|
Name |
Accession |
Description |
Interval |
E-value |
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
3-638 |
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: 914.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 3 PDLRKERAAATFNPELITHILDGSPENTRRRREIENLILNDPDFQHE-DYNFLTRSQRYEVAVKKSATMVKKMREFGIAD 81
Cdd:cd01150 1 PDLDKERASATFDWKALTHILEGGEENLRRKREVERELESDPLFQRElPSKHLSREELYEELKRKAKTDVERMGELMADD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 82 PEEIMWFKNSVHRGH---PEPLDLHLGMFLPTLLHQATEEQQERFFMPAWNLEITGTYAQTEMGHGTHLRGLETTATYDP 158
Cdd:cd01150 81 PEKMLALTNSLGGYDlslGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 159 KTQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITRGECYGLHAFVVPIREIGTHKPLPGITVGDIGPKFGYEEMDNG 238
Cdd:cd01150 161 LTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPGKNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMGLNGVDNG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 239 YLKMDNYRIPRENMLMKYAQVKPDGTYVKPLSN-KLTYGTMVFVRS----FLVGSAAQSLSKACTIAIRYSAVRRQSEIK 313
Cdd:cd01150 241 FLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDpNKRYGAMLGTRSggrvGLIYDAAMSLKKAATIAIRYSAVRRQFGPK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 314 RSEPEPQILDFQTQQYKLFPLLATAYAFHFLGRYIKETYMRINESIGQGDLSELPELHALTAGLKAFTTWTANAGIEECR 393
Cdd:cd01150 321 PSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGNSELLAELHALSAGLKAVATWTAAQGIQECR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 394 MACGGHGYSHSSGIPNIYVTFTPACTFEGENTVMMLQTARFLMKIYDQVQsgklvggmvsylndlpsqriqpqqvavwpt 473
Cdd:cd01150 401 EACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAF------------------------------ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 474 lvdinSLDSLTEAYKLRAARLVEIAAKNLQAQVSHRKSKEVAWNLTSVDLVRASEAHCHYVTVKVFADKLPKIQDRAVQA 553
Cdd:cd01150 451 -----SLADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQVHLRCAAKAHTEYTVLQRFHESVEEIVDPSVRA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 554 VLRNLCLLYSLYGISQKGGDFLEGNIITGAQMSQVNSRILELLTVTRPNAVALVDAFDFKDVTLGSVLGRYDGNVYENLF 633
Cdd:cd01150 526 VLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSPIGRYDGDVYENLF 605
|
....*
gi 66793429 634 EWAKK 638
Cdd:cd01150 606 EEARK 610
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
5-657 |
0e+00 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 661.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 5 LRKERAAATFNPELITHILDGSPENTRRRREIENLILNDPDFQHEDYNFLTRSQRYEVAVKKSATMVKKMREFGIADpEE 84
Cdd:PLN02443 7 LAGERNKAQFDVDAMKIVWAGSRHAFEVSDRMARLVASDPVFSKDNRTRLSRKELFKNTLRKAAHAWKRIIELRLTE-EE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 85 IMWFKNSVHRghPEPLDLHLGMFLPTLLHQATEEQQERFFMPAWNLEITGTYAQTEMGHGTHLRGLETTATYDPKTQEFI 164
Cdd:PLN02443 86 AGKLRSFVDE--PGYTDLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 165 LNSPTVTSIKWWPGGLGKTSNHAIVLAQLITRGECYGLHAFVVPIREIGTHKPLPGITVGDIGPKFG---YEEMDNGYLK 241
Cdd:PLN02443 164 IHSPTLTSSKWWPGGLGKVSTHAVVYARLITNGKDHGIHGFIVQLRSLDDHSPLPGVTVGDIGMKFGngaYNTMDNGFLR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 242 MDNYRIPRENMLMKYAQVKPDGTYVKP-LSNKLTYGTMVFVRSFLVGSAAQSLSKACTIAIRYSAVRRQSEIKRSEPEPQ 320
Cdd:PLN02443 244 FDHVRIPRDQMLMRLSKVTREGKYVQSdVPRQLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFGSQDGGPETQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 321 ILDFQTQQYKLFPLLATAYAFHFLGRYIKETYMRINESIGQGDLSELPELHALTAGLKAFTTWTANAGIEECRMACGGHG 400
Cdd:PLN02443 324 VIDYKTQQSRLFPLLASAYAFRFVGEWLKWLYTDVTQRLEANDFSTLPEAHACTAGLKSLTTSATADGIEECRKLCGGHG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 401 YSHSSGIPNIYVTFTPACTFEGENTVMMLQTARFLMKIYDQVQSGKLVGGMVSYL---NDLPSQRIQPQQVAVWptlvdI 477
Cdd:PLN02443 404 YLCSSGLPELFAVYVPACTYEGDNVVLLLQVARFLMKTVSQLGSGKKPVGTTAYMgrvQHLLQCRCGVQTAEDW-----L 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 478 NSlDSLTEAYKLRAARLVEIAAKNLqaqvSHRKSKEVAWNLTSVDLVRASEAHCHYVTVKVFADKLPK-IQDRAVQAVLR 556
Cdd:PLN02443 479 NP-SVVLEAFEARAARMAVTCAQNL----SKFENQEAGFQELSADLVEAAVAHCQLIVVSKFIEKLQQdIPGKGVKKQLQ 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 557 NLCLLYSLYGISQKGGDFLEGNIITGAQMSQVNSRILELLTVTRPNAVALVDAFDFKDVTLGSVLGRYDGNVYENLFEWA 636
Cdd:PLN02443 554 NLCYIYALYLLHKHLGDFLSTGCITPKQASLANDQLRSLYSQVRPNAVALVDAFNYTDHYLGSVLGRYDGNVYPKLYEEA 633
|
650 660
....*....|....*....|.
gi 66793429 637 KKSPLNKTEVHESYYKHLKPL 657
Cdd:PLN02443 634 WKDPLNDSVVPDGYEEYLRPL 654
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
5-648 |
3.45e-159 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 472.79 E-value: 3.45e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 5 LRKERAAATFNPELITHILDGSPENTRRRREIENLILNDPDFQ-HEDYNFLTRSQRYEVAVKKSATMVKKmreFGIADPE 83
Cdd:PTZ00460 4 LEEARKQVQFPVLEMTHLLYGNKEQFETFLERQKFIDNEPMFKvHPDYYNWSRQDQILLNAEKTREAHKH---LNLANPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 84 eiMWFKNSVHRGHPEPLDLHLGMFLPTLLHQATEEQQERFFMPAWNLEITGTYAQTEMGHGTHLRGLETTATYDPKTQEF 163
Cdd:PTZ00460 81 --YYTPNLLCPQGTFISTVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 164 ILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITRGECYGLHAFVVPIREIGTHKPLPGITVGDIGPKFGYEEMDNGYLKMD 243
Cdd:PTZ00460 159 VIHTPSVEAVKFWPGELGFLCNFALVYAKLIVNGKNKGVHPFMVRIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 244 NYRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGSAAQSLSKACTIAIRYSAVRRQSEIKRSEpEPQILD 323
Cdd:PTZ00460 239 HYRIPLDSLLARYIKVSEDGQVERQGNPKVSYASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNDNKQ-ENSVLE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 324 FQTQQYKLFPLLATAYAFHFLGRYIKETYMRINESIGQGDLSELPELHALTAGLKA-FTTWTANAGiEECRMACGGHGYS 402
Cdd:PTZ00460 318 YQTQQQKLLPLLAEFYACIFGGLKIKELVDDNFNRVQKNDFSLLQLTHAILSAAKAnYTYFVSNCA-EWCRLSCGGHGYA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 403 HSSGIPNIYVTFTPACTFEGENTVMMLQTARFLMKIYDQ-VQSGKLVGGMVSYLNdlpsqriqpqqvAVWPTLVDINSLD 481
Cdd:PTZ00460 397 HYSGLPAIYFDMSPNITLEGENQIMYLQLARYLLKQLQHaVQKPEKVPEYFNFLS------------HITEKLADQTTIE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 482 SLTEAYKLRAARLVEIAAKNLQAQVSHRKSKEVAWNLTS-VDLVRASEAHCHYVTVKVFADKLPKiQDRAVQAVLRNLCL 560
Cdd:PTZ00460 465 SLGQLLGLNCTILTIYAAKKIMDHINTGKDFQQSWDTKSgIALASAASRFIEYFNYLCFLDTINN-ANKSTKEILTQLAD 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 561 LYSLYGISQKGGDFLEGNIITGAQMSQVNSRILELLTVTRPNAVALVDAFDFKDVTLGSVLGRYDGNVYENLFEWA-KKS 639
Cdd:PTZ00460 544 LYGITMLLNNPQGLIEKGQITVEQIKLLQETREQLYPIIKPNALGLVEAFGLSDNSLRSLIGCHDGDPYENMYNWAsKEN 623
|
....*....
gi 66793429 640 PLNKTEVHE 648
Cdd:PTZ00460 624 SLNKQQVHQ 632
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
6-622 |
1.17e-88 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 290.61 E-value: 1.17e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 6 RKERAAATFNPELITHI--LDGSPENTRRRREIENLILND------PDFQHEDYNFLTRSQRYEVAVKKSAT-------- 69
Cdd:PLN02636 20 RIQRLSLHLSPVPLPKEeqLSRLVCARSIKLSVNTEKLSLymrgkhRDIQEKIYEFFNSRPDLQTPVEISKDehrelcmr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 70 -MVKKMREFGI-------ADPEEIMWFKNSVhrGHpepLDLHLGMFL--------PTLLHQATEEQQERFFMPAWNLEIT 133
Cdd:PLN02636 100 qLTGLVREAGIrpmkylvEDPAKYFAITEAV--GS---VDMSLGIKLgvqyslwgGSVINLGTKKHRDKYFDGIDNLDYP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 134 GTYAQTEMGHGTHLRGLETTATYDPKTQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLI-----TRGEC-YGLHAFVV 207
Cdd:PLN02636 175 GCFAMTELHHGSNVQGLQTTATFDPLTDEFVINTPNDGAIKWWIGNAAVHGKFATVFARLKlpthdSKGVSdMGVHAFIV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 208 PIREIGTHKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENMLMKYAQVKPDGTYVK--PLSNK---LTYGTMVFVR 282
Cdd:PLN02636 255 PIRDMKTHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGDVSRDGKYTSslPTINKrfaATLGELVGGR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 283 SFLVGSAAQSLSKACTIAIRYSAVRRQSEIKRsEPEPQILDFQTQQYKLFPLLATAYAFHFLGRYIKETYMRINESigqG 362
Cdd:PLN02636 335 VGLAYGSVGVLKASNTIAIRYSLLRQQFGPPK-QPEISILDYQSQQHKLMPMLASTYAFHFATEYLVERYSEMKKT---H 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 363 DLSELPELHALTAGLKAF-TTWTANAgIEECRMACGGHGYSHSS---GIPNIYVTFTpacTFEGENTVMMLQTARFLMKI 438
Cdd:PLN02636 411 DDQLVADVHALSAGLKAYiTSYTAKA-LSTCREACGGHGYAAVNrfgSLRNDHDIFQ---TFEGDNTVLLQQVAADLLKQ 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 439 YDQvqsgKLVGGMVS----YLNDLPSQRI-QPQQVAV-WPTLVDINSLDSLTEAYKLRAARLVEIAAKNLQAQvSHRKSK 512
Cdd:PLN02636 487 YKE----KFQGGTLSvtwnYLRESMNTYLsQPNPVTTrWEGEEHLRDPKFQLDAFRYRTSRLLQTAALRLRKH-SKTLGS 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 513 EVAWNLTSVDLVRASEAHCHYVTVKVFADKLPKIQDRAVQAVLRNLCLLYSLYGISQKGGDFLEGNIITGAQMSQVNsRI 592
Cdd:PLN02636 562 FGAWNRCLNHLLTLAESHIESVILAKFIEAVERCPDRSTRAALKLVCDLYALDRIWKDIGTYRNVDYVAPNKAKAIH-KL 640
|
650 660 670
....*....|....*....|....*....|.
gi 66793429 593 LELLTV-TRPNAVALVDAFDFKDVTLGSVLG 622
Cdd:PLN02636 641 TEYLSFqVRNVAKELVDAFGLPDHVTRAPIA 671
|
|
| ACOX |
pfam01756 |
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ... |
479-657 |
6.98e-81 |
|
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: 253.62 E-value: 6.98e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 479 SLDSLTEAYKLRAARLVEIAAKNLQAQVSHRKSKEVAWNLTSVDLVRASEAHCHYVTVKVFADKLPKIQDRAVQAVLRNL 558
Cdd:pfam01756 1 DPEVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNNQSVELVRAAKAHAEYFVLRTFVERLSTSLDPPLKPVLKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 559 CLLYSLYGISQKGGDFLEGNIITGAQMSQVNSRILELLTVTRPNAVALVDAFDFKDVTLGSVLGRYDGNVYENLFEWAKK 638
Cdd:pfam01756 81 CKLYALWTIEKHLGDFLQGGYLSPEQIDLIREAILELLAELRPNAVALVDAFDFPDFILNSALGRYDGNVYENLFEWAKK 160
|
170
....*....|....*....
gi 66793429 639 SPLNkTEVHESYYKHLKPL 657
Cdd:pfam01756 161 NPLN-TEVPPSYHEYLKPL 178
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
116-620 |
2.05e-73 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 249.69 E-value: 2.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 116 TEEQQERFFMPAWNLEITGTYAQTEMGHGTHLRGLETTATYDPKTQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLIT 195
Cdd:PLN02312 169 TKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINTPCESAQKYWIGGAANHATHTIVFSQLHI 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 196 RGECYGLHAFVVPIREIGTHKpLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENMLMKYAQVKPDGTYVKPLSNK--- 272
Cdd:PLN02312 249 NGKNEGVHAFIAQIRDQDGNI-CPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPdqr 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 273 -------LTYGtmvfvRSFLVGSAAQSLSKACTIAIRYSAVRRQSEIKRSEPEPQILDFQTQQYKLFPLLATAYAFHFLG 345
Cdd:PLN02312 328 fgaflapLTSG-----RVTIAVSAIYSSKVGLAIAIRYSLSRRAFSVTPNGPEVLLLDYPSHQRRLLPLLAKTYAMSFAA 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 346 RYIKETYMRinesigqgdlsELPE----LHALTAGLKAFTTWTANAGIEECRMACGGHGYSHSSGIPNIYVTFTPACTFE 421
Cdd:PLN02312 403 NDLKMIYVK-----------RTPEsnkaIHVVSSGFKAVLTWHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 422 GENTVMMLQTARFLMKIYDQVQS-GKLVGGM-VSYLNdlpsqriqpQQVAVWPTLVDINSLDSL---TEAYKLRAARLVE 496
Cdd:PLN02312 472 GDNNVLMQQVSKALLAEYVSAKKrNKPFKGLgLEHMN---------GPRPVIPTQLTSSTLRDSqfqLNLFCLRERDLLE 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 497 IAAKNLQAQVSHRKSKEVAWNLT---SVDLVRA-SEAhchyVTVKVFADKLPKIQDRAVQAVLRnlcLLYSLYGIS--QK 570
Cdd:PLN02312 543 RFASEVSELQSKGESREFAFLLSyqlAEDLGRAfSER----AILQTFLDAEANLPTGSLKDVLG---LLRSLYVLIslDE 615
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 66793429 571 GGDFLEGNIITGAQMSQVNSRILELLTVTRPNAVALVDAFDFKDVTLGSV 620
Cdd:PLN02312 616 DPSFLRYGYLSPDNVALVRKEVAKLCGELRPHALALVSSFGIPDAFLSPI 665
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
70-433 |
3.05e-61 |
|
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: 207.14 E-value: 3.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 70 MVKKMREFGiadPEEIMWFKNSVHRGHPEPLDLH----LGMFLPTLLHQATEEQQERFFMPAWNLEITGTYAQTEMGHGT 145
Cdd:cd00567 6 LRDSAREFA---AEELEPYARERRETPEEPWELLaelgLLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 146 HLRGLETTATYDPktQEFILNsptvtSIKWWPGGlGKTSNHAIVLAQLITRG-ECYGLHAFVVPIREigthkplPGITVG 224
Cdd:cd00567 83 DLAGIRTTARKDG--DGYVLN-----GRKIFISN-GGDADLFIVLARTDEEGpGHRGISAFLVPADT-------PGVTVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 225 DIGPKFGYEEMDNGYLKMDNYRIPRENMLMKYAQVKpdgtyvkplsnKLTYGTMVFVRSFLVGSAAQSLSKACTIAIRYS 304
Cdd:cd00567 148 RIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGF-----------ELAMKGLNVGRLLLAAVALGAARAALDEAVEYA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 305 AVRRQseikrsePEPQILDFQTQQYKLFPLLATAYAFHFLGRyikETYMRINEsigqgdlsELPELHALTAGLKAFTTWT 384
Cdd:cd00567 217 KQRKQ-------FGKPLAEFQAVQFKLADMAAELEAARLLLY---RAAWLLDQ--------GPDEARLEAAMAKLFATEA 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 66793429 385 ANAGIEECRMACGGHGYSHSSGIPNIYVTFTPACTFEGENTVMMLQTAR 433
Cdd:cd00567 279 AREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| Acyl-CoA_ox_N |
pfam14749 |
Acyl-coenzyme A oxidase N-terminal; Acyl-coenzyme A oxidase consists of three domains. An ... |
15-132 |
3.37e-47 |
|
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: 162.00 E-value: 3.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 15 NPELITHILDGSPENTRRRREIENLILNDPDFQH-EDYNFLTRSQRYEVAVKKSATMVKKMREFGIADPEEIMWFKNSVH 93
Cdd:pfam14749 1 DVEELTALLYGGEEKLERRREIESLIESDPEFSKpEDYYFLSREERYERALRKAKRLVKKLRELQIEDPEETLLLYLRGL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 66793429 94 RGHPEPLDLHLGMFLPTLLHQATEEQQERFFMPAWNLEI 132
Cdd:pfam14749 81 LDEGLPLGLHFGMFIPTLKGQGTDEQQAKWLPLAENFEI 119
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
99-437 |
8.08e-31 |
|
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: 124.57 E-value: 8.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 99 PLDLHLGmFLPTLLHQATEEQQERFFMPAWNLEITGTYAQTEMGHGTHLRGLETTATYDPktQEFILN-SptvtsiKWWP 177
Cdd:COG1960 86 PVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDG--DGYVLNgQ------KTFI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 178 GGlGKTSNHAIVLAQLITRGECYGLHAFVVPireigthKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENML---- 253
Cdd:COG1960 157 TN-APVADVILVLARTDPAAGHRGISLFLVP-------KDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLgeeg 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 254 --MKYAQvkpdgtyvkplsnkltyGTMVFVRsFLVGSAAQSLSKAC-TIAIRYSAVRRQSeiKRSepepqILDFQTQQYK 330
Cdd:COG1960 229 kgFKIAM-----------------STLNAGR-LGLAAQALGIAEAAlELAVAYAREREQF--GRP-----IADFQAVQHR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 331 LFPLLATAYAFHFLgryikeTYmRINESIGQGDlselpELHALTAGLKAFTTWTANAGIEECRMACGGHGYSHSSGIPNI 410
Cdd:COG1960 284 LADMAAELEAARAL------VY-RAAWLLDAGE-----DAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERL 351
|
330 340 350
....*....|....*....|....*....|
gi 66793429 411 YV---TFTpacTFEGENTVMMLQTARFLMK 437
Cdd:COG1960 352 YRdarILT---IYEGTNEIQRLIIARRLLG 378
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
116-253 |
2.39e-10 |
|
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: 62.76 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 116 TEEQQERFFMPAWNLEITGTYAQTEMGHGTHLRGLETTATYDPKTqeFILNSPtvtsiKWWPGGlGKTSNHAIVLAQLIT 195
Cdd:cd01151 110 SEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGG--YKLNGS-----KTWITN-SPIADVFVVWARNDE 181
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 66793429 196 RGEcygLHAFVVPireigthKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENML 253
Cdd:cd01151 182 TGK---IRGFILE-------RGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL 229
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
135-243 |
8.88e-10 |
|
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: 56.13 E-value: 8.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 135 TYAQTEMGHGTHLRGLETTAtYDPKTQEFILNsptvtSIKWWPGGlGKTSNHAIVLAQLITRGECYGLHAFVVPireigt 214
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLN-----GTKWWITN-AGIADLFLVLARTGGDDRHGGISLFLVP------ 67
|
90 100
....*....|....*....|....*....
gi 66793429 215 hKPLPGITVGDIGPKFGYEEMDNGYLKMD 243
Cdd:pfam02770 68 -KDAPGVSVRRIETKLGVRGLPTGELVFD 95
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
58-433 |
1.34e-09 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 60.59 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 58 QRYEVAVKKSATMVKKMRE---FGIADPEE------------IMWFKNSVHRGHPEPLDLHLGMFLPTLLHQATEEQQER 122
Cdd:cd01160 23 HEWEKAGEVPREVWRKAGEqglLGVGFPEEyggiggdllsaaVLWEELARAGGSGPGLSLHTDIVSPYITRAGSPEQKER 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 123 FFMPAWNLEITGTYAQTEMGHGTHLRGLETTATYDpkTQEFILNSPTV--TSikwwpgglGKTSNHAIVLAQliTRGECY 200
Cdd:cd01160 103 VLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKD--GDHYVLNGSKTfiTN--------GMLADVVIVVAR--TGGEAR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 201 GLHAFVVPIREIGThkplPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENMLMKyaqvkpdgtyvkplSNKLTYGTMVF 280
Cdd:cd01160 171 GAGGISLFLVERGT----PGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGE--------------ENKGFYYLMQN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 281 VRSFLVGSAAQSLSKA---CTIAIRYsaVRRQSEIKRSepepqILDFQTQQYKLFPLLATAYAfhflGRYIKETYMRINE 357
Cdd:cd01160 233 LPQERLLIAAGALAAAefmLEETRNY--VKQRKAFGKT-----LAQLQVVRHKIAELATKVAV----TRAFLDNCAWRHE 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66793429 358 sigQGdlsELPELHALTAglKAFTTWTANAGIEECRMACGGHGYSHSSGIPNIYVTFTPACTFEGENTVMMLQTAR 433
Cdd:cd01160 302 ---QG---RLDVAEASMA--KYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISR 369
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
116-436 |
2.14e-09 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 59.76 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 116 TEEQQERFFMPAWNLEITGTYAQTEMGHGTHLRGLETTATYDpkTQEFILNsptvtSIKWWPGGLGKTSNHaIVLAQliT 195
Cdd:cd01162 98 NDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVRE--GDHYVLN-----GSKAFISGAGDSDVY-VVMAR--T 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 196 RGE-CYGLHAFVVPireigthKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENMLMKYAQvkPDGTYVKPLSnklt 274
Cdd:cd01162 168 GGEgPKGISCFVVE-------KGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQ--GFGIAMAGLN---- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 275 yGTMVFVRSFLVGSAAQSLSKactiAIRYSAVRRQSeikrSEPepqILDFQTQQYKLFPLLATAYAFHFLGRyiketymR 354
Cdd:cd01162 235 -GGRLNIASCSLGAAQAALDL----ARAYLEERKQF----GKP---LADFQALQFKLADMATELVASRLMVR-------R 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 355 INESIGQGDlselPELHALTAGLKAFTTwtaNAGIEECRMAC---GGHGYSHSSGIPNIYVTFTPACTFEGENTVMMLQT 431
Cdd:cd01162 296 AASALDRGD----PDAVKLCAMAKRFAT---DECFDVANQALqlhGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLII 368
|
....*
gi 66793429 432 ARFLM 436
Cdd:cd01162 369 ARALL 373
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
100-258 |
1.18e-07 |
|
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: 54.20 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 100 LDLHLGMFLPTLLHQATEEQQERFFMPAWNLEITGTYAQTEMGHGTHLRGLETTATYDpkTQEFILNSPtvtsiKWWPGG 179
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKD--GDDYVLNGS-----KMWITN 153
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66793429 180 lGKTSNHAIVLAQLITRGECYGLHAFVVPireigthKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENMLMKYAQ 258
Cdd:cd01158 154 -GGEADFYIVFAVTDPSKGYRGITAFIVE-------RDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGE 224
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
104-253 |
2.29e-05 |
|
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: 46.96 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 104 LGMFLPTLLHQATEEQQERFFMPAWNLEITGTYAQTEMGHGTHLRGLETTATYDpkTQEFILNSPtvtsiKWWPGGlGKT 183
Cdd:cd01152 89 IDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRD--GDDWVVNGQ-----KIWTSG-AHY 160
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66793429 184 SNHAIVLAQLITRGECY-GLHAFVVPIREigthkplPGITVGDIGPKFGYEEMDNGYLkmDNYRIPRENML 253
Cdd:cd01152 161 ADWAWLLVRTDPEAPKHrGISILLVDMDS-------PGVTVRPIRSINGGEFFNEVFL--DDVRVPDANRV 222
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
102-438 |
6.22e-05 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 46.00 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 102 LHLGMFLPTLLHQATEEQQERFFMPAWNLEITGTYAQTEMGHGTHLRGLETTATYDPKTqeFILNSPtvtsiKWWPGglg 181
Cdd:PLN02526 112 VHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGG--WILNGQ-----KRWIG--- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 182 kTSNHAIVLAQLITRGECYGLHAFVVpireigtHKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENMLmkyaqvkp 261
Cdd:PLN02526 182 -NSTFADVLVIFARNTTTNQINGFIV-------KKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL-------- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 262 DGTYVKPLSNKLTYGTMVFVRSFLVGsAAQSLSKACTiaiRYSAVRRQSEIKrsepepqILDFQTQQYKLFPLLATAYAF 341
Cdd:PLN02526 246 PGVNSFQDTNKVLAVSRVMVAWQPIG-ISMGVYDMCH---RYLKERKQFGAP-------LAAFQINQEKLVRMLGNIQAM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 342 HFLGRYIKETYMRINESIGQGDLSelpelhaltaglKAFTTWTANAGIEECRMACGGHGYSHSSGIPNIYVTFTPACTFE 421
Cdd:PLN02526 315 FLVGWRLCKLYESGKMTPGHASLG------------KAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYE 382
|
330
....*....|....*..
gi 66793429 422 GENTVMMLQTARFLMKI 438
Cdd:PLN02526 383 GTYDINALVTGREITGI 399
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
110-411 |
2.09e-04 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (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: 173842 [Multi-domain] Cd Length: 407 Bit Score: 44.30 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 110 TLLHQATEEQQERFFMPAWNLEITGTYAQTEMGHGTHLRGLETTATYDPKtqefilNSPTVTSIKWW-PGGLGKTSNHAI 188
Cdd:cd01153 95 TLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQAD------GSWRINGVKRFiSAGEHDMSENIV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 189 --VLAQL--ITRGeCYGLHAFVVPIREIGTHKplPGITVGDIGPKFGYEEMDNGYLKMDNYR---IPRENMLMKYaqvkp 261
Cdd:cd01153 169 hlVLARSegAPPG-VKGLSLFLVPKFLDDGER--NGVTVARIEEKMGLHGSPTCELVFDNAKgelIGEEGMGLAQ----- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 262 dgtyvkplsnklTYGTMVFVRsflVGSAAQSLSKACT---IAIRYSAVRRQ--SEIKRSEPEPQILD------FQTQQyk 330
Cdd:cd01153 241 ------------MFAMMNGAR---LGVGTQGTGLAEAaylNALAYAKERKQggDLIKAAPAVTIIHHpdvrrsLMTQK-- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 331 lfpllATAYAFHFLGRY----IKETYMRINESIGQGDLSELPELhaLTAGLKAFTTWTANAGIEECRMACGGHGYSHSSG 406
Cdd:cd01153 304 -----AYAEGSRALDLYtatvQDLAERKATEGEDRKALSALADL--LTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYP 376
|
....*
gi 66793429 407 IPNIY 411
Cdd:cd01153 377 IEQYY 381
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
117-253 |
1.98e-03 |
|
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: 41.03 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66793429 117 EEQQERFFMPAWNLEITGTYAQTEMGHGTHLRGLETTAtyDPKTQEFILNSPtvtsiKWWPGGLGKtSNHAIVLAQLITR 196
Cdd:cd01157 99 DEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIINGQ-----KMWITNGGK-ANWYFLLARSDPD 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 66793429 197 GECYGLHAFVVPIREIGThkplPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENML 253
Cdd:cd01157 171 PKCPASKAFTGFIVEADT----PGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVL 223
|
|
| |
