|
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: 891.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 3 PDLRKERAAATFNPELITHILDGSPENTRRRREIENLILNDPDFQHE-DYNFLTRSQRYEVAVKKSATMVKKMREFGIAD 81
Cdd:cd01150 1 PDLDKERASATFDWKALTHILEGGEENLRRKREVERELESDPLFQRElPSKHLSREELYEELKRKAKTDVERMGELMADD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 82 PEEIMWFK-KLHMVNFVE--PVGLNYSMFIPTLLNQGTTAQQEKWMHPSQELQIIGTYAQTEMGHGTHLRGLETTATYDP 158
Cdd:cd01150 81 PEKMLALTnSLGGYDLSLgaKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 159 KTQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITRGECYGLHAFVVPIREIGTHKPLPGITVGDIGPKFGYEEMDNG 238
Cdd:cd01150 161 LTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPGKNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMGLNGVDNG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 239 YLKMDNYRIPRENMLMKYAQVKPDGTYVKPLSN-KLTYGTMVFVRS----FLVGSAAQSLSKACTIAIRYSAVRRQSEIK 313
Cdd:cd01150 241 FLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDpNKRYGAMLGTRSggrvGLIYDAAMSLKKAATIAIRYSAVRRQFGPK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 314 RSEPEPQILDFQTQQYKLFPLLATAYAFHFLGRYIKETYMRINESIGQGDLSELPELHALTAGLKAFTTWTANAGIEECR 393
Cdd:cd01150 321 PSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGNSELLAELHALSAGLKAVATWTAAQGIQECR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 394 MACGGHGYSHSSGIPNIYVTFTPACTFEGENTVMMLQTARFLMKIYDQVQsgklvggmvsylndlpsqriqpqqvavwpt 473
Cdd:cd01150 401 EACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAF------------------------------ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 474 lvdinSLDSLTEAYKLRAARLVEIAAKNLQAQVSHRKSKEVAWNLTSVDLVRASEAHCHYVTVKVFADKLPKIQDRAVQA 553
Cdd:cd01150 451 -----SLADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQVHLRCAAKAHTEYTVLQRFHESVEEIVDPSVRA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 554 VLRNLCLLYSLYGISQKGGDFLEGNIITGAQMSQVNSRILELLTVTRPNAVALVDAFDFKDVTLGSVLGRYDGNVYENLF 633
Cdd:cd01150 526 VLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSPIGRYDGDVYENLF 605
|
....*
gi 429484484 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: 660.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 5 LRKERAAATFNPELITHILDGSPENTRRRREIENLILNDPDFQHEDYNFLTRSQRYEVAVKKSATMVKKMREFGIADpEE 84
Cdd:PLN02443 7 LAGERNKAQFDVDAMKIVWAGSRHAFEVSDRMARLVASDPVFSKDNRTRLSRKELFKNTLRKAAHAWKRIIELRLTE-EE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 85 IMWFKklHMVNfvEP--VGLNYSMFIPTLLNQGTTAQQEKWMHPSQELQIIGTYAQTEMGHGTHLRGLETTATYDPKTQE 162
Cdd:PLN02443 86 AGKLR--SFVD--EPgyTDLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 163 FILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITRGECYGLHAFVVPIREIGTHKPLPGITVGDIGPKFG---YEEMDNGY 239
Cdd:PLN02443 162 FVIHSPTLTSSKWWPGGLGKVSTHAVVYARLITNGKDHGIHGFIVQLRSLDDHSPLPGVTVGDIGMKFGngaYNTMDNGF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 240 LKMDNYRIPRENMLMKYAQVKPDGTYVKP-LSNKLTYGTMVFVRSFLVGSAAQSLSKACTIAIRYSAVRRQSEIKRSEPE 318
Cdd:PLN02443 242 LRFDHVRIPRDQMLMRLSKVTREGKYVQSdVPRQLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFGSQDGGPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 319 PQILDFQTQQYKLFPLLATAYAFHFLGRYIKETYMRINESIGQGDLSELPELHALTAGLKAFTTWTANAGIEECRMACGG 398
Cdd:PLN02443 322 TQVIDYKTQQSRLFPLLASAYAFRFVGEWLKWLYTDVTQRLEANDFSTLPEAHACTAGLKSLTTSATADGIEECRKLCGG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 399 HGYSHSSGIPNIYVTFTPACTFEGENTVMMLQTARFLMKIYDQVQSGKLVGGMVSYL---NDLPSQRIQPQQVAVWptlv 475
Cdd:PLN02443 402 HGYLCSSGLPELFAVYVPACTYEGDNVVLLLQVARFLMKTVSQLGSGKKPVGTTAYMgrvQHLLQCRCGVQTAEDW---- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 476 dINSlDSLTEAYKLRAARLVEIAAKNLqaqvSHRKSKEVAWNLTSVDLVRASEAHCHYVTVKVFADKLPK-IQDRAVQAV 554
Cdd:PLN02443 478 -LNP-SVVLEAFEARAARMAVTCAQNL----SKFENQEAGFQELSADLVEAAVAHCQLIVVSKFIEKLQQdIPGKGVKKQ 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 555 LRNLCLLYSLYGISQKGGDFLEGNIITGAQMSQVNSRILELLTVTRPNAVALVDAFDFKDVTLGSVLGRYDGNVYENLFE 634
Cdd:PLN02443 552 LQNLCYIYALYLLHKHLGDFLSTGCITPKQASLANDQLRSLYSQVRPNAVALVDAFNYTDHYLGSVLGRYDGNVYPKLYE 631
|
650 660
....*....|....*....|...
gi 429484484 635 WAKKSPLNKTEVHESYYKHLKPL 657
Cdd:PLN02443 632 EAWKDPLNDSVVPDGYEEYLRPL 654
|
|
| ACOX |
pfam01756 |
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ... |
479-657 |
5.70e-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: 254.01 E-value: 5.70e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 479 SLDSLTEAYKLRAARLVEIAAKNLQAQVSHRKSKEVAWNLTSVDLVRASEAHCHYVTVKVFADKLPKIQDRAVQAVLRNL 558
Cdd:pfam01756 1 DPEVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNNQSVELVRAAKAHAEYFVLRTFVERLSTSLDPPLKPVLKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 559 CLLYSLYGISQKGGDFLEGNIITGAQMSQVNSRILELLTVTRPNAVALVDAFDFKDVTLGSVLGRYDGNVYENLFEWAKK 638
Cdd:pfam01756 81 CKLYALWTIEKHLGDFLQGGYLSPEQIDLIREAILELLAELRPNAVALVDAFDFPDFILNSALGRYDGNVYENLFEWAKK 160
|
170
....*....|....*....
gi 429484484 639 SPLNkTEVHESYYKHLKPL 657
Cdd:pfam01756 161 NPLN-TEVPPSYHEYLKPL 178
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
71-437 |
7.78e-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: 7.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 71 VKKMRE---FGIADPEEI--MWFKKLHMVNFVE-------PVGLNYSM---FIPTLLNQGTTAQQEKWMHPSQELQIIGT 135
Cdd:COG1960 42 WRKLAElglLGLTIPEEYggLGLSLVELALVLEelaradaSLALPVGVhngAAEALLRFGTEEQKERYLPRLASGEWIGA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 136 YAQTEMGHGTHLRGLETTATYDPktQEFILN-SptvtsiKWWPGGlGKTSNHAIVLAQLITRGECYGLHAFVVPireigt 214
Cdd:COG1960 122 FALTEPGAGSDAAALRTTAVRDG--DGYVLNgQ------KTFITN-APVADVILVLARTDPAAGHRGISLFLVP------ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 215 hKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENML------MKYAQvkpdgtyvkplsnkltyGTMVFVRsFLVGS 288
Cdd:COG1960 187 -KDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLgeegkgFKIAM-----------------STLNAGR-LGLAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 289 AAQSLSKAC-TIAIRYSAVRRQSeiKRSepepqILDFQTQQYKLFPLLATAYAFHFLgryikeTYmRINESIGQGDlsel 367
Cdd:COG1960 248 QALGIAEAAlELAVAYAREREQF--GRP-----IADFQAVQHRLADMAAELEAARAL------VY-RAAWLLDAGE---- 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429484484 368 pELHALTAGLKAFTTWTANAGIEECRMACGGHGYSHSSGIPNIYV---TFTpacTFEGENTVMMLQTARFLMK 437
Cdd:COG1960 310 -DAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRdarILT---IYEGTNEIQRLIIARRLLG 378
|
|
| |
|
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: 891.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 3 PDLRKERAAATFNPELITHILDGSPENTRRRREIENLILNDPDFQHE-DYNFLTRSQRYEVAVKKSATMVKKMREFGIAD 81
Cdd:cd01150 1 PDLDKERASATFDWKALTHILEGGEENLRRKREVERELESDPLFQRElPSKHLSREELYEELKRKAKTDVERMGELMADD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 82 PEEIMWFK-KLHMVNFVE--PVGLNYSMFIPTLLNQGTTAQQEKWMHPSQELQIIGTYAQTEMGHGTHLRGLETTATYDP 158
Cdd:cd01150 81 PEKMLALTnSLGGYDLSLgaKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 159 KTQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITRGECYGLHAFVVPIREIGTHKPLPGITVGDIGPKFGYEEMDNG 238
Cdd:cd01150 161 LTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPGKNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMGLNGVDNG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 239 YLKMDNYRIPRENMLMKYAQVKPDGTYVKPLSN-KLTYGTMVFVRS----FLVGSAAQSLSKACTIAIRYSAVRRQSEIK 313
Cdd:cd01150 241 FLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDpNKRYGAMLGTRSggrvGLIYDAAMSLKKAATIAIRYSAVRRQFGPK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 314 RSEPEPQILDFQTQQYKLFPLLATAYAFHFLGRYIKETYMRINESIGQGDLSELPELHALTAGLKAFTTWTANAGIEECR 393
Cdd:cd01150 321 PSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGNSELLAELHALSAGLKAVATWTAAQGIQECR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 394 MACGGHGYSHSSGIPNIYVTFTPACTFEGENTVMMLQTARFLMKIYDQVQsgklvggmvsylndlpsqriqpqqvavwpt 473
Cdd:cd01150 401 EACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAF------------------------------ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 474 lvdinSLDSLTEAYKLRAARLVEIAAKNLQAQVSHRKSKEVAWNLTSVDLVRASEAHCHYVTVKVFADKLPKIQDRAVQA 553
Cdd:cd01150 451 -----SLADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQVHLRCAAKAHTEYTVLQRFHESVEEIVDPSVRA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 554 VLRNLCLLYSLYGISQKGGDFLEGNIITGAQMSQVNSRILELLTVTRPNAVALVDAFDFKDVTLGSVLGRYDGNVYENLF 633
Cdd:cd01150 526 VLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSPIGRYDGDVYENLF 605
|
....*
gi 429484484 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: 660.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 5 LRKERAAATFNPELITHILDGSPENTRRRREIENLILNDPDFQHEDYNFLTRSQRYEVAVKKSATMVKKMREFGIADpEE 84
Cdd:PLN02443 7 LAGERNKAQFDVDAMKIVWAGSRHAFEVSDRMARLVASDPVFSKDNRTRLSRKELFKNTLRKAAHAWKRIIELRLTE-EE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 85 IMWFKklHMVNfvEP--VGLNYSMFIPTLLNQGTTAQQEKWMHPSQELQIIGTYAQTEMGHGTHLRGLETTATYDPKTQE 162
Cdd:PLN02443 86 AGKLR--SFVD--EPgyTDLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 163 FILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITRGECYGLHAFVVPIREIGTHKPLPGITVGDIGPKFG---YEEMDNGY 239
Cdd:PLN02443 162 FVIHSPTLTSSKWWPGGLGKVSTHAVVYARLITNGKDHGIHGFIVQLRSLDDHSPLPGVTVGDIGMKFGngaYNTMDNGF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 240 LKMDNYRIPRENMLMKYAQVKPDGTYVKP-LSNKLTYGTMVFVRSFLVGSAAQSLSKACTIAIRYSAVRRQSEIKRSEPE 318
Cdd:PLN02443 242 LRFDHVRIPRDQMLMRLSKVTREGKYVQSdVPRQLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFGSQDGGPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 319 PQILDFQTQQYKLFPLLATAYAFHFLGRYIKETYMRINESIGQGDLSELPELHALTAGLKAFTTWTANAGIEECRMACGG 398
Cdd:PLN02443 322 TQVIDYKTQQSRLFPLLASAYAFRFVGEWLKWLYTDVTQRLEANDFSTLPEAHACTAGLKSLTTSATADGIEECRKLCGG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 399 HGYSHSSGIPNIYVTFTPACTFEGENTVMMLQTARFLMKIYDQVQSGKLVGGMVSYL---NDLPSQRIQPQQVAVWptlv 475
Cdd:PLN02443 402 HGYLCSSGLPELFAVYVPACTYEGDNVVLLLQVARFLMKTVSQLGSGKKPVGTTAYMgrvQHLLQCRCGVQTAEDW---- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 476 dINSlDSLTEAYKLRAARLVEIAAKNLqaqvSHRKSKEVAWNLTSVDLVRASEAHCHYVTVKVFADKLPK-IQDRAVQAV 554
Cdd:PLN02443 478 -LNP-SVVLEAFEARAARMAVTCAQNL----SKFENQEAGFQELSADLVEAAVAHCQLIVVSKFIEKLQQdIPGKGVKKQ 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 555 LRNLCLLYSLYGISQKGGDFLEGNIITGAQMSQVNSRILELLTVTRPNAVALVDAFDFKDVTLGSVLGRYDGNVYENLFE 634
Cdd:PLN02443 552 LQNLCYIYALYLLHKHLGDFLSTGCITPKQASLANDQLRSLYSQVRPNAVALVDAFNYTDHYLGSVLGRYDGNVYPKLYE 631
|
650 660
....*....|....*....|...
gi 429484484 635 WAKKSPLNKTEVHESYYKHLKPL 657
Cdd:PLN02443 632 EAWKDPLNDSVVPDGYEEYLRPL 654
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
5-648 |
5.20e-159 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 472.41 E-value: 5.20e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 5 LRKERAAATFNPELITHILDGSPENTRRRREIENLILNDPDFQ-HEDYNFLTRSQRYEVAVKKSATMVKKmreFGIADPE 83
Cdd:PTZ00460 4 LEEARKQVQFPVLEMTHLLYGNKEQFETFLERQKFIDNEPMFKvHPDYYNWSRQDQILLNAEKTREAHKH---LNLANPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 84 eiMWFKKLHMVNFVEPVGLNYSMFIPTLLNQGTTAQQEKWMHPSQELQIIGTYAQTEMGHGTHLRGLETTATYDPKTQEF 163
Cdd:PTZ00460 81 --YYTPNLLCPQGTFISTVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 164 ILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITRGECYGLHAFVVPIREIGTHKPLPGITVGDIGPKFGYEEMDNGYLKMD 243
Cdd:PTZ00460 159 VIHTPSVEAVKFWPGELGFLCNFALVYAKLIVNGKNKGVHPFMVRIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 244 NYRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGSAAQSLSKACTIAIRYSAVRRQSEIKRSEpEPQILD 323
Cdd:PTZ00460 239 HYRIPLDSLLARYIKVSEDGQVERQGNPKVSYASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNDNKQ-ENSVLE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 324 FQTQQYKLFPLLATAYAFHFLGRYIKETYMRINESIGQGDLSELPELHALTAGLKA-FTTWTANAGiEECRMACGGHGYS 402
Cdd:PTZ00460 318 YQTQQQKLLPLLAEFYACIFGGLKIKELVDDNFNRVQKNDFSLLQLTHAILSAAKAnYTYFVSNCA-EWCRLSCGGHGYA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 403 HSSGIPNIYVTFTPACTFEGENTVMMLQTARFLMKIYDQ-VQSGKLVGGMVSYLNdlpsqriqpqqvAVWPTLVDINSLD 481
Cdd:PTZ00460 397 HYSGLPAIYFDMSPNITLEGENQIMYLQLARYLLKQLQHaVQKPEKVPEYFNFLS------------HITEKLADQTTIE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 482 SLTEAYKLRAARLVEIAAKNLQAQVSHRKSKEVAWNLTS-VDLVRASEAHCHYVTVKVFADKLPKiQDRAVQAVLRNLCL 560
Cdd:PTZ00460 465 SLGQLLGLNCTILTIYAAKKIMDHINTGKDFQQSWDTKSgIALASAASRFIEYFNYLCFLDTINN-ANKSTKEILTQLAD 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 561 LYSLYGISQKGGDFLEGNIITGAQMSQVNSRILELLTVTRPNAVALVDAFDFKDVTLGSVLGRYDGNVYENLFEWA-KKS 639
Cdd:PTZ00460 544 LYGITMLLNNPQGLIEKGQITVEQIKLLQETREQLYPIIKPNALGLVEAFGLSDNSLRSLIGCHDGDPYENMYNWAsKEN 623
|
....*....
gi 429484484 640 PLNKTEVHE 648
Cdd:PTZ00460 624 SLNKQQVHQ 632
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
6-622 |
1.09e-90 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 296.00 E-value: 1.09e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 6 RKERAAATFNPELITHI--LDGSPENTRRRREIENLILND------PDFQHEDYNFLTRSQRYEVAVKKSAT-------- 69
Cdd:PLN02636 20 RIQRLSLHLSPVPLPKEeqLSRLVCARSIKLSVNTEKLSLymrgkhRDIQEKIYEFFNSRPDLQTPVEISKDehrelcmr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 70 -MVKKMREFGI-------ADPEEimWFKKLHMVNFVE-----PVGLNYSMFIPTLLNQGTTAQQEKWMHPSQELQIIGTY 136
Cdd:PLN02636 100 qLTGLVREAGIrpmkylvEDPAK--YFAITEAVGSVDmslgiKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 137 AQTEMGHGTHLRGLETTATYDPKTQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLI-----TRGEC-YGLHAFVVPIR 210
Cdd:PLN02636 178 AMTELHHGSNVQGLQTTATFDPLTDEFVINTPNDGAIKWWIGNAAVHGKFATVFARLKlpthdSKGVSdMGVHAFIVPIR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 211 EIGTHKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENMLMKYAQVKPDGTYVK--PLSNK---LTYGTMVFVRSFL 285
Cdd:PLN02636 258 DMKTHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGDVSRDGKYTSslPTINKrfaATLGELVGGRVGL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 286 VGSAAQSLSKACTIAIRYSAVRRQSEIKRsEPEPQILDFQTQQYKLFPLLATAYAFHFLGRYIKETYMRINESigqGDLS 365
Cdd:PLN02636 338 AYGSVGVLKASNTIAIRYSLLRQQFGPPK-QPEISILDYQSQQHKLMPMLASTYAFHFATEYLVERYSEMKKT---HDDQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 366 ELPELHALTAGLKAF-TTWTANAgIEECRMACGGHGYSHSS---GIPNIYVTFTpacTFEGENTVMMLQTARFLMKIYDQ 441
Cdd:PLN02636 414 LVADVHALSAGLKAYiTSYTAKA-LSTCREACGGHGYAAVNrfgSLRNDHDIFQ---TFEGDNTVLLQQVAADLLKQYKE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 442 vqsgKLVGGMVS----YLNDLPSQRI-QPQQVAV-WPTLVDINSLDSLTEAYKLRAARLVEIAAKNLQAQvSHRKSKEVA 515
Cdd:PLN02636 490 ----KFQGGTLSvtwnYLRESMNTYLsQPNPVTTrWEGEEHLRDPKFQLDAFRYRTSRLLQTAALRLRKH-SKTLGSFGA 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 516 WNLTSVDLVRASEAHCHYVTVKVFADKLPKIQDRAVQAVLRNLCLLYSLYGISQKGGDFLEGNIITGAQMSQVNsRILEL 595
Cdd:PLN02636 565 WNRCLNHLLTLAESHIESVILAKFIEAVERCPDRSTRAALKLVCDLYALDRIWKDIGTYRNVDYVAPNKAKAIH-KLTEY 643
|
650 660
....*....|....*....|....*...
gi 429484484 596 LTV-TRPNAVALVDAFDFKDVTLGSVLG 622
Cdd:PLN02636 644 LSFqVRNVAKELVDAFGLPDHVTRAPIA 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 |
5.70e-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: 254.01 E-value: 5.70e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 479 SLDSLTEAYKLRAARLVEIAAKNLQAQVSHRKSKEVAWNLTSVDLVRASEAHCHYVTVKVFADKLPKIQDRAVQAVLRNL 558
Cdd:pfam01756 1 DPEVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNNQSVELVRAAKAHAEYFVLRTFVERLSTSLDPPLKPVLKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 559 CLLYSLYGISQKGGDFLEGNIITGAQMSQVNSRILELLTVTRPNAVALVDAFDFKDVTLGSVLGRYDGNVYENLFEWAKK 638
Cdd:pfam01756 81 CKLYALWTIEKHLGDFLQGGYLSPEQIDLIREAILELLAELRPNAVALVDAFDFPDFILNSALGRYDGNVYENLFEWAKK 160
|
170
....*....|....*....
gi 429484484 639 SPLNkTEVHESYYKHLKPL 657
Cdd:pfam01756 161 NPLN-TEVPPSYHEYLKPL 178
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
115-620 |
5.41e-78 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 262.02 E-value: 5.41e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 115 GTTAQQEKWMHPSQELQIIGTYAQTEMGHGTHLRGLETTATYDPKTQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLI 194
Cdd:PLN02312 168 GTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINTPCESAQKYWIGGAANHATHTIVFSQLH 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 195 TRGECYGLHAFVVPIREIGTHKpLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENMLMKYAQVKPDGTYVKPLSNK-- 272
Cdd:PLN02312 248 INGKNEGVHAFIAQIRDQDGNI-CPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPdq 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 273 --------LTYGtmvfvRSFLVGSAAQSLSKACTIAIRYSAVRRQSEIKRSEPEPQILDFQTQQYKLFPLLATAYAFHFL 344
Cdd:PLN02312 327 rfgaflapLTSG-----RVTIAVSAIYSSKVGLAIAIRYSLSRRAFSVTPNGPEVLLLDYPSHQRRLLPLLAKTYAMSFA 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 345 GRYIKETYMRinesigqgdlsELPE----LHALTAGLKAFTTWTANAGIEECRMACGGHGYSHSSGIPNIYVTFTPACTF 420
Cdd:PLN02312 402 ANDLKMIYVK-----------RTPEsnkaIHVVSSGFKAVLTWHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQSTF 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 421 EGENTVMMLQTARFLMKIYDQVQS-GKLVGGM-VSYLNdlpsqriqpQQVAVWPTLVDINSLDSL---TEAYKLRAARLV 495
Cdd:PLN02312 471 EGDNNVLMQQVSKALLAEYVSAKKrNKPFKGLgLEHMN---------GPRPVIPTQLTSSTLRDSqfqLNLFCLRERDLL 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 496 EIAAKNLQAQVSHRKSKEVAWNLT---SVDLVRA-SEAhchyVTVKVFADKLPKIQDRAVQAVLRnlcLLYSLYGIS--Q 569
Cdd:PLN02312 542 ERFASEVSELQSKGESREFAFLLSyqlAEDLGRAfSER----AILQTFLDAEANLPTGSLKDVLG---LLRSLYVLIslD 614
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 429484484 570 KGGDFLEGNIITGAQMSQVNSRILELLTVTRPNAVALVDAFDFKDVTLGSV 620
Cdd:PLN02312 615 EDPSFLRYGYLSPDNVALVRKEVAKLCGELRPHALALVSSFGIPDAFLSPI 665
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
106-433 |
2.69e-57 |
|
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: 196.74 E-value: 2.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 106 MFIPTLLNQGTTAQQEKWMHPSQELQIIGTYAQTEMGHGTHLRGLETTATYDPktQEFILNSptvtsIKWWPGGlGKTSN 185
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDG--DGYVLNG-----RKIFISN-GGDAD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 186 HAIVLAQLITRG-ECYGLHAFVVPIREigthkplPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENMLMKYAQVKpdgt 264
Cdd:cd00567 115 LFIVLARTDEEGpGHRGISAFLVPADT-------PGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGF---- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 265 yvkplsnKLTYGTMVFVRSFLVGSAAQSLSKACTIAIRYSAVRRQseikrsePEPQILDFQTQQYKLFPLLATAYAFHFL 344
Cdd:cd00567 184 -------ELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQ-------FGKPLAEFQAVQFKLADMAAELEAARLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 345 GRyikETYMRINEsigqgdlsELPELHALTAGLKAFTTWTANAGIEECRMACGGHGYSHSSGIPNIYVTFTPACTFEGEN 424
Cdd:cd00567 250 LY---RAAWLLDQ--------GPDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTA 318
|
....*....
gi 429484484 425 TVMMLQTAR 433
Cdd:cd00567 319 EIQRLIIAR 327
|
|
| Acyl-CoA_ox_N |
pfam14749 |
Acyl-coenzyme A oxidase N-terminal; Acyl-coenzyme A oxidase consists of three domains. An ... |
15-133 |
2.68e-45 |
|
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: 156.99 E-value: 2.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 15 NPELITHILDGSPENTRRRREIENLILNDPDFQH-EDYNFLTRSQRYEVAVKKSATMVKKMREFGIADPEEIMWFKKLHM 93
Cdd:pfam14749 1 DVEELTALLYGGEEKLERRREIESLIESDPEFSKpEDYYFLSREERYERALRKAKRLVKKLRELQIEDPEETLLLYLRGL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 429484484 94 VNFVEPVGLNYSMFIPTLLNQGTTAQQEKWMHPSQELQII 133
Cdd:pfam14749 81 LDEGLPLGLHFGMFIPTLKGQGTDEQQAKWLPLAENFEII 120
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
71-437 |
7.78e-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: 7.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 71 VKKMRE---FGIADPEEI--MWFKKLHMVNFVE-------PVGLNYSM---FIPTLLNQGTTAQQEKWMHPSQELQIIGT 135
Cdd:COG1960 42 WRKLAElglLGLTIPEEYggLGLSLVELALVLEelaradaSLALPVGVhngAAEALLRFGTEEQKERYLPRLASGEWIGA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 136 YAQTEMGHGTHLRGLETTATYDPktQEFILN-SptvtsiKWWPGGlGKTSNHAIVLAQLITRGECYGLHAFVVPireigt 214
Cdd:COG1960 122 FALTEPGAGSDAAALRTTAVRDG--DGYVLNgQ------KTFITN-APVADVILVLARTDPAAGHRGISLFLVP------ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 215 hKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENML------MKYAQvkpdgtyvkplsnkltyGTMVFVRsFLVGS 288
Cdd:COG1960 187 -KDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLgeegkgFKIAM-----------------STLNAGR-LGLAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 289 AAQSLSKAC-TIAIRYSAVRRQSeiKRSepepqILDFQTQQYKLFPLLATAYAFHFLgryikeTYmRINESIGQGDlsel 367
Cdd:COG1960 248 QALGIAEAAlELAVAYAREREQF--GRP-----IADFQAVQHRLADMAAELEAARAL------VY-RAAWLLDAGE---- 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429484484 368 pELHALTAGLKAFTTWTANAGIEECRMACGGHGYSHSSGIPNIYV---TFTpacTFEGENTVMMLQTARFLMK 437
Cdd:COG1960 310 -DAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRdarILT---IYEGTNEIQRLIIARRLLG 378
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
115-253 |
2.86e-11 |
|
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: 65.84 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 115 GTTAQQEKWMHPSQELQIIGTYAQTEMGHGTHLRGLETTATYDPKTqeFILNSPtvtsiKWWPGGlGKTSNHAIVLAQLI 194
Cdd:cd01151 109 GSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGG--YKLNGS-----KTWITN-SPIADVFVVWARND 180
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 429484484 195 TRGEcygLHAFVVPireigthKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENML 253
Cdd:cd01151 181 ETGK---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 429484484 135 TYAQTEMGHGTHLRGLETTAtYDPKTQEFILNsptvtSIKWWPGGlGKTSNHAIVLAQLITRGECYGLHAFVVPireigt 214
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLN-----GTKWWITN-AGIADLFLVLARTGGDDRHGGISLFLVP------ 67
|
90 100
....*....|....*....|....*....
gi 429484484 215 hKPLPGITVGDIGPKFGYEEMDNGYLKMD 243
Cdd:pfam02770 68 -KDAPGVSVRRIETKLGVRGLPTGELVFD 95
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
115-436 |
2.46e-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: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 115 GTTAQQEKWMHPSQELQIIGTYAQTEMGHGTHLRGLETTATYDpkTQEFILNSptvtsIKWWPGGLGKTSNHaIVLAQli 194
Cdd:cd01162 97 GNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVRE--GDHYVLNG-----SKAFISGAGDSDVY-VVMAR-- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 195 TRGE-CYGLHAFVVPireigthKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENMLMKYAQvkPDGTYVKPLSnkl 273
Cdd:cd01162 167 TGGEgPKGISCFVVE-------KGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQ--GFGIAMAGLN--- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 274 tyGTMVFVRSFLVGSAAQSLSKactiAIRYSAVRRQSeikrSEPepqILDFQTQQYKLFPLLATAYAFHFLGRyiketym 353
Cdd:cd01162 235 --GGRLNIASCSLGAAQAALDL----ARAYLEERKQF----GKP---LADFQALQFKLADMATELVASRLMVR------- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 354 RINESIGQGDlselPELHALTAGLKAFTTwtaNAGIEECRMAC---GGHGYSHSSGIPNIYVTFTPACTFEGENTVMMLQ 430
Cdd:cd01162 295 RAASALDRGD----PDAVKLCAMAKRFAT---DECFDVANQALqlhGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLI 367
|
....*.
gi 429484484 431 TARFLM 436
Cdd:cd01162 368 IARALL 373
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
106-433 |
8.85e-08 |
|
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: 54.81 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 106 MFIPTLLNQGTTAQQEKWMHPSQELQIIGTYAQTEMGHGTHLRGLETTATYDpkTQEFILNSPTV--TSikwwpgglGKT 183
Cdd:cd01160 86 IVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKD--GDHYVLNGSKTfiTN--------GML 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 184 SNHAIVLAQliTRGECYGLHAFVVPIREIGThkplPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENMLMKyaqvkpdg 263
Cdd:cd01160 156 ADVVIVVAR--TGGEARGAGGISLFLVERGT----PGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGE-------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 264 tyvkplSNKLTYGTMVFVRSFLVGSAAQSLSKA---CTIAIRYsaVRRQSEIKRSepepqILDFQTQQYKLFPLLATAYA 340
Cdd:cd01160 222 ------ENKGFYYLMQNLPQERLLIAAGALAAAefmLEETRNY--VKQRKAFGKT-----LAQLQVVRHKIAELATKVAV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 341 fhflGRYIKETYMRINEsigQGdlsELPELHALTAglKAFTTWTANAGIEECRMACGGHGYSHSSGIPNIYVTFTPACTF 420
Cdd:cd01160 289 ----TRAFLDNCAWRHE---QG---RLDVAEASMA--KYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIY 356
|
330
....*....|...
gi 429484484 421 EGENTVMMLQTAR 433
Cdd:cd01160 357 GGTTEIMKELISR 369
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
100-258 |
8.94e-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: 51.50 E-value: 8.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 100 VGLNYSMFIPTLLNQGTTAQQEKWMHPSQELQIIGTYAQTEMGHGTHLRGLETTATYDpkTQEFILNSPtvtsiKWWPGG 179
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKD--GDDYVLNGS-----KMWITN 153
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429484484 180 lGKTSNHAIVLAQLITRGECYGLHAFVVPireigthKPLPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENMLMKYAQ 258
Cdd:cd01158 154 -GGEADFYIVFAVTDPSKGYRGITAFIVE-------RDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGE 224
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
115-253 |
3.12e-05 |
|
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: 46.81 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 115 GTTAQQEKWMHPSQELQIIGTYAQTEMGHGTHLRGLETTAtyDPKTQEFILNSPtvtsiKWWPGGLGKtSNHAIVLAQLI 194
Cdd:cd01157 97 GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIINGQ-----KMWITNGGK-ANWYFLLARSD 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 429484484 195 TRGECYGLHAFVVPIREIGThkplPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENML 253
Cdd:cd01157 169 PDPKCPASKAFTGFIVEADT----PGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVL 223
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
110-411 |
6.57e-05 |
|
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: 45.84 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 110 TLLNQGTTAQQEKWMHPSQELQIIGTYAQTEMGHGTHLRGLETTATYDPKtqefilNSPTVTSIKWW-PGGLGKTSNHAI 188
Cdd:cd01153 95 TLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQAD------GSWRINGVKRFiSAGEHDMSENIV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 189 --VLAQL--ITRGeCYGLHAFVVPIREIGTHKplPGITVGDIGPKFGYEEMDNGYLKMDNYR---IPRENMLMKYaqvkp 261
Cdd:cd01153 169 hlVLARSegAPPG-VKGLSLFLVPKFLDDGER--NGVTVARIEEKMGLHGSPTCELVFDNAKgelIGEEGMGLAQ----- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 262 dgtyvkplsnklTYGTMVFVRsflVGSAAQSLSKACT---IAIRYSAVRRQ--SEIKRSEPEPQILD------FQTQQyk 330
Cdd:cd01153 241 ------------MFAMMNGAR---LGVGTQGTGLAEAaylNALAYAKERKQggDLIKAAPAVTIIHHpdvrrsLMTQK-- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 331 lfpllATAYAFHFLGRY----IKETYMRINESIGQGDLSELPELhaLTAGLKAFTTWTANAGIEECRMACGGHGYSHSSG 406
Cdd:cd01153 304 -----AYAEGSRALDLYtatvQDLAERKATEGEDRKALSALADL--LTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYP 376
|
....*
gi 429484484 407 IPNIY 411
Cdd:cd01153 377 IEQYY 381
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
102-253 |
6.32e-04 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 42.62 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429484484 102 LNYSM-FIPTLLNQGTTAQQEKWMHPSQELQIIGTYAQTEMGHGTHLRGLETTATYDpKTQEFILNSPtvtsiKWWPGGl 180
Cdd:PTZ00461 120 LAHSMlFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKD-SNGNYVLNGS-----KIWITN- 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429484484 181 GKTSNHAIVLAQLITRgecygLHAFVVpirEIGThkplPGITVGDIGPKFGYEEMDNGYLKMDNYRIPRENML 253
Cdd:PTZ00461 193 GTVADVFLIYAKVDGK-----ITAFVV---ERGT----KGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLL 253
|
|
| |
