|
Name |
Accession |
Description |
Interval |
E-value |
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
4-577 |
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: 836.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 4 SPLKVPALIQCLGMYDSSLAAKYLLHSLVFGSAVYSSGSERHLTYIQKIFRM-EIFGCFALTELSHGSNTKAIRTTAHYD 82
Cdd:cd01150 80 DPEKMLALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNlEIIGCFAQTELGHGSNLQGLETTATYD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 83 PATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGdQCHGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQNGLD 162
Cdd:cd01150 160 PLTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPG-KNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMGLNGVD 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 163 NGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFG 242
Cdd:cd01150 239 NGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 243 PT-EEEEIPVLEYPMQQWRLLPYLAAVYALDHFSKSLFLDLVELQRGLASGDrsarqAELGREIHALASASKPLASWTTQ 321
Cdd:cd01150 319 PKpSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGN-----SELLAELHALSAGLKAVATWTAA 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 322 QGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVHdgacfrsplksvdfldaypgil 401
Cdd:cd01150 394 QGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAFS---------------------- 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 402 dqkfevssvadcldSAVALAAYKWLVCYLLRETYQKLNQEKRSGSSDFEARNKCQVsHGRPLALAFVELTVVQRFHEHVH 481
Cdd:cd01150 452 --------------LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQV-HLRCAAKAHTEYTVLQRFHESVE 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 482 QpSVPPSLRAVLGRLSALYALWSLSRHAALLYRgGYFSGEQAGEVLESAVLALCSQLKDDAVALVDVIAPPDFVLDSPIG 561
Cdd:cd01150 517 E-IVDPSVRAVLKRLCDLYALWLLEEHIADFLE-GGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSPIG 594
|
570
....*....|....*.
gi 1771853615 562 RADGELYKNLWGAVLQ 577
Cdd:cd01150 595 RYDGDVYENLFEEARK 610
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
6-560 |
9.22e-120 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 370.26 E-value: 9.22e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 6 LKVPALIQCLGMYDSSLAAKYLLHSLVFGSAVYSSGSERHL-TYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPA 84
Cdd:PLN02312 133 LRKLALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHdKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 85 TEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGDQcHGLHPFIVQIRDPKTLLpMPGVMVGDIGKKLGQNGLDNG 164
Cdd:PLN02312 213 TEEFVINTPCESAQKYWIGGAANHATHTIVFSQLHINGKN-EGVHAFIAQIRDQDGNI-CPNIRIADCGHKIGLNGVDNG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 165 FAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPT 244
Cdd:PLN02312 291 RIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAFSVT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 245 EEE-EIPVLEYPMQQWRLLPYLAAVYALD---HFSKSLFLDlvelqrglasgdrsaRQAELGREIHALASASKPLASWTT 320
Cdd:PLN02312 371 PNGpEVLLLDYPSHQRRLLPLLAKTYAMSfaaNDLKMIYVK---------------RTPESNKAIHVVSSGFKAVLTWHN 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 321 QQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAhqvhdgACFR--SPLK--SVDFLDA 396
Cdd:PLN02312 436 MRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAEYV------SAKKrnKPFKglGLEHMNG 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 397 YPGILDQKFEVSSVAdclDSAVALAAYkwlvCYLLRETYQKLNQEKRSGSSDFEARNKCQVSH---GRPLALAFVELTVV 473
Cdd:PLN02312 510 PRPVIPTQLTSSTLR---DSQFQLNLF----CLRERDLLERFASEVSELQSKGESREFAFLLSyqlAEDLGRAFSERAIL 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 474 QRFHEhVHQPSVPPSLRAVLGRLSALYALWSLSRHAALLyRGGYFSGEQAGEVlESAVLALCSQLKDDAVALVDVIAPPD 553
Cdd:PLN02312 583 QTFLD-AEANLPTGSLKDVLGLLRSLYVLISLDEDPSFL-RYGYLSPDNVALV-RKEVAKLCGELRPHALALVSSFGIPD 659
|
....*..
gi 1771853615 554 FVLdSPI 560
Cdd:PLN02312 660 AFL-SPI 665
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
28-579 |
1.26e-107 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 338.35 E-value: 1.26e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 28 LHSLVFGSAVYSSGS-ERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFIIHSPDFEAAKFWVGNMG 106
Cdd:PLN02443 101 LHWGMFVPAIKGQGTeEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHSPTLTSSKWWPGGLG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 107 KTATHAVVFAKLCVPGDQcHGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQ---NGLDNGFAMFHKVRVPRQSLLNRMG 183
Cdd:PLN02443 181 KVSTHAVVYARLITNGKD-HGIHGFIVQLRSLDDHSPLPGVTVGDIGMKFGNgayNTMDNGFLRFDHVRIPRDQMLMRLS 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 184 DVTPEGTYVSpfKDVRQRFGasLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEE-EIPVLEYPMQQWRLL 262
Cdd:PLN02443 260 KVTREGKYVQ--SDVPRQLV--YGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFGSQDGGpETQVIDYKTQQSRLF 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 263 PYLAAVYA---LDHFSKSLFLDLVelQRgLASGDRSARQaelgrEIHALASASKPLASWTTQQGIQECREACGGHGYLAM 339
Cdd:PLN02443 336 PLLASAYAfrfVGEWLKWLYTDVT--QR-LEANDFSTLP-----EAHACTAGLKSLTTSATADGIEECRKLCGGHGYLCS 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 340 NRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAhQVHDGacfRSPLKSVDFLDAYPGILDQKFEVSSVADCLDSAVA 419
Cdd:PLN02443 408 SGLPELFAVYVPACTYEGDNVVLLLQVARFLMKTVS-QLGSG---KKPVGTTAYMGRVQHLLQCRCGVQTAEDWLNPSVV 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 420 LAAYKWLVCYLLRETYQKLNQeKRSGSSDFEARNKCQVShgrpLALAFVELTVVQRFHEHVHQPSVPPSLRAVLGRLSAL 499
Cdd:PLN02443 484 LEAFEARAARMAVTCAQNLSK-FENQEAGFQELSADLVE----AAVAHCQLIVVSKFIEKLQQDIPGKGVKKQLQNLCYI 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 500 YALWSLSRHAALLYRGGYFSGEQ---AGEVLESavlaLCSQLKDDAVALVDVIAPPDFVLDSPIGRADGELYKNLWGAVL 576
Cdd:PLN02443 559 YALYLLHKHLGDFLSTGCITPKQaslANDQLRS----LYSQVRPNAVALVDAFNYTDHYLGSVLGRYDGNVYPKLYEEAW 634
|
...
gi 1771853615 577 QES 579
Cdd:PLN02443 635 KDP 637
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
5-566 |
8.71e-107 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 336.45 E-value: 8.71e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 5 PLKVPALIQCLGMYDSSLAAKYLLHSLVFGSAVYSSGSERHL-TYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDP 83
Cdd:PLN02636 120 PAKYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRdKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDP 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 84 ATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVP-----GDQCHGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQ 158
Cdd:PLN02636 200 LTDEFVINTPNDGAIKWWIGNAAVHGKFATVFARLKLPthdskGVSDMGVHAFIVPIRDMKTHQVLPGVEIRDCGHKVGL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 159 NGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATR 238
Cdd:PLN02636 280 NGVDNGALRFRSVRIPRDNLLNRFGDVSRDGKYTSSLPTINKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLR 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 239 RQFGPTEEEEIPVLEYPMQQWRLLPYLAAVYALdHFSKSLfldLVELQrglaSGDRSARQAELGREIHALASASKPLASW 318
Cdd:PLN02636 360 QQFGPPKQPEISILDYQSQQHKLMPMLASTYAF-HFATEY---LVERY----SEMKKTHDDQLVADVHALSAGLKAYITS 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 319 TTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVHDGACFRSPLKSVDFLDAYp 398
Cdd:PLN02636 432 YTAKALSTCREACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQYKEKFQGGTLSVTWNYLRESMNTY- 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 399 giLDQKFEVSS----VADCLDSAVALAAYKWLVCYLLRETYQKLNQE-KRSGSsdFEARNKCqVSHGRPLALAFVELTVV 473
Cdd:PLN02636 511 --LSQPNPVTTrwegEEHLRDPKFQLDAFRYRTSRLLQTAALRLRKHsKTLGS--FGAWNRC-LNHLLTLAESHIESVIL 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 474 QRFHEHVhQPSVPPSLRAVLGRLSALYALWSLSRHAAlLYRGGYFSGEQAGEVLESAVLALCSQLKDDAVALVDVIAPPD 553
Cdd:PLN02636 586 AKFIEAV-ERCPDRSTRAALKLVCDLYALDRIWKDIG-TYRNVDYVAPNKAKAIHKLTEYLSFQVRNVAKELVDAFGLPD 663
|
570
....*....|...
gi 1771853615 554 FVLDSPIGRADGE 566
Cdd:PLN02636 664 HVTRAPIAMQSGA 676
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
51-581 |
1.03e-79 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 264.40 E-value: 1.03e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 51 KIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGdQCHGLHP 130
Cdd:PTZ00460 121 SLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHTPSVEAVKFWPGELGFLCNFALVYAKLIVNG-KNKGVHP 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 131 FIVQIRDPKTLLPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYvspfkdvrQRFG---ASLG 207
Cdd:PTZ00460 200 FMVRIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLARYIKVSEDGQV--------ERQGnpkVSYA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 208 SLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEEEIPVLEYPMQQWRLLPYLAAVYALDhFSKSLFLDLVELQ- 286
Cdd:PTZ00460 272 SMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNDNKQENSVLEYQTQQQKLLPLLAEFYACI-FGGLKIKELVDDNf 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 287 RGLASGDRSARQaelgrEIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQT 366
Cdd:PTZ00460 351 NRVQKNDFSLLQ-----LTHAILSAAKANYTYFVSNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQL 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 367 SNYLLGLLAHQVhdgacfrSPLKSV----DFLDAYPGILDQKFEVSSVADCLDSAVALaaykwlvcyLLRETYQKLNQEK 442
Cdd:PTZ00460 426 ARYLLKQLQHAV-------QKPEKVpeyfNFLSHITEKLADQTTIESLGQLLGLNCTI---------LTIYAAKKIMDHI 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 443 RSGSSDFEARNKCQVSHGRPLALAFVELTVVQRFHEHVHQPSvpPSLRAVLGRLSALYALWSLSRHAALLYRGGYFSGEQ 522
Cdd:PTZ00460 490 NTGKDFQQSWDTKSGIALASAASRFIEYFNYLCFLDTINNAN--KSTKEILTQLADLYGITMLLNNPQGLIEKGQITVEQ 567
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1771853615 523 AgEVLESAVLALCSQLKDDAVALVDVIAPPDFVLDSPIGRADGELYKNLWGAVLQESKV 581
Cdd:PTZ00460 568 I-KLLQETREQLYPIIKPNALGLVEAFGLSDNSLRSLIGCHDGDPYENMYNWASKENSL 625
|
|
| ACOX |
pfam01756 |
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ... |
415-599 |
3.43e-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: 208.55 E-value: 3.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 415 DSAVALAAYKWLVCYLLRETYQKLNQEKRSGSSDFEARNKCQVSHgRPLALAFVELTVVQRFHEHVHQpSVPPSLRAVLG 494
Cdd:pfam01756 1 DPEVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNNQSVEL-VRAAKAHAEYFVLRTFVERLST-SLDPPLKPVLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 495 RLSALYALWSLSRHAALLYRGGYFSGEQAGEVLEsAVLALCSQLKDDAVALVDVIAPPDFVLDSPIGRADGELYKNLWGA 574
Cdd:pfam01756 79 KLCKLYALWTIEKHLGDFLQGGYLSPEQIDLIRE-AILELLAELRPNAVALVDAFDFPDFILNSALGRYDGNVYENLFEW 157
|
170 180
....*....|....*....|....*
gi 1771853615 575 VLQESKVLERASWWPEFSvnKPVIG 599
Cdd:pfam01756 158 AKKNPLNTEVPPSYHEYL--KPLLK 180
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
15-373 |
4.02e-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: 153.46 E-value: 4.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 15 LGMYDSSLAAKYLLHSlVFGSAVYSSGSERHL-TYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPatEEFIIHsp 93
Cdd:COG1960 76 LARADASLALPVGVHN-GAAEALLRFGTEEQKeRYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDG--DGYVLN-- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 94 dfeAAKFWVGNmGKTATHAVVFAKLcVPGDQCHGLHPFIVqirdPKtllPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRV 173
Cdd:COG1960 151 ---GQKTFITN-APVADVILVLART-DPAAGHRGISLFLV----PK---DTPGVTVGRIEDKMGLRGSDTGELFFDDVRV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 174 PRQsllNRMGDvtpEGtyvspfkdvrQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLE 253
Cdd:COG1960 219 PAE---NLLGE---EG----------KGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGR------PIAD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 254 YPMQQWRLLPYLAAVYALdhfskslfldlvelqRGLAsgDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGG 333
Cdd:COG1960 277 FQAVQHRLADMAAELEAA---------------RALV--YRAAWLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGG 339
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1771853615 334 HGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGL 373
Cdd:COG1960 340 YGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGR 379
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
48-365 |
1.11e-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: 128.17 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 48 YIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPatEEFIIHSpdfeaAKFWVGNmGKTATHAVVFAKLCVPGDQCHG 127
Cdd:cd00567 60 YLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDG--DGYVLNG-----RKIFISN-GGDADLFIVLARTDEEGPGHRG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 128 LHPFIVqirdPKTllpMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVtpegtyvspfkdvrqrFGASLG 207
Cdd:cd00567 132 ISAFLV----PAD---TPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGG----------------FELAMK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 208 SLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPMQQWRLLPYLAAVYALDHFskslfldlvelqr 287
Cdd:cd00567 189 GLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGK------PLAEFQAVQFKLADMAAELEAARLL------------- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 288 glasGDRSARQAELGR-EIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLG-VLRDDNdPNCTYEGDNNILLQQ 365
Cdd:cd00567 250 ----LYRAAWLLDQGPdEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVErYLRDAR-AARIAEGTAEIQRLI 324
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
19-242 |
1.36e-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: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 19 DSSLAAKYLLH-SLVFGsAVYSSGSE-RHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATeeFIIHspdfe 96
Cdd:cd01151 87 DSGYRSFMSVQsSLVML-PIYDFGSEeQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGG--YKLN----- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 97 AAKFWVGNmGKTATHAVVFAKlCVPGDQCHGlhpFIVQiRDpktllpMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQ 176
Cdd:cd01151 159 GSKTWITN-SPIADVFVVWAR-NDETGKIRG---FILE-RG------MKGLSAPKIQGKFSLRASITGEIVMDNVFVPEE 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1771853615 177 SLLnrmgdvtPEGTYvspfkdvrqrFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFG 242
Cdd:cd01151 227 NLL-------PGAEG----------LRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFG 275
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
18-372 |
1.47e-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: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 18 YDSSLAAKYLLHSLVFGSAVYSSGSE-RHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDpaTEEFIIHspdfe 96
Cdd:cd01158 73 VDASVAVIVSVHNSLGANPIIKFGTEeQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKD--GDDYVLN----- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 97 AAKFWVGNMGKtATHAVVFAKlCVPGDQCHGLHPFIVqirdPKtllPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQ 176
Cdd:cd01158 146 GSKMWITNGGE-ADFYIVFAV-TDPSKGYRGITAFIV----ER---DTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 177 SLLNRMGdvtpEGtyvspfkdvrqrFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPM 256
Cdd:cd01158 217 NILGEEG----EG------------FKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGK------PIADFQG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 257 QQWRLlpylaAVYALDhfskslfldlVELQRGLasGDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGY 336
Cdd:cd01158 275 IQFKL-----ADMATE----------IEAARLL--TYKAARLKDNGEPFIKEAAMAKLFASEVAMRVTTDAVQIFGGYGY 337
|
330 340 350
....*....|....*....|....*....|....*...
gi 1771853615 337 laMNRLGVLRDDNDPNCT--YEGDNNILLQQTSNYLLG 372
Cdd:cd01158 338 --TKDYPVERYYRDAKITeiYEGTSEIQRLVIAKHLLK 373
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
18-362 |
1.65e-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: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 18 YDSSLAAKYLLHSLV-FGSAVYSSGSERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFIIHspdfe 96
Cdd:cd01161 98 MDLGFSVTLGAHQSIgFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKHYVLN----- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 97 AAKFWVGNmGKTATHAVVFAKLCV---PGDQCHGLHPFIVQiRDPKtllpmpGVMVGDIGKKLGQNGLDNGFAMFHKVRV 173
Cdd:cd01161 173 GSKIWITN-GGIADIFTVFAKTEVkdaTGSVKDKITAFIVE-RSFG------GVTNGPPEKKMGIKGSNTAEVYFEDVKI 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 174 PRQSLLNRMGDvtpegtyvspfkdvrqRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLE 253
Cdd:cd01161 245 PVENVLGEVGD----------------GFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGK------KIHE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 254 YPMQQWRLLPYLAAVYALDhfsKSLFLDLVELQRGlasgdrsarqaeLGREIHALASASKPLASWTTQQGIQECREACGG 333
Cdd:cd01161 303 FGLIQEKLANMAILQYATE---SMAYMTSGNMDRG------------LKAEYQIEAAISKVFASEAAWLVVDEAIQIHGG 367
|
330 340
....*....|....*....|....*....
gi 1771853615 334 HGYLAMNRLGVLRDDNDPNCTYEGDNNIL 362
Cdd:cd01161 368 MGFMREYGVERVLRDLRIFRIFEGTNEIL 396
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
17-371 |
2.16e-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: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 17 MYDSSLAAKYLLHSLVFGSAVYSSGSERHLT-YIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDpaTEEFIIHspdf 95
Cdd:cd01160 71 ARAGGSGPGLSLHTDIVSPYITRAGSPEQKErVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKD--GDHYVLN---- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 96 eAAKFWVGNmGKTATHAVVFAKLCVPGDQCHGLHPFIVQiRDpktllpMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPR 175
Cdd:cd01160 145 -GSKTFITN-GMLADVVIVVARTGGEARGAGGISLFLVE-RG------TPGFSRGRKLKKMGWKAQDTAELFFDDCRVPA 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 176 QSLLNRMGdvtpegtyvspfkdvrQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTeeeeipvleyp 255
Cdd:cd01160 216 ENLLGEEN----------------KGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKT----------- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 256 mqqwrllpyLAAVYALDHfskslflDLVELQRGLASG----DRSARQAELGREIHALASASKPLASWTTQQGIQECREAC 331
Cdd:cd01160 269 ---------LAQLQVVRH-------KIAELATKVAVTraflDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECVQLH 332
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1771853615 332 GGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLL 371
Cdd:cd01160 333 GGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQMV 372
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
19-361 |
1.06e-10 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 64.10 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 19 DSSLAAKYLLHSLVFGSAVYSSGSE-RHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATeeFIIhspdfEA 97
Cdd:PLN02526 103 DASCSTFILVHSSLAMLTIALCGSEaQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGG--WIL-----NG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 98 AKFWVGNmGKTATHAVVFAKlCVPGDQCHGlhpFIVQiRDPktllpmPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQS 177
Cdd:PLN02526 176 QKRWIGN-STFADVLVIFAR-NTTTNQING---FIVK-KGA------PGLKATKIENKIGLRMVQNGDIVLKDVFVPDED 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 178 LLnrmgdvtpegTYVSPFKDVRQrfgaslgSLSSGRVsIVSLAILNLKLAV-AIALRFSATRRQFGpteeeeIPVLEYPM 256
Cdd:PLN02526 244 RL----------PGVNSFQDTNK-------VLAVSRV-MVAWQPIGISMGVyDMCHRYLKERKQFG------APLAAFQI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 257 QQWRLLPYLAAVYAldhfsksLFLDLVELQRGLASGDRSARQAELGReihalasaskplaSWTTQQGIQEC---REACGG 333
Cdd:PLN02526 300 NQEKLVRMLGNIQA-------MFLVGWRLCKLYESGKMTPGHASLGK-------------AWITKKARETValgRELLGG 359
|
330 340
....*....|....*....|....*...
gi 1771853615 334 HGYLAMNRLGVLRDDNDPNCTYEGDNNI 361
Cdd:PLN02526 360 NGILADFLVAKAFCDLEPIYTYEGTYDI 387
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
60-164 |
3.66e-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: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 60 CFALTELSHGSNTKAIRTTAhYDPATEEFIIHspdfeAAKFWVGNmGKTATHAVVFAKLcVPGDQCHGLHPFIVqirdPK 139
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLN-----GTKWWITN-AGIADLFLVLART-GGDDRHGGISLFLV----PK 68
|
90 100
....*....|....*....|....*
gi 1771853615 140 TllpMPGVMVGDIGKKLGQNGLDNG 164
Cdd:pfam02770 69 D---APGVSVRRIETKLGVRGLPTG 90
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
4-338 |
2.89e-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: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 4 SPLKVPALIQCLGMYDSSLAAKYLLHSLVFGS-AVYSSGSERHlTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYD 82
Cdd:cd01162 61 SRLDASIIFEALSTGCVSTAAYISIHNMCAWMiDSFGNDEQRE-RFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVRE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 83 paTEEFIIhspdfEAAKFWVGNMGKTATHaVVFAKlcVPGDQCHGLHPFIVqirdPKTllpMPGVMVGDIGKKLGQNGLD 162
Cdd:cd01162 140 --GDHYVL-----NGSKAFISGAGDSDVY-VVMAR--TGGEGPKGISCFVV----EKG---TPGLSFGANEKKMGWNAQP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 163 NGFAMFHKVRVPRQsllNRMGdvtPEGtyvspfkdvrQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFG 242
Cdd:cd01162 203 TRAVIFEDCRVPVE---NRLG---GEG----------QGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 243 PteeeeiPVLEYPMQQWRLlpylaAVYALDHFSKSLFLDLVELQrgLASGDRSARqaelgreihALASASKPLAswtTQQ 322
Cdd:cd01162 267 K------PLADFQALQFKL-----ADMATELVASRLMVRRAASA--LDRGDPDAV---------KLCAMAKRFA---TDE 321
|
330
....*....|....*....
gi 1771853615 323 GIQECREAC---GGHGYLA 338
Cdd:cd01162 322 CFDVANQALqlhGGYGYLK 340
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
21-347 |
8.63e-08 |
|
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: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 21 SLAAKYLLHSLVFGSAVYSSGSE-RHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAhyDPATEEFIIHspdfeAAK 99
Cdd:cd01156 79 SVALSYGAHSNLCINQIYRNGSAaQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--EKKGDRYVLN-----GSK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 100 FWVGNmGKTATHAVVFAKlCVPGDQCHGLHPFIVQirdpktlLPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLL 179
Cdd:cd01156 152 MWITN-GPDADTLVVYAK-TDPSAGAHGITAFIVE-------KGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENIL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 180 NRMGdvtpEGTYVspfkdvrqrfgaSLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPMQQW 259
Cdd:cd01156 223 GGEN----KGVYV------------LMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQ------PIGEFQLVQG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 260 RllpyLAAVYALDHFSKSLfldLVELQRGLASGDRSARQAelgreihalASA---SKPLASWTTQQGIQecreACGGHGY 336
Cdd:cd01156 281 K----LADMYTRLNASRSY---LYTVAKACDRGNMDPKDA---------AGVilyAAEKATQVALDAIQ----ILGGNGY 340
|
330
....*....|....
gi 1771853615 337 L---AMNRLgvLRD 347
Cdd:cd01156 341 IndyPTGRL--LRD 352
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
202-363 |
1.61e-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: 45.32 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 202 FGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLEYPMQQWRLLPYLAAVYALdhfsKSLFLd 281
Cdd:pfam00441 4 FRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGR------PLIDFQLVRHKLAEMAAEIEAA----RLLVY- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 282 lvelqrglasgdRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNI 361
Cdd:pfam00441 73 ------------RAAEALDAGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEI 140
|
..
gi 1771853615 362 LL 363
Cdd:pfam00441 141 QR 142
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
15-336 |
3.44e-05 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 46.47 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 15 LGMYDSSLAAKYLLHSLVFGSAVYSSGS-ERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDpATEEFIIHsp 93
Cdd:PTZ00461 108 LSKYDPGFCLAYLAHSMLFVNNFYYSASpAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKD-SNGNYVLN-- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 94 dfeAAKFWVGNmGKTATHAVVFAKlcVPGDqchgLHPFIVQirdpktlLPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRV 173
Cdd:PTZ00461 185 ---GSKIWITN-GTVADVFLIYAK--VDGK----ITAFVVE-------RGTKGFTQGPKIDKCGMRASHMCQLFFEDVVV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 174 PRQSLLNRMGdvtpegtyvspfkdvrQRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeiPVLE 253
Cdd:PTZ00461 248 PAENLLGEEG----------------KGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGK------PISN 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 254 YPMQQwrllPYLAAVYALDHFSKSLfldLVELQRGLASGDrsarQAELGREIHALASAskPLASWTTQQGIQecreACGG 333
Cdd:PTZ00461 306 FGQIQ----RYIAEGYADTEAAKAL---VYSVSHNVHPGN----KNRLGSDAAKLFAT--PIAKKVADSAIQ----VMGG 368
|
...
gi 1771853615 334 HGY 336
Cdd:PTZ00461 369 MGY 371
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
37-361 |
2.02e-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: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 37 VYSSGS-ERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAhyDPATEEFIIHspdfeAAKFWVGNMGKtATHAVVF 115
Cdd:cd01157 93 VIISGNdEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITNGGK-ANWYFLL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 116 AKlCVPGDQCHGLHPFIVQIRDPKTllpmPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLnrmgdvTPEGTyvspf 195
Cdd:cd01157 165 AR-SDPDPKCPASKAFTGFIVEADT----PGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVL------IGEGA----- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 196 kdvrqRFGASLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPteeeeipvleyPMQQWRLLPYLAAVYALDhfs 275
Cdd:cd01157 229 -----GFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGK-----------LIAEHQAVSFMLADMAMK--- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 276 kslfldlVELQRglASGDRSARQAELGREIHALASASKPLASWTTQQGIQECREACGGHGYLAMNRLGVLRDDNDPNCTY 355
Cdd:cd01157 290 -------VELAR--LAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIY 360
|
....*.
gi 1771853615 356 EGDNNI 361
Cdd:cd01157 361 EGTSQI 366
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
11-261 |
4.22e-03 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 39.86 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 11 LIQCLGMYDSSLAA-----KYLLHS-LVFGSAVYSSGSERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAhyDPA 84
Cdd:PLN02519 90 LYHCIAMEEISRASgsvglSYGAHSnLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKA--ERV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 85 TEEFIIHspdfeAAKFWVGNmGKTATHAVVFAKLCVPGDQcHGLHPFIVQirdpktlLPMPGVMVGDIGKKLGQNGLDNG 164
Cdd:PLN02519 168 DGGYVLN-----GNKMWCTN-GPVAQTLVVYAKTDVAAGS-KGITAFIIE-------KGMPGFSTAQKLDKLGMRGSDTC 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771853615 165 FAMFHKVRVPRQSLLNRMGdvtpEGTYVspfkdvrqrfgaSLGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPt 244
Cdd:PLN02519 234 ELVFENCFVPEENVLGQEG----KGVYV------------MMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGR- 296
|
250
....*....|....*..
gi 1771853615 245 eeeeiPVLEYPMQQWRL 261
Cdd:PLN02519 297 -----PIGEFQFIQGKL 308
|
|
| |
