|
Name |
Accession |
Description |
Interval |
E-value |
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
19-648 |
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: 873.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 19 GPLDAYRARASFSWKELALFTEG-EGMLRFKKTIFSALENDPLFARspgADLSLEKYRELNFLRCKRIFEYDFLSVEDMF 97
Cdd:cd01150 1 PDLDKERASATFDWKALTHILEGgEENLRRKREVERELESDPLFQR---ELPSKHLSREELYEELKRKAKTDVERMGELM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 98 KS-PLK------------------------VFGSAVYSSGSERHLTYIQKIFRM-EIFGCFALTELSHGSNTKAIRTTAH 151
Cdd:cd01150 78 ADdPEKmlaltnslggydlslgaklglhlgLFGNAIKNLGTDEHQDYWLQGANNlEIIGCFAQTELGHGSNLQGLETTAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 152 YDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGdQCHGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQNG 231
Cdd:cd01150 158 YDPLTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPG-KNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMGLNG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 232 LDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQ 311
Cdd:cd01150 237 VDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 312 FGPT-EEEEIPVLEYPMQQWRLLPYLAAVYALDHFSKSLFLDLVELQRGLASGDrsarqAELGREIHALASASKPLASWT 390
Cdd:cd01150 317 FGPKpSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGN-----SELLAELHALSAGLKAVATWT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 391 TQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVHdgacfrsplksvdfldaypg 470
Cdd:cd01150 392 AAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAFS-------------------- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 471 ildqkfevssvadcldSAVALAAYKWLVCYLLRETYQKLNQEKRSGSSDFEARNKCQVsHGRPLALAFVELTVVQRFHEH 550
Cdd:cd01150 452 ----------------LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQV-HLRCAAKAHTEYTVLQRFHES 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 551 VHQpSVPPSLRAVLGRLSALYALWSLSRHAALLYRgGYFSGEQAGEVLESAVLALCSQLKDDAVALVDVIAPPDFVLDSP 630
Cdd:cd01150 515 VEE-IVDPSVRAVLKRLCDLYALWLLEEHIADFLE-GGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSP 592
|
650
....*....|....*...
gi 1771853650 631 IGRADGELYKNLWGAVLQ 648
Cdd:cd01150 593 IGRYDGDVYENLFEEARK 610
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
28-631 |
4.35e-110 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 347.53 E-value: 4.35e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 28 ASFSWKELALFTEGEGmLRFKKTIFSALENDPLFAR---------SPGADLSLEKYRELN-----FLRCKRIFE------ 87
Cdd:PLN02312 49 YAFDVKEMRKLLDGHN-LEDRDWLFGLMMQSDLFNSkrrggrvfvSPDYNQTMEQQREITmkrilYLLERGVFRgwltet 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 88 --------YDFLSVEDMFKSPLKV--------FGSAVYSSGSERHL-TYIQKIFRMEIFGCFALTELSHGSNTKAIRTTA 150
Cdd:PLN02312 128 gpeaelrkLALLEVIGIYDHSLAIklgvhfflWGGAIKFLGTKRHHdKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 151 HYDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGDQcHGLHPFIVQIRDPKTLLpMPGVMVGDIGKKLGQN 230
Cdd:PLN02312 208 TYDPKTEEFVINTPCESAQKYWIGGAANHATHTIVFSQLHINGKN-EGVHAFIAQIRDQDGNI-CPNIRIADCGHKIGLN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 231 GLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRR 310
Cdd:PLN02312 286 GVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRR 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 311 QFGPTEEE-EIPVLEYPMQQWRLLPYLAAVYALD---HFSKSLFLDlvelqrglasgdrsaRQAELGREIHALASASKPL 386
Cdd:PLN02312 366 AFSVTPNGpEVLLLDYPSHQRRLLPLLAKTYAMSfaaNDLKMIYVK---------------RTPESNKAIHVVSSGFKAV 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 387 ASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAhqvhdgACFR--SPLK--SV 462
Cdd:PLN02312 431 LTWHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAEYV------SAKKrnKPFKglGL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 463 DFLDAYPGILDQKFEVSSVAdclDSAVALAAYkwlvCYLLRETYQKLNQEKRSGSSDFEARNKCQVSH---GRPLALAFV 539
Cdd:PLN02312 505 EHMNGPRPVIPTQLTSSTLR---DSQFQLNLF----CLRERDLLERFASEVSELQSKGESREFAFLLSyqlAEDLGRAFS 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 540 ELTVVQRFHEhVHQPSVPPSLRAVLGRLSALYALWSLSRHAALLyRGGYFSGEQAGEVlESAVLALCSQLKDDAVALVDV 619
Cdd:PLN02312 578 ERAILQTFLD-AEANLPTGSLKDVLGLLRSLYVLISLDEDPSFL-RYGYLSPDNVALV-RKEVAKLCGELRPHALALVSS 654
|
650
....*....|..
gi 1771853650 620 IAPPDFVLdSPI 631
Cdd:PLN02312 655 FGIPDAFL-SPI 665
|
|
| ACOX |
pfam01756 |
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ... |
486-670 |
5.78e-64 |
|
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: 209.71 E-value: 5.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 486 DSAVALAAYKWLVCYLLRETYQKLNQEKRSGSSDFEARNKCQVSHgRPLALAFVELTVVQRFHEHVHQpSVPPSLRAVLG 565
Cdd:pfam01756 1 DPEVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNNQSVEL-VRAAKAHAEYFVLRTFVERLST-SLDPPLKPVLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 566 RLSALYALWSLSRHAALLYRGGYFSGEQAGEVLEsAVLALCSQLKDDAVALVDVIAPPDFVLDSPIGRADGELYKNLWGA 645
Cdd:pfam01756 79 KLCKLYALWTIEKHLGDFLQGGYLSPEQIDLIRE-AILELLAELRPNAVALVDAFDFPDFILNSALGRYDGNVYENLFEW 157
|
170 180
....*....|....*....|....*
gi 1771853650 646 VLQESKVLERASWWPEFSvnKPVIG 670
Cdd:pfam01756 158 AKKNPLNTEVPPSYHEYL--KPLLK 180
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
103-444 |
2.20e-37 |
|
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: 143.44 E-value: 2.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 103 VFGSAVYSSGSERHL-TYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPatEEFIIHspdfeAAKFWVGNmGKTAT 181
Cdd:COG1960 92 GAAEALLRFGTEEQKeRYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDG--DGYVLN-----GQKTFITN-APVAD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 182 HAVVFAKLcVPGDQCHGLHPFIVqirdPKtllPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQsllNRMGDvtpEGt 261
Cdd:COG1960 164 VILVLART-DPAAGHRGISLFLV----PK---DTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAE---NLLGE---EG- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 262 yvspfkdvrQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPMQQWRLLPYLAAVYA 341
Cdd:COG1960 229 ---------KGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGR------PIADFQAVQHRLADMAAELEA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 342 LdhfskslfldlvelqRGLAsgDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDND 421
Cdd:COG1960 294 A---------------RALV--YRAAWLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDAR 356
|
330 340
....*....|....*....|...
gi 1771853650 422 PNCTYEGDNNILLQQTSNYLLGL 444
Cdd:COG1960 357 ILTIYEGTNEIQRLIIARRLLGR 379
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
19-648 |
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: 873.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 19 GPLDAYRARASFSWKELALFTEG-EGMLRFKKTIFSALENDPLFARspgADLSLEKYRELNFLRCKRIFEYDFLSVEDMF 97
Cdd:cd01150 1 PDLDKERASATFDWKALTHILEGgEENLRRKREVERELESDPLFQR---ELPSKHLSREELYEELKRKAKTDVERMGELM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 98 KS-PLK------------------------VFGSAVYSSGSERHLTYIQKIFRM-EIFGCFALTELSHGSNTKAIRTTAH 151
Cdd:cd01150 78 ADdPEKmlaltnslggydlslgaklglhlgLFGNAIKNLGTDEHQDYWLQGANNlEIIGCFAQTELGHGSNLQGLETTAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 152 YDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGdQCHGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQNG 231
Cdd:cd01150 158 YDPLTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPG-KNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMGLNG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 232 LDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQ 311
Cdd:cd01150 237 VDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 312 FGPT-EEEEIPVLEYPMQQWRLLPYLAAVYALDHFSKSLFLDLVELQRGLASGDrsarqAELGREIHALASASKPLASWT 390
Cdd:cd01150 317 FGPKpSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGN-----SELLAELHALSAGLKAVATWT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 391 TQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVHdgacfrsplksvdfldaypg 470
Cdd:cd01150 392 AAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAFS-------------------- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 471 ildqkfevssvadcldSAVALAAYKWLVCYLLRETYQKLNQEKRSGSSDFEARNKCQVsHGRPLALAFVELTVVQRFHEH 550
Cdd:cd01150 452 ----------------LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQV-HLRCAAKAHTEYTVLQRFHES 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 551 VHQpSVPPSLRAVLGRLSALYALWSLSRHAALLYRgGYFSGEQAGEVLESAVLALCSQLKDDAVALVDVIAPPDFVLDSP 630
Cdd:cd01150 515 VEE-IVDPSVRAVLKRLCDLYALWLLEEHIADFLE-GGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSP 592
|
650
....*....|....*...
gi 1771853650 631 IGRADGELYKNLWGAVLQ 648
Cdd:cd01150 593 IGRYDGDVYENLFEEARK 610
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
28-631 |
4.35e-110 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 347.53 E-value: 4.35e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 28 ASFSWKELALFTEGEGmLRFKKTIFSALENDPLFAR---------SPGADLSLEKYRELN-----FLRCKRIFE------ 87
Cdd:PLN02312 49 YAFDVKEMRKLLDGHN-LEDRDWLFGLMMQSDLFNSkrrggrvfvSPDYNQTMEQQREITmkrilYLLERGVFRgwltet 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 88 --------YDFLSVEDMFKSPLKV--------FGSAVYSSGSERHL-TYIQKIFRMEIFGCFALTELSHGSNTKAIRTTA 150
Cdd:PLN02312 128 gpeaelrkLALLEVIGIYDHSLAIklgvhfflWGGAIKFLGTKRHHdKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 151 HYDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGDQcHGLHPFIVQIRDPKTLLpMPGVMVGDIGKKLGQN 230
Cdd:PLN02312 208 TYDPKTEEFVINTPCESAQKYWIGGAANHATHTIVFSQLHINGKN-EGVHAFIAQIRDQDGNI-CPNIRIADCGHKIGLN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 231 GLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRR 310
Cdd:PLN02312 286 GVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRR 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 311 QFGPTEEE-EIPVLEYPMQQWRLLPYLAAVYALD---HFSKSLFLDlvelqrglasgdrsaRQAELGREIHALASASKPL 386
Cdd:PLN02312 366 AFSVTPNGpEVLLLDYPSHQRRLLPLLAKTYAMSfaaNDLKMIYVK---------------RTPESNKAIHVVSSGFKAV 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 387 ASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAhqvhdgACFR--SPLK--SV 462
Cdd:PLN02312 431 LTWHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAEYV------SAKKrnKPFKglGL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 463 DFLDAYPGILDQKFEVSSVAdclDSAVALAAYkwlvCYLLRETYQKLNQEKRSGSSDFEARNKCQVSH---GRPLALAFV 539
Cdd:PLN02312 505 EHMNGPRPVIPTQLTSSTLR---DSQFQLNLF----CLRERDLLERFASEVSELQSKGESREFAFLLSyqlAEDLGRAFS 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 540 ELTVVQRFHEhVHQPSVPPSLRAVLGRLSALYALWSLSRHAALLyRGGYFSGEQAGEVlESAVLALCSQLKDDAVALVDV 619
Cdd:PLN02312 578 ERAILQTFLD-AEANLPTGSLKDVLGLLRSLYVLISLDEDPSFL-RYGYLSPDNVALV-RKEVAKLCGELRPHALALVSS 654
|
650
....*....|..
gi 1771853650 620 IAPPDFVLdSPI 631
Cdd:PLN02312 655 FGIPDAFL-SPI 665
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
57-650 |
3.16e-107 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 339.51 E-value: 3.16e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 57 NDPLFARSPGADLSLEkyrEL--NFLR-----CKRIFEYDfLSVEDMFKSPLKV------------FGSAVYSSGS-ERH 116
Cdd:PLN02443 44 SDPVFSKDNRTRLSRK---ELfkNTLRkaahaWKRIIELR-LTEEEAGKLRSFVdepgytdlhwgmFVPAIKGQGTeEQQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 117 LTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGDQc 196
Cdd:PLN02443 120 KKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHSPTLTSSKWWPGGLGKVSTHAVVYARLITNGKD- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 197 HGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQ---NGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSpfKDVRQRF 273
Cdd:PLN02443 199 HGIHGFIVQLRSLDDHSPLPGVTVGDIGMKFGNgayNTMDNGFLRFDHVRIPRDQMLMRLSKVTREGKYVQ--SDVPRQL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 274 GasLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEE-EIPVLEYPMQQWRLLPYLAAVYA---LDHFSKSL 349
Cdd:PLN02443 277 V--YGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFGSQDGGpETQVIDYKTQQSRLFPLLASAYAfrfVGEWLKWL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 350 FLDLVelQRgLASGDRSARQaelgrEIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGD 429
Cdd:PLN02443 355 YTDVT--QR-LEANDFSTLP-----EAHACTAGLKSLTTSATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACTYEGD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 430 NNILLQQTSNYLLGLLAhQVHDGacfRSPLKSVDFLDAYPGILDQKFEVSSVADCLDSAVALAAYKWLVCYLLRETYQKL 509
Cdd:PLN02443 427 NVVLLLQVARFLMKTVS-QLGSG---KKPVGTTAYMGRVQHLLQCRCGVQTAEDWLNPSVVLEAFEARAARMAVTCAQNL 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 510 NQeKRSGSSDFEARNKCQVShgrpLALAFVELTVVQRFHEHVHQPSVPPSLRAVLGRLSALYALWSLSRHAALLYRGGYF 589
Cdd:PLN02443 503 SK-FENQEAGFQELSADLVE----AAVAHCQLIVVSKFIEKLQQDIPGKGVKKQLQNLCYIYALYLLHKHLGDFLSTGCI 577
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1771853650 590 SGEQ---AGEVLESavlaLCSQLKDDAVALVDVIAPPDFVLDSPIGRADGELYKNLWGAVLQES 650
Cdd:PLN02443 578 TPKQaslANDQLRS----LYSQVRPNAVALVDAFNYTDHYLGSVLGRYDGNVYPKLYEEAWKDP 637
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
103-637 |
1.32e-102 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 327.97 E-value: 1.32e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 103 VFGSAVYSSGSERHL-TYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFIIHSPDFEAAKFWVGNMGKTAT 181
Cdd:PLN02636 147 LWGGSVINLGTKKHRdKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINTPNDGAIKWWIGNAAVHGK 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 182 HAVVFAKLCVP-----GDQCHGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDV 256
Cdd:PLN02636 227 FATVFARLKLPthdskGVSDMGVHAFIVPIRDMKTHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGDV 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 257 TPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEEEIPVLEYPMQQWRLLPYL 336
Cdd:PLN02636 307 SRDGKYTSSLPTINKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPKQPEISILDYQSQQHKLMPML 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 337 AAVYALdHFSKSLfldLVELQrglaSGDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVL 416
Cdd:PLN02636 387 ASTYAF-HFATEY---LVERY----SEMKKTHDDQLVADVHALSAGLKAYITSYTAKALSTCREACGGHGYAAVNRFGSL 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 417 RDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVHDGACFRSPLKSVDFLDAYpgiLDQKFEVSS----VADCLDSAVALA 492
Cdd:PLN02636 459 RNDHDIFQTFEGDNTVLLQQVAADLLKQYKEKFQGGTLSVTWNYLRESMNTY---LSQPNPVTTrwegEEHLRDPKFQLD 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 493 AYKWLVCYLLRETYQKLNQE-KRSGSsdFEARNKCqVSHGRPLALAFVELTVVQRFHEHVhQPSVPPSLRAVLGRLSALY 571
Cdd:PLN02636 536 AFRYRTSRLLQTAALRLRKHsKTLGS--FGAWNRC-LNHLLTLAESHIESVILAKFIEAV-ERCPDRSTRAALKLVCDLY 611
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853650 572 ALWSLSRHAAlLYRGGYFSGEQAGEVLESAVLALCSQLKDDAVALVDVIAPPDFVLDSPIGRADGE 637
Cdd:PLN02636 612 ALDRIWKDIG-TYRNVDYVAPNKAKAIHKLTEYLSFQVRNVAKELVDAFGLPDHVTRAPIAMQSGA 676
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
21-652 |
3.90e-79 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 264.79 E-value: 3.90e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 21 LDAYRARASFSWKELA--LFTEGEGMLRFKKtIFSALENDPLFARSPGAdlsLEKYRELNFLRC--KRIFEYDFLSVED- 95
Cdd:PTZ00460 4 LEEARKQVQFPVLEMThlLYGNKEQFETFLE-RQKFIDNEPMFKVHPDY---YNWSRQDQILLNaeKTREAHKHLNLANp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 96 -----MFKSPLKVFGSAVYSS---------GSERHLT-YIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFI 160
Cdd:PTZ00460 80 nyytpNLLCPQGTFISTVHFAmvipafqvlGTDEQINlWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 161 IHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGdQCHGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQNGLDNGFAMFH 240
Cdd:PTZ00460 160 IHTPSVEAVKFWPGELGFLCNFALVYAKLIVNG-KNKGVHPFMVRIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 241 KVRVPRQSLLNRMGDVTPEGTYvspfkdvrQRFG---ASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEE 317
Cdd:PTZ00460 239 HYRIPLDSLLARYIKVSEDGQV--------ERQGnpkVSYASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNDNK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 318 EEIPVLEYPMQQWRLLPYLAAVYALDhFSKSLFLDLVELQ-RGLASGDRSARQaelgrEIHALASASKPLASWTTQQGIQ 396
Cdd:PTZ00460 311 QENSVLEYQTQQQKLLPLLAEFYACI-FGGLKIKELVDDNfNRVQKNDFSLLQ-----LTHAILSAAKANYTYFVSNCAE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 397 ECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVhdgacfrSPLKSV----DFLDAYPGIL 472
Cdd:PTZ00460 385 WCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQLARYLLKQLQHAV-------QKPEKVpeyfNFLSHITEKL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 473 DQKFEVSSVADCLDSAVALaaykwlvcyLLRETYQKLNQEKRSGSSDFEARNKCQVSHGRPLALAFVELTVVQRFHEHVH 552
Cdd:PTZ00460 458 ADQTTIESLGQLLGLNCTI---------LTIYAAKKIMDHINTGKDFQQSWDTKSGIALASAASRFIEYFNYLCFLDTIN 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 553 QPSvpPSLRAVLGRLSALYALWSLSRHAALLYRGGYFSGEQAgEVLESAVLALCSQLKDDAVALVDVIAPPDFVLDSPIG 632
Cdd:PTZ00460 529 NAN--KSTKEILTQLADLYGITMLLNNPQGLIEKGQITVEQI-KLLQETREQLYPIIKPNALGLVEAFGLSDNSLRSLIG 605
|
650 660
....*....|....*....|
gi 1771853650 633 RADGELYKNLWGAVLQESKV 652
Cdd:PTZ00460 606 CHDGDPYENMYNWASKENSL 625
|
|
| ACOX |
pfam01756 |
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ... |
486-670 |
5.78e-64 |
|
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: 209.71 E-value: 5.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 486 DSAVALAAYKWLVCYLLRETYQKLNQEKRSGSSDFEARNKCQVSHgRPLALAFVELTVVQRFHEHVHQpSVPPSLRAVLG 565
Cdd:pfam01756 1 DPEVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNNQSVEL-VRAAKAHAEYFVLRTFVERLST-SLDPPLKPVLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 566 RLSALYALWSLSRHAALLYRGGYFSGEQAGEVLEsAVLALCSQLKDDAVALVDVIAPPDFVLDSPIGRADGELYKNLWGA 645
Cdd:pfam01756 79 KLCKLYALWTIEKHLGDFLQGGYLSPEQIDLIRE-AILELLAELRPNAVALVDAFDFPDFILNSALGRYDGNVYENLFEW 157
|
170 180
....*....|....*....|....*
gi 1771853650 646 VLQESKVLERASWWPEFSvnKPVIG 670
Cdd:pfam01756 158 AKKNPLNTEVPPSYHEYL--KPLLK 180
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
103-444 |
2.20e-37 |
|
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: 143.44 E-value: 2.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 103 VFGSAVYSSGSERHL-TYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPatEEFIIHspdfeAAKFWVGNmGKTAT 181
Cdd:COG1960 92 GAAEALLRFGTEEQKeRYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDG--DGYVLN-----GQKTFITN-APVAD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 182 HAVVFAKLcVPGDQCHGLHPFIVqirdPKtllPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQsllNRMGDvtpEGt 261
Cdd:COG1960 164 VILVLART-DPAAGHRGISLFLV----PK---DTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAE---NLLGE---EG- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 262 yvspfkdvrQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPMQQWRLLPYLAAVYA 341
Cdd:COG1960 229 ---------KGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGR------PIADFQAVQHRLADMAAELEA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 342 LdhfskslfldlvelqRGLAsgDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDND 421
Cdd:COG1960 294 A---------------RALV--YRAAWLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDAR 356
|
330 340
....*....|....*....|...
gi 1771853650 422 PNCTYEGDNNILLQQTSNYLLGL 444
Cdd:COG1960 357 ILTIYEGTNEIQRLIIARRLLGR 379
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
119-436 |
3.10e-32 |
|
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: 127.40 E-value: 3.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 119 YIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPatEEFIIHSpdfeaAKFWVGNmGKTATHAVVFAKLCVPGDQCHG 198
Cdd:cd00567 60 YLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDG--DGYVLNG-----RKIFISN-GGDADLFIVLARTDEEGPGHRG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 199 LHPFIVqirdPKTllpMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVtpegtyvspfkdvrqrFGASLG 278
Cdd:cd00567 132 ISAFLV----PAD---TPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGG----------------FELAMK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 279 SLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPMQQWRLLPYLAAVYALDHFskslfldlvelqr 358
Cdd:cd00567 189 GLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGK------PLAEFQAVQFKLADMAAELEAARLL------------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 359 glasGDRSARQAELGR-EIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLG-VLRDDNdPNCTYEGDNNILLQQ 436
Cdd:cd00567 250 ----LYRAAWLLDQGPdEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVErYLRDAR-AARIAEGTAEIQRLI 324
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
119-433 |
2.80e-16 |
|
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: 81.36 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 119 YIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFIIHspdfeAAKFWVGNmGKTATHAVVFAKLCV---PGDQ 195
Cdd:cd01161 129 YLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKHYVLN-----GSKIWITN-GGIADIFTVFAKTEVkdaTGSV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 196 CHGLHPFIVQiRDPKtllpmpGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDvtpegtyvspfkdvrqRFGA 275
Cdd:cd01161 203 KDKITAFIVE-RSFG------GVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGD----------------GFKV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 276 SLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPMQQWRLLPYLAAVYALDhfsKSLFLDLVE 355
Cdd:cd01161 260 AMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGK------KIHEFGLIQEKLANMAILQYATE---SMAYMTSGN 330
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853650 356 LQRGlasgdrsarqaeLGREIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNIL 433
Cdd:cd01161 331 MDRG------------LKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEIL 396
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
90-443 |
4.42e-16 |
|
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: 80.39 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 90 FLSVED-MFKSPLKVFGSavyssgSERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDpaTEEFIIHspdfeA 168
Cdd:cd01158 80 IVSVHNsLGANPIIKFGT------EEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKD--GDDYVLN-----G 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 169 AKFWVGNMGKtATHAVVFAKlCVPGDQCHGLHPFIVqirdPKtllPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQS 248
Cdd:cd01158 147 SKMWITNGGE-ADFYIVFAV-TDPSKGYRGITAFIV----ER---DTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKEN 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 249 LLNRMGdvtpEGtyvspfkdvrqrFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPMQ 328
Cdd:cd01158 218 ILGEEG----EG------------FKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGK------PIADFQGI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 329 QWRLlpylaAVYALDhfskslfldlVELQRGLasGDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGYl 408
Cdd:cd01158 276 QFKL-----ADMATE----------IEAARLL--TYKAARLKDNGEPFIKEAAMAKLFASEVAMRVTTDAVQIFGGYGY- 337
|
330 340 350
....*....|....*....|....*....|....*..
gi 1771853650 409 aMNRLGVLRDDNDPNCT--YEGDNNILLQQTSNYLLG 443
Cdd:cd01158 338 -TKDYPVERYYRDAKITeiYEGTSEIQRLVIAKHLLK 373
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
107-313 |
7.36e-16 |
|
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: 80.09 E-value: 7.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 107 AVYSSGSE-RHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATeeFIIHspdfeAAKFWVGNmGKTATHAVV 185
Cdd:cd01151 104 PIYDFGSEeQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGG--YKLN-----GSKTWITN-SPIADVFVV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 186 FAKlCVPGDQCHGlhpFIVQiRDpktllpMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLnrmgdvtPEGTYvsp 265
Cdd:cd01151 176 WAR-NDETGKIRG---FILE-RG------MKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-------PGAEG--- 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1771853650 266 fkdvrqrFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFG 313
Cdd:cd01151 235 -------LRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFG 275
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
127-442 |
1.75e-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: 60.21 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 127 EIFGCFALTELSHGSNTKAIRTTAHYDpaTEEFIIHspdfeAAKFWVGNmGKTATHAVVFAKLCVPGDQCHGLHPFIVQi 206
Cdd:cd01160 111 KKIGAIAMTEPGAGSDLQGIRTTARKD--GDHYVLN-----GSKTFITN-GMLADVVIVVARTGGEARGAGGISLFLVE- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 207 RDpktllpMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGdvtpegtyvspfkdvrQRFGASLGSLSSGRVS 286
Cdd:cd01160 182 RG------TPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEEN----------------KGFYYLMQNLPQERLL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 287 IVSLAILNLKLAVAIALRFSATRRQFGPTeeeeipvleypmqqwrllpyLAAVYALDHfskslflDLVELQRGLASG--- 363
Cdd:cd01160 240 IAAGALAAAEFMLEETRNYVKQRKAFGKT--------------------LAQLQVVRH-------KIAELATKVAVTraf 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 364 -DRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLL 442
Cdd:cd01160 293 lDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
90-409 |
3.79e-09 |
|
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: 58.99 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 90 FLSVEDMFKSPLKVFGSAvyssgsERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDpaTEEFIIhspdfEAA 169
Cdd:cd01162 82 YISIHNMCAWMIDSFGND------EQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVRE--GDHYVL-----NGS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 170 KFWVGNMGKTATHaVVFAKlcVPGDQCHGLHPFIVqirdPKTllpMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQsl 249
Cdd:cd01162 149 KAFISGAGDSDVY-VVMAR--TGGEGPKGISCFVV----EKG---TPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVE-- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 250 lNRMGdvtPEGtyvspfkdvrQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPMQQ 329
Cdd:cd01162 217 -NRLG---GEG----------QGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGK------PLADFQALQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 330 WRLlpylaAVYALDHFSKSLFLDLVELQrgLASGDRSARqaelgreihALASASKPLAswtTQQGIQECREAC---GGHG 406
Cdd:cd01162 277 FKL-----ADMATELVASRLMVRRAASA--LDRGDPDAV---------KLCAMAKRFA---TDECFDVANQALqlhGGYG 337
|
...
gi 1771853650 407 YLA 409
Cdd:cd01162 338 YLK 340
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
131-235 |
4.12e-09 |
|
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: 54.21 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 131 CFALTELSHGSNTKAIRTTAhYDPATEEFIIHspdfeAAKFWVGNmGKTATHAVVFAKLcVPGDQCHGLHPFIVqirdPK 210
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLN-----GTKWWITN-AGIADLFLVLART-GGDDRHGGISLFLV----PK 68
|
90 100
....*....|....*....|....*
gi 1771853650 211 TllpMPGVMVGDIGKKLGQNGLDNG 235
Cdd:pfam02770 69 D---APGVSVRRIETKLGVRGLPTG 90
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
112-432 |
4.29e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 59.10 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 112 GSE-RHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATeeFIIhspdfEAAKFWVGNmGKTATHAVVFAKlC 190
Cdd:PLN02526 125 GSEaQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGG--WIL-----NGQKRWIGN-STFADVLVIFAR-N 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 191 VPGDQCHGlhpFIVQiRDPktllpmPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLnrmgdvtpegTYVSPFKDVR 270
Cdd:PLN02526 196 TTTNQING---FIVK-KGA------PGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL----------PGVNSFQDTN 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 271 QrfgaslgSLSSGRVsIVSLAILNLKLAV-AIALRFSATRRQFGpteeeeIPVLEYPMQQWRLLPYLAAVYAldhfsksL 349
Cdd:PLN02526 256 K-------VLAVSRV-MVAWQPIGISMGVyDMCHRYLKERKQFG------APLAAFQINQEKLVRMLGNIQA-------M 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 350 FLDLVELQRGLASGDRSARQAELGReihalasaskplaSWTTQQGIQEC---REACGGHGYLAMNRLGVLRDDNDPNCTY 426
Cdd:PLN02526 315 FLVGWRLCKLYESGKMTPGHASLGK-------------AWITKKARETValgRELLGGNGILADFLVAKAFCDLEPIYTY 381
|
....*.
gi 1771853650 427 EGDNNI 432
Cdd:PLN02526 382 EGTYDI 387
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
108-418 |
1.33e-06 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 51.26 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 108 VYSSGSE-RHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAhyDPATEEFIIHspdfeAAKFWVGNmGKTATHAVVF 186
Cdd:cd01156 95 IYRNGSAaQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--EKKGDRYVLN-----GSKMWITN-GPDADTLVVY 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 187 AKlCVPGDQCHGLHPFIVQirdpktlLPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGdvtpEGTYVspf 266
Cdd:cd01156 167 AK-TDPSAGAHGITAFIVE-------KGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGEN----KGVYV--- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 267 kdvrqrfgaSLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPMQQWRllpyLAAVYALDHFS 346
Cdd:cd01156 232 ---------LMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQ------PIGEFQLVQGK----LADMYTRLNAS 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1771853650 347 KSLfldLVELQRGLASGDRSARQAelgreihalASA---SKPLASWTTQQGIQecreACGGHGYL---AMNRLgvLRD 418
Cdd:cd01156 293 RSY---LYTVAKACDRGNMDPKDA---------AGVilyAAEKATQVALDAIQ----ILGGNGYIndyPTGRL--LRD 352
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
273-434 |
1.86e-05 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 44.94 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 273 FGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPMQQWRLLPYLAAVYALdhfsKSLFLd 352
Cdd:pfam00441 4 FRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGR------PLIDFQLVRHKLAEMAAEIEAA----RLLVY- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 353 lvelqrglasgdRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNI 432
Cdd:pfam00441 73 ------------RAAEALDAGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEI 140
|
..
gi 1771853650 433 LL 434
Cdd:pfam00441 141 QR 142
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
108-432 |
2.33e-04 |
|
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD 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. MCAD is a homotetramer.
Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 44.11 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 108 VYSSGS-ERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAhyDPATEEFIIHspdfeAAKFWVGNMGKtATHAVVF 186
Cdd:cd01157 93 VIISGNdEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITNGGK-ANWYFLL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 187 AKlCVPGDQCHGLHPFIVQIRDPKTllpmPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLnrmgdvTPEGTyvspf 266
Cdd:cd01157 165 AR-SDPDPKCPASKAFTGFIVEADT----PGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVL------IGEGA----- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 267 kdvrqRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeipvleyPMQQWRLLPYLAAVYALDhfs 346
Cdd:cd01157 229 -----GFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGK-----------LIAEHQAVSFMLADMAMK--- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853650 347 kslfldlVELQRglASGDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTY 426
Cdd:cd01157 290 -------VELAR--LAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIY 360
|
....*.
gi 1771853650 427 EGDNNI 432
Cdd:cd01157 361 EGTSQI 366
|
|
| |
