaDLLREHRITHVTLPPAALAAL---PPDDLPD-------LRTLVVAGEACPAELVD 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 434 -WSKNvfRVpVLDHWWQTETgsPITASCVGLGNSKTPPPgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPG-- 510
Cdd:cd17652 223 rWAPG--RR-MINAYGPTET--TVCATMAGPLPGGGVPP--IGRPVPGTRVYVLDARLR--------------PVPPGvp 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 511 -----AFSGLWK---NQEAfkhLYFEKF-------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEES 573
Cdd:cd17652 282 gelyiAGAGLARgylNRPG---LTAERFvadpfgaPGsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAA 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 574 ILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPvAAFrnaVFVKQLPKTRSGKIPRSA 653
Cdd:cd17652 359 LTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVP-AAF---VVLDALPLTPNGKLDRRA 434
|
.
gi 32258701 654 L 654
Cdd:cd17652 435 L 435
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
126-654 |
1.34e-24 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 108.30 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIiydspVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PRK06087 38 DKIAV-----VDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 LSSRIDHVKPKVVVTASFGiepgRRVEYVPL---VEEALKIGQHKP--DKiliyNRPNMEAVPLApgRDLDWDEEMAKAq 280
Cdd:PRK06087 113 LVWVLNKCQAKMFFAPTLF----KQTRPVDLilpLQNQLPQLQQIVgvDK----LAPATSSLSLS--QIIADYEPLTTA- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 281 shdcVPVLSEHPLYILYTSGTTGLPKGVIRpTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNT 360
Cdd:PRK06087 182 ----ITTHGDELAAVLFTSGTEGLPKGVML-THNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGAR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 361 TVLYEgkpvgtpdagayfrvlaehgvaaLFTAPTAIRAIRQQDPGAALGKqysltrfkTLFVAGERCDVETLEWSKNVFR 440
Cdd:PRK06087 257 SVLLD-----------------------IFTPDACLALLEQQRCTCMLGA--------TPFIYDLLNLLEKQPADLSALR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 441 --------VP--VLDHWWQTET------GSpiTASC----VGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGN 500
Cdd:PRK06087 306 fflcggttIPkkVARECQQRGIkllsvyGS--TESSphavVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 501 IVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTV 580
Cdd:PRK06087 384 EASR---GPNVFMGYLDEPELTARALDEE--GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKI 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32258701 581 ADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvLEEIV-----KHVRQNIGPvaafRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:PRK06087 459 HDACVVAMPDERLGERSCAYVVLKAPHHSLT---LEEVVaffsrKRVAKYKYP----EHIVVIDKLPRTASGKIQKFLL 530
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
138-656 |
1.53e-24 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 108.14 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 138 NTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKV 217
Cdd:PLN02246 46 ATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 218 VVTASFGIEPGRRVEYVPLVEeALKIGQHkPDKILIYNrpnmeavplapgrdldwdeEMAKAQSHDC--VPVLSEHPLYI 295
Cdd:PLN02246 126 IITQSCYVDKLKGLAEDDGVT-VVTIDDP-PEGCLHFS-------------------ELTQADENELpeVEISPDDVVAL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 296 LYTSGTTGLPKGVirptggyavML-HWSM-SSIYGLQPGEVwwaaSDLGWVVGHSYICYGPLLH--GNTTVLYEGKPVGT 371
Cdd:PLN02246 185 PYSSGTTGLPKGV---------MLtHKGLvTSVAQQVDGEN----PNLYFHSDDVILCVLPMFHiySLNSVLLCGLRVGA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 372 P-------DAGAYFRVLAEHGV-AALFTAP----------------TAIR---------------AIRQQDPGAALGKQY 412
Cdd:PLN02246 252 AilimpkfEIGALLELIQRHKVtIAPFVPPivlaiakspvvekydlSSIRmvlsgaaplgkeledAFRAKLPNAVLGQGY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 413 SLTRfktlfvAGercdvetlewsknvfrvPVLdhwwqtetgspitASCvgLGNSKTP---PPGQAGKSVPGYNVMILDDN 489
Cdd:PLN02246 332 GMTE------AG-----------------PVL-------------AMC--LAFAKEPfpvKSGSCGTVVRNAELKIVDPE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 490 MQKLKARCL-GNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAG 568
Cdd:PLN02246 374 TGASLPRNQpGEICIR---GPQIMKGYLNDPEATANTIDKD--GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPA 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 569 AIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKHV--RQNIGPVaafrnaVFVKQLPKTRS 646
Cdd:PLN02246 449 ELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVvfYKRIHKV------FFVDSIPKAPS 522
|
570
....*....|
gi 32258701 647 GKIPRSALSA 656
Cdd:PLN02246 523 GKILRKDLRA 532
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
126-654 |
2.44e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 109.48 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfASKE 205
Cdd:PRK12467 527 ERPALVFG------EQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGG---------AYVP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 LSSRidhvkpkvvvtasfgiEPGRRVEYVpLVEEALKIGQHKPDKILIYNRP-NMEAVPLapgrDLDWDEEMAKAQSHDC 284
Cdd:PRK12467 592 LDPE----------------YPQDRLAYM-LDDSGVRLLLTQSHLLAQLPVPaGLRSLCL----DEPADLLCGYSGHNPE 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 285 VPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVLY 364
Cdd:PRK12467 651 VALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCV-IAERLQLAADDSMLMVSTFAFDLGVTEL-FGALASGATLHLL 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 365 EgkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPGAALgkqysLTRFKTLFVAGERCDVETL-EWSKNVFRVPV 443
Cdd:PRK12467 729 P--PDCARDAEAFAALMADQGVTVLKIVPSHLQAL-LQASRVAL-----PRPQRALVCGGEALQVDLLaRVRALGPGARL 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 444 LDHWWQTETGSPITA-SCVGLGNSKTPPPgqAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLWKNQEAF 522
Cdd:PRK12467 801 INHYGPTETTVGVSTyELSDEERDFGNVP--IGQPLANLGLYILDHYLN--------------PVPVGVVGELYIGGAGL 864
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 523 KHLYF-------EKF-------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADcAVV 586
Cdd:PRK12467 865 ARGYHrrpaltaERFvpdpfgaDGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVRE-AVV 943
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32258701 587 GKEDPLKGHVPLALCVLRKDINATEEQVL-EEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:PRK12467 944 LAQPGDAGLQLVAYLVPAAVADGAEHQATrDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
139-654 |
6.84e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 103.14 E-value: 6.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 139 TKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVV 218
Cdd:PLN02330 52 TGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 219 VT--ASFGIEPGRRVEYVPLVEEAlkigqhkpdkilIYNRPNMEAVPLAPGRDLDWDEEMAKAQSHDCVpvlsehplyIL 296
Cdd:PLN02330 132 VTndTNYGKVKGLGLPVIVLGEEK------------IEGAVNWKELLEAADRAGDTSDNEEILQTDLCA---------LP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 297 YTSGTTGLPKGVIRPTGGYAVMLhwsMSSIYGLQPgEVWWAASDLGWV-VGHSY----ICYGPLLHGNTTVLyegkpVGT 371
Cdd:PLN02330 191 FSSGTTGISKGVMLTHRNLVANL---CSSLFSVGP-EMIGQVVTLGLIpFFHIYgitgICCATLRNKGKVVV-----MSR 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 372 PDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPgaaLGKQYSLTRFK--TLFVAGERCDVETLEWSKNVF-RVPVLDHWW 448
Cdd:PLN02330 262 FELRTFLNALITQEVSFAPIVPPIILNL-VKNP---IVEEFDLSKLKlqAIMTAAAPLAPELLTAFEAKFpGVQVQEAYG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 449 QTEtgspitASCVGLGNSKtPPPGQA-------GKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQE 520
Cdd:PLN02330 338 LTE------HSCITLTHGD-PEKGHGiakknsvGFILPNLEVKFIDpDTGRSLPKNTPGELCVR---SQCVMQGYYNNKE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 521 AFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLAL 600
Cdd:PLN02330 408 ETDRTIDED--GWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAAC 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 32258701 601 CVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:PLN02330 486 VVINPKAKESEEDILN----FVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
132-668 |
1.07e-22 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 103.19 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 132 YDSPVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGaihslIFGGFASKELSsRID 211
Cdd:PRK06060 20 YDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARG-----VMAFLANPELH-RDD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 212 HVKPKVVVTASFGIEPGrrveyvPLVEealkigQHKPDKILiynrpnmEAVPLApgrdldwdEEMAKAQSHDCVPVLSEH 291
Cdd:PRK06060 94 HALAARNTEPALVVTSD------ALRD------RFQPSRVA-------EAAELM--------SEAARVAPGGYEPMGGDA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 292 PLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPgevwwaaSDLGWVVGHSYICYG-------PLLHGNTTVLy 364
Cdd:PRK06060 147 LAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTP-------EDTGLCSARMYFAYGlgnsvwfPLATGGSAVI- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 365 EGKPVGTPDAG---AYFRVLAEHGVAALFT------APTAIRAIRqqdpgaalgkqysltrfkTLFVAGERCDVETLEWS 435
Cdd:PRK06060 219 NSAPVTPEAAAilsARFGPSVLYGVPNFFArvidscSPDSFRSLR------------------CVVSAGEALELGLAERL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 436 KNVFR-VPVLDHWWQTETGSPITASCVGLGNsktppPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSG 514
Cdd:PRK06060 281 MEFFGgIPILDGIGSTEVGQTFVSNRVDEWR-----LGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVR---GPAIAKG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 515 LWKNQEAFkhLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKG 594
Cdd:PRK06060 353 YWNRPDSP--VANE---GWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGA 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 595 HVPLALCVlrkdiNATEEQVLEEIVKHV-RQNIGPVAAF----RNAVfVKQLPKTRSGKIPRSALSAIVNGKP-YKITST 668
Cdd:PRK06060 428 STLQAFLV-----ATSGATIDGSVMRDLhRGLLNRLSAFkvphRFAV-VDRLPRTPNGKLVRGALRKQSPTKPiWELSLT 501
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
144-680 |
7.57e-22 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 100.24 E-value: 7.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 144 TYKEVLEQVSKLAGVLVKH-GIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT-A 221
Cdd:PRK05620 40 TFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAdP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 222 SFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRPNMEAV---PLAPGR--DLDWdeemakaqshdcvPVLSEH-PLYI 295
Cdd:PRK05620 120 RLAEQLGEILKECPCVRAVVFIGPSDADSAAAHMPEGIKVYsyeALLDGRstVYDW-------------PELDETtAAAI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 296 LYTSGTTGLPKGVIrptggyavmlhWSMSSIYgLQPGEVWWAASdLGWVVGHSYICYGPLLHgnttVLYEGKPVGTPDAG 375
Cdd:PRK05620 187 CYSTGTTGAPKGVV-----------YSHRSLY-LQSLSLRTTDS-LAVTHGESFLCCVPIYH----VLSWGVPLAAFMSG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 376 AYFrVLAEHGVaalfTAPTAIRAIRQQDPGAALG-----------------KQYSLTrfkTLFVAGERCDVETLEWSKNV 438
Cdd:PRK05620 250 TPL-VFPGPDL----SAPTLAKIIATAMPRVAHGvptlwiqlmvhylknppERMSLQ---EIYVGGSAVPPILIKAWEER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 439 FRVPVLDHWWQTETgSPItascvglGNSKTPPPGQAGKSVPGYNV------------MILDDNMQKLKARCLGNIVVKLP 506
Cdd:PRK05620 322 YGVDVVHVWGMTET-SPV-------GTVARPPSGVSGEARWAYRVsqgrfpasleyrIVNDGQVMESTDRNEGEIQVRGN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 507 LPPGAFSGLWKNQEAFKHLYF---------EKFP--GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESIL 575
Cdd:PRK05620 394 WVTASYYHSPTEEGGGAASTFrgedvedanDRFTadGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 576 SHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALS 655
Cdd:PRK05620 474 AAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETA-ERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
570 580
....*....|....*....|....*
gi 32258701 656 AIVNGKPYKITsTIEDPSIFGHVEE 680
Cdd:PRK05620 553 QHLADGDFEII-KLKGPGESGESDS 576
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
88-651 |
1.23e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 99.30 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 88 KPWTKTLENKHSPSTRFVEG-MLNICYNAVDRHiengkGDKIAIIYdspvtnTKATFTYKEVLEQVSKLAGVLVKHGIKK 166
Cdd:PRK05605 13 KPWLQSYAPWTPHDLDYGDTtLVDLYDNAVARF-----GDRPALDF------FGATTTYAELGKQVRRAAAGLRALGVRP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 167 GDTVVIYMPMIPQAMYTMLACARIGAI---HSLIfggFASKELSSR-IDHvKPKVVV----TASF--GIEPGRRVEYV-- 234
Cdd:PRK05605 82 GDRVAIVLPNCPQHIVAFYAVLRLGAVvveHNPL---YTAHELEHPfEDH-GARVAIvwdkVAPTveRLRRTTPLETIvs 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 235 -------PLVEE-ALKIgqhkPDKILIYNRPNMEAVplAPGRdLDWDEEMAKA-----QSHDCVPVLSEHPLYILYTSGT 301
Cdd:PRK05605 158 vnmiaamPLLQRlALRL----PIPALRKARAALTGP--APGT-VPWETLVDAAiggdgSDVSHPRPTPDDVALILYTSGT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 302 TGLPKGVIRPTGGY---AVM-LHWsmssIYGLQPG-EVWWAASDLgwvvghsYICYGPLLHGNTTVLYEGKPV--GTPDA 374
Cdd:PRK05605 231 TGKPKGAQLTHRNLfanAAQgKAW----VPGLGDGpERVLAALPM-------FHAYGLTLCLTLAVSIGGELVllPAPDI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 375 GAYFRVLAEHGVAALFTAPTAIRAIRQqdpgAALGKQYSLTRFKTLFVAGERCDVETLEwsknvfrvpvldhWWQTETG- 453
Cdd:PRK05605 300 DLILDAMKKHPPTWLPGVPPLYEKIAE----AAEERGVDLSGVRNAFSGAMALPVSTVE-------------LWEKLTGg 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 454 -----------SPITascvgLGN--SKTPPPGQAGKSVPGYNVMILD-DNMQKLKARC-LGNIVVKlplPPGAFSGLWKN 518
Cdd:PRK05605 363 llvegygltetSPII-----VGNpmSDDRRPGYVGVPFPDTEVRIVDpEDPDETMPDGeEGELLVR---GPQVFKGYWNR 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 519 QEAFKHLYfekFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVG--KEDplkGHV 596
Cdd:PRK05605 435 PEETAKSF---LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGlpRED---GSE 508
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 32258701 597 PLALCVLRKDINATEEQVLEEivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 651
Cdd:PRK05605 509 EVVAAVVLEPGAALDPEGLRA---YCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
290-651 |
1.55e-21 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 96.56 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 290 EHPLYILYTSGTTGLPKGV-IRPTGGYAVMLH-------WSMSSI-YGLQP----GEVWWAASDL----GWVVGHSYICY 352
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVlLANKTFFAVPDIlqkeglnWVVGDVtYLPLPathiGGLWWILTCLihggLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 353 GPLlhgnttvlyegkpvgtpdagayFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkQYSlTRFKTLFVAGERC---DV 429
Cdd:cd17635 81 KSL----------------------FKILTTNAVTTTCLVPTLLSKLVSELKSAN---ATV-PSLRLIGYGGSRAiaaDV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 430 ETLEWSKNVfrvPVLDHWWQTETGspiTASCVGLGNSkTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPP 509
Cdd:cd17635 135 RFIEATGLT---NTAQVYGLSETG---TALCLPTDDD-SIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIK---SP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 510 GAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKE 589
Cdd:cd17635 205 ANMLGYWNNPERTAEVLID---GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEIS 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32258701 590 DPLKGHVpLALCVLRKDINatEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 651
Cdd:cd17635 282 DEEFGEL-VGLAVVASAEL--DENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
287-654 |
2.91e-21 |
|
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: 97.05 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 287 VLSEHP---LYILYTSGTTGLPKGVIRPTGGYAvMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVL 363
Cdd:cd17649 88 LLTHHPrqlAYVIYTSGSTGTPKGVAVSHGPLA-AHCQATAERYGLTPGDRELQFASFNFDGAHEQL-LPPLICGACVVL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 364 YEGKPVGTPDagAYFRVLAEHGVAALFTAPT-------AIRAIRQQDPGAalgkqysltrFKTLFVAGERCDVETLeWSK 436
Cdd:cd17649 166 RPDELWASAD--ELAEMVRELGVTVLDLPPAylqqlaeEADRTGDGRPPS----------LRLYIFGGEALSPELL-RRW 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 437 NVFRVPVLDHWWQTETGSPITASCVGLGNSKTPPPGQAGKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGLW 516
Cdd:cd17649 233 LKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYILDADLN--------------PVPVGVTGELY 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 517 KNQEAFKHLYF-------EKF-------PG--YYDTMD-AGYMDeEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGT 579
Cdd:cd17649 299 IGGEGLARGYLgrpeltaERFvpdpfgaPGsrLYRTGDlARWRD-DGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPG 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32258701 580 VADCAVVGKEDPLkGHVPLALCVLRKDinATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd17649 378 VREAAVVALDGAG-GKQLVAYVVLRAA--AAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
126-656 |
6.32e-21 |
|
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: 96.63 E-value: 6.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:cd17655 12 DHTAVVFED------QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 LSSRIDHVKPKVVVTASFGIEPGRRVEYVPLVEEalkigqhkpDKILIYNRPNMEavplapgrdldwdeemakaqshdcV 285
Cdd:cd17655 86 IQYILEDSGADILLTQSHLQPPIAFIGLIDLLDE---------DTIYHEESENLE------------------------P 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 286 PVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQpgevwwaASDLGWVVGHSY------IcYGPLLHGN 359
Cdd:cd17655 133 VSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGE-------HLRVALFASISFdasvteI-FASLLSGN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 360 TTVLYEGKPVGtpDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqysltRFKTLFVAGERCDVETLEWSKNVF 439
Cdd:cd17655 205 TLYIVRKETVL--DGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGL-------SLKHLIVGGEALSTELAKKIIELF 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 440 R--VPVLDHWWQTETgsPITAS---CVGLGNSKTPPPgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSG 514
Cdd:cd17655 276 GtnPTITNAYGPTET--TVDASiyqYEPETDQQVSVP--IGKPLGNTRIYILDQYGRPQPVGVAGELYIG---GEGVARG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 515 LWKNQEafkhLYFEKF------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVV 586
Cdd:cd17655 349 YLNRPE----LTAEKFvddpfvPGerMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVI 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32258701 587 GKEDPLKGHVPLALCVLRKDInaTEEQVLEEIVKHVRQNIGPvaafrnAVFVK--QLPKTRSGKIPRSALSA 656
Cdd:cd17655 425 ARKDEQGQNYLCAYIVSEKEL--PVAQLREFLARELPDYMIP------SYFIKldEIPLTPNGKVDRKALPE 488
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-654 |
8.19e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.49 E-value: 8.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfaske 205
Cdd:PRK12316 4566 DAVAVVFD------EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAY----------- 4628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 lssridhvkpkvvvtASFGIE-PGRRVEYvpLVEEAlkiGQHkpdkILIYNRPNMEAVPLAPGRD---LDWDEEMAKAQS 281
Cdd:PRK12316 4629 ---------------VPLDPEyPRERLAY--MMEDS---GAA----LLLTQSHLLQRLPIPDGLAslaLDRDEDWEGFPA 4684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 282 HDcvPVLSEHP---LYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHG 358
Cdd:PRK12316 4685 HD--PAVRLHPdnlAYVIYTSGSTGRPKGVAVSHGSLVNHLHA-TGERYELTPDDRVLQFMSFSFDGSHEGL-YHPLING 4760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 359 NTTVLyegKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAAlgkqySLTRFKTLFVAGERCDVETL-EWSKN 437
Cdd:PRK12316 4761 ASVVI---RDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDG-----EPPSLRVYCFGGEAVAQASYdLAWRA 4832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 438 VFRVPVLDHWWQTETG-SPITASCvglgnSKTPPPGQA----GKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAF 512
Cdd:PRK12316 4833 LKPVYLFNGYGPTETTvTVLLWKA-----RDGDACGAAympiGTPLGNRSGYVLDGQLN--------------PLPVGVA 4893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 513 SGLWKNQEAFKHLYF-------EKF-------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILS 576
Cdd:PRK12316 4894 GELYLGGEGVARGYLerpaltaERFvpdpfgaPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLRE 4973
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 577 HGTVADCAVVGKEDPLKGH-----VPLALCVLrkDINATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 651
Cdd:PRK12316 4974 HPAVREAVVIAQEGAVGKQlvgyvVPQDPALA--DADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDR 5051
|
...
gi 32258701 652 SAL 654
Cdd:PRK12316 5052 KAL 5054
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
144-648 |
1.46e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 95.72 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 144 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIH----------------------SLIFG-G 200
Cdd:PRK07798 30 TYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPvnvnyryvedelryllddsdavALVYErE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 201 FASK--ELSSRIDHVKPKVVVTASFGIEPGRR-VEYvplvEEALKIGqhkpdkiliynrpnmeavplAPGRDldwdeema 277
Cdd:PRK07798 110 FAPRvaEVLPRLPKLRTLVVVEDGSGNDLLPGaVDY----EDALAAG--------------------SPERD-------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 278 kaqshdcVPVLSEHPLYILYTSGTTGLPKGV--------------IRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDL-- 341
Cdd:PRK07798 158 -------FGERSPDDLYLLYTGGTTGMPKGVmwrqedifrvllggRDFATGEPIEDEEELAKRAAAGPGMRRFPAPPLmh 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 342 G---WVVghsyicYGPLLHGNTTVLYegkPVGTPDAGAYFRVLAEHGVAALFTAPTA-----IRAIRQqdpgaalGKQYS 413
Cdd:PRK07798 231 GagqWAA------FAALFSGQTVVLL---PDVRFDADEVWRTIEREKVNVITIVGDAmarplLDALEA-------RGPYD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 414 LTRFKTLFVAG----ERCDVETLEWSKNVFrvpVLDHWWQTETGSpitascVGLGNSKTPPPGQAGKSV-PGYNVMILDD 488
Cdd:PRK07798 295 LSSLFAIASGGalfsPSVKEALLELLPNVV---LTDSIGSSETGF------GGSGTVAKGAVHTGGPRFtIGPRTVVLDE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 489 NMQKLK---------ARClGNIvvklPLppgafsGLWKNQEAFKHLYFEK------FPGYYDTMDAgymdeEGYLYVMSR 553
Cdd:PRK07798 366 DGNPVEpgsgeigwiARR-GHI----PL------GYYKDPEKTAETFPTIdgvryaIPGDRARVEA-----DGTITLLGR 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 554 VDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFR 633
Cdd:PRK07798 430 GSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDL----AELRAHCRSSLAGYKVPR 505
|
570
....*....|....*
gi 32258701 634 NAVFVKQLPKTRSGK 648
Cdd:PRK07798 506 AIWFVDEVQRSPAGK 520
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
142-656 |
1.74e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 97.34 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 142 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfaskelssridhvkpkVVVTA 221
Cdd:PRK12316 536 TLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAY----------------------VPLDP 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 222 SFgiePGRRVEYvpLVEEAlKIGqhkpdkILIYNRPNMEAVPLAPGRD-LDWDEEMAKAQSH-DCVPVLS---EHPLYIL 296
Cdd:PRK12316 594 EY---PAERLAY--MLEDS-GVQ------LLLSQSHLGRKLPLAAGVQvLDLDRPAAWLEGYsEENPGTElnpENLAYVI 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 297 YTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGHsYICYGPLLHGNTTVLyeGKPVGTPDAGA 376
Cdd:PRK12316 662 YTSGSTGKPKGAGNRHRALSNRLCW-MQQAYGLGVGDTVLQKTPFSFDVSV-WEFFWPLMSGARLVV--AAPGDHRDPAK 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 377 YFRVLAEHGVAALFTAPTAIRAIrQQDPGAAlgkqySLTRFKTLFVAGERCDVETLEwskNVF-RVP---VLDHWWQTET 452
Cdd:PRK12316 738 LVELINREGVDTLHFVPSMLQAF-LQDEDVA-----SCTSLRRIVCSGEALPADAQE---QVFaKLPqagLYNLYGPTEA 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 453 GSPIT-ASCVGLGNSKTPppgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVklplppgAFSGLWKNQEAFKHLYFEKF- 530
Cdd:PRK12316 809 AIDVThWTCVEEGGDSVP----IGRPIANLACYILDANLEPVPVGVLGELYL-------AGRGLARGYHGRPGLTAERFv 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 531 PG-------YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEdplkGHVPLALCVL 603
Cdd:PRK12316 878 PSpfvagerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVL 953
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 32258701 604 RKDINATEEQVLEEIVKHVRQNIGPVaafrNAVFVKQLPKTRSGKIPRSALSA 656
Cdd:PRK12316 954 ESEGGDWREALKAHLAASLPEYMVPA----QWLALERLPLTPNGKLDRKALPA 1002
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
143-649 |
3.06e-20 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 94.88 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 143 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA- 221
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAAd 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 222 SFgiepgRRVEYVPLVEE-ALKIGQHKPDKILIYNRPNMEAV-----PLAPGRdLDWDEEMAKAQSHDCVPV------LS 289
Cdd:PRK08315 124 GF-----KDSDYVAMLYElAPELATCEPGQLQSARLPELRRViflgdEKHPGM-LNFDELLALGRAVDDAELaarqatLD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 290 EH-PLYILYTSGTTGLPKGvirptggyaVMLhwSMSSIyglqpgevwwaasdL--GWVVGHS---------------YIC 351
Cdd:PRK08315 198 PDdPINIQYTSGTTGFPKG---------ATL--THRNI--------------LnnGYFIGEAmklteedrlcipvplYHC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 352 YGPLL-------HGNTTVLyegkPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPGAAlgkQYSLTRFKTLFVAG 424
Cdd:PRK08315 253 FGMVLgnlacvtHGATMVY----PGEGFDPLATLAAVEEERCTALYGVPTMFIAE-LDHPDFA---RFDLSSLRTGIMAG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 425 ERCDVETLEwsknvfRVPVLDH-------WWQTETgSPI---TA---------SCVG------------LGNSKTPPPGQ 473
Cdd:PRK08315 325 SPCPIEVMK------RVIDKMHmsevtiaYGMTET-SPVstqTRtddplekrvTTVGralphlevkivdPETGETVPRGE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 474 AGKSVP-GYNVMilddnmqklkarclgnivvklplppgafSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMS 552
Cdd:PRK08315 398 QGELCTrGYSVM----------------------------KGYWNDPEKTAEAIDAD--GWMHTGDLAVMDEEGYVNIVG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 553 RVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLE---------EIVKHVR 623
Cdd:PRK08315 448 RIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDfcrgkiahyKIPRYIR 527
|
570 580
....*....|....*....|....*.
gi 32258701 624 qnigpvaafrnavFVKQLPKTRSGKI 649
Cdd:PRK08315 528 -------------FVDEFPMTVTGKI 540
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
144-654 |
3.45e-20 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 94.70 E-value: 3.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 144 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAI--------------HSL---------IFGG 200
Cdd:PRK07059 50 TYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVvvnvnplytpreleHQLkdsgaeaivVLEN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 201 FASKeLSSRIDHVKPKVVVTASFGIEPG----------RRV-EYVPlveeALKIGQHKPdkiliYNRPnmeavpLAPGRd 269
Cdd:PRK07059 130 FATT-VQQVLAKTAVKHVVVASMGDLLGfkghivnfvvRRVkKMVP----AWSLPGHVR-----FNDA------LAEGA- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 270 ldwdeemakAQSHDCVPVLSEHPLYILYTSGTTGLPKGvirptggyAVMLHWSMSSIYgLQpGEVWW-AASDLGWVVGH- 347
Cdd:PRK07059 193 ---------RQTFKPVKLGPDDVAFLQYTGGTTGVSKG--------ATLLHRNIVANV-LQ-MEAWLqPAFEKKPRPDQl 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 348 SYICYGPLLH-GNTTVlyegkpvgtpdagAYFRVLAEHGVAALFTAPTAIrairqqdPG--AALGKqYSLTRF---KTLF 421
Cdd:PRK07059 254 NFVCALPLYHiFALTV-------------CGLLGMRTGGRNILIPNPRDI-------PGfiKELKK-YQVHIFpavNTLY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 422 VA-GERCDVETLEWSKNVFRV--------PVLDHWWQTeTGSPITAscvGLGNSKTPP------------PGQAGKSVPG 480
Cdd:PRK07059 313 NAlLNNPDFDKLDFSKLIVANgggmavqrPVAERWLEM-TGCPITE---GYGLSETSPvatcnpvdatefSGTIGLPLPS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 481 YNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINV 560
Cdd:PRK07059 389 TEVSIRDDDGNDLPLGEPGEICIR---GPQVMAGYWNRPDETAKVMTAD--GFFRTGDVGVMDERGYTKIVDRKKDMILV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 561 AGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVpLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQ 640
Cdd:PRK07059 464 SGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEA-VKLFVVKKDPALTE----EDVKAFCKERLTNYKRPKFVEFRTE 538
|
570
....*....|....
gi 32258701 641 LPKTRSGKIPRSAL 654
Cdd:PRK07059 539 LPKTNVGKILRREL 552
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
86-654 |
4.66e-20 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 94.52 E-value: 4.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 86 WYKPWTKTLENKHSPSTRFVEGMLNICYNAVDRHIENGkgdkiaiiyDSPVTNTKATF--TYKEVLEQVSKLA-GVLVKH 162
Cdd:PLN02574 17 WYSPETGIYSSKHPPVPLPSDPNLDAVSFIFSHHNHNG---------DTALIDSSTGFsiSYSELQPLVKSMAaGLYHVM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 163 GIKKGDTVV------IYMPMIpqamytMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASFGIE--PGRRVEyV 234
Cdd:PLN02574 88 GVRQGDVVLlllpnsVYFPVI------FLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEklSPLGVP-V 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 235 PLVEEALKIgqhkpDKILIYNRPNMEAVPLAPgrdldwdeemakaqshDCV--PVLSEHPLY-ILYTSGTTGLPKGVIRP 311
Cdd:PLN02574 161 IGVPENYDF-----DSKRIEFPKFYELIKEDF----------------DFVpkPVIKQDDVAaIMYSSGTTGASKGVVLT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 312 TGGYAVMLHWSM---SSIYGLQPGE-VWWAASDLGWVVGHSYICYGPLLHGNTTVLYEgkpvgTPDAGAYFRVLAEHGVA 387
Cdd:PLN02574 220 HRNLIAMVELFVrfeASQYEYPGSDnVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMR-----RFDASDMVKVIDRFKVT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 388 ALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTLFVAGERCDVEtlEWSKNVFRVPVLDHWWQTETGSPITAscvGLGNSK 467
Cdd:PLN02574 295 HFPVVPPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQ--DFVQTLPHVDFIQGYGMTESTAVGTR---GFNTEK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 468 TPPPGQAGKSVPGYNVMILDdnmqkLKARCLgnivvklpLPPGAFSGLW-----------KNQEAFKHLYFEKfpGYYDT 536
Cdd:PLN02574 370 LSKYSSVGLLAPNMQAKVVD-----WSTGCL--------LPPGNCGELWiqgpgvmkgylNNPKATQSTIDKD--GWLRT 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 537 MDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLE 616
Cdd:PLN02574 435 GDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVIN 514
|
570 580 590
....*....|....*....|....*....|....*...
gi 32258701 617 EIVKHVrqniGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:PLN02574 515 YVAKQV----APYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
62-115 |
5.94e-20 |
|
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: 83.68 E-value: 5.94e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 32258701 62 YKTHFAASVTDPERFWGKAAEQISWYKPWTKTLENKHSPSTR-FVEGMLNICYNA 115
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPFDKVLDGSNGPFAKwFVGGKLNVCYNC 55
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
447-651 |
6.90e-20 |
|
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: 91.56 E-value: 6.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 447 WW----QTETGSPITASCVglgnskTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLppgAFSGLWKNQEAF 522
Cdd:cd17637 139 FWslygQTETSGLVTLSPY------RERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPL---VFQGYWNLPELT 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 523 KHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRV--DDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLAL 600
Cdd:cd17637 210 AYTFRN---GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAV 286
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 32258701 601 CVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 651
Cdd:cd17637 287 CVLKPGATLTA----DELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
142-651 |
1.45e-19 |
|
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: 92.12 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 142 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 221
Cdd:cd05914 7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 222 sfgiepgrrveyvplveealkigqhKPDKILIynrpnmeavplapgrdldwdeemakaqshdcvpvlsehplyILYTSGT 301
Cdd:cd05914 87 -------------------------DEDDVAL-----------------------------------------INYTSGT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 302 TGLPKGVIRP--------TGGYAVMLhwsmssiygLQPGEVWWAASDLGwvvgHSYICYG----PLLHGNTTVLYEGKPV 369
Cdd:cd05914 101 TGNSKGVMLTyrnivsnvDGVKEVVL---------LGKGDKILSILPLH----HIYPLTFtlllPLLNGAHVVFLDKIPS 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 370 GTPDAGAYFRVLAEHGVAALF-----------------------TAPTAIRAIRQQdPGAALGKQYSlTRFKTLFVAGER 426
Cdd:cd05914 168 AKIIALAFAQVTPTLGVPVPLviekifkmdiipkltlkkfkfklAKKINNRKIRKL-AFKKVHEAFG-GNIKEFVIGGAK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 427 CDVETLEWSKNVfRVPVLDHWWQTETGsPITAScvglgnskTPPP----GQAGKSVPGYNVMILDDNMQKLKarclGNIV 502
Cdd:cd05914 246 INPDVEEFLRTI-GFPYTIGYGMTETA-PIISY--------SPPNrirlGSAGKVIDGVEVRIDSPDPATGE----GEII 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 503 VKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVI-NVAGHRISAGAIEESILSHGTVA 581
Cdd:cd05914 312 VR---GPNVMKGYYKNPEATAEAFDKD--GWFHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVL 386
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32258701 582 DCAVVGKEDPLKGHV---PLALCVLRKDINATEEQVLEEIVKHVRQNigpVAAFRNAVFVK----QLPKTRSGKIPR 651
Cdd:cd05914 387 ESLVVVQEKKLVALAyidPDFLDVKALKQRNIIDAIKWEVRDKVNQK---VPNYKKISKVKivkeEFEKTPKGKIKR 460
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
136-655 |
1.59e-19 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 92.64 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 136 VTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKP 215
Cdd:PRK05852 37 VTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 216 KVVVTASFGiePGRRVEyvplveealkiGQHKPDKILIYNRPNMEAVPLAPGRDLDWDEEMAKAQShdcVPV-LSEHPLY 294
Cdd:PRK05852 117 RVVLIDADG--PHDRAE-----------PTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEPTPATS---TPEgLRPDDAM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 295 ILYTSGTTGLPKGVIRPTGGYAVMLHwSMSSIYGLQPGEVWWAASdlgwvvghsyicygPLLHGNTTV------LYEGKP 368
Cdd:PRK05852 181 IMFTGGTTGLPKMVPWTHANIASSVR-AIITGYRLSPRDATVAVM--------------PLYHGHGLIaallatLASGGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 369 VGTPDAGAY----FRVLAEHGVAALFTAPTAIRAIRQQDPGAalgKQYSLTRFKTLFVagERC----DVETLEWSKNVFR 440
Cdd:PRK05852 246 VLLPARGRFsahtFWDDIKAVGATWYTAVPTIHQILLERAAT---EPSGRKPAALRFI--RSCsaplTAETAQALQTEFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 441 VPVLDHWWQTETGSPITASCV-GLGNSKTP--PPGQAGKSVpGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWK 517
Cdd:PRK05852 321 APVVCAFGMTEATHQVTTTQIeGIGQTENPvvSTGLVGRST-GAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 518 NQEA-FKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHV 596
Cdd:PRK05852 400 ITAAnFTD-------GWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEA 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32258701 597 PLALCVLRKDINATEeqvlEEIVKHVRQNIGPV---AAFRNAvfvKQLPKTRSGKIPRSALS 655
Cdd:PRK05852 473 VAAVIVPRESAPPTA----EELVQFCRERLAAFeipASFQEA---SGLPHTAKGSLDRRAVA 527
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
144-658 |
5.84e-19 |
|
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: 90.47 E-value: 5.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 144 TYKEVLEQVSKLaGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASF 223
Cdd:cd05909 9 TYRKLLTGAIAL-ARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 224 GIEPGRRVEYVPLVEEA-------LKIGQHKPDKILIYnrPNMEAVPLAPGRDLDwdeemakaqshdCVPVLSEHPLYIL 296
Cdd:cd05909 88 FIEKLKLHHLFDVEYDArivyledLRAKISKADKCKAF--LAGKFPPKWLLRIFG------------VAPVQPDDPAVIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 297 YTSGTTGLPKGVirptggyaVMLHWSMSS-------IYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLY----E 365
Cdd:cd05909 154 FTSGSEGLPKGV--------VLSHKNLLAnveqitaIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHpnplD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 366 GKPVGtpdagayfRVLAEHGVAALFTAPTAIRAIrqqdpgAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLD 445
Cdd:cd05909 226 YKKIP--------ELIYDKKATILLGTPTFLRGY------ARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 446 HWWQTETgSPITAScvglgNSKTPP--PGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAF 522
Cdd:cd05909 292 GYGTTEC-SPVISV-----NTPQSPnkEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVR---GPNVMLGYLNEPELT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 523 KHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSH-GTVADCAVVGKEDPLKGHVpLALC 601
Cdd:cd05909 363 SFAFGD---GWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEK-IVLL 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 32258701 602 VLRKDINATEeqvLEEIVKHVrqNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIV 658
Cdd:cd05909 439 TTTTDTDPSS---LNDILKNA--GISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
141-653 |
7.97e-19 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 90.38 E-value: 7.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 141 ATFTYKEVLEQVSKLAGVLVKHGiKKGDTVVIympMIPQAM---YTMLACARIGAIHSLIF---GGFASKELSSRIDHVK 214
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG-KPGDRVLL---LAPPGLdfvAAFLGCLYAGAIAVPLPpptPGRHAERLAAILADAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 215 PKVVVTASfgiepgrrvEYVPLVEEALKigqhkpdkiliynrpNMEAVPLAPGRDLDWDEEMAKAQSHDCVPVLSEhPLY 294
Cdd:cd05931 99 PRVVLTTA---------AALAAVRAFAA---------------SRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDD-IAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 295 ILYTSGTTGLPKGV-IRptggYAVMLH--WSMSSIYGLQPGEVWwaAS------DLGWVVGhsyICyGPLLHGNTTVL-- 363
Cdd:cd05931 154 LQYTSGSTGTPKGVvVT----HRNLLAnvRQIRRAYGLDPGDVV--VSwlplyhDMGLIGG---LL-TPLYSGGPSVLms 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 364 ---YEGKPVGtpdagaYFRVLAEHGvaALFT-APT-----AIRAIRQQDPGAalgkqYSLTRFKTLFVAGERCDVETLE- 433
Cdd:cd05931 224 paaFLRRPLR------WLRLISRYR--ATISaAPNfaydlCVRRVRDEDLEG-----LDLSSWRVALNGAEPVRPATLRr 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 434 ---------WSKNVFR-------------VPVLDHWWQTETGSPITASCVGLGNSKTPPPGQA----GKSVPGYNVMILD 487
Cdd:cd05931 291 faeafapfgFRPEAFRpsyglaeatlfvsGGPPGTGPVVLRVDRDALAGRAVAVAADDPAARElvscGRPLPDQEVRIVD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 488 DN-MQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKFP----GYYDTMDAGYMDEeGYLYVMSRVDDVINVAG 562
Cdd:cd05931 371 PEtGRELPDGEVGEIWVR---GPSVASGYWGRPEATAETFGALAAtdegGWLRTGDLGFLHD-GELYITGRLKDLIIVRG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 563 HRISAGAIEESILSH------GTVADCAVVGKEDplkGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGpVAAfRNAV 636
Cdd:cd05931 447 RNHYPQDIEATAEEAhpalrpGCVAAFSVPDDGE---ERLVVVAEVERGADPADLAAIAAAIRAAVAREHG-VAP-ADVV 521
|
570
....*....|....*....
gi 32258701 637 FVKQ--LPKTRSGKIPRSA 653
Cdd:cd05931 522 LVRPgsIPRTSSGKIQRRA 540
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
292-651 |
2.09e-18 |
|
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: 87.33 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 292 PLYILYTSGTTGLPKGVirptggyavML-HWSMSSiYGLQPGEVwwaasdLGWVVGHSYICYGPLLH------GNTTVLY 364
Cdd:cd05917 4 VINIQFTSGTTGSPKGA---------TLtHHNIVN-NGYFIGER------LGLTEQDRLCIPVPLFHcfgsvlGVLACLT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 365 EGKPVGTP----DAGAYFRVLAEHGVAALFTAPTA-IRAIRQQDPgaalgKQYSLTRFKTLFVAGERCDVETLEWSKNVF 439
Cdd:cd05917 68 HGATMVFPspsfDPLAVLEAIEKEKCTALHGVPTMfIAELEHPDF-----DKFDLSSLRTGIMAGAPCPPELMKRVIEVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 440 RVP-VLDHWWQTETgSPIT------------------------ASCVGLGNSKTPPPGQAGK-SVPGYNVMIlddnmqkl 493
Cdd:cd05917 143 NMKdVTIAYGMTET-SPVStqtrtddsiekrvntvgrimphteAKIVDPEGGIVPPVGVPGElCIRGYSVMK-------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 494 karclgnivvklplppgafsGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEES 573
Cdd:cd05917 214 --------------------GYWNDPEKTAEAIDGD--GWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEF 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32258701 574 ILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 651
Cdd:cd05917 272 LHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTE----EDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
121-660 |
2.50e-18 |
|
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: 88.88 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 121 ENGKGDKIAIIYDspvTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGG 200
Cdd:cd05906 21 ERGPTKGITYIDA---DGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 201 FASKELSSRIDHVK--------PKVVVTAsfgiepgrrvEYVPLVEEALKIGQHKPDKILIYnrpnmeavplapgrdldw 272
Cdd:cd05906 98 PTYDEPNARLRKLRhiwqllgsPVVLTDA----------ELVAEFAGLETLSGLPGIRVLSI------------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 273 DEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVirptggyaVMLHWSM-------SSIYGLQPGEVWwaasdLGWVv 345
Cdd:cd05906 150 EELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAV--------PLTHRNIlarsagkIQHNGLTPQDVF-----LNWV- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 346 ghsyicygPLLHGNTTVLYEGKPVgtpDAGA----------------YFRVLAEHGVAALFtAPT-AIRAIRQQDPGAAl 408
Cdd:cd05906 216 --------PLDHVGGLVELHLRAV---YLGCqqvhvpteeiladplrWLDLIDRYRVTITW-APNfAFALLNDLLEEIE- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 409 GKQYSLTRFKTLFVAGERCDVET-------LEWSK---NVFRvPVldhWWQTETGSPITASCVglgnSKTPPPGQA---- 474
Cdd:cd05906 283 DGTWDLSSLRYLVNAGEAVVAKTirrllrlLEPYGlppDAIR-PA---FGMTETCSGVIYSRS----FPTYDHSQAlefv 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 475 --GKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLppgAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEeGYLYVMS 552
Cdd:cd05906 355 slGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPV---VTKGYYNNPEANAEAFTED--GWFRTGDLGFLDN-GNLTITG 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 553 RVDDVINVAG-----HRISAgAIEE-SILSHGTVADCAVvgkEDPLKGHVPLALC-VLRKDINATEEQVLEEIVKHVRQN 625
Cdd:cd05906 429 RTKDTIIVNGvnyysHEIEA-AVEEvPGVEPSFTAAFAV---RDPGAETEELAIFfVPEYDLQDALSETLRAIRSVVSRE 504
|
570 580 590
....*....|....*....|....*....|....*.
gi 32258701 626 IGPVAAFRNAVFVKQLPKTRSGKIPRSAL-SAIVNG 660
Cdd:cd05906 505 VGVSPAYLIPLPKEEIPKTSLGKIQRSKLkAAFEAG 540
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
141-665 |
4.03e-18 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 88.14 E-value: 4.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 141 ATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT 220
Cdd:PRK05857 40 SALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 221 AsfgiePGRRVEyvplvEEALKIGQHKPDKIliynRPNMEAVPLAPGRDLDWDEEMAKAQSHdcvpvlSEHPLYILYTSG 300
Cdd:PRK05857 120 A-----PGSKMA-----SSAVPEALHSIPVI----AVDIAAVTRESEHSLDAASLAGNADQG------SEDPLAMIFTSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 301 TTGLPKGVIRPTGGYAVM--------LHW--------SMSSIYGLQPGEVWWAASdlgwvvghsyiCygpLLHGNTTVly 364
Cdd:PRK05857 180 TTGEPKAVLLANRTFFAVpdilqkegLNWvtwvvgetTYSPLPATHIGGLWWILT-----------C---LMHGGLCV-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 365 egkpVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqySLTRFKTLFVAGER---CDVETLEWSKnvfrV 441
Cdd:PRK05857 244 ----TGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANA----TVPSLRLVGYGGSRaiaADVRFIEATG----V 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 442 PVLDHWWQTETGSpiTASCVGLGNSKTP--PPGQAGKSVPGYNVMILDDN------MQKLKARCLGNIVVKlplPPGAFS 513
Cdd:PRK05857 312 RTAQVYGLSETGC--TALCLPTDDGSIVkiEAGAVGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIK---SPANML 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 514 GLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLK 593
Cdd:PRK05857 387 GYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEF 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32258701 594 GH-VPLALcVLRKDINATEEQVLEE-IVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYKI 665
Cdd:PRK05857 464 GAlVGLAV-VASAELDESAARALKHtIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARV 536
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
290-656 |
4.70e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 87.35 E-value: 4.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 290 EHPLYILYTSGTTGLPKGVIRPTGGYAvmlhwsmSSIYGLqpGEVW-WAASDL-----------GWVVGhsyiCYGPLLH 357
Cdd:PRK07787 128 DAPALIVYTSGTTGPPKGVVLSRRAIA-------ADLDAL--AEAWqWTADDVlvhglplfhvhGLVLG----VLGPLRI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 358 GNTtVLYEGKPvgTPDAgaYFRVLAEHGvAALFTAPTAIRAIrQQDPGAAlgKQYSLTRfktLFVAGE----RCDVETLE 433
Cdd:PRK07787 195 GNR-FVHTGRP--TPEA--YAQALSEGG-TLYFGVPTVWSRI-AADPEAA--RALRGAR---LLVSGSaalpVPVFDRLA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 434 WSKNVfrvPVLDHWWQTETgsPITASCVGLGNSKtppPGQAGKSVPGYNVMILDDNMQKLKA--RCLGNIVVKlplPPGA 511
Cdd:PRK07787 263 ALTGH---RPVERYGMTET--LITLSTRADGERR---PGWVGLPLAGVETRLVDEDGGPVPHdgETVGELQVR---GPTL 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 512 FSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVD-DVINVAGHRISAGAIEESILSHGTVADCAVVGKED 590
Cdd:PRK07787 332 FDGYLNRPDATAAAFTAD--GWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPD 409
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32258701 591 PLKGHVPLALCVLRKDINAteeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 656
Cdd:PRK07787 410 DDLGQRIVAYVVGADDVAA------DELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
126-654 |
4.87e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 87.53 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDSPVtntkatFTYKEVLEQVSKLAGVLVKHGiKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PRK07638 16 NKIAIKENDRV------LTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 LSSRIDHVKPKVVVTASFGIEPGRRVEyvplveealkigqhkpdkiliynrpnmeavplapGRDLDWDE--EMAKAQSHD 283
Cdd:PRK07638 89 LKERLAISNADMIVTERYKLNDLPDEE----------------------------------GRVIEIDEwkRMIEKYLPT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 284 CVPV--LSEHPLYILYTSGTTGLPKGVIRPtggyavmlHWS-MSSI------YGLQPGEVWWAASDLGwvvgHSYICYGP 354
Cdd:PRK07638 135 YAPIenVQNAPFYMGFTSGSTGKPKAFLRA--------QQSwLHSFdcnvhdFHMKREDSVLIAGTLV----HSLFLYGA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 355 L--LHGNTTVLYEGK--PVGTPDAgayfrvLAEHGVAALFTAPTAIRAIrqqdpgaalgkqYSLTRFK----TLFVAGER 426
Cdd:PRK07638 203 IstLYVGQTVHLMRKfiPNQVLDK------LETENISVMYTVPTMLESL------------YKENRVIenkmKIISSGAK 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 427 CDVETLEWSKNVFRVPVLDHWWQTETGSPITAScvgLGNSKTPPPGQAGKsvPGYNVMILDDNM--QKLKARCLGNIVVK 504
Cdd:PRK07638 265 WEAEAKEKIKNIFPYAKLYEFYGASELSFVTAL---VDEESERRPNSVGR--PFHNVQVRICNEagEEVQKGEIGTVYVK 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 505 LPLppgAFSGlWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCA 584
Cdd:PRK07638 340 SPQ---FFMG-YIIGGVLARELNAD--GWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIV 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 585 VVGKEDPLKGHVPLALCvlrkDINATEEQvleeIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:PRK07638 414 VIGVPDSYWGEKPVAII----KGSATKQQ----LKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
142-591 |
5.09e-18 |
|
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: 87.86 E-value: 5.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 142 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 221
Cdd:cd17641 11 EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 222 SFG-----IEPGRR---VEYVPLVEEAlkiGQHKpdkiliYNRPNMEAVP--LAPGRDLDWD-----EEMAKAQSHDCVP 286
Cdd:cd17641 91 DEEqvdklLEIADRipsVRYVIYCDPR---GMRK------YDDPRLISFEdvVALGRALDRRdpglyEREVAAGKGEDVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 287 VLSehplyilYTSGTTGLPKGVIRPTGGYAvmlhwSMSSIY----GLQPGEVWWAASDLGWVVGHSYICYGPLLHGN--- 359
Cdd:cd17641 162 VLC-------TTSGTTGKPKLAMLSHGNFL-----GHCAAYlaadPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFivn 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 360 -----TTVLYEGKPVG------TP---------------DAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGA------- 406
Cdd:cd17641 230 fpeepETMMEDLREIGptfvllPPrvwegiaadvrarmmDATPFKRFMFELGMKLGLRALDRGKRGRPVSLWLrlaswla 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 407 ------ALGKQYSLTRFKTLFVAGERCDVETLEWsknvFR---VPVLDHWWQTETGSPITASCVGlgnskTPPPGQAGKS 477
Cdd:cd17641 310 dallfrPLRDRLGFSRLRSAATGGAALGPDTFRF----FHaigVPLKQLYGQTELAGAYTVHRDG-----DVDPDTVGVP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 478 VPGYNVMIldDNMqklkarclGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDV 557
Cdd:cd17641 381 FPGTEVRI--DEV--------GEILVR---SPGVFVGYYKNPEATAEDFDED--GWLHTGDAGYFKENGHLVVIDRAKDV 445
|
490 500 510
....*....|....*....|....*....|....*
gi 32258701 558 INVA-GHRISAGAIEESILSHGTVADCAVVGKEDP 591
Cdd:cd17641 446 GTTSdGTRFSPQFIENKLKFSPYIAEAVVLGAGRP 480
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
114-359 |
5.30e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 88.01 E-value: 5.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 114 NAVDRHiengkGDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAI 193
Cdd:PRK08279 45 EAAARH-----PDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 194 HSLIFGGFASKELSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEAlkiGQHKPDKILIYnrPNMEAVPLAPGRDLDWD 273
Cdd:PRK08279 114 VALLNTQQRGAVLAHSLNLVDAKHLIVGE---------ELVEAFEEA---RADLARPPRLW--VAGGDTLDDPEGYEDLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 274 EEMAKAQSHD---CVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWwaasdlgwvvghsYI 350
Cdd:PRK08279 180 AAAAGAPTTNpasRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGG-FGGLLRLTPDDVL-------------YC 245
|
....*....
gi 32258701 351 CYgPLLHGN 359
Cdd:PRK08279 246 CL-PLYHNT 253
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
141-654 |
5.64e-18 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 88.95 E-value: 5.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 141 ATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT 220
Cdd:PRK10252 482 YQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLIT 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 221 ASfgiepgrrveyvplvEEALKIgQHKPD-KILIYNrpnmeaVPLAPgrdldwdeemakAQSHDCVPVLSEHPLYILYTS 299
Cdd:PRK10252 562 TA---------------DQLPRF-ADVPDlTSLCYN------APLAP------------QGAAPLQLSQPHHTAYIIFTS 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 300 GTTGLPKGVIrpTGGYAVM--LHWsMSSIYGLQPG----------------EVWWaasdlgwvvghsyicygPLLHGNTT 361
Cdd:PRK10252 608 GSTGRPKGVM--VGQTAIVnrLLW-MQNHYPLTADdvvlqktpcsfdvsvwEFFW-----------------PFIAGAKL 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 362 VLyeGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQ-DPGAALGKQYSLTRfktLFVAGERCDVEtlewsknvfr 440
Cdd:PRK10252 668 VM--AEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASlTPEGARQSCASLRQ---VFCSGEALPAD---------- 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 441 vpVLDHWWQTeTGSPI------TASCVGLgnSKTPPPGQA-----GKSVP-GYNV-----MILDDNMQklkarclgnivv 503
Cdd:PRK10252 733 --LCREWQQL-TGAPLhnlygpTEAAVDV--SWYPAFGEElaavrGSSVPiGYPVwntglRILDARMR------------ 795
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 504 klPLPPGAfSGlwknqeafkHLYF-----------------EKF------PG--YYDTMDAGYMDEEGYLYVMSRVDDVI 558
Cdd:PRK10252 796 --PVPPGV-AG---------DLYLtgiqlaqgylgrpdltaSRFiadpfaPGerMYRTGDVARWLDDGAVEYLGRSDDQL 863
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 559 NVAGHRISAGAIEESILSHGTVADCAVV-----------GKEDPLKGHVPlALCVLRKDINATEEQVLEEIVKHVRqnig 627
Cdd:PRK10252 864 KIRGQRIELGEIDRAMQALPDVEQAVTHacvinqaaatgGDARQLVGYLV-SQSGLPLDTSALQAQLRERLPPHMV---- 938
|
570 580
....*....|....*....|....*..
gi 32258701 628 PVAafrnAVFVKQLPKTRSGKIPRSAL 654
Cdd:PRK10252 939 PVV----LLQLDQLPLSANGKLDRKAL 961
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
133-654 |
7.00e-18 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 87.62 E-value: 7.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 133 DSPV-TNTKATFTYKEVLEQVSKLAGVLVKH-GIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSR- 209
Cdd:PRK08751 40 DRPAyHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQl 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 210 IDHVKPKVVVTASFG-----IEPGRRVEYVPLVEEALKIGQHKPDKILIYNRPNMEAVP-LAPGRDLDWDEEMAKAQSHD 283
Cdd:PRK08751 120 IDSGASVLVVIDNFGttvqqVIADTPVKQVITTGLGDMLGFPKAALVNFVVKYVKKLVPeYRINGAIRFREALALGRKHS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 284 CVPVLSEHP--LYILYTSGTTGLPKGvirptggyAVMLHWSMssIYGLQPGEVWWAASDLGWVVGHSYICYGPLLH---- 357
Cdd:PRK08751 200 MPTLQIEPDdiAFLQYTGGTTGVAKG--------AMLTHRNL--VANMQQAHQWLAGTGKLEEGCEVVITALPLYHifal 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 358 -GNTTVLYE----GKPVGTP-DAGAYFRVLAEhgvaALFTAPTAIRAIRQ---QDPGAAlgkQYSLTRFKTLFVAGERCD 428
Cdd:PRK08751 270 tANGLVFMKiggcNHLISNPrDMPGFVKELKK----TRFTAFTGVNTLFNgllNTPGFD---QIDFSSLKMTLGGGMAVQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 429 VETLEWSKNVFRVPVLDHWWQTETgSPitASCVglgNSKTPPP--GQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlp 506
Cdd:PRK08751 343 RSVAERWKQVTGLTLVEAYGLTET-SP--AACI---NPLTLKEynGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK-- 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 507 lPPGAFSGLWKNQEAFKHLYfeKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVV 586
Cdd:PRK08751 415 -GPQVMKGYWKRPEETAKVM--DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAV 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32258701 587 GKEDPLKGHVpLALCVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:PRK08751 492 GVPDEKSGEI-VKVVIVKKDPALTAEDVKA----HARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
133-654 |
7.82e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 87.51 E-value: 7.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 133 DSPV-TNTKATFTYKEVLEQVSKLAGVLVKH-GIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRI 210
Cdd:PRK05677 39 DKPAfSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 211 DHVKPK-VVVTASF-----GIEPGRRVEYVPLVEEAlkiGQHKPDKILI--------------YNRPNmeAVP----LAP 266
Cdd:PRK05677 119 NDSGAKaLVCLANMahlaeKVLPKTGVKHVIVTEVA---DMLPPLKRLLinavvkhvkkmvpaYHLPQ--AVKfndaLAK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 267 GRDLDWDEemAKAQSHDcVPVLSehplyilYTSGTTGLPKG-VIRPTGGYAVMLHWSMSSIYGLQPG-EVWWAASDLGWV 344
Cdd:PRK05677 194 GAGQPVTE--ANPQADD-VAVLQ-------YTGGTTGVAKGaMLTHRNLVANMLQCRALMGSNLNEGcEILIAPLPLYHI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 345 VGHSYICYGPLLHGNTTVLyegkpVGTP-DAGAYFRVLAEH------GVAALFTAPTAIRAIRQQDpgaalgkqysLTRF 417
Cdd:PRK05677 264 YAFTFHCMAMMLIGNHNIL-----ISNPrDLPAMVKELGKWkfsgfvGLNTLFVALCNNEAFRKLD----------FSAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 418 KTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETgSPItascVGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARC 497
Cdd:PRK05677 329 KLTLSGGMALQLATAERWKEVTGCAICEGYGMTET-SPV----VSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 498 LGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSH 577
Cdd:PRK05677 404 VGELCVK---GPQVMKGYWQRPEATDEILDSD--GWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAAL 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32258701 578 GTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEeivkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:PRK05677 479 PGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVME----HMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
108-626 |
9.34e-18 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 86.88 E-value: 9.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 108 MLNICynavdRHIE---NGKGDKIAIIY----DSPVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGD-TVVIYMPMIPq 179
Cdd:PRK09274 5 MANIA-----RHLPraaQERPDQLAVAVpggrGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMrAVLMVTPSLE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 180 aMYT-MLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVtasfGIEP---GRR--------VEYVPLVEEALKIGQHK 247
Cdd:PRK09274 79 -FFAlTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFI----GIPKahlARRlfgwgkpsVRRLVTVGGRLLWGGTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 248 PDKILIynRPNMEAVPLApgrDLDWDEEMAkaqshdcvpvlsehplyILYTSGTTGLPKGVIRPTGGYAVMLHwSMSSIY 327
Cdd:PRK09274 154 LATLLR--DGAAAPFPMA---DLAPDDMAA-----------------ILFTSGSTGTPKGVVYTHGMFEAQIE-ALREDY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 328 GLQPGEVwwaasDLgwvvgHSYicygPL--LH----GNTTVLYE---GKPvGTPDAGAYFRVLAEHGVAALFTAPTAIRA 398
Cdd:PRK09274 211 GIEPGEI-----DL-----PTF----PLfaLFgpalGMTSVIPDmdpTRP-ATVDPAKLFAAIERYGVTNLFGSPALLER 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 399 IRQqdpgAALGKQYSLTRFKTLFVAG--------ERC------DVETLewskNVF----RVPV---------LDHWWQTE 451
Cdd:PRK09274 276 LGR----YGEANGIKLPSLRRVISAGapvpiaviERFramlppDAEIL----TPYgateALPIssiesreilFATRAATD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 452 TGSPItasCVglgnsktpppgqaGKSVPGYNVMILD---------DNMQKLKARCLGNIVVKLPL-------PPGA--FS 513
Cdd:PRK09274 348 NGAGI---CV-------------GRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPMvtrsyynRPEAtrLA 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 514 GLWKNQEAFKHlyfekfpgyyDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKedPLK 593
Cdd:PRK09274 412 KIPDGQGDVWH----------RMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGV--GVP 479
|
570 580 590
....*....|....*....|....*....|....
gi 32258701 594 GHVPLALCV-LRKDINATEEQVLEEIVKHVRQNI 626
Cdd:PRK09274 480 GAQRPVLCVeLEPGVACSKSALYQELRALAAAHP 513
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
143-656 |
1.01e-17 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 87.21 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 143 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPqAMY-TMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 221
Cdd:PLN02479 46 YTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIP-AMYeAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 222 SfgiepgrrvEYVPLVEEALKI------GQHKPDKILIYNRPNMEAVPL--APGRDL--------DWDEEMAKAQSHDcv 285
Cdd:PLN02479 125 Q---------EFFTLAEEALKIlaekkkSSFKPPLLIVIGDPTCDPKSLqyALGKGAieyekfleTGDPEFAWKPPAD-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 286 pvlSEHPLYILYTSGTTGLPKGVI-RPTGGYAVMLhwSMSSIYGLQPGEVW-WAASDL---GWvvghsyiCYG---PLLH 357
Cdd:PLN02479 194 ---EWQSIALGYTSGTTASPKGVVlHHRGAYLMAL--SNALIWGMNEGAVYlWTLPMFhcnGW-------CFTwtlAALC 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 358 GNTTVLYEgkpvgtPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALgkqYSLTRFKTLFVAGERCDVETL-EWSK 436
Cdd:PLN02479 262 GTNICLRQ------VTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETI---LPLPRVVHVMTAGAAPPPSVLfAMSE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 437 NVFRVPvldHWWQ-TETGSPITASCVGLGNSKTPPPGQA------GKSVPGYNVMILDD--NMQKLKA--RCLGNIVVKl 505
Cdd:PLN02479 333 KGFRVT---HTYGlSETYGPSTVCAWKPEWDSLPPEEQArlnarqGVRYIGLEGLDVVDtkTMKPVPAdgKTMGEIVMR- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 506 plPPGAFSGLWKNQEAFKhlyfEKFP-GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCA 584
Cdd:PLN02479 409 --GNMVMKGYLKNPKANE----EAFAnGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEAS 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32258701 585 VVGKEDPLKGHVPLALCVLRKDINATEEQVL-EEIVKHVRQNIGPVAAFRNAVFvKQLPKTRSGKIPRSALSA 656
Cdd:PLN02479 483 VVARPDERWGESPCAFVTLKPGVDKSDEAALaEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRA 554
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
295-649 |
1.56e-17 |
|
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: 84.47 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 295 ILYTSGTTGLPKGVIrptggyavMLHwsmssiygLQPGEVWWAASDLGWVV-GHSYICYGPLLH------GNTTVLYEGK 367
Cdd:cd17638 5 IMFTSGTTGRSKGVM--------CAH--------RQTLRAAAAWADCADLTeDDRYLIINPFFHtfgykaGIVACLLTGA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 368 ---PVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAalgKQYSLTRFKTLFVAGERCDVETLEWSKNVFRV-PV 443
Cdd:cd17638 69 tvvPVAVFDVDAILEAIERERITVLPGPPTLFQSLLDH-PGR---KKFDLSSLRAAVTGAATVPVELVRRMRSELGFeTV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 444 LDHWWQTETGspiTASCVGLGNSKTPPPGQAGKSVPGYNVMILDDnmqklkarclGNIVVKlplPPGAFSGLWKNQEAFK 523
Cdd:cd17638 145 LTAYGLTEAG---VATMCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLVR---GYNVMQGYLDDPEATA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 524 HLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVL 603
Cdd:cd17638 209 EAIDAD--GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVA 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 32258701 604 RKDINATEEQVleeiVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKI 649
Cdd:cd17638 287 RPGVTLTEEDV----IAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
144-654 |
2.49e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 85.57 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 144 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVtasf 223
Cdd:PRK06164 37 SRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLV---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 224 gIEPG-RRVEYVPLVEEALKIGQHKPDKILIYNRPNMEAVPLAPGRDLD-WDEEMAKAQSHDCVPVLSEHPLYILY-TSG 300
Cdd:PRK06164 113 -VWPGfKGIDFAAILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQlFALPDPAPPAAAGERAADPDAGALLFtTSG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 301 TTGLPKGVIRPTGgyAVMLH-WSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGplLHGNTTVLYEgkPVGtpDAGAYFR 379
Cdd:PRK06164 192 TTSGPKLVLHRQA--TLLRHaRAIARAYGYDPGAVLLAALPFCGVFGFSTLLGA--LAGGAPLVCE--PVF--DAARTAR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 380 VLAEHGVAALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTlFVAGERcdvETLEWsknvfrvpVLDHwwqtetGSPITas 459
Cdd:PRK06164 264 ALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFAS-FAPALG---ELAAL--------ARAR------GVPLT-- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 460 cvGL-GNSK----------TPP------PGQAGKSvPGYNVMILD-DNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEA 521
Cdd:PRK06164 324 --GLyGSSEvqalvalqpaTDPvsvrieGGGRPAS-PEARVRARDpQDGALLPDGESGEIEIR---APSLMRGYLDNPDA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 522 FKHLYFEKfpGYYDTMDAGYMDEEG-YLYVmSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEdpLKGH-VPLA 599
Cdd:PRK06164 398 TARALTDD--GYFRTGDLGYTRGDGqFVYQ-TRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT--RDGKtVPVA 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 32258701 600 LCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSG---KIPRSAL 654
Cdd:PRK06164 473 FVIPTDGASPDE----AGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL 526
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
273-656 |
3.25e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 85.05 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 273 DEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTggyavmlhwSMSSIYGlqpgeVWWAASDLGWV-VGHSYIC 351
Cdd:PRK13383 157 DPATAGAEESGGRPAVAAPGRIVLLTSGTTGKPKGVPRAP---------QLRSAVG-----VWVTILDRTRLrTGSRISV 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 352 YGPLLHGN-----TTVLYEGKPVGTP---DAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPgaALGKQYSLTRFKTLFVA 423
Cdd:PRK13383 223 AMPMFHGLglgmlMLTIALGGTVLTHrhfDAEAALAQASLHRADAFTAVPVVLARILELPP--RVRARNPLPQLRVVMSS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 424 GERCDVETLEWSKNVFRVPVLDHWWQTEtgspitascVGLGNSKTPP-----PGQAGKSVPGYNVMILDDNMQKLKARCL 498
Cdd:PRK13383 301 GDRLDPTLGQRFMDTYGDILYNGYGSTE---------VGIGALATPAdlrdaPETVGKPVAGCPVRILDRNNRPVGPRVT 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 499 GNIVVKLPLPPGAFSGlwKNQEAFkhlyfekFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHG 578
Cdd:PRK13383 372 GRIFVGGELAGTRYTD--GGGKAV-------VDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHP 442
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32258701 579 TVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPvaafRNAVFVKQLPKTRSGKIPRSALSA 656
Cdd:PRK13383 443 AVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQP----RDINIVSSIPRNPTGKVLRKELPG 516
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
262-654 |
4.67e-17 |
|
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: 84.44 E-value: 4.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 262 VPLAPGRDLDWDEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLH-WSmsSIYGL--QPGEVWWAA 338
Cdd:cd17650 65 VPIDPDYPAERLQYMLEDSGAKLLLTQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHaWR--REYELdsFPVRLLQMA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 339 SdLGWVVGHSYICYGpLLHGNTTVLYegkPVGTP-DAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaALGKQYSLTRF 417
Cdd:cd17650 143 S-FSFDVFAGDFARS-LLNGGTLVIC---PDEVKlDPAALYDLILKSRITLMESTPALIRPVMAY----VYRNGLDLSAM 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 418 KTLFVAGERCDVETLEWSKNVF--RVPVLDHWWQTET---GSPITASCVGLGNSKTPPpgqAGKSVPGYNVMILDDNMQk 492
Cdd:cd17650 214 RLLIVGSDGCKAQDFKTLAARFgqGMRIINSYGVTEAtidSTYYEEGRDPLGDSANVP---IGRPLPNTAMYVLDERLQ- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 493 lkarclgnivvklPLPPGAFSGLW---------------KNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDV 557
Cdd:cd17650 290 -------------PQPVGVAGELYiggagvargylnrpeLTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQ 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 558 INVAGHRISAGAIEESILSHGTVADCAVVGKEDPlKGHVPL-ALCVLRKDINATEeqVLEEIVKHVRQNIGPvAAFrnaV 636
Cdd:cd17650 357 VKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGEARLcAYVVAAATLNTAE--LRAFLAKELPSYMIP-SYY---V 429
|
410
....*....|....*...
gi 32258701 637 FVKQLPKTRSGKIPRSAL 654
Cdd:cd17650 430 QLDALPLTPNGKVDRRAL 447
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
472-654 |
5.20e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 84.72 E-value: 5.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 472 GQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVM 551
Cdd:PRK08974 378 GSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVK---GPQVMLGYWQRPEATDEVIKD---GWLATGDIAVMDEEGFLRIV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 552 SRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVpLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAA 631
Cdd:PRK08974 452 DRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEA-VKIFVVKKDPSLTE----EELITHCRRHLTGYKV 526
|
170 180
....*....|....*....|...
gi 32258701 632 FRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:PRK08974 527 PKLVEFRDELPKSNVGKILRREL 549
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
201-656 |
1.33e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.83 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 201 FASKELS--------SRIDH------VKPKVVVtasfGIEPGRRVE--------------YVPLVEEalkigqHKPDKI- 251
Cdd:PRK12467 1595 FGEQELTygelnrraNRLAHrlialgVGPEVLV----GIAVERSLEmvvgllailkaggaYVPLDPE------YPRERLa 1664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 252 ----------LIYNRPNMEAVPLAPG-RDLDWDEEMAKAQSHDCV-PVLSEHP---LYILYTSGTTGLPKGVIRPTGGYA 316
Cdd:PRK12467 1665 ymiedsgielLLTQSHLQARLPLPDGlRSLVLDQEDDWLEGYSDSnPAVNLAPqnlAYVIYTSGSTGRPKGAGNRHGALV 1744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 317 VMLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVLyeGKPVGTPDAGAYFRVLAEHGVAALFTAPTAI 396
Cdd:PRK12467 1745 NRLCA-TQEAYQLSAADVVLQFTSFAFDVSVWEL-FWPLINGARLVI--APPGAHRDPEQLIQLIERQQVTTLHFVPSML 1820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 397 RAIRQQDPgaALGKQYSLTRfktLFVAGERCDVETLE-WSKNVFRVPVLDHWWQTETGSPIT---ASCVGLGNSKTPPPG 472
Cdd:PRK12467 1821 QQLLQMDE--QVEHPLSLRR---VVCGGEALEVEALRpWLERLPDTGLFNLYGPTETAVDVThwtCRRKDLEGRDSVPIG 1895
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 473 QAGKSVPGYnvmILDDNMQKLKARCLGNIVVKlplppGAfsGLWKNQEAFKHLYFEKF-------PG--YYDTMDAGYMD 543
Cdd:PRK12467 1896 QPIANLSTY---ILDASLNPVPIGVAGELYLG-----GV--GLARGYLNRPALTAERFvadpfgtVGsrLYRTGDLARYR 1965
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 544 EEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDP----LKGH-VPLALCVLRKDInatEEQVLEEI 618
Cdd:PRK12467 1966 ADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGAngkqLVAYvVPTDPGLVDDDE---AQVALRAI 2042
|
490 500 510
....*....|....*....|....*....|....*....
gi 32258701 619 VK-HVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 656
Cdd:PRK12467 2043 LKnHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPA 2081
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
255-656 |
1.53e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 83.15 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 255 NRPNMEAVPLAPGRDLD-----WDEEMAKAqsHDCVP---VLSEHPLYILYTSGTTGLPKGViRPTGGYAVMLHWSMSSI 326
Cdd:PRK13388 109 HRPLLDGLDLPGVRVLDvdtpaYAELVAAA--GALTPhreVDAMDPFMLIFTSGTTGAPKAV-RCSHGRLAFAGRALTER 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 327 YGLQPGEVwwaasdlgwvvghSYICYgPLLHGNTTV------LYEGKPVGTPDAGAYFRVLA---EHGvAALFT----AP 393
Cdd:PRK13388 186 FGLTRDDV-------------CYVSM-PLFHSNAVMagwapaVASGAAVALPAKFSASGFLDdvrRYG-ATYFNyvgkPL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 394 TAIRAIRQQDPGAalgkQYSLTR-FKTlfVAGERcDVEtlEWSKNvFRVPVLDHWWQTETGSPITAScvglgnsKTPPPG 472
Cdd:PRK13388 251 AYILATPERPDDA----DNPLRVaFGN--EASPR-DIA--EFSRR-FGCQVEDGYGSSEGAVIVVRE-------PGTPPG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 473 QAGKSVPGynVMILDDNMQKLKARC--------------LGNIVVKLPlpPGAFSGLWKNQEA----FKHlyfekfpGYY 534
Cdd:PRK13388 314 SIGRGAPG--VAIYNPETLTECAVArfdahgallnadeaIGELVNTAG--AGFFEGYYNNPEAtaerMRH-------GMY 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 535 DTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQv 614
Cdd:PRK13388 383 WSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDA- 461
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 32258701 615 LEEIVkHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 656
Cdd:PRK13388 462 FAAFL-AAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
272-656 |
2.14e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 82.81 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 272 WDEEMAkAQSHDCVPVLSEHP--LYILY-TSGTTGLPKGVI---RPTGGYAVMLhwsmSSIYGLQPGEVwwaasdlgwvv 345
Cdd:PRK07867 132 WADELA-AHRDAEPPFRVADPddLFMLIfTSGTSGDPKAVRcthRKVASAGVML----AQRFGLGPDDV----------- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 346 ghSYICYgPLLHGNTTVlyegkpvgtpdaGAYFRVLAEHGVAAL---FTAPTAIRAIRQQdpGAA----LGK--QYSLT- 415
Cdd:PRK07867 196 --CYVSM-PLFHSNAVM------------AGWAVALAAGASIALrrkFSASGFLPDVRRY--GATyanyVGKplSYVLAt 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 416 ------RFKTLFVA----GERCDVETLEwskNVFRVPVLDHWWQTETGSPITascvglgnsKTP--PPGQAGKSVPGYNV 483
Cdd:PRK07867 259 perpddADNPLRIVygneGAPGDIARFA---RRFGCVVVDGFGSTEGGVAIT---------RTPdtPPGALGPLPPGVAI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 484 M-----------ILDDNMQKLKARCLGNIVVklPLPPGAFSGLWKNQEAFKhlyfEKF-PGYYDTMDAGYMDEEGYLYVM 551
Cdd:PRK07867 327 VdpdtgtecppaEDADGRLLNADEAIGELVN--TAGPGGFEGYYNDPEADA----ERMrGGVYWSGDLAYRDADGYAYFA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 552 SRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIvkHVRQNIGPVAA 631
Cdd:PRK07867 401 GRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFL--AAQPDLGPKQW 478
|
410 420
....*....|....*....|....*
gi 32258701 632 FRNAVFVKQLPKTRSGKIPRSALSA 656
Cdd:PRK07867 479 PSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
126-654 |
2.31e-16 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 82.62 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDSPvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PRK07514 17 DAPFIETPDG-----LRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 LSSRIDHVKPKVVVTAsfgiePGRRVEYVPLVEEAlkigqhkpdkiliyNRPNMEavPLAPGRDLDWDEEMAKA-QSHDC 284
Cdd:PRK07514 92 LDYFIGDAEPALVVCD-----PANFAWLSKIAAAA--------------GAPHVE--TLDADGTGSLLEAAAAApDDFET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 285 VPVLSEHPLYILYTSGTTGLPKGvirptggyAVMLHWSMSSiYGLQPGEVW-WAASDlgwVVGHSYicygPLLH------ 357
Cdd:PRK07514 151 VPRGADDLAAILYTSGTTGRSKG--------AMLSHGNLLS-NALTLVDYWrFTPDD---VLIHAL----PIFHthglfv 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 358 -GNTTVLYEGKPVGTP--DAGAYFRVLAE----HGVAALFTaptaiRAIrqQDPGaaLGKQysLTRFKTLFVAGErcdve 430
Cdd:PRK07514 215 aTNVALLAGASMIFLPkfDPDAVLALMPRatvmMGVPTFYT-----RLL--QEPR--LTRE--AAAHMRLFISGS----- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 431 tlewsknvfrVPVLD---HWWQTETGSPI------TASCVglgNSKTP-----PPGQAGKSVPGYNVMILD-DNMQKLKA 495
Cdd:PRK07514 279 ----------APLLAethREFQERTGHAIlerygmTETNM---NTSNPydgerRAGTVGFPLPGVSLRVTDpETGAELPP 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 496 RCLGNIVVKlplPPGAFSGLW----KNQEAFKHlyfekfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIE 571
Cdd:PRK07514 346 GEIGMIEVK---GPNVFKGYWrmpeKTAEEFRA------DGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVE 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 572 ESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVkhvrqniGPVAAF---RNAVFVKQLPKTRSGK 648
Cdd:PRK07514 417 GEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALK-------GRLARFkqpKRVFFVDELPRNTMGK 489
|
....*.
gi 32258701 649 IPRSAL 654
Cdd:PRK07514 490 VQKNLL 495
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
143-622 |
2.60e-16 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 82.13 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 143 FTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTAS 222
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 223 FGIEPGRRveyvPLVEEALkigqhkpdkiliynrPNMEAVPLAPGRDLD-WDEEMAKAQ-SHDCVPVLSEHPLYILYTSG 300
Cdd:cd05932 87 LDDWKAMA----PGVPEGL---------------ISISLPPPSAANCQYqWDDLIAQHPpLEERPTRFPEQLATLIYTSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 301 TTGLPKGVIRPTGGYAvmlhWSMSSI---YGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYE-----------G 366
Cdd:cd05932 148 TTGQPKGVMLTFGSFA----WAAQAGiehIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAEsldtfvedvqrA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 367 KP---VGTPDAGAYF--RVLAEHGVAA---LFTAPTAIRAIRQQdpgaaLGKQYSLTRFKTLFVAGERCDVETLEWSKNV 438
Cdd:cd05932 224 RPtlfFSVPRLWTKFqqGVQDKIPQQKlnlLLKIPVVNSLVKRK-----VLKGLGLDQCRLAGCGSAPVPPALLEWYRSL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 439 fRVPVLDHWWQTETgSPITASCVGlGNSKTpppGQAGKSVPGYNVMILDDnmqklkarclGNIVVKlplPPGAFSGLWKN 518
Cdd:cd05932 299 -GLNILEAYGMTEN-FAYSHLNYP-GRDKI---GTVGNAGPGVEVRISED----------GEILVR---SPALMMGYYKD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 519 QEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVA-GHRISAGAIEESILSHGTVADCAVVGKEDPlkghVP 597
Cdd:cd05932 360 PEATAEAFTAD--GFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSGLP----AP 433
|
490 500 510
....*....|....*....|....*....|....*..
gi 32258701 598 LALCVL------------RKDINATEEQVLEEIVKHV 622
Cdd:cd05932 434 LALVVLseearlradafaRAELEASLRAHLARVNSTL 470
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
126-654 |
3.16e-16 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 82.09 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDSPvTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:cd05915 9 GRKEVVSRLH-TGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 LSSRIDHVKPKVVVTASfgiepgrrvEYVPLVEEALKIgqhkpdkiliynRPNMEAVPLAPGRDLDWDEEMAKAQSH--D 283
Cdd:cd05915 88 IAYILNHAEDKVLLFDP---------NLLPLVEAIRGE------------LKTVQHFVVMDEKAPEGYLAYEEALGEeaD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 284 CVPVLSEHPLYILYTSGTTGLPKGVIRP-TGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTV 362
Cdd:cd05915 147 PVRVPERAACGMAYTTGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 363 LYEgkpvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIrqQDPGAALGKQYSLTrfkTLFVAGERCDVETLEWSKNVFRVP 442
Cdd:cd05915 227 PGP-----RLDPASLVELFDGEGVTFTAGVPTVWLAL--ADYLESTGHRLKTL---RRLVVGGSAAPRSLIARFERMGVE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 443 VLDHWWQTETGSPITAsCVGLGNSKTPPPGQAG--KSVPGYN-----VMILDDNMQKLKARclGNIVVKLPLPPGA-FSG 514
Cdd:cd05915 297 VRQGYGLTETSPVVVQ-NFVKSHLESLSEEEKLtlKAKTGLPiplvrLRVADEEGRPVPKD--GKALGEVQLKGPWiTGG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 515 LWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKG 594
Cdd:cd05915 374 YYGNEEATRSALTPD--GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQ 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32258701 595 HVPLALCVLrKDINATEeqvlEEIVKHVRQNIGPVAAF-RNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd05915 452 ERPLAVVVP-RGEKPTP----EELNEHLLKAGFAKWQLpDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
126-656 |
4.25e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.08 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDspvtntKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfaske 205
Cdd:PRK12316 2018 EAIAVVFG------DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAY----------- 2080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 lssridhvkpkVVVTASFgiePGRRVEYvpLVEEAlkiGQHkpdkILIYNRPNMEAVPLAPG---RDLDWDEEMAKAQSH 282
Cdd:PRK12316 2081 -----------VPLDPNY---PAERLAY--MLEDS---GAA----LLLTQRHLLERLPLPAGvarLPLDRDAEWADYPDT 2137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 283 DCVPVLSEHPL-YILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGHSYiCYGPLLHGNTT 361
Cdd:PRK12316 2138 APAVQLAGENLaYVIYTSGSTGLPKGVAVSHGALVAHCQA-AGERYELSPADCELQFMSFSFDGAHEQ-WFHPLLNGARV 2215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 362 VLyegKPVGTPDAGAYFRVLAEHGVAALFTAPT-----AIRAIRQQDPGAAlgkqysltrfKTLFVAGERCDVETLE-WS 435
Cdd:PRK12316 2216 LI---RDDELWDPEQLYDEMERHGVTILDFPPVylqqlAEHAERDGRPPAV----------RVYCFGGEAVPAASLRlAW 2282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 436 KNVFRVPVLDHWWQTETG-SPITASC--VGLGNSKTPPPGQAGKSVPGYnvmILDDNMQklkarclgnivvklPLPPGAF 512
Cdd:PRK12316 2283 EALRPVYLFNGYGPTEAVvTPLLWKCrpQDPCGAAYVPIGRALGNRRAY---ILDADLN--------------LLAPGMA 2345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 513 SGLWKNQEAFKHLYFEKfPG-----------------YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESIL 575
Cdd:PRK12316 2346 GELYLGGEGLARGYLNR-PGltaerfvpdpfsasgerLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQ 2424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 576 SHGTVADCAVVGKEDPlkGHVPLALCVLRKDInatEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALS 655
Cdd:PRK12316 2425 AHPAVREAVVVAQDGA--SGKQLVAYVVPDDA---AEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALP 2499
|
.
gi 32258701 656 A 656
Cdd:PRK12316 2500 K 2500
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
144-655 |
7.32e-16 |
|
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: 80.43 E-value: 7.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 144 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASkelsSRIDHVkpkvvVTASF 223
Cdd:cd17653 24 TYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPS----ARIQAI-----LRTSG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 224 GiepgrrveyvplveealkigqhkpdKILIYNrpnmeavplapgrdlDWDEEMAkaqshdcvpvlsehplYILYTSGTTG 303
Cdd:cd17653 95 A-------------------------TLLLTT---------------DSPDDLA----------------YIIFTSGSTG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 304 LPKGVIRPTGGYAVMLhWSMSSIYGLQPG----EVWWAASDLG-WVVghsyicYGPLLHGNTTVLyegkpvgtPDAGAYF 378
Cdd:cd17653 119 IPKGVMVPHRGVLNYV-SQPPARLDVGPGsrvaQVLSIAFDACiGEI------FSTLCNGGTLVL--------ADPSDPF 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 379 RVLAEHgVAALFTAPTAIRAIRQQDpgaalgkqysLTRFKTLFVAGERCdvetlewSKnvfrvPVLDHWWQ--------- 449
Cdd:cd17653 184 AHVART-VDALMSTPSILSTLSPQD----------FPNLKTIFLGGEAV-------PP-----SLLDRWSPgrrlynayg 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 450 -TETgspitaSCVGLGNSKTppPGQA---GKSVPGYNVMILDDNMQKLKARCLGNIVVklpLPPGAFSGLWKNQEA---- 521
Cdd:cd17653 241 pTEC------TISSTMTELL--PGQPvtiGKPIPNSTCYILDADLQPVPEGVVGEICI---SGVQVARGYLGNPALtask 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 522 FKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESIL-SHGTVADCAVVGKEDPLKGHV-PLa 599
Cdd:cd17653 310 FVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLqSQPEVTQAAAIVVNGRLVAFVtPE- 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 32258701 600 lcvlrkdiNATEEQVLEEIVKHVRQNIGP---VAafrnavfVKQLPKTRSGKIPRSALS 655
Cdd:cd17653 389 --------TVDVDGLRSELAKHLPSYAVPdriIA-------LDSFPLTANGKVDRKALR 432
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
294-655 |
1.05e-15 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 80.14 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 294 YILYTSGTTGLPKGVIRPTGGyAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSY--ICYGpLLHGNTTVLYEGKPVGT 371
Cdd:cd17648 98 YAIYTSGTTGKPKGVLVEHGS-VVNLRTSLSERYFGRDNGDEAVLFFSNYVFDFFVeqMTLA-LLNGQKLVVPPDEMRFD 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 372 PDagAYFRVLAEHGVAALFTAPTAIRAIRqqdpgaaLGKQYSLTRfktLFVAGERCDVETLEWSKNVFRVPVLDHWWQTE 451
Cdd:cd17648 176 PD--RFYAYINREKVTYLSGTPSVLQQYD-------LARLPHLKR---VDAAGEEFTAPVFEKLRSRFAGLIINAYGPTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 452 TGspITascvglgNSKTPPPGQA------GKSVPGYNVMILDDNMQklkarclgnivvklPLPPGAFSGL---------- 515
Cdd:cd17648 244 TT--VT-------NHKRFFPGDQrfdkslGRPVRNTKCYVLNDAMK--------------RVPVGAVGELylggdgvarg 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 516 WKNQEAfkhLYFEKF----------------PGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGT 579
Cdd:cd17648 301 YLNRPE---LTAERFlpnpfqteqerargrnARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 580 VADCAVVGKEDPLKGHVPlalcvLRKDINA---TEEQVLEE--IVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd17648 378 VRECAVVAKEDASQAQSR-----IQKYLVGyylPEPGHVPEsdLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
.
gi 32258701 655 S 655
Cdd:cd17648 453 P 453
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
133-657 |
1.31e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 80.25 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 133 DSPV-TNTKATFTYKEVLEQVSKLAGVLVKH-GIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRI 210
Cdd:PRK12492 39 DRPAfSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 211 DHVKPKVVVTAS-FG-----IEPGRRVEYvpLVEeaLKIGQHKP-----------DKIL----IYNRPnmEAVP----LA 265
Cdd:PRK12492 119 KDSGARALVYLNmFGklvqeVLPDTGIEY--LIE--AKMGDLLPaakgwlvntvvDKVKkmvpAYHLP--QAVPfkqaLR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 266 PGRDLdwdEEMAKAQSHDCVPVLSehplyilYTSGTTGLPKGVIRPTGG--------YAVMLHWSMSSIYGLQPG-EVWW 336
Cdd:PRK12492 193 QGRGL---SLKPVPVGLDDIAVLQ-------YTGGTTGLAKGAMLTHGNlvanmlqvRACLSQLGPDGQPLMKEGqEVMI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 337 AASDLGWVVGHSYICYGPLLHGNTTVLyegkpVGTP-DAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAalgKQYSLT 415
Cdd:PRK12492 263 APLPLYHIYAFTANCMCMMVSGNHNVL-----ITNPrDIPGFIKELGKWRFSALLGLNTLFVALMDH-PGF---KDLDFS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 416 RFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETgSPItASCVGLGNSKTPppGQAGKSVPGYNVMILDDNMQKLKA 495
Cdd:PRK12492 334 ALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTET-SPV-ASTNPYGELARL--GTVGIPVPGTALKVIDDDGNELPL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 496 RCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESIL 575
Cdd:PRK12492 410 GERGELCIK---GPQVMKGYWQQPEATAEALDAE--GWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVM 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 576 SHGTVADCAVVGKEDPLKGHVpLALCVLRKDINATeeqvLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALS 655
Cdd:PRK12492 485 AHPKVANCAAIGVPDERSGEA-VKLFVVARDPGLS----VEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
..
gi 32258701 656 AI 657
Cdd:PRK12492 560 DI 561
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
262-656 |
2.98e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 80.39 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 262 VPLAPG-RDLDWDEEMAKAQSHD-CVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAAS 339
Cdd:PRK12316 3166 LPLAQGvQVLDLDRGDENYAEANpAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCW-MQQAYGLGVGDRVLQFT 3244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 340 DLGWVVGHSYIcYGPLLHGNTTVLyeGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIrQQDPGAAlgkqySLTRFKT 419
Cdd:PRK12316 3245 TFSFDVFVEEL-FWPLMSGARVVL--AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAF-LEEEDAH-----RCTSLKR 3315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 420 LFVAGERCDVETLEwsKNVFRVPVLDHWWQTETGSPITASCVGLGNSKTPPpgqAGKSVPGYNVMILDDNMQKLKARCLG 499
Cdd:PRK12316 3316 IVCGGEALPADLQQ--QVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAVP---IGRPIANRACYILDGSLEPVPVGALG 3390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 500 NIVVK-LPLPPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHG 578
Cdd:PRK12316 3391 ELYLGgEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHP 3470
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32258701 579 TVADCAVVGKE-DPLKGHVPLalcvlrkdiNATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 656
Cdd:PRK12316 3471 WVREAVVLAVDgRQLVAYVVP---------EDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
289-648 |
1.17e-14 |
|
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: 75.88 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 289 SEHPLYILYTSGTTGLPKGVirptggyavmlHWSMSSIYGLQPG----------EVWWAASDLGWVVGHSYICYGPLLHG 358
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGV-----------MWRQEDIFRMLMGgadfgtgeftPSEDAHKAAAAAAGTVMFPAPPLMHG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 359 NTTVLYEGKPVGTP---------DAGAYFRVLAEHGVAALFTAPTA-----IRAIRqqDPGAalgkqYSLTRFKTLFVAG 424
Cdd:cd05924 71 TGSWTAFGGLLGGQtvvlpddrfDPEEVWRTIEKHKVTSMTIVGDAmarplIDALR--DAGP-----YDLSSLFAISSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 425 ercdvetLEWSKNVfRVPVLDHWWQ---------TETGSpitascVGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLK- 494
Cdd:cd05924 144 -------ALLSPEV-KQGLLELVPNitlvdafgsSETGF------TGSGHSAGSGPETGPFTRANPDTVVLDDDGRVVPp 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 495 -ARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEK--FPGYYDTMDAGymdeeGYLYVMSRVDDVINVAGHRISAGAIE 571
Cdd:cd05924 210 gSGGVGWIARRGHIPLGYYGDEAKTAETFPEVDGVRyaVPGDRATVEAD-----GTVTLLGRGSVCINTGGEKVFPEEVE 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32258701 572 ESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGK 648
Cdd:cd05924 285 EALKSHPAVYDVLVVGRPDERWGQEVVAVVQLREGAGVDL----EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
126-654 |
1.48e-14 |
|
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: 76.54 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDSPVTntkatfTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHslifggfaske 205
Cdd:cd12114 2 DATAVICGDGTL------TYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAY----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 lssridhvkpkVVVTASfgiEPGRRVEYvpLVEEA---LKIGQHKPDKILIYNR--PNMEAVPLAPGRDldwdEEMAKAQ 280
Cdd:cd12114 65 -----------VPVDID---QPAARREA--ILADAgarLVLTDGPDAQLDVAVFdvLILDLDALAAPAP----PPPVDVA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 281 SHDcvpvlsehPLYILYTSGTTGLPKGV-IRPTGGYAVMLhwSMSSIYGLQPGEVWWAASDLGW---VvghsYICYGPLL 356
Cdd:cd12114 125 PDD--------LAYVIFTSGSTGTPKGVmISHRAALNTIL--DINRRFAVGPDDRVLALSSLSFdlsV----YDIFGALS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 357 HGNTTVLYEGKPVGTPDAGAyfRVLAEHGV--------------AALFTAPTAIRAIRQQ---------DPGAALGKQYS 413
Cdd:cd12114 191 AGATLVLPDEARRRDPAHWA--ELIERHGVtlwnsvpallemllDVLEAAQALLPSLRLVllsgdwiplDLPARLRALAP 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 414 LTRFKTLFVAgercdVETLEWSkNVFRV-PVLDHWWQTETGSPItascvglgnsktppPGQAgksvpgYNVMildDNMQK 492
Cdd:cd12114 269 DARLISLGGA-----TEASIWS-IYHPIdEVPPDWRSIPYGRPL--------------ANQR------YRVL---DPRGR 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 493 lkarclgnivvklPLPP-----------GAFSGLWKNQEAFKHLYFEKFPG--YYDTMDAGYMDEEGYLYVMSRVDDVIN 559
Cdd:cd12114 320 -------------DCPDwvpgelwiggrGVALGYLGDPELTAARFVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVK 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 560 VAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVpLALCVLRKDINATEEQVLEE-IVKHVRQNIGPvaafRNAVFV 638
Cdd:cd12114 387 VRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRL-AAFVVPDNDGTPIAPDALRAfLAQTLPAYMIP----SRVIAL 461
|
570
....*....|....*.
gi 32258701 639 KQLPKTRSGKIPRSAL 654
Cdd:cd12114 462 EALPLTANGKVDRAAL 477
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
531-656 |
2.50e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 75.08 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 531 PGYYDTMDAGYMDEeGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVlrKDINAT 610
Cdd:PRK07824 233 PGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVV--GDGGPA 309
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 32258701 611 EeqVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 656
Cdd:PRK07824 310 P--TLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
135-654 |
2.88e-14 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 75.94 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 135 PVTNTkatfTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAI-HSLIFGGFAsKELSSRIDHV 213
Cdd:PRK06018 36 PIVRT----TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAIcHTVNPRLFP-EQIAWIINHA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 214 KPKVVVTasfgiepgrRVEYVPLVEealKIGQHKP--DKILIY-NRPNMEAVPLA---------PGRDLD--W---DEEM 276
Cdd:PRK06018 111 EDRVVIT---------DLTFVPILE---KIADKLPsvERYVVLtDAAHMPQTTLKnavayeewiAEADGDfaWktfDENT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 277 AKAqshdcvpvlsehplyILYTSGTTGLPKGVIrptggYAvmlHWS--MSSIYGLQPGEVWWAASDLGW-VVghsyicyg 353
Cdd:PRK06018 179 AAG---------------MCYTSGTTGDPKGVL-----YS---HRSnvLHALMANNGDALGTSAADTMLpVV-------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 354 PLLHGNT-TVLYEGKPVGTP--------DAGAYFRVLAEHGVAalFTA--PTAIRAIRQQDPGAALgkqySLTRFKTLFV 422
Cdd:PRK06018 228 PLFHANSwGIAFSAPSMGTKlvmpgaklDGASVYELLDTEKVT--FTAgvPTVWLMLLQYMEKEGL----KLPHLKMVVC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 423 AGERCDVETLEWSKNvFRVPVLDHWWQTETgSPI-TASCVGLGNSKTPPPGQ------AGKSVPGYNVMILDDNMQKL-- 493
Cdd:PRK06018 302 GGSAMPRSMIKAFED-MGVEVRHAWGMTEM-SPLgTLAALKPPFSKLPGDARldvlqkQGYPPFGVEMKITDDAGKELpw 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 494 KARCLGNIVVKLPLPPGAFSGLWKNQeafkhlyFEKfPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEES 573
Cdd:PRK06018 380 DGKTFGRLKVRGPAVAAAYYRVDGEI-------LDD-DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 574 ILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSA 653
Cdd:PRK06018 452 AVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATR----EEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTA 527
|
.
gi 32258701 654 L 654
Cdd:PRK06018 528 L 528
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
114-659 |
6.60e-14 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 74.64 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 114 NAVDRHIENgkgDKIAIIYDSpvtntkATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAI 193
Cdd:PRK10946 29 DILTRHAAS---DAIAVICGE------RQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 194 HSLIFGGFASKELSSRIDHVKPKVVVtASFGIEPGRRVEYVplveEALKIGQHKPDKILIYNRPnmeavplaPGRDLD-W 272
Cdd:PRK10946 100 PVNALFSHQRSELNAYASQIEPALLI-ADRQHALFSDDDFL----NTLVAEHSSLRVVLLLNDD--------GEHSLDdA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 273 DEEmaKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSmSSIYGLQPGEVwwaasdlgwvvghsYICY 352
Cdd:PRK10946 167 INH--PAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRS-VEICGFTPQTR--------------YLCA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 353 GPLLH-------GNTTVLYEGKPV---GTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQYSLTRFKTLFV 422
Cdd:PRK10946 230 LPAAHnypmsspGALGVFLAGGTVvlaPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQA--IAEGGSRAQLASLKLLQV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 423 AGERCDvETLewsknVFRVPVL-------------------------DHWWQTEtGSPITascvglgnsktpppgqagks 477
Cdd:PRK10946 308 GGARLS-ETL-----ARRIPAElgcqlqqvfgmaeglvnytrlddsdERIFTTQ-GRPMS-------------------- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 478 vPGYNVMILDDNmqklkarclGNivvklPLPPG-----------AFSGLWK----NQEAFKHlyfekfPGYYDTMDAGYM 542
Cdd:PRK10946 361 -PDDEVWVADAD---------GN-----PLPQGevgrlmtrgpyTFRGYYKspqhNASAFDA------NGFYCSGDLVSI 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 543 DEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATeeqvleEIVKHV 622
Cdd:PRK10946 420 DPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAV------QLRRFL 493
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 32258701 623 RQNigPVAAFR---NAVFVKQLPKTRSGKIPRSALSAIVN 659
Cdd:PRK10946 494 REQ--GIAEFKlpdRVECVDSLPLTAVGKVDKKQLRQWLA 531
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
292-647 |
1.08e-13 |
|
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: 72.72 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 292 PLYILYTSGTTGLPKGVIRPTGgyAVMLH-WSMSSIYGLQPGEVwwaasdlgwvvghsYICYGPLLH------GNTTVLY 364
Cdd:cd17636 2 PVLAIYTAAFSGRPNGALLSHQ--ALLAQaLVLAVLQAIDEGTV--------------FLNSGPLFHigtlmfTLATFHA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 365 EGKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdpgaalgkqysltrfktlFVAGERCDVETL-------EWS 435
Cdd:cd17636 66 GGTNVFVRrvDAEEVLELIEAERCTHAFLLPPTIDQIVE-------------------LNADGLYDLSSLrsspaapEWN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 436 KNVfrvPVLDHWW--------QTETGSPITAScvGLGNSKTpppGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPL 507
Cdd:cd17636 127 DMA---TVDTSPWgrkpggygQTEVMGLATFA--ALGGGAI---GGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 508 ppgAFSGLWK----NQEAFKHlyfekfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADC 583
Cdd:cd17636 199 ---VMAGYWNrpevNARRTRG-------GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADA 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32258701 584 AVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSG 647
Cdd:cd17636 269 AVIGVPDPRWAQSVKAIVVLKPGASVTE----AELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
290-654 |
1.17e-13 |
|
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: 73.62 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 290 EHPLYILYTSGTTGLPKGVIrPTGGYAVMLHWSMSSIYGL-QPGEVWWAASdLGWVVGHSYIcYGPLLHGNTTVLYEGKP 368
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVM-IEHQSLVNLSHGLIKEYGItSSDRVLQFAS-IAFDVAAEEI-YVTLLSGATLVLRPEEM 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 369 VGTPDA----------------GAYFRVLAEHGVAALFTAPTAIRAIrqqdpgaalgkqysltrfktlFVAGERCDVETL 432
Cdd:cd17644 183 RSSLEDfvqyiqqwqltvlslpPAYWHLLVLELLLSTIDLPSSLRLV---------------------IVGGEAVQPELV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 433 E-WSKNVF-RVPVLDHWWQTEtgSPITASCVGL-----GNSKTPPpgqAGKSVPGYNVMILDDNMQKLKARCLGNIVV-K 504
Cdd:cd17644 242 RqWQKNVGnFIQLINVYGPTE--ATIAATVCRLtqlteRNITSVP---IGRPIANTQVYILDENLQPVPVGVPGELHIgG 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 505 LPLPPGAFSGLWKNQEAFKHLYFEKFPG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVAD 582
Cdd:cd17644 317 VGLARGYLNRPELTAEKFISHPFNSSESerLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKT 396
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32258701 583 CAVVGKEDPLKGHVPLALCVLRKD-INATEEqvLEEIVKHVRQNIGPVAAFrnaVFVKQLPKTRSGKIPRSAL 654
Cdd:cd17644 397 AVVIVREDQPGNKRLVAYIVPHYEeSPSTVE--LRQFLKAKLPDYMIPSAF---VVLEELPLTPNGKIDRRAL 464
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
295-649 |
2.33e-13 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 73.80 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 295 ILYTSGTTGLPKGVirptggyavML-HWS-MSSIygLQPGEVWWAASD------------LGWVVghsyICYGPLLHGNT 360
Cdd:PRK08633 787 IIFSSGSEGEPKGV---------MLsHHNiLSNI--EQISDVFNLRNDdvilsslpffhsFGLTV----TLWLPLLEGIK 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 361 TVlYEGKPVgtpDAGAYFRVLAEHGVAALFTAPTAIRA-IRQQ--DPgaalgkqyslTRFKTL--FVAG-ERCDVETLEW 434
Cdd:PRK08633 852 VV-YHPDPT---DALGIAKLVAKHRATILLGTPTFLRLyLRNKklHP----------LMFASLrlVVAGaEKLKPEVADA 917
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 435 SKNVFRVPVLDHWWQTETGSPITAS-----CVGLGNSKTPPPGQAGKSVPGYNVMILD-DNMQKLKARCLGNIVVKlplP 508
Cdd:PRK08633 918 FEEKFGIRILEGYGATETSPVASVNlpdvlAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIG---G 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 509 PGAFSGLWKNQ----EAFKHLyfeKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESI--LSHGTVAD 582
Cdd:PRK08633 995 PQVMKGYLGDPektaEVIKDI---DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELakALGGEEVV 1071
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32258701 583 CAVVGKEDPLKGHvplALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFrnaVFVKQLPKTRSGKI 649
Cdd:PRK08633 1072 FAVTAVPDEKKGE---KLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRY---FKVEALPLLGSGKL 1132
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
536-651 |
2.57e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 72.38 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 536 TMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINateeqvL 615
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEID------P 368
|
90 100 110
....*....|....*....|....*....|....*.
gi 32258701 616 EEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPR 651
Cdd:PRK08308 369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSR 404
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
274-654 |
4.94e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 72.05 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 274 EEMAKAQSHDCV-PVLSEHPL-YILYTSGTTGLPKGVI---RPTggyavMLHWSMSSIyglqPGEVWWAASDLGW-VVgh 347
Cdd:PRK07008 158 ETLVGAQDGDYDwPRFDENQAsSLCYTSGTTGNPKGALyshRST-----VLHAYGAAL----PDAMGLSARDAVLpVV-- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 348 syicygPLLHGNTTVL-YEGKPVGTP--------DAGAYFRVLAEHGVAalFTA--PTAIRAIRQQDPGAALgkqySLTR 416
Cdd:PRK07008 227 ------PMFHVNAWGLpYSAPLTGAKlvlpgpdlDGKSLYELIEAERVT--FSAgvPTVWLGLLNHMREAGL----RFST 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 417 FKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETgSPITASCVgLGNSKTPPPGQA--------GKSVPGYNVMILDD 488
Cdd:PRK07008 295 LRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEM-SPLGTLCK-LKWKHSQLPLDEqrkllekqGRVIYGVDMKIVGD 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 489 NMQKL--KARCLGNIVVKLPlppgafsglWKNQEAFKHlyfEKFP---GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGH 563
Cdd:PRK07008 373 DGRELpwDGKAFGDLQVRGP---------WVIDRYFRG---DASPlvdGWFPTGDVATIDADGFMQITDRSKDVIKSGGE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 564 RISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEeqvlEEIVKHVRqniGPVAAFR---NAVFVKQ 640
Cdd:PRK07008 441 WISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTR----EELLAFYE---GKVAKWWipdDVVFVDA 513
|
410
....*....|....
gi 32258701 641 LPKTRSGKIPRSAL 654
Cdd:PRK07008 514 IPHTATGKLQKLKL 527
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
250-654 |
1.07e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 72.12 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 250 KILIYNRPNMEAVPLAPGR---DLDWDEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSI 326
Cdd:PRK12467 3194 KLLLTQAHLLEQLPAPAGDtalTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCW-IAEA 3272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 327 YGLQPGEVWWAASDLGWVVGHSYIcYGPLLHGNTTVLYEGKpVGTPDagAYFRVLAEHGVAALFTAPTAIRAIrqqdpgA 406
Cdd:PRK12467 3273 YELDANDRVLLFMSFSFDGAQERF-LWTLICGGCLVVRDND-LWDPE--ELWQAIHAHRISIACFPPAYLQQF------A 3342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 407 ALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF-RVPVLDHWWQTETGSPITASCVGLGNSKTPPPGQAGKSVPGYNVMI 485
Cdd:PRK12467 3343 EDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLkPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYV 3422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 486 LDDNMQklkarclgnivvklPLPPGAFSGLWKNQEAFKHLYFEK------------FPG----YYDTMDAGYMDEEGYLY 549
Cdd:PRK12467 3423 LDGQLN--------------PVPVGVAGELYIGGVGLARGYHQRpsltaerfvadpFSGsggrLYRTGDLARYRADGVIE 3488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 550 VMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKeDPLKGHVPLALCVLrkdiNATEEQVLEEIVKHVRQNIGPV 629
Cdd:PRK12467 3489 YLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVP----ADPQGDWRETLRDHLAASLPDY 3563
|
410 420
....*....|....*....|....*
gi 32258701 630 AAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:PRK12467 3564 MVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
141-617 |
6.14e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 68.26 E-value: 6.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 141 ATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVvt 220
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 221 asfgiepgrrveyvplveealkIGqhkpdkiliynrpnmeaVPLApgrdldwDEEMAkaqshdcvpvlsehplyILYTSG 300
Cdd:cd05910 79 ----------------------IG-----------------IPKA-------DEPAA-----------------ILFTSG 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 301 TTGLPKGVIRPTGGYAVMLHwSMSSIYGLQPGEVWWAASDLgwvvghsYICYGPLLhGNTTVLYEGKPV--GTPDAGAYF 378
Cdd:cd05910 96 STGTPKGVVYRHGTFAAQID-ALRQLYGIRPGEVDLATFPL-------FALFGPAL-GLTSVIPDMDPTrpARADPQKLV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 379 RVLAEHGVAALFTAPTAIRAIRQQdpGAALGKQysLTRFKTLFVAGERCDVETLEWSKNVF--RVPVLDHWWQTETgSPI 456
Cdd:cd05910 167 GAIRQYGVSIVFGSPALLERVARY--CAQHGIT--LPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEA-LPV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 457 TA-SCVGLGNSKTPPPGQA-----GKSVPGYNVMILD---------DNMQKLKARCLGNIVVKLPL---------PPGAF 512
Cdd:cd05910 242 SSiGSRELLATTTAATSGGagtcvGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTvtptyvnrpVATAL 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 513 SGLWKNQEAFKHlyfekfpgyyDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPL 592
Cdd:cd05910 322 AKIDDNSEGFWH----------RMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPG 391
|
490 500
....*....|....*....|....*
gi 32258701 593 KGHvPLaLCVLRKDINATEEQVLEE 617
Cdd:cd05910 392 CQL-PV-LCVEPLPGTITPRARLEQ 414
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
119-660 |
1.08e-11 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 67.61 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 119 HIENGKGDKIAIIYdspvtnTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIG------A 192
Cdd:PRK04813 10 EFAQTQPDFPAYDY------LGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayipvD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 193 IHSlifggfASKELSSRIDHVKPKVVVTASfgiepgrrveyvPLVEEALKIGQHKPDKIliynrpnMEAvpLAPGRDLDW 272
Cdd:PRK04813 84 VSS------PAERIEMIIEVAKPSLIIATE------------ELPLEILGIPVITLDEL-------KDI--FATGNPYDF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 273 DEEMakaQSHDCVpvlsehplYILYTSGTTGLPKGV-IRptggYAVML---HWsMSSIYGLQPGEVWWAAS----DLGwv 344
Cdd:PRK04813 137 DHAV---KGDDNY--------YIIFTSGTTGKPKGVqIS----HDNLVsftNW-MLEDFALPEGPQFLNQApysfDLS-- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 345 VGHSYICygpLLHGNTTVLYEgKPVgTPDAGAYFRVLAEHGVAALFTAPTAIRaIRQQDPGAAlGKQY-SLTRFktLFvA 423
Cdd:PRK04813 199 VMDLYPT---LASGGTLVALP-KDM-TANFKQLFETLPQLPINVWVSTPSFAD-MCLLDPSFN-EEHLpNLTHF--LF-C 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 424 GERCDVETLEwsKNVFRVP---VLDHWWQTETGSPITASCVG---LGNSKTPPPGQAgKsvPGYNVMILDDNMQKLKARC 497
Cdd:PRK04813 269 GEELPHKTAK--KLLERFPsatIYNTYGPTEATVAVTSIEITdemLDQYKRLPIGYA-K--PDSPLLIIDEEGTKLPDGE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 498 LGNIVVKLP-LPPGAFSGLWKNQEAFKHlyFEKFPGYYdTMDAGYMDEeGYLYVMSRVDDVINVAGHRISAGAIEESILS 576
Cdd:PRK04813 344 QGEIVISGPsVSKGYLNNPEKTAEAFFT--FDGQPAYH-TGDAGYLED-GLLFYQGRIDFQIKLNGYRIELEEIEQNLRQ 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 577 HGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSA 656
Cdd:PRK04813 420 SSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIE 499
|
....
gi 32258701 657 IVNG 660
Cdd:PRK04813 500 EVNK 503
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
475-653 |
1.66e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 67.34 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 475 GKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLyfeKFPGYYDTMDAGYMdEEGYLYVMSRV 554
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVR---GPSLMSGYFRDEESQDVL---AADGWLDTGDLGYL-LDGYLYITGRA 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 555 DDVINVAGHRISAGAIEESILSHGTV--ADCAVVGKEDPlKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGpVAAF 632
Cdd:PRK09192 461 KDLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQE-NGEKIVLLVQCRISDEERRGQLIHALAALVRSEFG-VEAA 538
|
170 180
....*....|....*....|.
gi 32258701 633 RNAVFVKQLPKTRSGKIPRSA 653
Cdd:PRK09192 539 VELVPPHSLPRTSSGKLSRAK 559
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
270-654 |
1.83e-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: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 270 LDWDEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASdlgwvvgHSY 349
Cdd:cd17656 108 LEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQFAT-------CSF 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 350 -ICY----GPLLHGNTtvLYEGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdpgaalgKQYS---LTRFKTLF 421
Cdd:cd17656 181 dVCYqeifSTLLSGGT--LYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSE-------REFInrfPTCVKHII 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 422 VAGERCDVETLewSKNVFR---VPVLDHWWQTETgSPITASCVGLGNS--KTPPpgqAGKSVPGYNVMILDDNMQKLKAR 496
Cdd:cd17656 252 TAGEQLVITNE--FKEMLHehnVHLHNHYGPSET-HVVTTYTINPEAEipELPP---IGKPISNTWIYILDQEQQLQPQG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 497 CLGNIVVK-LPLPPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESIL 575
Cdd:cd17656 326 IVGELYISgASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLL 405
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32258701 576 SHGTVADCAVVGKEDPLKGHVPLALCVLRKDINatEEQVLEEIVKHVRQNIGPvAAFrnaVFVKQLPKTRSGKIPRSAL 654
Cdd:cd17656 406 NHPGVSEAVVLDKADDKGEKYLCAYFVMEQELN--ISQLREYLAKQLPEYMIP-SFF---VPLDQLPLTPNGKVDRKAL 478
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
144-668 |
3.25e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 66.36 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 144 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVT--- 220
Cdd:PLN02860 34 TGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTdet 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 221 -ASFGIEPG----RRVEYVPLVEEALKIGQHKPDKILIYNrPNMEAVPLAPGRDLDWDEEMAkaqshdcvpVLsehplyI 295
Cdd:PLN02860 114 cSSWYEELQndrlPSLMWQVFLESPSSSVFIFLNSFLTTE-MLKQRALGTTELDYAWAPDDA---------VL------I 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 296 LYTSGTTGLPKGVirpTGGYAVMLHWSMSSIYglqpgevwwaasdlgwVVGHS----YICYGPLLH------GNTTVLYE 365
Cdd:PLN02860 178 CFTSGTTGRPKGV---TISHSALIVQSLAKIA----------------IVGYGeddvYLHTAPLCHigglssALAMLMVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 366 GKPVGTP--DAGAYFRVLAEHGVAALFTAPTAIRAIRQqdPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVF-RVP 442
Cdd:PLN02860 239 ACHVLLPkfDAKAALQAIKQHNVTSMITVPAMMADLIS--LTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFpNAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 443 VLDHWWQTETGSPIT----------------ASCVGLGNSKTPPPGQA--GKSVPGYNVMILDDNMQKLkarclGNIVVK 504
Cdd:PLN02860 317 LFSAYGMTEACSSLTfmtlhdptlespkqtlQTVNQTKSSSVHQPQGVcvGKPAPHVELKIGLDESSRV-----GRILTR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 505 lplPPGAFSGLW-KNQEAFKHLYFEkfpGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADC 583
Cdd:PLN02860 392 ---GPHVMLGYWgQNSETASVLSND---GWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 584 AVVGKEDPLKGHVPLALCVLR---------KDINATEEQVLEEIVK-HVRQnigpvaafrnavfvkqlpKTRSG-KIPRs 652
Cdd:PLN02860 466 VVVGVPDSRLTEMVVACVRLRdgwiwsdneKENAKKNLTLSSETLRhHCRE------------------KNLSRfKIPK- 526
|
570
....*....|....*.
gi 32258701 653 alSAIVNGKPYKITST 668
Cdd:PLN02860 527 --LFVQWRKPFPLTTT 540
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
142-647 |
7.08e-11 |
|
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: 65.15 E-value: 7.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 142 TFTYKEVLEQVSKLAGVLVK-HGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIfggfaSKELSSRidhvkpkvvvt 220
Cdd:cd05937 5 TWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFI-----NYNLSGD----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 221 asfgiepgrrveyvPLVEeALKIGQhkpDKILIYNrpnmeavplapgrdldwdeemakaqshdcvpvlSEHPLYILYTSG 300
Cdd:cd05937 69 --------------PLIH-CLKLSG---SRFVIVD---------------------------------PDDPAILIYTSG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 301 TTGLPKGVIRPTGGYAVMLhWSMSSIYGLQPGEVWwaasdlgwvvghsYICYgPLLHGNTTVLyegkpvgtpdagAYFRV 380
Cdd:cd05937 98 TTGLPKAAAISWRRTLVTS-NLLSHDLNLKNGDRT-------------YTCM-PLYHGTAAFL------------GACNC 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 381 LAEHGVAAL---FTAPT------AIRAIRQQDPGAALgkQYSLT----------RFKTLFVAGERCDVetleWSK--NVF 439
Cdd:cd05937 151 LMSGGTLALsrkFSASQfwkdvrDSGATIIQYVGELC--RYLLStppspydrdhKVRVAWGNGLRPDI----WERfrERF 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 440 RVPVLDHWWQTETG---------SPITASCVG---------LGNSKTP----PPGQagksvpgynvMILDDNMQKLKARC 497
Cdd:cd05937 225 NVPEIGEFYAATEGvfaltnhnvGDFGAGAIGhhglirrwkFENQVVLvkmdPETD----------DPIRDPKTGFCVRA 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 498 L----GNIVVKLPLPP-GAFSGLWKNQEAFKHLY----FEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAG 568
Cdd:cd05937 295 PvgepGEMLGRVPFKNrEAFQGYLHNEDATESKLvrdvFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTT 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 569 AIEESILSHGTVADCAVVGKEDP-LKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNigpVAAFRNAVFVKQLPKTRSG 647
Cdd:cd05937 375 EVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEESSAVPTEFTKSLLASLARKN---LPSYAVPLFLRLTEEVATT 451
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
531-659 |
1.02e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 64.25 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 531 PGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINAt 610
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSIS- 401
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 32258701 611 eeqvLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVN 659
Cdd:PRK07445 402 ----LEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAV 446
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
475-658 |
7.96e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 61.94 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 475 GKSVPGYNVMILDDNMQKLKARCLGNIVVKLP-LPPG--AFSGLWKNQEAfkhlyfekfPGYYDTMDAGYMDEEGYLYVM 551
Cdd:PRK07768 363 GPPLPGLEVRVVDEDGQVLPPRGVGVIELRGEsVTPGylTMDGFIPAQDA---------DGWLDTGDLGYLTEEGEVVVC 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 552 SRVDDVINVAGHRISAGAIEESILS-HGTVADCAV-VGKEDPLK--GHVPLALCVLRKDInATEEQVLEEIVKHVRQNIG 627
Cdd:PRK07768 434 GRVKDVIIMAGRNIYPTDIERAAARvEGVRPGNAVaVRLDAGHSreGFAVAVESNAFEDP-AEVRRIRHQVAHEVVAEVG 512
|
170 180 190
....*....|....*....|....*....|...
gi 32258701 628 pvAAFRNAVFVK--QLPKTRSGKIPRSALSAIV 658
Cdd:PRK07768 513 --VRPRNVVVLGpgSIPKTPSGKLRRANAAELV 543
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
144-590 |
1.16e-09 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 61.08 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 144 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAihslifggfaskelssridhvkpkVVVTAsf 223
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNI------------------------PIVTV-- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 224 giepgrrveYVPLVEEALKIGQHKPDKILIYNRPNmeavplapgrdldwDEEMAkaqshdCvpvlsehplyILYTSGTTG 303
Cdd:cd17639 61 ---------YATLGEDALIHSLNETECSAIFTDGK--------------PDDLA------C----------IMYTSGSTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 304 LPKGVirptggyaVMLHWSM-SSIYGLqpgevwwaasdLGWVVGH-----SYICYGPLLH-----GNTTVLYEGKPVG-- 370
Cdd:cd17639 102 NPKGV--------MLTHGNLvAGIAGL-----------GDRVPELlgpddRYLAYLPLAHifelaAENVCLYRGGTIGyg 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 371 TP-------------DAGAyFR--VLAehGVAALF-TAPTAIRA-------IRQQ------------------------- 402
Cdd:cd17639 163 SPrtltdkskrgckgDLTE-FKptLMV--GVPAIWdTIRKGVLAklnpmggLKRTlfwtayqsklkalkegpgtplldel 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 403 ---DPGAALGkqyslTRFKTLFVAGERCDVETLEWSkNVFRVPVLDHWWQTET--GSPI------TASCVGLgnsktPPP 471
Cdd:cd17639 240 vfkKVRAALG-----GRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETcaGGTVqdpgdlETGRVGP-----PLP 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 472 GQAGK--SVPGYNVMILDDNMQklkarclGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLY 549
Cdd:cd17639 309 CCEIKlvDWEEGGYSTDKPPPR-------GEILIR---GPNVFKGYYKNPEKTKEAFDGD--GWFHTGDIGEFHPDGTLK 376
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 32258701 550 VMSRVDD-VINVAGHRISAGAIEESILSHGTVADCAVVGKED 590
Cdd:cd17639 377 IIDRKKDlVKLQNGEYIALEKLESIYRSNPLVNNICVYADPD 418
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
142-540 |
1.64e-09 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 60.91 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 142 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVI-------YMPMIPQAMYTMLACARIGAIHSLIFGGFAskELSSRIDHVK 214
Cdd:cd05921 25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLIlsgnsieHALMALAAMYAGVPAAPVSPAYSLMSQDLA--KLKHLFELLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 215 PKVVVtASFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRPNMEAVPlaPGRDLDwdeEMAKAQSHDCVPVLsehply 294
Cdd:cd05921 103 PGLVF-AQDAAPFARALAAIFPLGTPLVVSRNAVAGRGAISFAELAATP--PTAAVD---AAFAAVGPDTVAKF------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 295 iLYTSGTTGLPKGVI---RPTGGYAVMlhwsMSSIYGLQPGEVWWAASDLGWvvGHSY---ICYGPLLH-GNTTVLYEGK 367
Cdd:cd05921 171 -LFTSGSTGLPKAVIntqRMLCANQAM----LEQTYPFFGEEPPVLVDWLPW--NHTFggnHNFNLVLYnGGTLYIDDGK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 368 PvgTPDA-GAYFRVLAEHGVAALFTAPTA----IRAIRQQDpgaALGKQYsLTRFKTLFVAGERCDVETLEWSKNV---- 438
Cdd:cd05921 244 P--MPGGfEETLRNLREISPTVYFNVPAGwemlVAALEKDE---ALRRRF-FKRLKLMFYAGAGLSQDVWDRLQALavat 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 439 --FRVPVLDHWWQTETGsPITASCVGL----GNSKTPPPGQAGKSVPgynvmilddNMQKLKARCLGnivvklplpPGAF 512
Cdd:cd05921 318 vgERIPMMAGLGATETA-PTATFTHWPtersGLIGLPAPGTELKLVP---------SGGKYEVRVKG---------PNVT 378
|
410 420
....*....|....*....|....*...
gi 32258701 513 SGLWKNQEAFKHLYFEKfpGYYDTMDAG 540
Cdd:cd05921 379 PGYWRQPELTAQAFDEE--GFYCLGDAA 404
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
141-644 |
1.78e-09 |
|
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: 60.45 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 141 ATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVt 220
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 221 asfgiepgrrveyvplVEEAlkigqhkpdkiliynrpnmeavplapgrdldwdeemakaqshdcvpvlsehpLYIlYTSG 300
Cdd:cd05940 81 ----------------VDAA----------------------------------------------------LYI-YTSG 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 301 TTGLPKGvirptggyAVMLHwsmssiyglqpgEVWWAAsdlGWVVGHSyicygpLLHGNTTVLYEGKPVgtpdagaYfrv 380
Cdd:cd05940 92 TTGLPKA--------AIISH------------RRAWRG---GAFFAGS------GGALPSDVLYTCLPL-------Y--- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 381 laeHGVAALFTAPTAIRAirqqdpGA--ALGKQYSLTRF--------KTLFV-AGERC---------------------- 427
Cdd:cd05940 133 ---HSTALIVGWSACLAS------GAtlVIRKKFSASNFwddirkyqATIFQyIGELCryllnqppkpterkhkvrmifg 203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 428 -----DVetleWS--KNVFRVP-VLDHWWQTETGSpitascvGLGN--SKtppPGQAGKS------VPGYNVMILD-DNM 490
Cdd:cd05940 204 nglrpDI----WEefKERFGVPrIAEFYAATEGNS-------GFINffGK---PGAIGRNpsllrkVAPLALVKYDlESG 269
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 491 QKL---KARCL-------GNIVVKL-PLPPgaFSGLWKNQEAFKHLY---FEKFPGYYDTMDAGYMDEEGYLYVMSRVDD 556
Cdd:cd05940 270 EPIrdaEGRCIkvprgepGLLISRInPLEP--FDGYTDPAATEKKILrdvFKKGDAWFNTGDLMRLDGEGFWYFVDRLGD 347
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 557 VINVAGHRISAGAIEESILSHGTVADCAVVGKEDP-LKGHVPLALCVLRkdinATEEQVLEEIVKHVRQNIGPVAAFRNA 635
Cdd:cd05940 348 TFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQ----PNEEFDLSALAAHLEKNLPGYARPLFL 423
|
....*....
gi 32258701 636 VFVKQLPKT 644
Cdd:cd05940 424 RLQPEMEIT 432
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
142-658 |
6.62e-09 |
|
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: 58.71 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 142 TFTYKEvLEQVS-KLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGaihslifGGFASKELS---SRIDH----V 213
Cdd:cd05918 24 SLTYAE-LDRLSsRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAG-------GAFVPLDPShplQRLQEilqdT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 214 KPKVVVTasfgiepgrrveyvplveealkigqHKPDkiliynrpnmeavplapgrdldwdeemakaqshdcvpvlseHPL 293
Cdd:cd05918 96 GAKVVLT-------------------------SSPS-----------------------------------------DAA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 294 YILYTSGTTGLPKGVIRPTGGYAVMLHwSMSSIYGLQPGEVWWAASdlgwvvghSY---IC----YGPLLHGNTTVLyeg 366
Cdd:cd05918 110 YVIFTSGSTGKPKGVVIEHRALSTSAL-AHGRALGLTSESRVLQFA--------SYtfdVSileiFTTLAAGGCLCI--- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 367 kpvgTPDA---GAYFRVLAEHGVAALFTAPTAIRAIRQQDpgaalgkqysLTRFKTLFVAGE---RCDVETleWSKnvfR 440
Cdd:cd05918 178 ----PSEEdrlNDLAGFINRLRVTWAFLTPSVARLLDPED----------VPSLRTLVLGGEaltQSDVDT--WAD---R 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 441 VPVLDHWWQTETgspiTASCVGLGNSKTPPPGQAGKSVPGyNVMILD-DNMQKLkarclgnivvklpLPPGAFSGLW--- 516
Cdd:cd05918 239 VRLINAYGPAEC----TIAATVSPVVPSTDPRNIGRPLGA-TCWVVDpDNHDRL-------------VPIGAVGELLieg 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 517 ------------KNQEAF-KHLYFEKFPGY------YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSH 577
Cdd:cd05918 301 pilargylndpeKTAAAFiEDPAWLKQEGSgrgrrlYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQS 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 578 GTVAD--CAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFRNA--------------VFVKQL 641
Cdd:cd05918 381 LPGAKevVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKlrqrlpsymvpsvfLPLSHL 460
|
570
....*....|....*..
gi 32258701 642 PKTRSGKIPRSALSAIV 658
Cdd:cd05918 461 PLTASGKIDRRALRELA 477
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
290-656 |
1.55e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.26 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 290 EHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGEVWWAASDLGWVVGhSYICYGPLLHGNTTVLyeGKPV 369
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAERLQW-MQATYALDDSDVLMQKAPISFDVS-VWECFWPLITGCRLVL--AGPG 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 370 GTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQdPGAAlgkqySLTRFKTLFVAGERCDVEtlewsknvFRVPVLDHWWQ 449
Cdd:PRK05691 1349 EHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDE-PLAA-----ACTSLRRLFSGGEALPAE--------LRNRVLQRLPQ 1414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 450 tetgspitascVGLGNSKTPPpgQAGKSVPGYNVMIlDDNMQKLKARCLGNIVVKL------PLPPGAF-------SGLW 516
Cdd:PRK05691 1415 -----------VQLHNRYGPT--ETAINVTHWQCQA-EDGERSPIGRPLGNVLCRVldaelnLLPPGVAgelciggAGLA 1480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 517 KNQEAFKHLYFEKF-------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVG 587
Cdd:PRK05691 1481 RGYLGRPALTAERFvpdplgeDGarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLV 1560
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32258701 588 KEDpLKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFRnavfVKQLPKTRSGKIPRSALSA 656
Cdd:PRK05691 1561 REG-AAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIR----LDQMPLGPSGKLDRRALPE 1624
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
144-593 |
1.74e-08 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 57.61 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 144 TYKEVLEQVSKLAGVLVKHGIKKGDT--VVIYMPMIPQAMYTMLACARigaiHSLIfggfaskelssridhvkpkvvvta 221
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYA----YSLV------------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 222 sfgiepgrrveYVPLVEealKIGqhkPDKIL-IYNRPNMEAVPLAPGRDL-DWDE--EMAKAQSHDCVPVLSEHPLYILY 297
Cdd:cd05927 59 -----------TVPLYD---TLG---PEAIEyILNHAEISIVFCDAGVKVySLEEfeKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 298 TSGTTGLPKGVIrptggyavMLHWSMSSIYglqpgevwwAASDLGWVVGHS------YICYGPLLH-----GNTTVLYEG 366
Cdd:cd05927 122 TSGTTGNPKGVM--------LTHGNIVSNV---------AGVFKILEILNKinptdvYISYLPLAHifervVEALFLYHG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 367 KPVGtpdagaYF----RVLAEHgVAALftAPT--------------AIRAIRQQDPG-------AALG-KQYSLT----- 415
Cdd:cd05927 185 AKIG------FYsgdiRLLLDD-IKAL--KPTvfpgvprvlnriydKIFNKVQAKGPlkrklfnFALNyKLAELRsgvvr 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 416 -------------------RFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITASCVG---LGNSKTPPPGQ 473
Cdd:cd05927 256 aspfwdklvfnkikqalggNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGdtsVGHVGGPLPCA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 474 AGK--SVPGYNVMILDDNMQklkarclGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEGYLYVM 551
Cdd:cd05927 336 EVKlvDVPEMNYDAKDPNPR-------GEVCIR---GPNVFSGYYKDPEKTAEALDED--GWLHTGDIGEWLPNGTLKII 403
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 32258701 552 SRVDDVINVA-GHRISAGAIEESILSHGTVADCAVVGkeDPLK 593
Cdd:cd05927 404 DRKKNIFKLSqGEYVAPEKIENIYARSPFVAQIFVYG--DSLK 444
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
126-653 |
1.83e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.26 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDSPVTNTKATFTYKEVLEQVSKLAGVLVKHGiKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKE 205
Cdd:PRK05691 24 DRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 206 -----LSSRIDHVKPKVVVTASfgiepgrrveyvPLVEEALKIGQHKPDkiliyNRPNMEAV-PLAPGRDLDWDEEMAKA 279
Cdd:PRK05691 103 hhqerLLSIIADAEPRLLLTVA------------DLRDSLLQMEELAAA-----NAPELLCVdTLDPALAEAWQEPALQP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 280 qshdcvpvlsEHPLYILYTSGTTGLPKGViRPTGGYAVMLHWSMSSIYGLQPGE----VWWAA--SDLGWVVGhsyiCYG 353
Cdd:PRK05691 166 ----------DDIAFLQYTSGSTALPKGV-QVSHGNLVANEQLIRHGFGIDLNPddviVSWLPlyHDMGLIGG----LLQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 354 PLLHGNTTVL-----YEGKPV----------GTPDAGAYF-------RVlAEHGVAAL--------FTAPTAIRairqQD 403
Cdd:PRK05691 231 PIFSGVPCVLmspayFLERPLrwleaiseygGTISGGPDFayrlcseRV-SESALERLdlsrwrvaYSGSEPIR----QD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 404 PGAALGKQYSLTRFK-------------TLFVAGE---------RCDVETLewSKNVFrvpvldhwwQTETGSPITaSCv 461
Cdd:PRK05691 306 SLERFAEKFAACGFDpdsffasyglaeaTLFVSGGrrgqgipalELDAEAL--ARNRA---------EPGTGSVLM-SC- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 462 glgnsktpppgqaGKSVPGYNVMILDDN-MQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfPG--YYDTMD 538
Cdd:PRK05691 373 -------------GRSQPGHAVLIVDPQsLEVLGDNRVGEIWAS---GPSIAHGYWRNPEASAKTFVEH-DGrtWLRTGD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 539 AGYMdEEGYLYVMSRVDDVINVAGHRISAGAIEESI------LSHGTVADCAVvgKEDPLKGhVPLALCVLRKDINATEE 612
Cdd:PRK05691 436 LGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTVerevevVRKGRVAAFAV--NHQGEEG-IGIAAEISRSVQKILPP 511
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 32258701 613 QVLeeiVKHVRQNIGpvAAFRNAVFV------KQLPKTRSGKIPRSA 653
Cdd:PRK05691 512 QAL---IKSIRQAVA--EACQEAPSVvlllnpGALPKTSSGKLQRSA 553
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
136-654 |
3.57e-08 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 56.41 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 136 VTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFaskelssridhvkp 215
Cdd:cd17645 17 VVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY-------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 216 kvvvtasfgiePGRRVEYVPLVEEAlkigqhkpdKILIYNRPNMeavplapgrdldwdeemakaqshdcvpvlsehpLYI 295
Cdd:cd17645 83 -----------PGERIAYMLADSSA---------KILLTNPDDL---------------------------------AYV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 296 LYTSGTTGLPKGVIRPTGGYAVMLHWSMSSiYGLQPGEVWWAASDLG-----WVVgHSYICYGPLLHgnttVLYEGKPVG 370
Cdd:cd17645 110 IYTSGSTGLPKGVMIEHHNLVNLCEWHRPY-FGVTPADKSLVYASFSfdasaWEI-FPHLTAGAALH----VVPSERRLD 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 371 TPDAGAYFRvlaEHGVAALFTaPTairairqqdPGAALGKQYSLTRFKTLFVAGERCDVetleWSKNVFRVpvLDHWWQT 450
Cdd:cd17645 184 LDALNDYFN---QEGITISFL-PT---------GAAEQFMQLDNQSLRVLLTGGDKLKK----IERKGYKL--VNNYGPT 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 451 ETGSPITASCVGLGNSKTPppgqAGKSVPGYNVMILDDNMQKLKARCLGNIVVklplppgAFSGLWKNQEAFKHLYFEKF 530
Cdd:cd17645 245 ENTVVATSFEIDKPYANIP----IGKPIDNTRVYILDEALQLQPIGVAGELCI-------AGEGLARGYLNRPELTAEKF 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 531 ------PG--YYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDplKGHVPlALCV 602
Cdd:cd17645 314 ivhpfvPGerMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKED--ADGRK-YLVA 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 32258701 603 LrkdINATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSAL 654
Cdd:cd17645 391 Y---VTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
142-591 |
5.25e-08 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 55.89 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 142 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 221
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 222 sfgiepgrrveyvpLVEEALKIGQHKPdkiliynrpnmeavPLAPGRDLDwdeemakaqshdcvpvlseHPLYILYTSGT 301
Cdd:cd05939 83 --------------LLDPLLTQSSTEP--------------PSQDDVNFR-------------------DKLFYIYTSGT 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 302 TGLPKGvirptggyAVMLHWSMSSI-------YGLQPGEVWW--------AASDLGwvVGHSyicygpLLHGNTTVLYEg 366
Cdd:cd05939 116 TGLPKA--------AVIVHSRYYRIaagayyaFGMRPEDVVYdclplyhsAGGIMG--VGQA------LLHGSTVVIRK- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 367 kpvgTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGKQysltRFKTLFVAGERCDVetleWSKNV--FRVP-V 443
Cdd:cd05939 179 ----KFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKH----NVRLAVGNGLRPQI----WEQFVrrFGIPqI 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 444 LDHWWQTETGSPI-----TASCVGLgNSKTPPpgqagKSVPGYNVMILDDNMQKLKAR---CL-----------GNIVVK 504
Cdd:cd05939 247 GEFYGATEGNSSLvnidnHVGACGF-NSRILP-----SVYPIRLIKVDEDTGELIRDSdglCIpcqpgepgllvGKIIQN 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 505 LPLPpgAFSGLWKNQEAFKHLY---FEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIeESILSHGT-V 580
Cdd:cd05939 321 DPLR--RFDGYVNEGATNKKIArdvFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEV-EGILSNVLgL 397
|
490
....*....|.
gi 32258701 581 ADCAVVGKEDP 591
Cdd:cd05939 398 EDVVVYGVEVP 408
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
131-664 |
5.34e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 53.05 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 131 IYDSPVTNTkatFTYKEVLEQvSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLI-FGGFASKELSS- 208
Cdd:PRK06814 650 AVEDPVNGP---LTYRKLLTG-AFVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMInFSAGIANILSAc 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 209 RIDHVKpkVVVTASFGIEPGRrveYVPLVE-----------EALKIGQHKPDKILIYNRPNMEAVPLaPGRDldwdeema 277
Cdd:PRK06814 726 KAAQVK--TVLTSRAFIEKAR---LGPLIEalefgiriiylEDVRAQIGLADKIKGLLAGRFPLVYF-CNRD-------- 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 278 kaqshdcvpvlSEHPLYILYTSGTTGLPKGVirptggyaVMLHWSM-SSIYGLQpGEVWWAASDLgwV-----VGHSYIC 351
Cdd:PRK06814 792 -----------PDDPAVILFTSGSEGTPKGV--------VLSHRNLlANRAQVA-ARIDFSPEDK--VfnalpVFHSFGL 849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 352 YG----PLLHGNTTVLYegkpvgtPDAGAYfRVLAE--HGVAA--LFTAPTAIRA-IRQQDPgaalgkqYSLTRFKTLFV 422
Cdd:PRK06814 850 TGglvlPLLSGVKVFLY-------PSPLHY-RIIPEliYDTNAtiLFGTDTFLNGyARYAHP-------YDFRSLRYVFA 914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 423 AGERCDVETLEWSKNVFRVPVLDHWWQTETgSPITAScvglgnsKTP---PPGQAGKSVPGynvmilddnmqklkarclg 499
Cdd:PRK06814 915 GAEKVKEETRQTWMEKFGIRILEGYGVTET-APVIAL-------NTPmhnKAGTVGRLLPG------------------- 967
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 500 nIVVKL-PLP------------PGAFSGLWKnqeAFKHLYFEKFP-GYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRI 565
Cdd:PRK06814 968 -IEYRLePVPgideggrlfvrgPNVMLGYLR---AENPGVLEPPAdGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMI 1043
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 566 SAGAIEESILSHGTVADCAVVGKEDPLKGHvPLALCVLRKDINAteeqvlEEIVKHVRQN-IGPVAAFRNAVFVKQLPKT 644
Cdd:PRK06814 1044 SLAAVEELAAELWPDALHAAVSIPDARKGE-RIILLTTASDATR------AAFLAHAKAAgASELMVPAEIITIDEIPLL 1116
|
570 580
....*....|....*....|
gi 32258701 645 RSGKIPRSALSAIVNGKPYK 664
Cdd:PRK06814 1117 GTGKIDYVAVTKLAEEAAAK 1136
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
531-648 |
1.37e-06 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 51.63 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 531 PGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHvplALCVLRKDINAT 610
Cdd:PRK08043 590 RGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGE---ALVLFTTDSELT 666
|
90 100 110
....*....|....*....|....*....|....*....
gi 32258701 611 EEQVLeeivKHVRQNIGP-VAAFRNAVFVKQLPKTRSGK 648
Cdd:PRK08043 667 REKLQ----QYAREHGVPeLAVPRDIRYLKQLPLLGSGK 701
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
141-309 |
1.70e-06 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 51.30 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 141 ATFTYKEVLEQVSKLAGVL-VKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVv 219
Cdd:cd17632 66 ETITYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLL- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 220 TASfgiepgrrVEYVPLVEEALKIGQhKPDKILIYN-RPNMEA---------VPLAP-GR-----DLDWDEEMAKAQSHD 283
Cdd:cd17632 145 AVS--------AEHLDLAVEAVLEGG-TPPRLVVFDhRPEVDAhraalesarERLAAvGIpvttlTLIAVRGRDLPPAPL 215
|
170 180
....*....|....*....|....*..
gi 32258701 284 CVPVLSEHPLYIL-YTSGTTGLPKGVI 309
Cdd:cd17632 216 FRPEPDDDPLALLiYTSGSTGTPKGAM 242
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
144-545 |
2.90e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 50.43 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 144 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAI-------HSLIFGGFAskELSSRIDHVKPK 216
Cdd:PRK12582 82 TYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPaapvspaYSLMSHDHA--KLKHLFDLVKPR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 217 VVVtasfgiepgrrVEYVPLVEEALKI-GQHKPDKILIYNRPNMEA-VPLA------PGRDLdwdEEMAKAQSHDCVPvl 288
Cdd:PRK12582 160 VVF-----------AQSGAPFARALAAlDLLDVTVVHVTGPGEGIAsIAFAdlaatpPTAAV---AAAIAAITPDTVA-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 289 sehplYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVwwaASDLGWVVGH----SYICYGPLLHGNTTvLY 364
Cdd:PRK12582 224 -----KYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPP---PVSLDWMPWNhtmgGNANFNGLLWGGGT-LY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 365 --EGKPVgtpdAGAY---FRVLAEHGVAALFTAPTAIRAI---RQQDP----------------GAALgKQYSLTRFKTL 420
Cdd:PRK12582 295 idDGKPL----PGMFeetIRNLREISPTVYGNVPAGYAMLaeaMEKDDalrrsffknlrlmaygGATL-SDDLYERMQAL 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 421 FVAgercdvETLEwsknvfRVPVLDHWWQTETgSPITASC---------VGLgnsktPPPGQAGKSVPgynvmilddNMQ 491
Cdd:PRK12582 370 AVR------TTGH------RIPFYTGYGATET-APTTTGThwdtervglIGL-----PLPGVELKLAP---------VGD 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 32258701 492 KLKARCLGNIVVKlplppgafsGLWKNQEAFKHLYFEKfpGYYDTMDAG-YMDEE 545
Cdd:PRK12582 423 KYEVRVKGPNVTP---------GYHKDPELTAAAFDEE--GFYRLGDAArFVDPD 466
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
144-370 |
2.81e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 47.42 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 144 TYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACAR-------IGA-------IHSLifggfASKELSSR 209
Cdd:PLN02387 108 TYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRqnitvvtIYAslgeealCHSL-----NETEVTTV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 210 I-DHVKPKVVVTASFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRPNMEAVplapGRDLDWDEEMAKAQShdcVPVl 288
Cdd:PLN02387 183 IcDSKQLKKLIDISSQLETVKRVIYMDDEGVDSDSSLSGSSNWTVSSFSEVEKL----GKENPVDPDLPSPND---IAV- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 289 sehplyILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVwwaasdlgwvvghsYICYGPLLH-----GNTTVL 363
Cdd:PLN02387 255 ------IMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDV--------------YLAYLPLAHilelaAESVMA 314
|
....*..
gi 32258701 364 YEGKPVG 370
Cdd:PLN02387 315 AVGAAIG 321
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
126-333 |
3.45e-05 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 47.13 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 126 DKIAIIYDSPVTNTKA-TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLifggfask 204
Cdd:cd17647 3 ERTCVVETPSLNSSKTrSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSV-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 205 elssrIDHVKPkvvvtasfgiePGRRVEYvplveealkIGQHKPdKILIynrpNMEAVPLAPGRdldwdeemakaqshDC 284
Cdd:cd17647 75 -----IDPAYP-----------PARQNIY---------LGVAKP-RGLI----VIRAAGVVVGP--------------DS 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 32258701 285 VPVLSehplyilYTSGTTGLPKGVIRPTGGYAVMLHWsMSSIYGLQPGE 333
Cdd:cd17647 111 NPTLS-------FTSGSEGIPKGVLGRHFSLAYYFPW-MAKRFNLSEND 151
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
534-657 |
8.75e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.31 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 534 YDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHvpLALCVLRKDINATEEQ 613
Cdd:PRK05691 4104 YRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKH--LVGYLVPHQTVLAQGA 4181
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 32258701 614 VLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAI 657
Cdd:PRK05691 4182 LLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPAL 4225
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
475-655 |
2.49e-04 |
|
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: 44.02 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 475 GKSVPGYNVMILDDNMQKLKARCLGNIVVKlplPPGAFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMdEEGYLYVMSRV 554
Cdd:cd05908 317 GKPIDETDIRICDEDNKILPDGYIGHIQIR---GKNVTPGYYNNPEATAKVFTDD--GWLKTGDLGFI-RNGRLVITGRE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 555 DDVI-----NVAGHRISAGAIEESILSHGTVADCAVVGKEDplKGHVPLALCVLRKDINATEEQVlEEIVKHVRQNIGpv 629
Cdd:cd05908 391 KDIIfvngqNVYPHDIERIAEELEGVELGRVVACGVNNSNT--RNEEIFCFIEHRKSEDDFYPLG-KKIKKHLNKRGG-- 465
|
170 180
....*....|....*....|....*.
gi 32258701 630 AAFRNAVFVKQLPKTRSGKIPRSALS 655
Cdd:cd05908 466 WQINEVLPIRRIPKTTSGKVKRYELA 491
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
142-357 |
2.98e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 44.20 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 142 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTA 221
Cdd:PTZ00216 121 YITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 222 sfgiepGRRV-EYVPLVEEALKigqhkPDKILIYNRPNMEAVPLAPGRDLDWDEEMAKAQShdcvpVLSEHPL------- 293
Cdd:PTZ00216 201 ------GKNVpNLLRLMKSGGM-----PNTTIIYLDSLPASVDTEGCRLVAWTDVVAKGHS-----AGSHHPLnipennd 264
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32258701 294 ---YILYTSGTTGLPKGVIRPTG----GYAVMLHWSMSSIYGLQPGEVwwaasdlgwvvghsYICYGPLLH 357
Cdd:PTZ00216 265 dlaLIMYTSGTTGDPKGVMHTHGsltaGILALEDRLNDLIGPPEEDET--------------YCSYLPLAH 321
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
142-574 |
4.43e-03 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 40.03 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 142 TFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYtmlacARIGAIHSlifGGFASKELSSR--------IDHV 213
Cdd:cd05933 8 TLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFI-----AAVGAIFA---GGIAVGIYTTNspeacqyvAETS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 214 KPKVVVtasfgIEPGRRVEYVPLVEEALKigqhKPDKILIYNRPNMEAVP--------LAPGRDLDWDEEMAKAQSHD-- 283
Cdd:cd05933 80 EANILV-----VENQKQLQKILQIQDKLP----HLKAIIQYKEPLKEKEPnlyswdefMELGRSIPDEQLDAIISSQKpn 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 284 --CVpvlsehplyILYTSGTTGLPKGV------IRPTGGYAVMlhwSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPL 355
Cdd:cd05933 151 qcCT---------LIYTSGTTGMPKGVmlshdnITWTAKAASQ---HMDLRPATVGQESVVSYLPLSHIAAQILDIWLPI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 356 LHGNTT--------------VLYEGKP---VGTP---------------DAGAYFRVLAEHGVAALFTAPTAIRAIRQQD 403
Cdd:cd05933 219 KVGGQVyfaqpdalkgtlvkTLREVRPtafMGVPrvwekiqekmkavgaKSGTLKRKIASWAKGVGLETNLKLMGGESPS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 404 PG--------------AALGkqysLTRFKTLFVAGERCDVETLEW--SKNVfrvPVLDHWWQTETGSPITAScvGLGNSK 467
Cdd:cd05933 299 PLfyrlakklvfkkvrKALG----LDRCQKFFTGAAPISRETLEFflSLNI---PIMELYGMSETSGPHTIS--NPQAYR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32258701 468 TpppGQAGKSVPGYNVMILDDNMQKLKARCL-GNIVvklplppgaFSGLWKNQEAFKHLYFEKfpGYYDTMDAGYMDEEG 546
Cdd:cd05933 370 L---LSCGKALPGCKTKIHNPDADGIGEICFwGRHV---------FMGYLNMEDKTEEAIDED--GWLHSGDLGKLDEDG 435
|
490 500
....*....|....*....|....*....
gi 32258701 547 YLYVMSRVDDVINVA-GHRISAGAIEESI 574
Cdd:cd05933 436 FLYITGRIKELIITAgGENVPPVPIEDAV 464
|
|
| |
