|
Name |
Accession |
Description |
Interval |
E-value |
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
4-642 |
0e+00 |
|
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.
Pssm-ID: 173839 [Multi-domain] Cd Length: 610 Bit Score: 867.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 4 PLIDKYRKMATFDWKKLKAAVEG-EEHVRLKSEVVAKMKSEPVFHR--DYRVLSREEQREVVHQRWKKIVEWGLFKDPyS 80
Cdd:cd01150 1 PDLDKERASATFDWKALTHILEGgEENLRRKREVERELESDPLFQRelPSKHLSREELYEELKRKAKTDVERMGELMA-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 81 DLENFHALTETLEAYDQGTSARLFLHGNVFGAAVKSMGTDRHKDLIQKTENN-EIVGAFCLTEVGHGSNTAEIQTTATFD 159
Cdd:cd01150 80 DPEKMLALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNlEIIGCFAQTELGHGSNLQGLETTATYD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 160 --NGELVFNTPSVSAIKCWAGNLAHSATHVVVYAQLHVEGKNEGFHGFVIQVRCPRTFQTLPGITIGDMGSKPGcWQGVE 237
Cdd:cd01150 160 plTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPGKNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMG-LNGVD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 238 NGWMEFKNHRAPLSALLNKGCDITPDGKYVTSFKSASEKQSVSLGTLSVGRLGIIAKGMMACTFASTIAIRYSVARRQFG 317
Cdd:cd01150 239 NGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 318 PvKGAENEIPVLEYPLQQYRLFPYLSAAICIRIFQKKFVGHFTEYMMRVIMGeksdeLSEFSKEVHALSSGAKPVATWLG 397
Cdd:cd01150 319 P-KPSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQG-----NSELLAELHALSAGLKAVATWTA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 398 VESLGEARKACGGHGYLQMSRLNTLRDDNDPSQTFEGENFMILQQTSNILLGKAQSIGSietpmstmsflnqkpskfssw 477
Cdd:cd01150 393 AQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAFS--------------------- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 478 ssnpVNDVLSAYRYLTYHLLQTTSAEAYRLKASGKNSFEVRNEIQiHRAVNLSVAYTEHTMIHWVQQFLKEIEDQSVKPV 557
Cdd:cd01150 452 ----LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQ-VHLRCAAKAHTEYTVLQRFHESVEEIVDPSVRAV 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 558 LQKVLNLFSLFLLERHLATLYItGYASGGKFGEDLREKLRLAVAELKPEAIALVDSIAPDDFILHSALGASDGKAYEHIM 637
Cdd:cd01150 527 LKRLCDLYALWLLEEHIADFLE-GGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSPIGRYDGDVYENLF 605
|
....*
gi 17540842 638 EEFRK 642
Cdd:cd01150 606 EEARK 610
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
10-639 |
2.95e-98 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 315.62 E-value: 2.95e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 10 RKMATFDWKKLKAAVEGEEHVRLKSEVVAKM-KSEPVFHRDYRV-LSREEQ-----REVVHQrWKKIVEWGLFKDPYSDL 82
Cdd:PLN02443 11 RNKAQFDVDAMKIVWAGSRHAFEVSDRMARLvASDPVFSKDNRTrLSRKELfkntlRKAAHA-WKRIIELRLTEEEAGKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 83 ENFhaltetleaYDQgtSARLFLHGNVFGAAVKSMGTD-RHKDLIQKTENNEIVGAFCLTEVGHGSNTAEIQTTATFD-- 159
Cdd:PLN02443 90 RSF---------VDE--PGYTDLHWGMFVPAIKGQGTEeQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDpk 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 160 NGELVFNTPSVSAIKCWAGNLAHSATHVVVYAQLHVEGKNEGFHGFVIQVRCPRTFQTLPGITIGDMGSK--PGCWQGVE 237
Cdd:PLN02443 159 TDEFVIHSPTLTSSKWWPGGLGKVSTHAVVYARLITNGKDHGIHGFIVQLRSLDDHSPLPGVTVGDIGMKfgNGAYNTMD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 238 NGWMEFKNHRAPLSALLNKGCDITPDGKYVTSFKSaseKQSVsLGTLSVGRLGIIAKGMMACTFASTIAIRYSVARRQFG 317
Cdd:PLN02443 239 NGFLRFDHVRIPRDQMLMRLSKVTREGKYVQSDVP---RQLV-YGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 318 PvKGAENEIPVLEYPLQQYRLFPYLSAAICIRifqkkFVGHFTEYMMRVIMgeKSDELSEFS--KEVHALSSGAKPVATW 395
Cdd:PLN02443 315 S-QDGGPETQVIDYKTQQSRLFPLLASAYAFR-----FVGEWLKWLYTDVT--QRLEANDFStlPEAHACTAGLKSLTTS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 396 LGVESLGEARKACGGHGYLQMSRLNTLRDDNDPSQTFEGENFMILQQTSNILLGKAQSIGSIETPMSTMSFLNQKPSKFS 475
Cdd:PLN02443 387 ATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACTYEGDNVVLLLQVARFLMKTVSQLGSGKKPVGTTAYMGRVQHLLQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 476 SWSsnpvnDVLSAYRYL-TYHLLQTTSAEAYRL---KASGKNSFEVRNEIQIHRAVNLSVAYTEHTMIHWVQQFL----K 547
Cdd:PLN02443 467 CRC-----GVQTAEDWLnPSVVLEAFEARAARMavtCAQNLSKFENQEAGFQELSADLVEAAVAHCQLIVVSKFIeklqQ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 548 EIEDQSVKPVLQKVLNLFSLFLLERHLATLYITGYASgGKFGEDLREKLRLAVAELKPEAIALVDSIAPDDFILHSALGA 627
Cdd:PLN02443 542 DIPGKGVKKQLQNLCYIYALYLLHKHLGDFLSTGCIT-PKQASLANDQLRSLYSQVRPNAVALVDAFNYTDHYLGSVLGR 620
|
650
....*....|..
gi 17540842 628 SDGKAYEHIMEE 639
Cdd:PLN02443 621 YDGNVYPKLYEE 632
|
|
| ACOX |
pfam01756 |
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ... |
483-650 |
7.36e-46 |
|
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts acyl-CoA into trans-2- enoyl-CoA.
Pssm-ID: 460314 [Multi-domain] Cd Length: 180 Bit Score: 160.79 E-value: 7.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 483 NDVLSAYRYLTYHLLQTTSAEAYRLKASGKNSFEVRNEIQIHRaVNLSVAYTEHTMIHWVQQFLKEIEDQSVKPVLQKVL 562
Cdd:pfam01756 3 EVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNNQSVEL-VRAAKAHAEYFVLRTFVERLSTSLDPPLKPVLKKLC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 563 NLFSLFLLERHLATLYITGYASGgKFGEDLREKLRLAVAELKPEAIALVDSIAPDDFILHSALGASDGKAYEHIMEEFRK 642
Cdd:pfam01756 82 KLYALWTIEKHLGDFLQGGYLSP-EQIDLIREAILELLAELRPNAVALVDAFDFPDFILNSALGRYDGNVYENLFEWAKK 160
|
....*...
gi 17540842 643 YTNEQPRW 650
Cdd:pfam01756 161 NPLNTEVP 168
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
51-451 |
2.37e-33 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 131.89 E-value: 2.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 51 RVLSREEQREVVHQRWKKIVEWGLFKDPYS--------DLENFHALTETLEAYDQGTSARLFLHgNVFGAAVKSMGTDRH 122
Cdd:COG1960 27 EAREWDREGEFPRELWRKLAELGLLGLTIPeeygglglSLVELALVLEELARADASLALPVGVH-NGAAEALLRFGTEEQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 123 KD-LIQKTENNEIVGAFCLTEVGHGSNTAEIQTTATFDNGELVFN-TpsvsaiKCWAGNlAHSATHVVVYAQLHVEGKNE 200
Cdd:COG1960 106 KErYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNgQ------KTFITN-APVADVILVLARTDPAAGHR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 201 GFHGFVIqvrcPRtfqTLPGITIGDMGSKPGcWQGVENGWMEFKNHRAPLSALL---NKGcditpdgkyvtsFKSAsekq 277
Cdd:COG1960 179 GISLFLV----PK---DTPGVTVGRIEDKMG-LRGSDTGELFFDDVRVPAENLLgeeGKG------------FKIA---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 278 svsLGTLSVGRLGIIAKGMMACTFASTIAIRYSVARRQFGPvkgaeneiPVLEYPLQQYRLfpylsAAICIRIfqkkfvg 357
Cdd:COG1960 235 ---MSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGR--------PIADFQAVQHRL-----ADMAAEL------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 358 hfteYMMRVIM---GEKSDElsefSKEVHALSSGAKPVATWLGVESLGEARKACGGHGYLQ---MSRLntLRdDNDPSQT 431
Cdd:COG1960 292 ----EAARALVyraAWLLDA----GEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTReypLERL--YR-DARILTI 360
|
410 420
....*....|....*....|
gi 17540842 432 FEGENFMILQQTSNILLGKA 451
Cdd:COG1960 361 YEGTNEIQRLIIARRLLGRP 380
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
4-642 |
0e+00 |
|
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.
Pssm-ID: 173839 [Multi-domain] Cd Length: 610 Bit Score: 867.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 4 PLIDKYRKMATFDWKKLKAAVEG-EEHVRLKSEVVAKMKSEPVFHR--DYRVLSREEQREVVHQRWKKIVEWGLFKDPyS 80
Cdd:cd01150 1 PDLDKERASATFDWKALTHILEGgEENLRRKREVERELESDPLFQRelPSKHLSREELYEELKRKAKTDVERMGELMA-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 81 DLENFHALTETLEAYDQGTSARLFLHGNVFGAAVKSMGTDRHKDLIQKTENN-EIVGAFCLTEVGHGSNTAEIQTTATFD 159
Cdd:cd01150 80 DPEKMLALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNlEIIGCFAQTELGHGSNLQGLETTATYD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 160 --NGELVFNTPSVSAIKCWAGNLAHSATHVVVYAQLHVEGKNEGFHGFVIQVRCPRTFQTLPGITIGDMGSKPGcWQGVE 237
Cdd:cd01150 160 plTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPGKNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMG-LNGVD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 238 NGWMEFKNHRAPLSALLNKGCDITPDGKYVTSFKSASEKQSVSLGTLSVGRLGIIAKGMMACTFASTIAIRYSVARRQFG 317
Cdd:cd01150 239 NGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 318 PvKGAENEIPVLEYPLQQYRLFPYLSAAICIRIFQKKFVGHFTEYMMRVIMGeksdeLSEFSKEVHALSSGAKPVATWLG 397
Cdd:cd01150 319 P-KPSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQG-----NSELLAELHALSAGLKAVATWTA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 398 VESLGEARKACGGHGYLQMSRLNTLRDDNDPSQTFEGENFMILQQTSNILLGKAQSIGSietpmstmsflnqkpskfssw 477
Cdd:cd01150 393 AQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAFS--------------------- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 478 ssnpVNDVLSAYRYLTYHLLQTTSAEAYRLKASGKNSFEVRNEIQiHRAVNLSVAYTEHTMIHWVQQFLKEIEDQSVKPV 557
Cdd:cd01150 452 ----LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQ-VHLRCAAKAHTEYTVLQRFHESVEEIVDPSVRAV 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 558 LQKVLNLFSLFLLERHLATLYItGYASGGKFGEDLREKLRLAVAELKPEAIALVDSIAPDDFILHSALGASDGKAYEHIM 637
Cdd:cd01150 527 LKRLCDLYALWLLEEHIADFLE-GGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSPIGRYDGDVYENLF 605
|
....*
gi 17540842 638 EEFRK 642
Cdd:cd01150 606 EEARK 610
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
10-639 |
2.95e-98 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 315.62 E-value: 2.95e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 10 RKMATFDWKKLKAAVEGEEHVRLKSEVVAKM-KSEPVFHRDYRV-LSREEQ-----REVVHQrWKKIVEWGLFKDPYSDL 82
Cdd:PLN02443 11 RNKAQFDVDAMKIVWAGSRHAFEVSDRMARLvASDPVFSKDNRTrLSRKELfkntlRKAAHA-WKRIIELRLTEEEAGKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 83 ENFhaltetleaYDQgtSARLFLHGNVFGAAVKSMGTD-RHKDLIQKTENNEIVGAFCLTEVGHGSNTAEIQTTATFD-- 159
Cdd:PLN02443 90 RSF---------VDE--PGYTDLHWGMFVPAIKGQGTEeQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDpk 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 160 NGELVFNTPSVSAIKCWAGNLAHSATHVVVYAQLHVEGKNEGFHGFVIQVRCPRTFQTLPGITIGDMGSK--PGCWQGVE 237
Cdd:PLN02443 159 TDEFVIHSPTLTSSKWWPGGLGKVSTHAVVYARLITNGKDHGIHGFIVQLRSLDDHSPLPGVTVGDIGMKfgNGAYNTMD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 238 NGWMEFKNHRAPLSALLNKGCDITPDGKYVTSFKSaseKQSVsLGTLSVGRLGIIAKGMMACTFASTIAIRYSVARRQFG 317
Cdd:PLN02443 239 NGFLRFDHVRIPRDQMLMRLSKVTREGKYVQSDVP---RQLV-YGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 318 PvKGAENEIPVLEYPLQQYRLFPYLSAAICIRifqkkFVGHFTEYMMRVIMgeKSDELSEFS--KEVHALSSGAKPVATW 395
Cdd:PLN02443 315 S-QDGGPETQVIDYKTQQSRLFPLLASAYAFR-----FVGEWLKWLYTDVT--QRLEANDFStlPEAHACTAGLKSLTTS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 396 LGVESLGEARKACGGHGYLQMSRLNTLRDDNDPSQTFEGENFMILQQTSNILLGKAQSIGSIETPMSTMSFLNQKPSKFS 475
Cdd:PLN02443 387 ATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACTYEGDNVVLLLQVARFLMKTVSQLGSGKKPVGTTAYMGRVQHLLQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 476 SWSsnpvnDVLSAYRYL-TYHLLQTTSAEAYRL---KASGKNSFEVRNEIQIHRAVNLSVAYTEHTMIHWVQQFL----K 547
Cdd:PLN02443 467 CRC-----GVQTAEDWLnPSVVLEAFEARAARMavtCAQNLSKFENQEAGFQELSADLVEAAVAHCQLIVVSKFIeklqQ 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 548 EIEDQSVKPVLQKVLNLFSLFLLERHLATLYITGYASgGKFGEDLREKLRLAVAELKPEAIALVDSIAPDDFILHSALGA 627
Cdd:PLN02443 542 DIPGKGVKKQLQNLCYIYALYLLHKHLGDFLSTGCIT-PKQASLANDQLRSLYSQVRPNAVALVDAFNYTDHYLGSVLGR 620
|
650
....*....|..
gi 17540842 628 SDGKAYEHIMEE 639
Cdd:PLN02443 621 YDGNVYPKLYEE 632
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
15-620 |
7.33e-91 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 296.68 E-value: 7.33e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 15 FDWKKLKAAVEGEeHVRLKSEVVAKMKSEPVFHR-----------DYRvLSREEQREVVHQRWKKIVEWGLFKD------ 77
Cdd:PLN02312 51 FDVKEMRKLLDGH-NLEDRDWLFGLMMQSDLFNSkrrggrvfvspDYN-QTMEQQREITMKRILYLLERGVFRGwltetg 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 78 PYSDLENFhALTETLEAYDQGTSARLFLHGNVFGAAVKSMGTDRHKD-LIQKTENNEIVGAFCLTEVGHGSNTAEIQTTA 156
Cdd:PLN02312 129 PEAELRKL-ALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDkWLKDTEDYVVKGCFAMTELGHGSNVRGIETVT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 157 TFD--NGELVFNTPSVSAIKCWAGNLAHSATHVVVYAQLHVEGKNEGFHGFVIQVRCPRTfQTLPGITIGDMGSKPGCwQ 234
Cdd:PLN02312 208 TYDpkTEEFVINTPCESAQKYWIGGAANHATHTIVFSQLHINGKNEGVHAFIAQIRDQDG-NICPNIRIADCGHKIGL-N 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 235 GVENGWMEFKNHRAPLSALLNKGCDITPDGKYVTSFKSASEKQSVSLGTLSVGRLGIIAKGMMACTFASTIAIRYSVARR 314
Cdd:PLN02312 286 GVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRR 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 315 QFGpVKGAENEIPVLEYPLQQYRLFPYLSaaiciRIFQKKFVGHFTEYMMrvimgekSDELSEFSKEVHALSSGAKPVAT 394
Cdd:PLN02312 366 AFS-VTPNGPEVLLLDYPSHQRRLLPLLA-----KTYAMSFAANDLKMIY-------VKRTPESNKAIHVVSSGFKAVLT 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 395 WLGVESLGEARKACGGHGYLQMSRLNTLRDDNDPSQTFEGENFMILQQTSNILLGKAQSIGSIETPMSTMSF--LNQK-- 470
Cdd:PLN02312 433 WHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAEYVSAKKRNKPFKGLGLehMNGPrp 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 471 --PSKFSSWSSNPVNDVLSAYRYLTYHLLQTTSAEAYRLKASGKN-SFEVRNEIQIhrAVNLSVAYTEHTMIHWVQQFLK 547
Cdd:PLN02312 513 viPTQLTSSTLRDSQFQLNLFCLRERDLLERFASEVSELQSKGESrEFAFLLSYQL--AEDLGRAFSERAILQTFLDAEA 590
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17540842 548 EIEDQSVKPVLQKVLNLFSLFLLERHLATL-YitGYASGGKFGEDLREKLRLAvAELKPEAIALVDSIA-PDDFI 620
Cdd:PLN02312 591 NLPTGSLKDVLGLLRSLYVLISLDEDPSFLrY--GYLSPDNVALVRKEVAKLC-GELRPHALALVSSFGiPDAFL 662
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
53-635 |
1.42e-82 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 274.81 E-value: 1.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 53 LSREEQREVVHQRWKKIV-EWGL--FKDPYSDLENFHALTETLEAYDQGTSARLFLHGNVFGAAVKSMGTDRHKD-LIQK 128
Cdd:PLN02636 88 ISKDEHRELCMRQLTGLVrEAGIrpMKYLVEDPAKYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDkYFDG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 129 TENNEIVGAFCLTEVGHGSNTAEIQTTATFD--NGELVFNTPSVSAIKCWAGNLAHSATHVVVYAQLHVEG------KNE 200
Cdd:PLN02636 168 IDNLDYPGCFAMTELHHGSNVQGLQTTATFDplTDEFVINTPNDGAIKWWIGNAAVHGKFATVFARLKLPThdskgvSDM 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 201 GFHGFVIQVRCPRTFQTLPGITIGDMGSKPGCwQGVENGWMEFKNHRAPLSALLNKGCDITPDGKYVTSFKSASEKQSVS 280
Cdd:PLN02636 248 GVHAFIVPIRDMKTHQVLPGVEIRDCGHKVGL-NGVDNGALRFRSVRIPRDNLLNRFGDVSRDGKYTSSLPTINKRFAAT 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 281 LGTLSVGRLGIIAKGMMACTFASTIAIRYSVARRQFGPVKgaENEIPVLEYPLQQYRLFPYLSAAicirifqkkFVGHF- 359
Cdd:PLN02636 327 LGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPK--QPEISILDYQSQQHKLMPMLAST---------YAFHFa 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 360 TEYMMRVIMGEKSDELSEFSKEVHALSSGAKPVATWLGVESLGEARKACGGHGYLQMSRLNTLRDDNDPSQTFEGENFMI 439
Cdd:PLN02636 396 TEYLVERYSEMKKTHDDQLVADVHALSAGLKAYITSYTAKALSTCREACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVL 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 440 LQQTSNILLGKAQSIGSIETPMSTMSFLNQKPSKFSSwSSNPV-------------NDVLSAYRYLTYHLLQTTsaeAYR 506
Cdd:PLN02636 476 LQQVAADLLKQYKEKFQGGTLSVTWNYLRESMNTYLS-QPNPVttrwegeehlrdpKFQLDAFRYRTSRLLQTA---ALR 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 507 LKASGKN--SFEVRNEIQIHrAVNLSVAYTEHTMIHWVQQFLKEIEDQSVKPVLQKVLNLFSLFLLERHLATLYITGYAS 584
Cdd:PLN02636 552 LRKHSKTlgSFGAWNRCLNH-LLTLAESHIESVILAKFIEAVERCPDRSTRAALKLVCDLYALDRIWKDIGTYRNVDYVA 630
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 17540842 585 GGKFG--EDLREKLRLavaELKPEAIALVDSIAPDDFILHSALGASDGKAYEH 635
Cdd:PLN02636 631 PNKAKaiHKLTEYLSF---QVRNVAKELVDAFGLPDHVTRAPIAMQSGAYSEY 680
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
5-638 |
1.21e-75 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 255.16 E-value: 1.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 5 LIDKYRKMATFDWKKLKAAVEGEEHVRLK-SEVVAKMKSEPVF--HRDYRVLSREEQREVVHQRWKKIVEwglfkdpYSD 81
Cdd:PTZ00460 3 MLEEARKQVQFPVLEMTHLLYGNKEQFETfLERQKFIDNEPMFkvHPDYYNWSRQDQILLNAEKTREAHK-------HLN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 82 LENFHALTETLeAYDQGTsarlFLHGNVFG---AAVKSMGTDRHKDL-IQKTENNEIVGAFCLTEVGHGSNTAEIQTTAT 157
Cdd:PTZ00460 76 LANPNYYTPNL-LCPQGT----FISTVHFAmviPAFQVLGTDEQINLwMPSLLNFEIVGCYAQTELGHGSDVQNLETTAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 158 FD--NGELVFNTPSVSAIKCWAGNLAHSATHVVVYAQLHVEGKNEGFHGFVIQVRCPRTFQTLPGITIGDMGSKPGcWQG 235
Cdd:PTZ00460 151 YDkqTNEFVIHTPSVEAVKFWPGELGFLCNFALVYAKLIVNGKNKGVHPFMVRIRDKETHKPLQGVEVGDIGPKMG-YAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 236 VENGWMEFKNHRAPLSALLNKGCDITPDGKYVtsfKSASEKqsVSLGTLSVGRLGIIAKGMMACTFASTIAIRYSVARRQ 315
Cdd:PTZ00460 230 KDNGFLSFDHYRIPLDSLLARYIKVSEDGQVE---RQGNPK--VSYASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 316 FGPVKGAENEipVLEYPLQQYRLFPYLSAAICIrIFQKKFVGHFT-EYMMRVimgEKSDelseFS--KEVHALSSGAKPV 392
Cdd:PTZ00460 305 FTNDNKQENS--VLEYQTQQQKLLPLLAEFYAC-IFGGLKIKELVdDNFNRV---QKND----FSllQLTHAILSAAKAN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 393 ATWLGVESLGEARKACGGHGYLQMSRLNTLRDDNDPSQTFEGENFMILQQTSNILLGKAQSIGSieTPMSTMSFLNqkps 472
Cdd:PTZ00460 375 YTYFVSNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQLARYLLKQLQHAVQ--KPEKVPEYFN---- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 473 kFSSWSSNPVNDVLSAYRYLTY------HLLQTTSAEAYRLKASGKNSFEVRNE---IQIHRAVNLSVAYteHTMIhwvq 543
Cdd:PTZ00460 449 -FLSHITEKLADQTTIESLGQLlglnctILTIYAAKKIMDHINTGKDFQQSWDTksgIALASAASRFIEY--FNYL---- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 544 QFLKEIE--DQSVKPVLQKVLNLFSLFLLERHLATLYITGYASGGKFG--EDLREKLrlaVAELKPEAIALVDSIAPDDF 619
Cdd:PTZ00460 522 CFLDTINnaNKSTKEILTQLADLYGITMLLNNPQGLIEKGQITVEQIKllQETREQL---YPIIKPNALGLVEAFGLSDN 598
|
650
....*....|....*....
gi 17540842 620 ILHSALGASDGKAYEHIME 638
Cdd:PTZ00460 599 SLRSLIGCHDGDPYENMYN 617
|
|
| ACOX |
pfam01756 |
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ... |
483-650 |
7.36e-46 |
|
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts acyl-CoA into trans-2- enoyl-CoA.
Pssm-ID: 460314 [Multi-domain] Cd Length: 180 Bit Score: 160.79 E-value: 7.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 483 NDVLSAYRYLTYHLLQTTSAEAYRLKASGKNSFEVRNEIQIHRaVNLSVAYTEHTMIHWVQQFLKEIEDQSVKPVLQKVL 562
Cdd:pfam01756 3 EVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNNQSVEL-VRAAKAHAEYFVLRTFVERLSTSLDPPLKPVLKKLC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 563 NLFSLFLLERHLATLYITGYASGgKFGEDLREKLRLAVAELKPEAIALVDSIAPDDFILHSALGASDGKAYEHIMEEFRK 642
Cdd:pfam01756 82 KLYALWTIEKHLGDFLQGGYLSP-EQIDLIREAILELLAELRPNAVALVDAFDFPDFILNSALGRYDGNVYENLFEWAKK 160
|
....*...
gi 17540842 643 YTNEQPRW 650
Cdd:pfam01756 161 NPLNTEVP 168
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
51-451 |
2.37e-33 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 131.89 E-value: 2.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 51 RVLSREEQREVVHQRWKKIVEWGLFKDPYS--------DLENFHALTETLEAYDQGTSARLFLHgNVFGAAVKSMGTDRH 122
Cdd:COG1960 27 EAREWDREGEFPRELWRKLAELGLLGLTIPeeygglglSLVELALVLEELARADASLALPVGVH-NGAAEALLRFGTEEQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 123 KD-LIQKTENNEIVGAFCLTEVGHGSNTAEIQTTATFDNGELVFN-TpsvsaiKCWAGNlAHSATHVVVYAQLHVEGKNE 200
Cdd:COG1960 106 KErYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNgQ------KTFITN-APVADVILVLARTDPAAGHR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 201 GFHGFVIqvrcPRtfqTLPGITIGDMGSKPGcWQGVENGWMEFKNHRAPLSALL---NKGcditpdgkyvtsFKSAsekq 277
Cdd:COG1960 179 GISLFLV----PK---DTPGVTVGRIEDKMG-LRGSDTGELFFDDVRVPAENLLgeeGKG------------FKIA---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 278 svsLGTLSVGRLGIIAKGMMACTFASTIAIRYSVARRQFGPvkgaeneiPVLEYPLQQYRLfpylsAAICIRIfqkkfvg 357
Cdd:COG1960 235 ---MSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGR--------PIADFQAVQHRL-----ADMAAEL------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 358 hfteYMMRVIM---GEKSDElsefSKEVHALSSGAKPVATWLGVESLGEARKACGGHGYLQ---MSRLntLRdDNDPSQT 431
Cdd:COG1960 292 ----EAARALVyraAWLLDA----GEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTReypLERL--YR-DARILTI 360
|
410 420
....*....|....*....|
gi 17540842 432 FEGENFMILQQTSNILLGKA 451
Cdd:COG1960 361 YEGTNEIQRLIIARRLLGRP 380
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
56-414 |
4.50e-28 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 115.46 E-value: 4.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 56 EEQREVvhqrWKKIVEWGLFKDPYSDLENFHALTETLEAYDQgtsARLFLhgnvFGAAVKSMGTDRHKD-LIQKTENNEI 134
Cdd:cd00567 1 EEQREL----RDSAREFAAEELEPYARERRETPEEPWELLAE---LGLLL----GAALLLAYGTEEQKErYLPPLASGEA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 135 VGAFCLTEVGHGSNTAEIQTTATFDNGELVfntpsVSAIKCWAGNLAHsATHVVVYAQLHVEGK-NEGFHGFVIqvrcPR 213
Cdd:cd00567 70 IAAFALTEPGAGSDLAGIRTTARKDGDGYV-----LNGRKIFISNGGD-ADLFIVLARTDEEGPgHRGISAFLV----PA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 214 tfqTLPGITIGDMGSKPGcWQGVENGWMEFKNHRAPLSALLNKGcditpdGKYVtsfksasekqSVSLGTLSVGRLGIIA 293
Cdd:cd00567 140 ---DTPGVTVGRIWDKMG-MRGSGTGELVFDDVRVPEDNLLGEE------GGGF----------ELAMKGLNVGRLLLAA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 294 KGMMACTFASTIAIRYSVARRQFGPvkgaeneiPVLEYPLQQYRLFPylsAAICIrifqkkfvghfteYMMRVIMGEKSD 373
Cdd:cd00567 200 VALGAARAALDEAVEYAKQRKQFGK--------PLAEFQAVQFKLAD---MAAEL-------------EAARLLLYRAAW 255
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 17540842 374 ELSEFSKEVHALSSGAKPVATWLGVESLGEARKACGGHGYL 414
Cdd:cd00567 256 LLDQGPDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYS 296
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
90-317 |
4.30e-14 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 74.23 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 90 ETLEAYDQGTSARLFLHGNVFGAAVKSMGTDRHK-DLIQKTENNEIVGAFCLTEVGHGSNTAEIQTTATFDNGELVFNtp 168
Cdd:cd01158 68 EELAKVDASVAVIVSVHNSLGANPIIKFGTEEQKkKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLN-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 169 svsAIKCWAGNLAHsATHVVVYAQLHVEGKNEGFHGFVIqvrcPRTFqtlPGITIGDMGSKPGCwQGVENGWMEFKNHRA 248
Cdd:cd01158 146 ---GSKMWITNGGE-ADFYIVFAVTDPSKGYRGITAFIV----ERDT---PGLSVGKKEDKLGI-RGSSTTELIFEDVRV 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17540842 249 PLSALLnkgcditpdGKYVTSFKSAsekqsvsLGTLSVGRLGI------IAKGMMACtfastiAIRYSVARRQFG 317
Cdd:cd01158 214 PKENIL---------GEEGEGFKIA-------MQTLDGGRIGIaaqalgIAQAALDA------AVDYAKERKQFG 266
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
137-244 |
1.24e-11 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 61.14 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 137 AFCLTEVGHGSNTAEIQTTA-TFDNGELVfntpsVSAIKCWAGNlAHSATHVVVYAQLHVEGKNEGFHGFVIQvrcprtf 215
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWV-----LNGTKWWITN-AGIADLFLVLARTGGDDRHGGISLFLVP------- 67
|
90 100
....*....|....*....|....*....
gi 17540842 216 QTLPGITIGDMGSKPGcWQGVENGWMEFK 244
Cdd:pfam02770 68 KDAPGVSVRRIETKLG-VRGLPTGELVFD 95
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
90-450 |
3.06e-11 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 65.54 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 90 ETLEAYDQGTSARLFLHgNVFGAAVKSMGTDRHK-DLIQKTENNEIVGAFCLTEVGHGSNTAEIQTTATFDNGELVFNtp 168
Cdd:cd01162 70 EALSTGCVSTAAYISIH-NMCAWMIDSFGNDEQReRFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLN-- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 169 svsAIKCWAGNLAHSATHVVVyAQLHVEGKnEGFHGFVIQvrcprtfQTLPGITIGDMGSKPGcWQGVENGWMEFKNHRA 248
Cdd:cd01162 147 ---GSKAFISGAGDSDVYVVM-ARTGGEGP-KGISCFVVE-------KGTPGLSFGANEKKMG-WNAQPTRAVIFEDCRV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 249 PLSALLNkgcditPDGkyvtsfksasEKQSVSLGTLSVGRLGIIAKGMMACTFASTIAIRYSVARRQFGPvkgaeneiPV 328
Cdd:cd01162 214 PVENRLG------GEG----------QGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGK--------PL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 329 LEYPLQQYRLfpylsAAICIRIfqkkfvghfteYMMRVIMGEKSDELSEFSKEVHALSSGAKPVATWLGVESLGEARKAC 408
Cdd:cd01162 270 ADFQALQFKL-----ADMATEL-----------VASRLMVRRAASALDRGDPDAVKLCAMAKRFATDECFDVANQALQLH 333
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 17540842 409 GGHGYLQMSRLNTLRDDNDPSQTFEGENFMILQQTSNILLGK 450
Cdd:cd01162 334 GGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
88-338 |
5.76e-11 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 64.69 E-value: 5.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 88 LTETLEAYDQGTSARLFLHGNVFGAAVKSMGTDRHKD-LIQKTENNEIVGAFCLTEVGHGSNTAEIQTTATFDNGELVFN 166
Cdd:cd01151 79 IAREVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQkYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 167 tpsvsAIKCWAGNlAHSATHVVVYAQLHVEGKnegFHGFVIQvrcprtfQTLPGITIGDMGSKPGcWQGVENGWMEFKNH 246
Cdd:cd01151 159 -----GSKTWITN-SPIADVFVVWARNDETGK---IRGFILE-------RGMKGLSAPKIQGKFS-LRASITGEIVMDNV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 247 RAPLSALLNKgcditpdgkyVTSFKSasekqsvSLGTLSVGRLGIIAKGMMACTFASTIAIRYSVARRQFGPvkgaenei 326
Cdd:cd01151 222 FVPEENLLPG----------AEGLRG-------PFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGR-------- 276
|
250
....*....|..
gi 17540842 327 PVLEYPLQQYRL 338
Cdd:cd01151 277 PLAAFQLVQKKL 288
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
118-436 |
4.46e-10 |
|
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer.
Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 62.10 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 118 GTDRHKD-LIQKTENNEIVGAFCLTEVGHGSNTAEIQTTATF--DNGELVFNtpsvsAIKCWAGNlAHSATHVVVYAQLH 194
Cdd:cd01161 121 GTEAQKEkYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLN-----GSKIWITN-GGIADIFTVFAKTE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 195 VE----GKNEGFHGFVIQvrcpRTFQtlpGITIGDMGSKPGCwQGVENGWMEFKNHRAPLSALLnkgcditpdGKYVTSF 270
Cdd:cd01161 195 VKdatgSVKDKITAFIVE----RSFG---GVTNGPPEKKMGI-KGSNTAEVYFEDVKIPVENVL---------GEVGDGF 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 271 KsasekqsVSLGTLSVGRLGI---IAKGMMACTfasTIAIRYSVARRQFGPvkgaeneiPVLEYPLQQYRLfpylsaaic 347
Cdd:cd01161 258 K-------VAMNILNNGRFGMgaaLIGTMKRCI---EKAVDYANNRKQFGK--------KIHEFGLIQEKL--------- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 348 IRIFQKKFVGHFTEYMMRVIMGEKSdeLSEFSKEVhALSSGAKPVATWLGVEslgEARKACGGHGYLQMSRLNTLRDDND 427
Cdd:cd01161 311 ANMAILQYATESMAYMTSGNMDRGL--KAEYQIEA-AISKVFASEAAWLVVD---EAIQIHGGMGFMREYGVERVLRDLR 384
|
....*....
gi 17540842 428 PSQTFEGEN 436
Cdd:cd01161 385 IFRIFEGTN 393
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
27-317 |
4.25e-09 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 59.05 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 27 EEHVRLKsEVVAKMKSEPV--FHRDYrvlsrEEQREVVHQRWKKIVEWGL----FKDPY----SDLENFHALTETLeAYD 96
Cdd:cd01160 1 EEHDAFR-DVVRRFFAKEVapFHHEW-----EKAGEVPREVWRKAGEQGLlgvgFPEEYggigGDLLSAAVLWEEL-ARA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 97 QGTSARLFLHGNVFGAAVKSMGTDRHKD-LIQKTENNEIVGAFCLTEVGHGSNTAEIQTTATFD------NGELVFNTps 169
Cdd:cd01160 74 GGSGPGLSLHTDIVSPYITRAGSPEQKErVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDgdhyvlNGSKTFIT-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 170 vsaikcwagNLAHSATHVVVYAQLHVEGKNEGFHGFVIQvrcprtfQTLPGITIGDMGSKPGcWQGVENGWMEFKNHRAP 249
Cdd:cd01160 152 ---------NGMLADVVIVVARTGGEARGAGGISLFLVE-------RGTPGFSRGRKLKKMG-WKAQDTAELFFDDCRVP 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17540842 250 LSALL---NKGcditpdgkyvtsFKSAsekqsvsLGTLSVGRLGIIAKGMMACTFASTIAIRYSVARRQFG 317
Cdd:cd01160 215 AENLLgeeNKG------------FYYL-------MQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFG 266
|
|
| Acyl-CoA_ox_N |
pfam14749 |
Acyl-coenzyme A oxidase N-terminal; Acyl-coenzyme A oxidase consists of three domains. An ... |
26-135 |
2.85e-06 |
|
Acyl-coenzyme A oxidase N-terminal; Acyl-coenzyme A oxidase consists of three domains. An N-terminal alpha-helical domain, a beta sheet domain (pfam02770) and a C-terminal catalytic domain (pfam01756). This entry represents the N-terminal alpha-helical domain.
Pssm-ID: 464295 [Multi-domain] Cd Length: 120 Bit Score: 46.82 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 26 GEEHVRLKSEVVAKMKSEPVFH--RDYRVLSREEQREVVHQR----WKKIVEWGLfkdpYSDLENFHALTETLeaYDQGT 99
Cdd:pfam14749 12 GEEKLERRREIESLIESDPEFSkpEDYYFLSREERYERALRKakrlVKKLRELQI----EDPEETLLLYLRGL--LDEGL 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 17540842 100 SarLFLHGNVFGAAVKSMGTD-RHKDLIQKTENNEIV 135
Cdd:pfam14749 86 P--LGLHFGMFIPTLKGQGTDeQQAKWLPLAENFEII 120
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
133-347 |
5.13e-03 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 39.86 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 133 EIVGAFCLTEVGHGSNTAEIQTTATFDNGELVFNtpsvsAIKCWAGNlAHSATHVVVYAQLHVEGKNEGFHGFVIQvrcp 212
Cdd:PLN02519 141 EHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLN-----GNKMWCTN-GPVAQTLVVYAKTDVAAGSKGITAFIIE---- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17540842 213 rtfQTLPGITIGDMGSKPGcWQGVENGWMEFKNHRAPLSALLNKgcditpDGKYVTSFKSASEKQSVslgTLSVGRLGIi 292
Cdd:PLN02519 211 ---KGMPGFSTAQKLDKLG-MRGSDTCELVFENCFVPEENVLGQ------EGKGVYVMMSGLDLERL---VLAAGPLGL- 276
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17540842 293 akgMMACTfasTIAIRYSVARRQFGPVKGA----ENEIPVLEYPLQQYRLFPYLSAAIC 347
Cdd:PLN02519 277 ---MQACL---DVVLPYVRQREQFGRPIGEfqfiQGKLADMYTSLQSSRSYVYSVARDC 329
|
|
| |
