|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
4-666 |
0e+00 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 1390.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 4 GVDHLAFERNKAQFDVEDMKIIWAGSRQDFELSDRISRLVASDPAFRKDDRTTLDRKELFKNTLRKAAYAWKRINELRLN 83
Cdd:PLN02443 3 GVDHLAGERNKAQFDVDAMKIVWAGSRHAFEVSDRMARLVASDPVFSKDNRTRLSRKELFKNTLRKAAHAWKRIIELRLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 84 EQEAYKLRSFVDQPAFTDLHWGMFVPAIQGQGTDEQQQKWLPLAYRMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEF 163
Cdd:PLN02443 83 EEEAGKLRSFVDEPGYTDLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 164 VIHSPTLTSSKWWPGGLGKISTHAVAYARLIIGGEDHGVHGFIVQLRSLDDHLPLPGITIGDIGMKFGNAAYNTMDNGVL 243
Cdd:PLN02443 163 VIHSPTLTSSKWWPGGLGKVSTHAVVYARLITNGKDHGIHGFIVQLRSLDDHSPLPGVTVGDIGMKFGNGAYNTMDNGFL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 244 RFDHVRIPRNQMLMRVSQVTREGKYVSSNVPRQLVYGTMVNVRQKIVADASVALSRAVCIATRYSAVRRQFGSHNGGLET 323
Cdd:PLN02443 243 RFDHVRIPRDQMLMRLSKVTREGKYVQSDVPRQLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFGSQDGGPET 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 324 QVIDYKTQQARLFPLLASAYAFRFVGGWLKWLYMDVTERLQANDFSTLPEAHACTAGLKSLTTTATADGIEECRKLCGGH 403
Cdd:PLN02443 323 QVIDYKTQQSRLFPLLASAYAFRFVGEWLKWLYTDVTQRLEANDFSTLPEAHACTAGLKSLTTSATADGIEECRKLCGGH 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 404 GYLCSSGLPELFAVYVPACTYEGDNVVLLLQVARHLMKTVSQLGSGNKPVGTTAYMARVEQLMQYHSDVEKAEDWLKPNV 483
Cdd:PLN02443 403 GYLCSSGLPELFAVYVPACTYEGDNVVLLLQVARFLMKTVSQLGSGKKPVGTTAYMGRVQHLLQCRCGVQTAEDWLNPSV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 484 VLEAFEARASRMSVACAQNLSKFANPEEaGFQELAADLVDAAVAHCQLIVVSKFIEKLQQDIPGKGVKKQLEVLCSIYAL 563
Cdd:PLN02443 483 VLEAFEARAARMAVTCAQNLSKFENQEA-GFQELSADLVEAAVAHCQLIVVSKFIEKLQQDIPGKGVKKQLQNLCYIYAL 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 564 FLLHKHLGDFLSTGCINPKQGSLASEQLRNLYSQVRPNAIALVDAFNYTDHYLGSILGRYDGNVYPKLYEEAWKDPLNDS 643
Cdd:PLN02443 562 YLLHKHLGDFLSTGCITPKQASLANDQLRSLYSQVRPNAVALVDAFNYTDHYLGSVLGRYDGNVYPKLYEEAWKDPLNDS 641
|
650 660
....*....|....*....|...
gi 1448281235 644 VVPDGFKEYIQPMLKQQLRNARL 666
Cdd:PLN02443 642 VVPDGYEEYLRPLLKQQLRTARL 664
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
7-637 |
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: 629.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 7 HLAFERNKAQFDVEDMKIIWAGSRQDFELSDRISRLVASDPAF-RKDDRTTLDRKELFKNTLRKAAYAWKRINELRLNEQ 85
Cdd:cd01150 2 DLDKERASATFDWKALTHILEGGEENLRRKREVERELESDPLFqRELPSKHLSREELYEELKRKAKTDVERMGELMADDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 86 EAYK------LRSFVDQPAFTDLHWGMFVPAIQGQGTDEQQQKWLPLAYRMQIIGCYAQTELGHGSNVQGLETTATFDPK 159
Cdd:cd01150 82 EKMLaltnslGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 160 TDEFVIHSPTLTSSKWWPGGLGKISTHAVAYARLIIGGEDHGVHGFIVQLRSLDDHLPLPGITIGDIGMKFGnaaYNTMD 239
Cdd:cd01150 162 TQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPGKNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMG---LNGVD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 240 NGVLRFDHVRIPRNQMLMRVSQVTREGKYVSSNVPRQLVYGTM----VNVRQKIVADASVALSRAVCIATRYSAVRRQFG 315
Cdd:cd01150 239 NGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMlgtrSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 316 SHNGGLETQVIDYKTQQARLFPLLASAYAFRFVGGWLKWLYMDVTERLQANDFSTLPEAHACTAGLKSLTTTATADGIEE 395
Cdd:cd01150 319 PKPSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGNSELLAELHALSAGLKAVATWTAAQGIQE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 396 CRKLCGGHGYLCSSGLPELFAVYVPACTYEGDNVVLLLQVARHLMKtvsqlgsgnkpvgttaymarveqlmqyhsdveKA 475
Cdd:cd01150 399 CREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLK--------------------------------KY 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 476 EDWLKPNVVLEAFEARASRMSVACAQNLSKF----ANPEEAgFQELAADLVDAAVAHCQLIVVSKFIEKLQQDIPgKGVK 551
Cdd:cd01150 447 AQAFSLADYLEAYEWLAAHLLRHAAAQLEKLkksgSGSFEA-RNNSQVHLRCAAKAHTEYTVLQRFHESVEEIVD-PSVR 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 552 KQLEVLCSIYALFLLHKHLGDFLSTGCINPKQGSLASEQLRNLYSQVRPNAIALVDAFNYTDHYLGSILGRYDGNVYPKL 631
Cdd:cd01150 525 AVLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSPIGRYDGDVYENL 604
|
....*.
gi 1448281235 632 YEEAWK 637
Cdd:cd01150 605 FEEARK 610
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
11-666 |
7.78e-146 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 438.51 E-value: 7.78e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 11 ERNKAQFDVEDMKIIWAGSRQDFELSDRISRLVASDPAFRKD-DRTTLDRKELFKNTLRKAAYAWKRINelrLNEQEAYK 89
Cdd:PTZ00460 7 ARKQVQFPVLEMTHLLYGNKEQFETFLERQKFIDNEPMFKVHpDYYNWSRQDQILLNAEKTREAHKHLN---LANPNYYT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 90 LRSFVDQPAF-TDLHWGMFVPAIQGQGTDEQQQKWLPLAYRMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHSP 168
Cdd:PTZ00460 84 PNLLCPQGTFiSTVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 169 TLTSSKWWPGGLGKISTHAVAYARLIIGGEDHGVHGFIVQLRSLDDHLPLPGITIGDIGMKFGnaaYNTMDNGVLRFDHV 248
Cdd:PTZ00460 164 SVEAVKFWPGELGFLCNFALVYAKLIVNGKNKGVHPFMVRIRDKETHKPLQGVEVGDIGPKMG---YAVKDNGFLSFDHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 249 RIPRNQMLMRVSQVTREGKYVSSNVPRqLVYGTMVNVRQKIVADASVALSRAVCIATRYSAVRRQFGSHNGGlETQVIDY 328
Cdd:PTZ00460 241 RIPLDSLLARYIKVSEDGQVERQGNPK-VSYASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNDNKQ-ENSVLEY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 329 KTQQARLFPLLASAYAFRFVGGWLKWLYMDVTERLQANDFSTLPEAHACTAGLKSLTTTATADGIEECRKLCGGHGYLCS 408
Cdd:PTZ00460 319 QTQQQKLLPLLAEFYACIFGGLKIKELVDDNFNRVQKNDFSLLQLTHAILSAAKANYTYFVSNCAEWCRLSCGGHGYAHY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 409 SGLPELFAVYVPACTYEGDNVVLLLQVARHLMKTVSQLGSgnKPVGTTAYMARVEQLMQYHSDVEKAED---WLKPNVVL 485
Cdd:PTZ00460 399 SGLPAIYFDMSPNITLEGENQIMYLQLARYLLKQLQHAVQ--KPEKVPEYFNFLSHITEKLADQTTIESlgqLLGLNCTI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 486 EAFEArASRMsvacAQNLSKFANPEEAGFQELAADLVDAAVAHCQLIVVSKFIEKLQQdiPGKGVKKQLEVLCSIYALFL 565
Cdd:PTZ00460 477 LTIYA-AKKI----MDHINTGKDFQQSWDTKSGIALASAASRFIEYFNYLCFLDTINN--ANKSTKEILTQLADLYGITM 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 566 LHKHLGDFLSTGCINPKQGSLASEQLRNLYSQVRPNAIALVDAFNYTDHYLGSILGRYDGNVYPKLYEEAWKD-PLNDSV 644
Cdd:PTZ00460 550 LLNNPQGLIEKGQITVEQIKLLQETREQLYPIIKPNALGLVEAFGLSDNSLRSLIGCHDGDPYENMYNWASKEnSLNKQQ 629
|
650 660
....*....|....*....|..
gi 1448281235 645 VPDGFKEyiqpmLKQQLRNARL 666
Cdd:PTZ00460 630 VHQGVNY-----LMKMEIKAKL 646
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
115-616 |
2.96e-90 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 295.23 E-value: 2.96e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 115 GTDEQQQKWLPLAYRMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHSPTLTSSKWWPGGLGKISTHAVAYARLI 194
Cdd:PLN02636 156 GTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINTPNDGAIKWWIGNAAVHGKFATVFARLK 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 195 I------GGEDHGVHGFIVQLRSLDDHLPLPGITIGDIGMKFGnaaYNTMDNGVLRFDHVRIPRNQMLMRVSQVTREGKY 268
Cdd:PLN02636 236 LpthdskGVSDMGVHAFIVPIRDMKTHQVLPGVEIRDCGHKVG---LNGVDNGALRFRSVRIPRDNLLNRFGDVSRDGKY 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 269 VSS----NVPRQLVYGTMVNVRQKIVADASVALSRAVCIATRYSAVRRQFGSHNGGlETQVIDYKTQQARLFPLLASAYA 344
Cdd:PLN02636 313 TSSlptiNKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPPKQP-EISILDYQSQQHKLMPMLASTYA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 345 FRFVGGWLKWLYmdvTERLQANDFSTLPEAHACTAGLKSLTTTATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACTY 424
Cdd:PLN02636 392 FHFATEYLVERY---SEMKKTHDDQLVADVHALSAGLKAYITSYTAKALSTCREACGGHGYAAVNRFGSLRNDHDIFQTF 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 425 EGDNVVLLLQVARHLMKTVSQLGSGNKPVGTTAYMArvEQLMQYHSDV-------EKAEDWLKPNVVLEAFEARASRMSV 497
Cdd:PLN02636 469 EGDNTVLLQQVAADLLKQYKEKFQGGTLSVTWNYLR--ESMNTYLSQPnpvttrwEGEEHLRDPKFQLDAFRYRTSRLLQ 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 498 ACAQNLSKFANpEEAGF---QELAADLVDAAVAHCQLIVVSKFIEKLQQdIPGKGVKKQLEVLCSIYALFLLHKHLGDFL 574
Cdd:PLN02636 547 TAALRLRKHSK-TLGSFgawNRCLNHLLTLAESHIESVILAKFIEAVER-CPDRSTRAALKLVCDLYALDRIWKDIGTYR 624
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1448281235 575 STGCINPKQGSLASEQLRNLYSQVRPNAIALVDAFNYTDHYL 616
Cdd:PLN02636 625 NVDYVAPNKAKAIHKLTEYLSFQVRNVAKELVDAFGLPDHVT 666
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
104-619 |
1.82e-80 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 268.95 E-value: 1.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 104 WGmfvPAIQGQGTDEQQQKWLPLAYRMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHSPTLTSSKWWPGGLGKI 183
Cdd:PLN02312 160 WG---GAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINTPCESAQKYWIGGAANH 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 184 STHAVAYARLIIGGEDHGVHGFIVQLRSLDDHLpLPGITIGDIGMKFGnaaYNTMDNGVLRFDHVRIPRNQMLMRVSQVT 263
Cdd:PLN02312 237 ATHTIVFSQLHINGKNEGVHAFIAQIRDQDGNI-CPNIRIADCGHKIG---LNGVDNGRIWFDNLRIPRENLLNSVADVS 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 264 REGKYVSS-NVPRQLVYGTM-------VNVRQKIVADASVALSravcIATRYSAVRRQFGSHNGGLETQVIDYKTQQARL 335
Cdd:PLN02312 313 PDGKYVSAiKDPDQRFGAFLapltsgrVTIAVSAIYSSKVGLA----IAIRYSLSRRAFSVTPNGPEVLLLDYPSHQRRL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 336 FPLLASAYAFRFVGGWLKWLYMDVTerlqandfstlPEA----HACTAGLKSLTTTATADGIEECRKLCGGHGYLCSSGL 411
Cdd:PLN02312 389 LPLLAKTYAMSFAANDLKMIYVKRT-----------PESnkaiHVVSSGFKAVLTWHNMRTLQECREACGGQGLKTENRV 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 412 PELFAVYVPACTYEGDNVVLLLQVARHLM----------KTVSQLG----SGNKPVGTTAYMARVEQLMQYHSDVEKaed 477
Cdd:PLN02312 458 GQLKAEYDVQSTFEGDNNVLMQQVSKALLaeyvsakkrnKPFKGLGlehmNGPRPVIPTQLTSSTLRDSQFQLNLFC--- 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 478 wLKPNVVLEAFearASRMSVACAQNLSKfanpeEAGFQELAADLVDAAVAHCQLIVVSKFIEKlQQDIPGKGVKKQLEVL 557
Cdd:PLN02312 535 -LRERDLLERF---ASEVSELQSKGESR-----EFAFLLSYQLAEDLGRAFSERAILQTFLDA-EANLPTGSLKDVLGLL 604
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1448281235 558 CSIYALFLLHKHlGDFLSTGCINPKQGSLASEQLRNLYSQVRPNAIALVDAFNYTDHYLGSI 619
Cdd:PLN02312 605 RSLYVLISLDED-PSFLRYGYLSPDNVALVRKEVAKLCGELRPHALALVSSFGIPDAFLSPI 665
|
|
| ACOX |
pfam01756 |
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ... |
481-658 |
1.82e-57 |
|
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: 191.99 E-value: 1.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 481 PNVVLEAFEARASRMSVACAQNL----SKFANPEEAgFQELAADLVDAAVAHCQLIVVSKFIEKLQQDIPgKGVKKQLEV 556
Cdd:pfam01756 2 PEVLLKAFEWRAARLLREAAEKLqallKSGKSQFEA-WNNQSVELVRAAKAHAEYFVLRTFVERLSTSLD-PPLKPVLKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 557 LCSIYALFLLHKHLGDFLSTGCINPKQGSLASEQLRNLYSQVRPNAIALVDAFNYTDHYLGSILGRYDGNVYPKLYEEAW 636
Cdd:pfam01756 80 LCKLYALWTIEKHLGDFLQGGYLSPEQIDLIREAILELLAELRPNAVALVDAFDFPDFILNSALGRYDGNVYENLFEWAK 159
|
170 180
....*....|....*....|..
gi 1448281235 637 KDPLNdSVVPDGFKEYIQPMLK 658
Cdd:pfam01756 160 KNPLN-TEVPPSYHEYLKPLLK 180
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
58-437 |
3.93e-45 |
|
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: 163.61 E-value: 3.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 58 DRKELFKNTLRkaAYAWKRINEL-RLNEQEAYKLRSFVDQpaftdLHWGMFVPAIQGQGTDEQQQKWLPLAYRMQIIGCY 136
Cdd:cd00567 1 EEQRELRDSAR--EFAAEELEPYaRERRETPEEPWELLAE-----LGLLLGAALLLAYGTEEQKERYLPPLASGEAIAAF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 137 AQTELGHGSNVQGLETTATFDPktDEFVihsptLTSSKWWPGGlGKISTHAVAYARLIIGGEDH-GVHGFIVQLRSlddh 215
Cdd:cd00567 74 ALTEPGAGSDLAGIRTTARKDG--DGYV-----LNGRKIFISN-GGDADLFIVLARTDEEGPGHrGISAFLVPADT---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 216 lplPGITIGDIGMKFGNAAyntMDNGVLRFDHVRIPRNQMLMrvsqvtREGKYVSsnvprqLVYGTMVNVRQKIVAdASV 295
Cdd:cd00567 142 ---PGVTVGRIWDKMGMRG---SGTGELVFDDVRVPEDNLLG------EEGGGFE------LAMKGLNVGRLLLAA-VAL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 296 ALSRAVC-IATRYSAVRRQFGshnggleTQVIDYKTQQARLFPLLASAYAFRFvggwlkwLYMDVTERLQANDfstlPEA 374
Cdd:cd00567 203 GAARAALdEAVEYAKQRKQFG-------KPLAEFQAVQFKLADMAAELEAARL-------LLYRAAWLLDQGP----DEA 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1448281235 375 HACTAGLKSLTTTATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACTYEGDNVVLLLQVAR 437
Cdd:cd00567 265 RLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| Acyl-CoA_ox_N |
pfam14749 |
Acyl-coenzyme A oxidase N-terminal; Acyl-coenzyme A oxidase consists of three domains. An ... |
18-133 |
2.22e-37 |
|
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: 135.03 E-value: 2.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 18 DVEDMKIIWAGSRQDFELSDRISRLVASDPAFRKD-DRTTLDRKELFKNTLRKAAYAWKRINELRL---NEQEAYKLRSF 93
Cdd:pfam14749 1 DVEELTALLYGGEEKLERRREIESLIESDPEFSKPeDYYFLSREERYERALRKAKRLVKKLRELQIedpEETLLLYLRGL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1448281235 94 VDQPAFTDLHWGMFVPAIQGQGTDEQQQKWLPLAYRMQII 133
Cdd:pfam14749 81 LDEGLPLGLHFGMFIPTLKGQGTDEQQAKWLPLAENFEII 120
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
102-442 |
2.79e-34 |
|
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: 134.58 E-value: 2.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 102 LHWGmFVPAIQGQGTDEQQQKWLPLAYRMQIIGCYAQTELGHGSNVQGLETTATfdPKTDEFVIhsptlTSSKWWPGGlG 181
Cdd:COG1960 89 VHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAV--RDGDGYVL-----NGQKTFITN-A 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 182 KISTHAVAYARLIIGGEDHGVHGFIVqlrslddHLPLPGITIGDIGMKFGnaaYNTMDNGVLRFDHVRIPRNQMLMrvsq 261
Cdd:COG1960 160 PVADVILVLARTDPAAGHRGISLFLV-------PKDTPGVTVGRIEDKMG---LRGSDTGELFFDDVRVPAENLLG---- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 262 vtREGKyvssnvPRQLVYGTMVNVRQKIVADASVALSRAVCIATRYSAVRRQFGSHNGglETQVIdyktqQARLFPLLAS 341
Cdd:COG1960 226 --EEGK------GFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIA--DFQAV-----QHRLADMAAE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 342 AYAFRfvggwlkWLYMDVTERLQANDfstlpEAHACTAGLKSLTTTATADGIEECRKLCGGHGYLCSSGLpELFAVYVPA 421
Cdd:COG1960 291 LEAAR-------ALVYRAAWLLDAGE-----DAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPL-ERLYRDARI 357
|
330 340
....*....|....*....|..
gi 1448281235 422 CT-YEGDNVVLLLQVARHLMKT 442
Cdd:COG1960 358 LTiYEGTNEIQRLIIARRLLGR 379
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
102-439 |
1.19e-16 |
|
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: 82.16 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 102 LHWGMFVPAIQGQGTDEQQQKWLPLAYRMQIIGCYAQTELGHGSNVQGLETTATFDpkTDEFVIH-SPTLTSSKWwpggL 180
Cdd:cd01160 82 LHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKD--GDHYVLNgSKTFITNGM----L 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 181 GKISTHAVayarlIIGGEDHGVHG---FIVQlrslddhLPLPGITIGDIGMKFGNAAYNTMDngvLRFDHVRIPRNQMLm 257
Cdd:cd01160 156 ADVVIVVA-----RTGGEARGAGGislFLVE-------RGTPGFSRGRKLKKMGWKAQDTAE---LFFDDCRVPAENLL- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 258 rvSQVTREGKYVSSNVPRQlvygtmvnvRQKIVADASVALSRAVCIATRYSAVRRQFGSHNGglETQVIDYKTqqARLFP 337
Cdd:cd01160 220 --GEENKGFYYLMQNLPQE---------RLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLA--QLQVVRHKI--AELAT 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 338 LLASAYAFrfvggwlkwLYMDVTERLQANdfstLPEAHACTAglKSLTTTATADGIEECRKLCGGHGYLCSSGLPELFAV 417
Cdd:cd01160 285 KVAVTRAF---------LDNCAWRHEQGR----LDVAEASMA--KYWATELQNRVAYECVQLHGGWGYMREYPIARAYRD 349
|
330 340
....*....|....*....|..
gi 1448281235 418 YVPACTYEGDNVVLLLQVARHL 439
Cdd:cd01160 350 ARVQPIYGGTTEIMKELISRQM 371
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
105-315 |
3.68e-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: 80.87 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 105 GMFvpAIQGQGTDEQQQKWLPLAYRMQIIGCYAQTELGHGSNVQGLETTATFDPKTdefvihsPTLTSSKWWPGGlGKIS 184
Cdd:cd01151 101 VML--PIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGG-------YKLNGSKTWITN-SPIA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 185 THAVAYARLIiggEDHGVHGFIVQlRSlddhlpLPGITIGDIGMKFGNAAYNTmdnGVLRFDHVRIPRNQMLMRVSQVtr 264
Cdd:cd01151 171 DVFVVWARND---ETGKIRGFILE-RG------MKGLSAPKIQGKFSLRASIT---GEIVMDNVFVPEENLLPGAEGL-- 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1448281235 265 egkyvssnvprQLVYGTMVNVRQKIVADASVALSRAVCIATRYSAVRRQFG 315
Cdd:cd01151 236 -----------RGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFG 275
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
115-444 |
4.84e-13 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 71.42 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 115 GTDEQQQKWLPLAYRMQIIGCYAQTELGHGSNVQGLETTATFDPKtdefvihSPTLTSSKWWPGGlgkiSTHA---VAYA 191
Cdd:PLN02526 125 GSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEG-------GWILNGQKRWIGN----STFAdvlVIFA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 192 RliiGGEDHGVHGFIVQLRSlddhlplPGITIGDIGMKFGnaaYNTMDNGVLRFDHVRIPRNQMLMRVSQVTREGKYVSs 271
Cdd:PLN02526 194 R---NTTTNQINGFIVKKGA-------PGLKATKIENKIG---LRMVQNGDIVLKDVFVPDEDRLPGVNSFQDTNKVLA- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 272 nvprqlvygtmvnVRQKIVADASVALSRAVC-IATRYSAVRRQFGShnggletQVIDYKTQQARLFPLLASAYAFRFVGG 350
Cdd:PLN02526 260 -------------VSRVMVAWQPIGISMGVYdMCHRYLKERKQFGA-------PLAAFQINQEKLVRMLGNIQAMFLVGW 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 351 WLKWLYmdvterlqanDFSTLPEAHACTAglKSLTTTATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACTYEGDNVV 430
Cdd:PLN02526 320 RLCKLY----------ESGKMTPGHASLG--KAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDI 387
|
330
....*....|....
gi 1448281235 431 LLLQVARHLMKTVS 444
Cdd:PLN02526 388 NALVTGREITGIAS 401
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
98-256 |
5.34e-13 |
|
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: 71.15 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 98 AFTDLHWGMFVPAIQGQGTDEQQQKWLPLAYRMQIIGCYAQTELGHGSNVQGLETTATFDpkTDEFVIhsptlTSSKWWP 177
Cdd:cd01158 79 VIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKD--GDDYVL-----NGSKMWI 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1448281235 178 GGlGKISTHAVAYARLIIGGEDHGVHGFIVqlrslddHLPLPGITIGDIGMKFGNAAYNTMdngVLRFDHVRIPRNQML 256
Cdd:cd01158 152 TN-GGEADFYIVFAVTDPSKGYRGITAFIV-------ERDTPGLSVGKKEDKLGIRGSSTT---ELIFEDVRVPKENIL 219
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
58-440 |
8.36e-12 |
|
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: 67.47 E-value: 8.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 58 DRKELFK-NTLRKAA-------Y--------AWKRINELRLNEQEAYKLRSFVdqpAFTDLHwGMFVPAIQGQGTDEQQQ 121
Cdd:cd01162 28 DQKKHFPvDVLRKAAelgfggiYirddvggsGLSRLDASIIFEALSTGCVSTA---AYISIH-NMCAWMIDSFGNDEQRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 122 KWLPLAYRMQIIGCYAQTELGHGSNVQGLETTATFDpkTDEFVihsptLTSSKWWPGGLGKISTHAVAyARliIGGED-H 200
Cdd:cd01162 104 RFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVRE--GDHYV-----LNGSKAFISGAGDSDVYVVM-AR--TGGEGpK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 201 GVHGFIVQlrslDDhlpLPGITIGDIGMKFGnaaYNTMDNGVLRFDHVRIPRNQMLmrvsqvTREGKyvSSNVPRQLVYG 280
Cdd:cd01162 174 GISCFVVE----KG---TPGLSFGANEKKMG---WNAQPTRAVIFEDCRVPVENRL------GGEGQ--GFGIAMAGLNG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 281 TMVNvrqkiVADASV-ALSRAVCIATRYSAVRRQFGShnggletQVIDYKTQQARLFPLLASAYAFRFvggwlkwLYMDV 359
Cdd:cd01162 236 GRLN-----IASCSLgAAQAALDLARAYLEERKQFGK-------PLADFQALQFKLADMATELVASRL-------MVRRA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 360 TERLQANDfstlPEAHACTAGLKSLTTTATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACTYEGDNVVLLLQVARHL 439
Cdd:cd01162 297 ASALDRGD----PDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARAL 372
|
.
gi 1448281235 440 M 440
Cdd:cd01162 373 L 373
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
115-321 |
5.35e-11 |
|
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: 65.18 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 115 GTDEQQQKWLPLAYRMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFvihspTLTSSKWW--PGGLGKISThavAYAR 192
Cdd:cd01161 121 GTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKHY-----VLNGSKIWitNGGIADIFT---VFAK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 193 LIIGGED----HGVHGFIVQlRSLDdhlplpGITIGDIGMKFGNAAYNTMDngvLRFDHVRIPRNQMLMRVSqvtrEGKY 268
Cdd:cd01161 193 TEVKDATgsvkDKITAFIVE-RSFG------GVTNGPPEKKMGIKGSNTAE---VYFEDVKIPVENVLGEVG----DGFK 258
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1448281235 269 VSSNVprqlvygtMVNVRQKIVADASVALSRAVCIATRYSAVRRQFGS--HNGGL 321
Cdd:cd01161 259 VAMNI--------LNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKkiHEFGL 305
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
135-246 |
6.70e-11 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 59.22 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 135 CYAQTELGHGSNVQGLETTAtFDPKTDEFVIHsptltSSKWWPGGlGKISTHAVAYARLIIGGEDHGVHGFIVQLRsldd 214
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLN-----GTKWWITN-AGIADLFLVLARTGGDDRHGGISLFLVPKD---- 69
|
90 100 110
....*....|....*....|....*....|..
gi 1448281235 215 hlpLPGITIGDIGMKFGnaaYNTMDNGVLRFD 246
Cdd:pfam02770 70 ---APGVSVRRIETKLG---VRGLPTGELVFD 95
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
84-262 |
3.24e-09 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) 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. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 59.28 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 84 EQEAYKLRSFVDQPAFTDlhwGMFVPAIQGQGTDEQQQKWLPLAYRMQIIGCYAQTELGHGSNVQGLETTATFDpkTDEF 163
Cdd:cd01152 72 REEMAAAGAPVPFNQIGI---DLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRD--GDDW 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 164 VIhsptlTSSKWWpgglgkiSTHAvAYARLIIG-------GEDH-GVHGFIVQLRSlddhlplPGITIGDIGMKFGNAAY 235
Cdd:cd01152 147 VV-----NGQKIW-------TSGA-HYADWAWLlvrtdpeAPKHrGISILLVDMDS-------PGVTVRPIRSINGGEFF 206
|
170 180
....*....|....*....|....*..
gi 1448281235 236 NTMdngvlRFDHVRIPRNqmlMRVSQV 262
Cdd:cd01152 207 NEV-----FLDDVRVPDA---NRVGEV 225
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
103-317 |
3.13e-06 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 49.94 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 103 HWGMFVPAIQGQGTDEQQQKWLPLAYRMQIIGCYAQTELGHGSNVQGLETTATFDpKTDEFVihsptLTSSKWWpgglgk 182
Cdd:PTZ00461 122 HSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKD-SNGNYV-----LNGSKIW------ 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 183 ISTHAVAYARLIIGGEDHGVHGFIVQLRSlddhlplPGITIGDIGMKFGNAAYNTMDngvLRFDHVRIPRNQMLmrvsqv 262
Cdd:PTZ00461 190 ITNGTVADVFLIYAKVDGKITAFVVERGT-------KGFTQGPKIDKCGMRASHMCQ---LFFEDVVVPAENLL------ 253
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1448281235 263 TREGKYvssnvprqlVYGTMVNVRQKIVADASVAL---SRAVCIATRYSAVRRQFGSH 317
Cdd:PTZ00461 254 GEEGKG---------MVGMMRNLELERVTLAAMAVgiaERSVELMTSYASERKAFGKP 302
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
115-257 |
6.80e-04 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) 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. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 42.38 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1448281235 115 GTDEQQQKWL-PLaYRMQIIGCYAQTELG-HGSNVQGLETTATFDpkTDEFVIHSptltsSKWWPGGLG----KIsthAV 188
Cdd:cd01155 108 GSEEQKKQWLePL-LDGKIRSAFAMTEPDvASSDATNIECSIERD--GDDYVING-----RKWWSSGAGdprcKI---AI 176
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1448281235 189 AYARLIIGGED-HGVHGFI-VQLRSlddhlplPGITIGDIGMKFGNaayntMDN----GVLRFDHVRIPRNQMLM 257
Cdd:cd01155 177 VMGRTDPDGAPrHRQQSMIlVPMDT-------PGVTIIRPLSVFGY-----DDAphghAEITFDNVRVPASNLIL 239
|
|
| |
