|
Name |
Accession |
Description |
Interval |
E-value |
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
19-636 |
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: 848.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 19 GPLDAYRARASFSWKELALFTEG-EGMLRFKKTIFSALENDPLFARspgADLSLEKYRELNFLRCKRIFEYDFLSVEDMF 97
Cdd:cd01150 1 PDLDKERASATFDWKALTHILEGgEENLRRKREVERELESDPLFQR---ELPSKHLSREELYEELKRKAKTDVERMGELM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 98 KS-PLKVPALIQCLGMYDSSLAAKYLLHSLVFGSAVYSSGSERHLTYIQKIFRM-EIFGCFALTELSHGSNTKAIRTTAH 175
Cdd:cd01150 78 ADdPEKMLALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNlEIIGCFAQTELGHGSNLQGLETTAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 176 YDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGdQCHGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQNG 255
Cdd:cd01150 158 YDPLTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPG-KNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMGLNG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 256 LDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQ 335
Cdd:cd01150 237 VDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 336 FGPT-EEEEIPVLEYPMQQWRLLPYLAAVYALDHFSKSLFLDLVELQRGLASGDrsarqAELGREIHALASASKPLASWT 414
Cdd:cd01150 317 FGPKpSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGN-----SELLAELHALSAGLKAVATWT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 415 TQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVHdgacfrsplksvdfldaypg 494
Cdd:cd01150 392 AAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAFS-------------------- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 495 ildqkfevssvadcldSAVALAAYKWLVCYLLRETYQKLNQEKRSGSSDFEARNKCQVsHGRPLALAFVELTVVQRFHEH 574
Cdd:cd01150 452 ----------------LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQV-HLRCAAKAHTEYTVLQRFHES 514
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853648 575 VHQpSVPPSLRAVLGRLSALYALWSLSRHAALLYRgGYFSGEQAGEVLESAVLALCSQLYKN 636
Cdd:cd01150 515 VEE-IVDPSVRAVLKRLCDLYALWLLEEHIADFLE-GGFLGGQDVKAVREALLALLPQLRPD 574
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
28-633 |
7.33e-117 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 364.86 E-value: 7.33e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 28 ASFSWKELALFTEGEGmLRFKKTIFSALENDPLFAR---------SPGADLSLEKYRELNFlrcKRIFeydFLSVEDMFK 98
Cdd:PLN02312 49 YAFDVKEMRKLLDGHN-LEDRDWLFGLMMQSDLFNSkrrggrvfvSPDYNQTMEQQREITM---KRIL---YLLERGVFR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 99 ---------SPLKVPALIQCLGMYDSSLAAKYLLHSLVFGSAVYSSGSERHL-TYIQKIFRMEIFGCFALTELSHGSNTK 168
Cdd:PLN02312 122 gwltetgpeAELRKLALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHdKWLKDTEDYVVKGCFAMTELGHGSNVR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 169 AIRTTAHYDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGDQcHGLHPFIVQIRDPKTLLpMPGVMVGDIG 248
Cdd:PLN02312 202 GIETVTTYDPKTEEFVINTPCESAQKYWIGGAANHATHTIVFSQLHINGKN-EGVHAFIAQIRDQDGNI-CPNIRIADCG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 249 KKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALR 328
Cdd:PLN02312 280 HKIGLNGVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 329 FSATRRQFGPTEEE-EIPVLEYPMQQWRLLPYLAAVYALD---HFSKSLFLDlvelqrglasgdrsaRQAELGREIHALA 404
Cdd:PLN02312 360 YSLSRRAFSVTPNGpEVLLLDYPSHQRRLLPLLAKTYAMSfaaNDLKMIYVK---------------RTPESNKAIHVVS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 405 SASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAhqvhdgACFR--SP 482
Cdd:PLN02312 425 SGFKAVLTWHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAEYV------SAKKrnKP 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 483 LK--SVDFLDAYPGILDQKFEVSSVAdclDSAVALAAYkwlvCYLLRETYQKLNQEKRSGSSDFEARNKCQVSH---GRP 557
Cdd:PLN02312 499 FKglGLEHMNGPRPVIPTQLTSSTLR---DSQFQLNLF----CLRERDLLERFASEVSELQSKGESREFAFLLSyqlAED 571
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853648 558 LALAFVELTVVQRFHEhVHQPSVPPSLRAVLGRLSALYALWSLSRHAALLyRGGYFSGEQAGEVlESAVLALCSQL 633
Cdd:PLN02312 572 LGRAFSERAILQTFLD-AEANLPTGSLKDVLGLLRSLYVLISLDEDPSFL-RYGYLSPDNVALV-RKEVAKLCGEL 644
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
68-597 |
1.96e-101 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 324.89 E-value: 1.96e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 68 DLSLEKYRELNFLRCKRIF-EYDFLSVEDMFKSPLKVPALIQCLGMYDSSLAAKYLLHSLVFGSAVYSSGSERHL-TYIQ 145
Cdd:PLN02636 87 EISKDEHRELCMRQLTGLVrEAGIRPMKYLVEDPAKYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRdKYFD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 146 KIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVP-----GDQC 220
Cdd:PLN02636 167 GIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINTPNDGAIKWWIGNAAVHGKFATVFARLKLPthdskGVSD 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 221 HGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGAS 300
Cdd:PLN02636 247 MGVHAFIVPIRDMKTHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGDVSRDGKYTSSLPTINKRFAAT 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 301 LGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEEEIPVLEYPMQQWRLLPYLAAVYALdHFSKSLfldLVEL 380
Cdd:PLN02636 327 LGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPKQPEISILDYQSQQHKLMPMLASTYAF-HFATEY---LVER 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 381 QrglaSGDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQ 460
Cdd:PLN02636 403 Y----SEMKKTHDDQLVADVHALSAGLKAYITSYTAKALSTCREACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQ 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 461 TSNYLLGLLAHQVHDGACFRSPLKSVDFLDAYpgiLDQKFEVSS----VADCLDSAVALAAYKWLVCYLLRETYQKLNQE 536
Cdd:PLN02636 479 VAADLLKQYKEKFQGGTLSVTWNYLRESMNTY---LSQPNPVTTrwegEEHLRDPKFQLDAFRYRTSRLLQTAALRLRKH 555
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1771853648 537 -KRSGSsdFEARNKCqVSHGRPLALAFVELTVVQRFHEHVhQPSVPPSLRAVLGRLSALYAL 597
Cdd:PLN02636 556 sKTLGS--FGAWNRC-LNHLLTLAESHIESVILAKFIEAV-ERCPDRSTRAALKLVCDLYAL 613
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
57-641 |
4.11e-97 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 312.54 E-value: 4.11e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 57 NDPLFARSPGADLSLEkyrEL--NFLR-----CKRIFEYDfLSVEDMFKSPLKV--PALIQclgmydsslaakylLHSLV 127
Cdd:PLN02443 44 SDPVFSKDNRTRLSRK---ELfkNTLRkaahaWKRIIELR-LTEEEAGKLRSFVdePGYTD--------------LHWGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 128 FGSAVYSSGS-ERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFIIHSPDFEAAKFWVGNMGKTATH 206
Cdd:PLN02443 106 FVPAIKGQGTeEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHSPTLTSSKWWPGGLGKVSTH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 207 AVVFAKLCVPGDQcHGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQ---NGLDNGFAMFHKVRVPRQSLLNRMGDVTPE 283
Cdd:PLN02443 186 AVVYARLITNGKD-HGIHGFIVQLRSLDDHSPLPGVTVGDIGMKFGNgayNTMDNGFLRFDHVRIPRDQMLMRLSKVTRE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 284 GTYVSpfKDVRQRFGasLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEE-EIPVLEYPMQQWRLLPYLAA 362
Cdd:PLN02443 265 GKYVQ--SDVPRQLV--YGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFGSQDGGpETQVIDYKTQQSRLFPLLAS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 363 VYA---LDHFSKSLFLDLVelQRgLASGDRSARQaelgrEIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGV 439
Cdd:PLN02443 341 AYAfrfVGEWLKWLYTDVT--QR-LEANDFSTLP-----EAHACTAGLKSLTTSATADGIEECRKLCGGHGYLCSSGLPE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 440 LRDDNDPNCTYEGDNNILLQQTSNYLLGLLAhQVHDGacfRSPLKSVDFLDAYPGILDQKFEVSSVADCLDSAVALAAYK 519
Cdd:PLN02443 413 LFAVYVPACTYEGDNVVLLLQVARFLMKTVS-QLGSG---KKPVGTTAYMGRVQHLLQCRCGVQTAEDWLNPSVVLEAFE 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 520 WLVCYLLRETYQKLNQeKRSGSSDFEARNKCQVShgrpLALAFVELTVVQRFHEHVHQPSVPPSLRAVLGRLSALYALWS 599
Cdd:PLN02443 489 ARAARMAVTCAQNLSK-FENQEAGFQELSADLVE----AAVAHCQLIVVSKFIEKLQQDIPGKGVKKQLQNLCYIYALYL 563
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1771853648 600 LSRHAALLYRGGYFSGEQAgevlesavlALCSQLYKNLWGAV 641
Cdd:PLN02443 564 LHKHLGDFLSTGCITPKQA---------SLANDQLRSLYSQV 596
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
146-617 |
4.16e-73 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 248.61 E-value: 4.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 146 KIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGdQCHGLHP 225
Cdd:PTZ00460 121 SLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHTPSVEAVKFWPGELGFLCNFALVYAKLIVNG-KNKGVHP 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 226 FIVQIRDPKTLLPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYvspfkdvrQRFG---ASLG 302
Cdd:PTZ00460 200 FMVRIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLARYIKVSEDGQV--------ERQGnpkVSYA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 303 SLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEEEIPVLEYPMQQWRLLPYLAAVYALDhFSKSLFLDLVELQ- 381
Cdd:PTZ00460 272 SMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNDNKQENSVLEYQTQQQKLLPLLAEFYACI-FGGLKIKELVDDNf 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 382 RGLASGDRSARQaelgrEIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQT 461
Cdd:PTZ00460 351 NRVQKNDFSLLQ-----LTHAILSAAKANYTYFVSNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQL 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 462 SNYLLGLLAHQVhdgacfrSPLKSV----DFLDAYPGILDQKFEVSSVADCLDSAVALaaykwlvcyLLRETYQKLNQEK 537
Cdd:PTZ00460 426 ARYLLKQLQHAV-------QKPEKVpeyfNFLSHITEKLADQTTIESLGQLLGLNCTI---------LTIYAAKKIMDHI 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 538 RSGSSDFEARNKCQVSHGRPLALAFVELTVVQRFHEHVHQPSvpPSLRAVLGRLSALYALWSLSRHAALLYRGGYFSGEQ 617
Cdd:PTZ00460 490 NTGKDFQQSWDTKSGIALASAASRFIEYFNYLCFLDTINNAN--KSTKEILTQLADLYGITMLLNNPQGLIEKGQITVEQ 567
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
110-468 |
8.86e-41 |
|
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: 153.07 E-value: 8.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 110 LGMYDSSLAAKYLLHSlVFGSAVYSSGSERHL-TYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPatEEFIIHsp 188
Cdd:COG1960 76 LARADASLALPVGVHN-GAAEALLRFGTEEQKeRYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDG--DGYVLN-- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 189 dfeAAKFWVGNmGKTATHAVVFAKLcVPGDQCHGLHPFIVqirdPKtllPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRV 268
Cdd:COG1960 151 ---GQKTFITN-APVADVILVLART-DPAAGHRGISLFLV----PK---DTPGVTVGRIEDKMGLRGSDTGELFFDDVRV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 269 PRQsllNRMGDvtpEGtyvspfkdvrQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLE 348
Cdd:COG1960 219 PAE---NLLGE---EG----------KGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGR------PIAD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 349 YPMQQWRLLPYLAAVYALdhfskslfldlvelqRGLAsgDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGG 428
Cdd:COG1960 277 FQAVQHRLADMAAELEAA---------------RALV--YRAAWLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGG 339
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1771853648 429 HGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGL 468
Cdd:COG1960 340 YGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
|
|
| ACOX |
pfam01756 |
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ... |
510-665 |
9.74e-39 |
|
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: 141.14 E-value: 9.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 510 DSAVALAAYKWLVCYLLRETYQKLNQEKRSGSSDFEARNKCQVSHgRPLALAFVELTVVQRFHEHVHQpSVPPSLRAVLG 589
Cdd:pfam01756 1 DPEVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNNQSVEL-VRAAKAHAEYFVLRTFVERLST-SLDPPLKPVLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 590 RLSALYALWSLSRHAALLYRGGYFSGEQAGEVLEsAVLALCSQL-----------------------------YKNLWGA 640
Cdd:pfam01756 79 KLCKLYALWTIEKHLGDFLQGGYLSPEQIDLIRE-AILELLAELrpnavalvdafdfpdfilnsalgrydgnvYENLFEW 157
|
170 180
....*....|....*....|....*
gi 1771853648 641 VLQESKVLERASWWPEFSvnKPVIG 665
Cdd:pfam01756 158 AKKNPLNTEVPPSYHEYL--KPLLK 180
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
143-460 |
2.23e-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: 127.79 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 143 YIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPatEEFIIHSpdfeaAKFWVGNmGKTATHAVVFAKLCVPGDQCHG 222
Cdd:cd00567 60 YLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDG--DGYVLNG-----RKIFISN-GGDADLFIVLARTDEEGPGHRG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 223 LHPFIVqirdPKTllpMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVtpegtyvspfkdvrqrFGASLG 302
Cdd:cd00567 132 ISAFLV----PAD---TPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGG----------------FELAMK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 303 SLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPMQQWRLLPYLAAVYALDHFskslfldlvelqr 382
Cdd:cd00567 189 GLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGK------PLAEFQAVQFKLADMAAELEAARLL------------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 383 glasGDRSARQAELGR-EIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLG-VLRDDNdPNCTYEGDNNILLQQ 460
Cdd:cd00567 250 ----LYRAAWLLDQGPdEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVErYLRDAR-AARIAEGTAEIQRLI 324
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
114-337 |
1.63e-17 |
|
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: 85.10 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 114 DSSLAAKYLLH-SLVFGsAVYSSGSE-RHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATeeFIIHspdfe 191
Cdd:cd01151 87 DSGYRSFMSVQsSLVML-PIYDFGSEeQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGG--YKLN----- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 192 AAKFWVGNmGKTATHAVVFAKlCVPGDQCHGlhpFIVQiRDpktllpMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQ 271
Cdd:cd01151 159 GSKTWITN-SPIADVFVVWAR-NDETGKIRG---FILE-RG------MKGLSAPKIQGKFSLRASITGEIVMDNVFVPEE 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853648 272 SLLnrmgdvtPEGTYvspfkdvrqrFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFG 337
Cdd:cd01151 227 NLL-------PGAEG----------LRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFG 275
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
113-467 |
1.75e-17 |
|
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: 84.63 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 113 YDSSLAAKYLLHSLVFGSAVYSSGSE-RHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDpaTEEFIIHspdfe 191
Cdd:cd01158 73 VDASVAVIVSVHNSLGANPIIKFGTEeQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKD--GDDYVLN----- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 192 AAKFWVGNMGKtATHAVVFAKlCVPGDQCHGLHPFIVqirdPKtllPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQ 271
Cdd:cd01158 146 GSKMWITNGGE-ADFYIVFAV-TDPSKGYRGITAFIV----ER---DTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 272 SLLNRMGdvtpEGtyvspfkdvrqrFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPM 351
Cdd:cd01158 217 NILGEEG----EG------------FKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGK------PIADFQG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 352 QQWRLlpylaAVYALDhfskslfldlVELQRGLasGDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGY 431
Cdd:cd01158 275 IQFKL-----ADMATE----------IEAARLL--TYKAARLKDNGEPFIKEAAMAKLFASEVAMRVTTDAVQIFGGYGY 337
|
330 340 350
....*....|....*....|....*....|....*...
gi 1771853648 432 laMNRLGVLRDDNDPNCT--YEGDNNILLQQTSNYLLG 467
Cdd:cd01158 338 --TKDYPVERYYRDAKITeiYEGTSEIQRLVIAKHLLK 373
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
113-457 |
1.98e-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: 81.75 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 113 YDSSLAAKYLLHSLV-FGSAVYSSGSERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFIIHspdfe 191
Cdd:cd01161 98 MDLGFSVTLGAHQSIgFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKHYVLN----- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 192 AAKFWVGNmGKTATHAVVFAKLCV---PGDQCHGLHPFIVQiRDPKtllpmpGVMVGDIGKKLGQNGLDNGFAMFHKVRV 268
Cdd:cd01161 173 GSKIWITN-GGIADIFTVFAKTEVkdaTGSVKDKITAFIVE-RSFG------GVTNGPPEKKMGIKGSNTAEVYFEDVKI 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 269 PRQSLLNRMGDvtpegtyvspfkdvrqRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLE 348
Cdd:cd01161 245 PVENVLGEVGD----------------GFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGK------KIHE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 349 YPMQQWRLLPYLAAVYALDhfsKSLFLDLVELQRGlasgdrsarqaeLGREIHALASASKPLASWTTQQGIQECREACGG 428
Cdd:cd01161 303 FGLIQEKLANMAILQYATE---SMAYMTSGNMDRG------------LKAEYQIEAAISKVFASEAAWLVVDEAIQIHGG 367
|
330 340
....*....|....*....|....*....
gi 1771853648 429 HGYLAMNRLGVLRDDNDPNCTYEGDNNIL 457
Cdd:cd01161 368 MGFMREYGVERVLRDLRIFRIFEGTNEIL 396
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
112-466 |
2.53e-11 |
|
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: 65.98 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 112 MYDSSLAAKYLLHSLVFGSAVYSSGSERHLT-YIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDpaTEEFIIHspdf 190
Cdd:cd01160 71 ARAGGSGPGLSLHTDIVSPYITRAGSPEQKErVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKD--GDHYVLN---- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 191 eAAKFWVGNmGKTATHAVVFAKLCVPGDQCHGLHPFIVQiRDpktllpMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPR 270
Cdd:cd01160 145 -GSKTFITN-GMLADVVIVVARTGGEARGAGGISLFLVE-RG------TPGFSRGRKLKKMGWKAQDTAELFFDDCRVPA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 271 QSLLNRMGdvtpegtyvspfkdvrQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTeeeeipvleyp 350
Cdd:cd01160 216 ENLLGEEN----------------KGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKT----------- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 351 mqqwrllpyLAAVYALDHfskslflDLVELQRGLASG----DRSARQAELGREIHALASASKPLASWTTQQGIQECREAC 426
Cdd:cd01160 269 ---------LAQLQVVRH-------KIAELATKVAVTraflDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECVQLH 332
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1771853648 427 GGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLL 466
Cdd:cd01160 333 GGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
114-456 |
1.24e-10 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 64.10 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 114 DSSLAAKYLLHSLVFGSAVYSSGSE-RHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATeeFIIhspdfEA 192
Cdd:PLN02526 103 DASCSTFILVHSSLAMLTIALCGSEaQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGG--WIL-----NG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 193 AKFWVGNmGKTATHAVVFAKlCVPGDQCHGlhpFIVQiRDPktllpmPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQS 272
Cdd:PLN02526 176 QKRWIGN-STFADVLVIFAR-NTTTNQING---FIVK-KGA------PGLKATKIENKIGLRMVQNGDIVLKDVFVPDED 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 273 LLnrmgdvtpegTYVSPFKDVRQrfgaslgSLSSGRVsIVSLAILNLKLAV-AIALRFSATRRQFGpteeeeIPVLEYPM 351
Cdd:PLN02526 244 RL----------PGVNSFQDTNK-------VLAVSRV-MVAWQPIGISMGVyDMCHRYLKERKQFG------APLAAFQI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 352 QQWRLLPYLAAVYAldhfsksLFLDLVELQRGLASGDRSARQAELGReihalasaskplaSWTTQQGIQEC---REACGG 428
Cdd:PLN02526 300 NQEKLVRMLGNIQA-------MFLVGWRLCKLYESGKMTPGHASLGK-------------AWITKKARETValgRELLGG 359
|
330 340
....*....|....*....|....*...
gi 1771853648 429 HGYLAMNRLGVLRDDNDPNCTYEGDNNI 456
Cdd:PLN02526 360 NGILADFLVAKAFCDLEPIYTYEGTYDI 387
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
155-259 |
4.09e-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: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 155 CFALTELSHGSNTKAIRTTAhYDPATEEFIIHspdfeAAKFWVGNmGKTATHAVVFAKLcVPGDQCHGLHPFIVqirdPK 234
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLN-----GTKWWITN-AGIADLFLVLART-GGDDRHGGISLFLV----PK 68
|
90 100
....*....|....*....|....*
gi 1771853648 235 TllpMPGVMVGDIGKKLGQNGLDNG 259
Cdd:pfam02770 69 D---APGVSVRRIETKLGVRGLPTG 90
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
99-433 |
3.39e-08 |
|
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: 55.91 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 99 SPLKVPALIQCLGMYDSSLAAKYLLHSLVFGS-AVYSSGSERHlTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYD 177
Cdd:cd01162 61 SRLDASIIFEALSTGCVSTAAYISIHNMCAWMiDSFGNDEQRE-RFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVRE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 178 paTEEFIIhspdfEAAKFWVGNMGKTATHaVVFAKlcVPGDQCHGLHPFIVqirdPKTllpMPGVMVGDIGKKLGQNGLD 257
Cdd:cd01162 140 --GDHYVL-----NGSKAFISGAGDSDVY-VVMAR--TGGEGPKGISCFVV----EKG---TPGLSFGANEKKMGWNAQP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 258 NGFAMFHKVRVPRQsllNRMGdvtPEGtyvspfkdvrQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFG 337
Cdd:cd01162 203 TRAVIFEDCRVPVE---NRLG---GEG----------QGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 338 PteeeeiPVLEYPMQQWRLlpylaAVYALDHFSKSLFLDLVELQrgLASGDRSARqaelgreihALASASKPLAswtTQQ 417
Cdd:cd01162 267 K------PLADFQALQFKL-----ADMATELVASRLMVRRAASA--LDRGDPDAV---------KLCAMAKRFA---TDE 321
|
330
....*....|....*....
gi 1771853648 418 GIQECREAC---GGHGYLA 433
Cdd:cd01162 322 CFDVANQALqlhGGYGYLK 340
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
116-442 |
1.00e-07 |
|
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: 54.72 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 116 SLAAKYLLHSLVFGSAVYSSGSE-RHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAhyDPATEEFIIHspdfeAAK 194
Cdd:cd01156 79 SVALSYGAHSNLCINQIYRNGSAaQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--EKKGDRYVLN-----GSK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 195 FWVGNmGKTATHAVVFAKlCVPGDQCHGLHPFIVQirdpktlLPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLL 274
Cdd:cd01156 152 MWITN-GPDADTLVVYAK-TDPSAGAHGITAFIVE-------KGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENIL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 275 NRMGdvtpEGTYVspfkdvrqrfgaSLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPMQQW 354
Cdd:cd01156 223 GGEN----KGVYV------------LMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQ------PIGEFQLVQG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 355 RllpyLAAVYALDHFSKSLfldLVELQRGLASGDRSARQAelgreihalASA---SKPLASWTTQQGIQecreACGGHGY 431
Cdd:cd01156 281 K----LADMYTRLNASRSY---LYTVAKACDRGNMDPKDA---------AGVilyAAEKATQVALDAIQ----ILGGNGY 340
|
330
....*....|....
gi 1771853648 432 L---AMNRLgvLRD 442
Cdd:cd01156 341 IndyPTGRL--LRD 352
|
|
| Acyl-CoA_ox_N |
pfam14749 |
Acyl-coenzyme A oxidase N-terminal; Acyl-coenzyme A oxidase consists of three domains. An ... |
31-153 |
1.79e-05 |
|
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: 44.51 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 31 SWKELALFTEG-EGMLRFKKTIFSALENDPLFA-RSPGADLSLEKYRELNFLRCKRIFEYdflsVEDMFKSPLKVPALIQ 108
Cdd:pfam14749 1 DVEELTALLYGgEEKLERRREIESLIESDPEFSkPEDYYFLSREERYERALRKAKRLVKK----LRELQIEDPEETLLLY 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1771853648 109 CLGMYDSSLAakYLLHSLVFGSAVYSSGSERHLTY-IQKIFRMEIF 153
Cdd:pfam14749 77 LRGLLDEGLP--LGLHFGMFIPTLKGQGTDEQQAKwLPLAENFEII 120
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
297-458 |
2.19e-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: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 297 FGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPMQQWRLLPYLAAVYALdhfsKSLFLd 376
Cdd:pfam00441 4 FRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGR------PLIDFQLVRHKLAEMAAEIEAA----RLLVY- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 377 lvelqrglasgdRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNI 456
Cdd:pfam00441 73 ------------RAAEALDAGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEI 140
|
..
gi 1771853648 457 LL 458
Cdd:pfam00441 141 QR 142
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
110-431 |
3.96e-05 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 46.47 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 110 LGMYDSSLAAKYLLHSLVFGSAVYSSGS-ERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDpATEEFIIHsp 188
Cdd:PTZ00461 108 LSKYDPGFCLAYLAHSMLFVNNFYYSASpAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKD-SNGNYVLN-- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 189 dfeAAKFWVGNmGKTATHAVVFAKlcVPGDqchgLHPFIVQirdpktlLPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRV 268
Cdd:PTZ00461 185 ---GSKIWITN-GTVADVFLIYAK--VDGK----ITAFVVE-------RGTKGFTQGPKIDKCGMRASHMCQLFFEDVVV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 269 PRQSLLNRMGdvtpegtyvspfkdvrQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLE 348
Cdd:PTZ00461 248 PAENLLGEEG----------------KGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGK------PISN 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 349 YPMQQwrllPYLAAVYALDHFSKSLfldLVELQRGLASGDrsarQAELGREIHALASAskPLASWTTQQGIQecreACGG 428
Cdd:PTZ00461 306 FGQIQ----RYIAEGYADTEAAKAL---VYSVSHNVHPGN----KNRLGSDAAKLFAT--PIAKKVADSAIQ----VMGG 368
|
...
gi 1771853648 429 HGY 431
Cdd:PTZ00461 369 MGY 371
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
132-456 |
2.31e-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: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 132 VYSSGS-ERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAhyDPATEEFIIHspdfeAAKFWVGNMGKtATHAVVF 210
Cdd:cd01157 93 VIISGNdEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITNGGK-ANWYFLL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 211 AKlCVPGDQCHGLHPFIVQIRDPKTllpmPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLnrmgdvTPEGTyvspf 290
Cdd:cd01157 165 AR-SDPDPKCPASKAFTGFIVEADT----PGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVL------IGEGA----- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 291 kdvrqRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeipvleyPMQQWRLLPYLAAVYALDhfs 370
Cdd:cd01157 229 -----GFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGK-----------LIAEHQAVSFMLADMAMK--- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 371 kslfldlVELQRglASGDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTY 450
Cdd:cd01157 290 -------VELAR--LAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIY 360
|
....*.
gi 1771853648 451 EGDNNI 456
Cdd:cd01157 361 EGTSQI 366
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
106-356 |
4.90e-03 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 39.86 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 106 LIQCLGMYDSSLAA-----KYLLHS-LVFGSAVYSSGSERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAhyDPA 179
Cdd:PLN02519 90 LYHCIAMEEISRASgsvglSYGAHSnLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKA--ERV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 180 TEEFIIHspdfeAAKFWVGNmGKTATHAVVFAKLCVPGDQcHGLHPFIVQirdpktlLPMPGVMVGDIGKKLGQNGLDNG 259
Cdd:PLN02519 168 DGGYVLN-----GNKMWCTN-GPVAQTLVVYAKTDVAAGS-KGITAFIIE-------KGMPGFSTAQKLDKLGMRGSDTC 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853648 260 FAMFHKVRVPRQSLLNRMGdvtpEGTYVspfkdvrqrfgaSLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPt 339
Cdd:PLN02519 234 ELVFENCFVPEENVLGQEG----KGVYV------------MMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGR- 296
|
250
....*....|....*..
gi 1771853648 340 eeeeiPVLEYPMQQWRL 356
Cdd:PLN02519 297 -----PIGEFQFIQGKL 308
|
|
| |
