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Conserved domains on  [gi|30089972|ref|NP_004026|]
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peroxisomal acyl-coenzyme A oxidase 1 isoform a [Homo sapiens]

Protein Classification

acyl-CoA oxidase( domain architecture ID 10100166)

acyl-CoA oxidase catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
3-637 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: 891.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972   3 PDLRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHE-DLNFLTRSQRYEVAVRKSAIMVKKMREFGIAD 81
Cdd:cd01150   1 PDLDKERASATFDWKALTHILEGGEENLRRKREVERELESDPLFQRElPSKHLSREELYEELKRKAKTDVERMGELMADD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  82 PDEIMWFKN---FVHRGRPEPLDLHLGMFLPTLLHQATAEQQERFFMPAWNLEIIGTYAQTEMGHGTHLRGLETTATYDP 158
Cdd:cd01150  81 PEKMLALTNslgGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 159 ETQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNG 238
Cdd:cd01150 161 LTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPGKNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMGLNGVDNG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 239 YLKMDNHRIPRENMLMKYAQVKPDGTYVKPLSN-KLTYGTMVFVRS----FLVGEAARALSKACTIAIRYSAVRHQSEIK 313
Cdd:cd01150 241 FLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDpNKRYGAMLGTRSggrvGLIYDAAMSLKKAATIAIRYSAVRRQFGPK 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 314 PGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIGQGDLSELPELHALTAGLKAFTSWTANTGIEACR 393
Cdd:cd01150 321 PSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGNSELLAELHALSAGLKAVATWTAAQGIQECR 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 394 MACGGHGYSHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSYDQvhsgklvcgmvsylndlpsqriqpqqvavwpt 473
Cdd:cd01150 401 EACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQ-------------------------------- 448
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 474 mvdINSPESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFSEKLLKIQDKAIQA 553
Cdd:cd01150 449 ---AFSLADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQVHLRCAAKAHTEYTVLQRFHESVEEIVDPSVRA 525
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 554 VLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLF 633
Cdd:cd01150 526 VLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSPIGRYDGDVYENLF 605

                ....
gi 30089972 634 EWAK 637
Cdd:cd01150 606 EEAR 609
 
Name Accession Description Interval E-value
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
3-637 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: 891.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972   3 PDLRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHE-DLNFLTRSQRYEVAVRKSAIMVKKMREFGIAD 81
Cdd:cd01150   1 PDLDKERASATFDWKALTHILEGGEENLRRKREVERELESDPLFQRElPSKHLSREELYEELKRKAKTDVERMGELMADD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  82 PDEIMWFKN---FVHRGRPEPLDLHLGMFLPTLLHQATAEQQERFFMPAWNLEIIGTYAQTEMGHGTHLRGLETTATYDP 158
Cdd:cd01150  81 PEKMLALTNslgGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 159 ETQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNG 238
Cdd:cd01150 161 LTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPGKNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMGLNGVDNG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 239 YLKMDNHRIPRENMLMKYAQVKPDGTYVKPLSN-KLTYGTMVFVRS----FLVGEAARALSKACTIAIRYSAVRHQSEIK 313
Cdd:cd01150 241 FLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDpNKRYGAMLGTRSggrvGLIYDAAMSLKKAATIAIRYSAVRRQFGPK 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 314 PGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIGQGDLSELPELHALTAGLKAFTSWTANTGIEACR 393
Cdd:cd01150 321 PSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGNSELLAELHALSAGLKAVATWTAAQGIQECR 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 394 MACGGHGYSHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSYDQvhsgklvcgmvsylndlpsqriqpqqvavwpt 473
Cdd:cd01150 401 EACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQ-------------------------------- 448
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 474 mvdINSPESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFSEKLLKIQDKAIQA 553
Cdd:cd01150 449 ---AFSLADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQVHLRCAAKAHTEYTVLQRFHESVEEIVDPSVRA 525
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 554 VLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLF 633
Cdd:cd01150 526 VLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSPIGRYDGDVYENLF 605

                ....
gi 30089972 634 EWAK 637
Cdd:cd01150 606 EEAR 609
PLN02443 PLN02443
acyl-coenzyme A oxidase
5-651 0e+00

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 646.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972    5 LRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHEDLNFLTRSQRYEVAVRKSAIMVKKMREFGIADpDE 84
Cdd:PLN02443   7 LAGERNKAQFDVDAMKIVWAGSRHAFEVSDRMARLVASDPVFSKDNRTRLSRKELFKNTLRKAAHAWKRIIELRLTE-EE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972   85 IMWFKNFVHRgrPEPLDLHLGMFLPTLLHQATAEQQERFFMPAWNLEIIGTYAQTEMGHGTHLRGLETTATYDPETQEFI 164
Cdd:PLN02443  86 AGKLRSFVDE--PGYTDLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  165 LNSPTVTSIKWWPGGLGKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFG---YDEIDNGYLK 241
Cdd:PLN02443 164 IHSPTLTSSKWWPGGLGKVSTHAVVYARLITNGKDHGIHGFIVQLRSLDDHSPLPGVTVGDIGMKFGngaYNTMDNGFLR 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  242 MDNHRIPRENMLMKYAQVKPDGTYVKP-LSNKLTYGTMVFVRSFLVGEAARALSKACTIAIRYSAVRHQSEIKPGEPEPQ 320
Cdd:PLN02443 244 FDHVRIPRDQMLMRLSKVTREGKYVQSdVPRQLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFGSQDGGPETQ 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  321 ILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIGQGDLSELPELHALTAGLKAFTSWTANTGIEACRMACGGHG 400
Cdd:PLN02443 324 VIDYKTQQSRLFPLLASAYAFRFVGEWLKWLYTDVTQRLEANDFSTLPEAHACTAGLKSLTTSATADGIEECRKLCGGHG 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  401 YSHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSYDQVHSGKLVCGMVSYL---NDLPSQRIQPQQVAVWPtmvdi 477
Cdd:PLN02443 404 YLCSSGLPELFAVYVPACTYEGDNVVLLLQVARFLMKTVSQLGSGKKPVGTTAYMgrvQHLLQCRCGVQTAEDWL----- 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  478 nSPESLTEAYKLRAARLVEIAAKNLQKevihRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFSEKLLK-IQDKAIQAVLR 556
Cdd:PLN02443 479 -NPSVVLEAFEARAARMAVTCAQNLSK----FENQEAGFQELSADLVEAAVAHCQLIVVSKFIEKLQQdIPGKGVKKQLQ 553
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  557 SLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFEWA 636
Cdd:PLN02443 554 NLCYIYALYLLHKHLGDFLSTGCITPKQASLANDQLRSLYSQVRPNAVALVDAFNYTDHYLGSVLGRYDGNVYPKLYEEA 633
                        650
                 ....*....|....*
gi 30089972  637 KNSPLNKAEVHESYK 651
Cdd:PLN02443 634 WKDPLNDSVVPDGYE 648
ACOX pfam01756
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ...
479-656 5.17e-77

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: 243.61  E-value: 5.17e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972   479 SPESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFSEKLLKIQDKAIQAVLRSL 558
Cdd:pfam01756   1 DPEVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNNQSVELVRAAKAHAEYFVLRTFVERLSTSLDPPLKPVLKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972   559 CLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFEWAKN 638
Cdd:pfam01756  81 CKLYALWTIEKHLGDFLQGGYLSPEQIDLIREAILELLAELRPNAVALVDAFDFPDFILNSALGRYDGNVYENLFEWAKK 160
                         170
                  ....*....|....*....
gi 30089972   639 SPLNKaEVHESY-KHLKSL 656
Cdd:pfam01756 161 NPLNT-EVPPSYhEYLKPL 178
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
99-439 1.61e-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: 126.49  E-value: 1.61e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  99 PLDLHLGmFLPTLLHQATAEQQERFFMPAWNLEIIGTYAQTEMGHGTHLRGLETTATYDPEtqEFILN-SptvtsiKWWP 177
Cdd:COG1960  86 PVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGD--GYVLNgQ------KTFI 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 178 GGlGKTSNHAIVLAQLITKGKCYGLHAFIVPireigthKPLPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENML---- 253
Cdd:COG1960 157 TN-APVADVILVLARTDPAAGHRGISLFLVP-------KDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLgeeg 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 254 --MKYAQvkpdgtyvkplsnkltyGTMVFVRSFL----VGEAARALskacTIAIRYSAVRHQseikPGEPepqILDFQTQ 327
Cdd:COG1960 229 kgFKIAM-----------------STLNAGRLGLaaqaLGIAEAAL----ELAVAYAREREQ----FGRP---IADFQAV 280
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 328 QYKLFPLLATAYAfqfvgayMKETYHRINEGIGQGDlselpELHALTAGLKAFTSWTANTGIEACRMACGGHGYSHCSGL 407
Cdd:COG1960 281 QHRLADMAAELEA-------ARALVYRAAWLLDAGE-----DAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPL 348
                       330       340       350
                ....*....|....*....|....*....|..
gi 30089972 408 PNIYVNFTPSCTFEGENTVMMLQTARFLMKSY 439
Cdd:COG1960 349 ERLYRDARILTIYEGTNEIQRLIIARRLLGRP 380
 
Name Accession Description Interval E-value
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
3-637 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: 891.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972   3 PDLRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHE-DLNFLTRSQRYEVAVRKSAIMVKKMREFGIAD 81
Cdd:cd01150   1 PDLDKERASATFDWKALTHILEGGEENLRRKREVERELESDPLFQRElPSKHLSREELYEELKRKAKTDVERMGELMADD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  82 PDEIMWFKN---FVHRGRPEPLDLHLGMFLPTLLHQATAEQQERFFMPAWNLEIIGTYAQTEMGHGTHLRGLETTATYDP 158
Cdd:cd01150  81 PEKMLALTNslgGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 159 ETQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNG 238
Cdd:cd01150 161 LTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPGKNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMGLNGVDNG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 239 YLKMDNHRIPRENMLMKYAQVKPDGTYVKPLSN-KLTYGTMVFVRS----FLVGEAARALSKACTIAIRYSAVRHQSEIK 313
Cdd:cd01150 241 FLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDpNKRYGAMLGTRSggrvGLIYDAAMSLKKAATIAIRYSAVRRQFGPK 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 314 PGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIGQGDLSELPELHALTAGLKAFTSWTANTGIEACR 393
Cdd:cd01150 321 PSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGNSELLAELHALSAGLKAVATWTAAQGIQECR 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 394 MACGGHGYSHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSYDQvhsgklvcgmvsylndlpsqriqpqqvavwpt 473
Cdd:cd01150 401 EACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQ-------------------------------- 448
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 474 mvdINSPESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFSEKLLKIQDKAIQA 553
Cdd:cd01150 449 ---AFSLADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQVHLRCAAKAHTEYTVLQRFHESVEEIVDPSVRA 525
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 554 VLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLF 633
Cdd:cd01150 526 VLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSPIGRYDGDVYENLF 605

                ....
gi 30089972 634 EWAK 637
Cdd:cd01150 606 EEAR 609
PLN02443 PLN02443
acyl-coenzyme A oxidase
5-651 0e+00

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 646.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972    5 LRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHEDLNFLTRSQRYEVAVRKSAIMVKKMREFGIADpDE 84
Cdd:PLN02443   7 LAGERNKAQFDVDAMKIVWAGSRHAFEVSDRMARLVASDPVFSKDNRTRLSRKELFKNTLRKAAHAWKRIIELRLTE-EE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972   85 IMWFKNFVHRgrPEPLDLHLGMFLPTLLHQATAEQQERFFMPAWNLEIIGTYAQTEMGHGTHLRGLETTATYDPETQEFI 164
Cdd:PLN02443  86 AGKLRSFVDE--PGYTDLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  165 LNSPTVTSIKWWPGGLGKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFG---YDEIDNGYLK 241
Cdd:PLN02443 164 IHSPTLTSSKWWPGGLGKVSTHAVVYARLITNGKDHGIHGFIVQLRSLDDHSPLPGVTVGDIGMKFGngaYNTMDNGFLR 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  242 MDNHRIPRENMLMKYAQVKPDGTYVKP-LSNKLTYGTMVFVRSFLVGEAARALSKACTIAIRYSAVRHQSEIKPGEPEPQ 320
Cdd:PLN02443 244 FDHVRIPRDQMLMRLSKVTREGKYVQSdVPRQLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFGSQDGGPETQ 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  321 ILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIGQGDLSELPELHALTAGLKAFTSWTANTGIEACRMACGGHG 400
Cdd:PLN02443 324 VIDYKTQQSRLFPLLASAYAFRFVGEWLKWLYTDVTQRLEANDFSTLPEAHACTAGLKSLTTSATADGIEECRKLCGGHG 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  401 YSHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSYDQVHSGKLVCGMVSYL---NDLPSQRIQPQQVAVWPtmvdi 477
Cdd:PLN02443 404 YLCSSGLPELFAVYVPACTYEGDNVVLLLQVARFLMKTVSQLGSGKKPVGTTAYMgrvQHLLQCRCGVQTAEDWL----- 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  478 nSPESLTEAYKLRAARLVEIAAKNLQKevihRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFSEKLLK-IQDKAIQAVLR 556
Cdd:PLN02443 479 -NPSVVLEAFEARAARMAVTCAQNLSK----FENQEAGFQELSADLVEAAVAHCQLIVVSKFIEKLQQdIPGKGVKKQLQ 553
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  557 SLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFEWA 636
Cdd:PLN02443 554 NLCYIYALYLLHKHLGDFLSTGCITPKQASLANDQLRSLYSQVRPNAVALVDAFNYTDHYLGSVLGRYDGNVYPKLYEEA 633
                        650
                 ....*....|....*
gi 30089972  637 KNSPLNKAEVHESYK 651
Cdd:PLN02443 634 WKDPLNDSVVPDGYE 648
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
5-659 4.27e-158

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 469.71  E-value: 4.27e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972    5 LRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQ-HEDLNFLTRSQRYEVAVRKSAIMVKKmreFGIADPd 83
Cdd:PTZ00460   4 LEEARKQVQFPVLEMTHLLYGNKEQFETFLERQKFIDNEPMFKvHPDYYNWSRQDQILLNAEKTREAHKH---LNLANP- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972   84 eIMWFKNFVHRGRPEPLDLHLGMFLPTLLHQATAEQQERFFMPAWNLEIIGTYAQTEMGHGTHLRGLETTATYDPETQEF 163
Cdd:PTZ00460  80 -NYYTPNLLCPQGTFISTVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  164 ILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNGYLKMD 243
Cdd:PTZ00460 159 VIHTPSVEAVKFWPGELGFLCNFALVYAKLIVNGKNKGVHPFMVRIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  244 NHRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGEAARALSKACTIAIRYSAVRHQSEIKPGEpEPQILD 323
Cdd:PTZ00460 239 HYRIPLDSLLARYIKVSEDGQVERQGNPKVSYASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNDNKQ-ENSVLE 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  324 FQTQQYKLFPLLATAYAFQFVGAYMKE----TYHRINegigQGDLSELPELHALTAGLKA-FTSWTANTGiEACRMACGG 398
Cdd:PTZ00460 318 YQTQQQKLLPLLAEFYACIFGGLKIKElvddNFNRVQ----KNDFSLLQLTHAILSAAKAnYTYFVSNCA-EWCRLSCGG 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  399 HGYSHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSYDQVhsgklvcgmVSYLNDLPS--QRIQPQQVavwpTMVD 476
Cdd:PTZ00460 393 HGYAHYSGLPAIYFDMSPNITLEGENQIMYLQLARYLLKQLQHA---------VQKPEKVPEyfNFLSHITE----KLAD 459
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  477 INSPESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTS-VDLVRASEAHCHYVVVKLFSEkllKIQDKA--IQA 553
Cdd:PTZ00460 460 QTTIESLGQLLGLNCTILTIYAAKKIMDHINTGKDFQQSWDTKSgIALASAASRFIEYFNYLCFLD---TINNANksTKE 536
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  554 VLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLF 633
Cdd:PTZ00460 537 ILTQLADLYGITMLLNNPQGLIEKGQITVEQIKLLQETREQLYPIIKPNALGLVEAFGLSDNSLRSLIGCHDGDPYENMY 616
                        650       660
                 ....*....|....*....|....*..
gi 30089972  634 EWA-KNSPLNKAEVHESYKHLKSLQSK 659
Cdd:PTZ00460 617 NWAsKENSLNKQQVHQGVNYLMKMEIK 643
PLN02636 PLN02636
acyl-coenzyme A oxidase
110-622 6.22e-94

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 304.47  E-value: 6.22e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  110 TLLHQATAEQQERFFMPAWNLEIIGTYAQTEMGHGTHLRGLETTATYDPETQEFILNSPTVTSIKWWPGGLGKTSNHAIV 189
Cdd:PLN02636 151 SVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINTPNDGAIKWWIGNAAVHGKFATV 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  190 LAQLI-----TKG-KCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENMLMKYAQVKPDG 263
Cdd:PLN02636 231 FARLKlpthdSKGvSDMGVHAFIVPIRDMKTHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGDVSRDG 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  264 TYVK--PLSNK---LTYGTMVFVRSFLVGEAARALSKACTIAIRYSAVRHQSEiKPGEPEPQILDFQTQQYKLFPLLATA 338
Cdd:PLN02636 311 KYTSslPTINKrfaATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFG-PPKQPEISILDYQSQQHKLMPMLAST 389
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  339 YAFQFVGAYMKETYHRINEgigQGDLSELPELHALTAGLKAF-TSWTANTgIEACRMACGGHGYSHCSGLPNIYVNFTPS 417
Cdd:PLN02636 390 YAFHFATEYLVERYSEMKK---THDDQLVADVHALSAGLKAYiTSYTAKA-LSTCREACGGHGYAAVNRFGSLRNDHDIF 465
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  418 CTFEGENTVMMLQTARFLMKSYDQVHSGKLVCGMVSYLNDLPSQRI-QPQQVAV-WPTMVDINSPESLTEAYKLRAARLV 495
Cdd:PLN02636 466 QTFEGDNTVLLQQVAADLLKQYKEKFQGGTLSVTWNYLRESMNTYLsQPNPVTTrWEGEEHLRDPKFQLDAFRYRTSRLL 545
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  496 EIAAKNLQKEvihrkSKEV----AWNLTSVDLVRASEAHCHYVVVKLFSEKLLKIQDKAIQAVLRSLCLLYSLYGISQNA 571
Cdd:PLN02636 546 QTAALRLRKH-----SKTLgsfgAWNRCLNHLLTLAESHIESVILAKFIEAVERCPDRSTRAALKLVCDLYALDRIWKDI 620
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 30089972  572 GDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLG 622
Cdd:PLN02636 621 GTYRNVDYVAPNKAKAIHKLTEYLSFQVRNVAKELVDAFGLPDHVTRAPIA 671
ACOX pfam01756
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ...
479-656 5.17e-77

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: 243.61  E-value: 5.17e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972   479 SPESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFSEKLLKIQDKAIQAVLRSL 558
Cdd:pfam01756   1 DPEVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNNQSVELVRAAKAHAEYFVLRTFVERLSTSLDPPLKPVLKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972   559 CLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFEWAKN 638
Cdd:pfam01756  81 CKLYALWTIEKHLGDFLQGGYLSPEQIDLIREAILELLAELRPNAVALVDAFDFPDFILNSALGRYDGNVYENLFEWAKK 160
                         170
                  ....*....|....*....
gi 30089972   639 SPLNKaEVHESY-KHLKSL 656
Cdd:pfam01756 161 NPLNT-EVPPSYhEYLKPL 178
PLN02312 PLN02312
acyl-CoA oxidase
116-620 1.26e-71

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 245.07  E-value: 1.26e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  116 TAEQQERFFMPAWNLEIIGTYAQTEMGHGTHLRGLETTATYDPETQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLIT 195
Cdd:PLN02312 169 TKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINTPCESAQKYWIGGAANHATHTIVFSQLHI 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  196 KGKCYGLHAFIVPIREIGTHKpLPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENMLMKYAQVKPDGTYVKPLSNK--- 272
Cdd:PLN02312 249 NGKNEGVHAFIAQIRDQDGNI-CPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPdqr 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  273 -------LTYGTMVFVRSflvgeaARALSK-ACTIAIRYSAVRHQSEIKPGEPEPQILDFQTQQYKLFPLLATAYAFQFV 344
Cdd:PLN02312 328 fgaflapLTSGRVTIAVS------AIYSSKvGLAIAIRYSLSRRAFSVTPNGPEVLLLDYPSHQRRLLPLLAKTYAMSFA 401
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  345 GAYMKETYhrinegigqgdLSELPE----LHALTAGLKAFTSWTANTGIEACRMACGGHGYSHCSGLPNIYVNFTPSCTF 420
Cdd:PLN02312 402 ANDLKMIY-----------VKRTPEsnkaIHVVSSGFKAVLTWHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQSTF 470
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  421 EGENTVMMLQTARFLMKSYDQVHS-GKLVCGM-VSYLNDlpSQRIQPQQVavwpTMVDINSPESLTEAYKLRAARLVEIA 498
Cdd:PLN02312 471 EGDNNVLMQQVSKALLAEYVSAKKrNKPFKGLgLEHMNG--PRPVIPTQL----TSSTLRDSQFQLNLFCLRERDLLERF 544
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  499 AKNLQKEVIHRKSKEVAWNLT---SVDLVRAseahchyvvvklFSEK-----LLKIQDKAIQAVLRS-LCLLYSLYGISQ 569
Cdd:PLN02312 545 ASEVSELQSKGESREFAFLLSyqlAEDLGRA------------FSERailqtFLDAEANLPTGSLKDvLGLLRSLYVLIS 612
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 30089972  570 NAGD--FLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSV 620
Cdd:PLN02312 613 LDEDpsFLRYGYLSPDNVALVRKEVAKLCGELRPHALALVSSFGIPDAFLSPI 665
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
68-433 1.92e-55

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: 191.73  E-value: 1.92e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  68 AIMVKKMREFGiadPDEIMWFKNFVHRGRPEPLDLH----LGMFLPTLLHQATAEQQERFFMPAWNLEIIGTYAQTEMGH 143
Cdd:cd00567   4 RELRDSAREFA---AEELEPYARERRETPEEPWELLaelgLLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 144 GTHLRGLETTATYDPEtqEFILNsptvtSIKWWPGGlGKTSNHAIVLAQLITKGK-CYGLHAFIVPIREigthkplPGIT 222
Cdd:cd00567  81 GSDLAGIRTTARKDGD--GYVLN-----GRKIFISN-GGDADLFIVLARTDEEGPgHRGISAFLVPADT-------PGVT 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 223 VGDIGPKFGYDEIDNGYLKMDNHRIPRENMLMKYAQVKpdgtyvkplsnKLTYGTMVFVRSFLVGEAARALSKACTIAIR 302
Cdd:cd00567 146 VGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGF-----------ELAMKGLNVGRLLLAAVALGAARAALDEAVE 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 303 YSAVRHQseikPGEPepqILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRinegigqgdlsELPELHALTAGLKAFTS 382
Cdd:cd00567 215 YAKQRKQ----FGKP---LAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQ-----------GPDEARLEAAMAKLFAT 276
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 30089972 383 WTANTGIEACRMACGGHGYSHCSGLPNIYVNFTPSCTFEGENTVMMLQTAR 433
Cdd:cd00567 277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
Acyl-CoA_ox_N pfam14749
Acyl-coenzyme A oxidase N-terminal; Acyl-coenzyme A oxidase consists of three domains. An ...
15-133 1.23e-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: 163.15  E-value: 1.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972    15 NPELLTHILDGSPEKTRRRREIENMILNDPDFQH-EDLNFLTRSQRYEVAVRKSAIMVKKMREFGIADPDEIMWFKNFVH 93
Cdd:pfam14749   1 DVEELTALLYGGEEKLERRREIESLIESDPEFSKpEDYYFLSREERYERALRKAKRLVKKLRELQIEDPEETLLLYLRGL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 30089972    94 RGRPEPLDLHLGMFLPTLLHQATAEQQERFFMPAWNLEII 133
Cdd:pfam14749  81 LDEGLPLGLHFGMFIPTLKGQGTDEQQAKWLPLAENFEII 120
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
99-439 1.61e-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: 126.49  E-value: 1.61e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  99 PLDLHLGmFLPTLLHQATAEQQERFFMPAWNLEIIGTYAQTEMGHGTHLRGLETTATYDPEtqEFILN-SptvtsiKWWP 177
Cdd:COG1960  86 PVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGD--GYVLNgQ------KTFI 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 178 GGlGKTSNHAIVLAQLITKGKCYGLHAFIVPireigthKPLPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENML---- 253
Cdd:COG1960 157 TN-APVADVILVLARTDPAAGHRGISLFLVP-------KDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLgeeg 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 254 --MKYAQvkpdgtyvkplsnkltyGTMVFVRSFL----VGEAARALskacTIAIRYSAVRHQseikPGEPepqILDFQTQ 327
Cdd:COG1960 229 kgFKIAM-----------------STLNAGRLGLaaqaLGIAEAAL----ELAVAYAREREQ----FGRP---IADFQAV 280
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 328 QYKLFPLLATAYAfqfvgayMKETYHRINEGIGQGDlselpELHALTAGLKAFTSWTANTGIEACRMACGGHGYSHCSGL 407
Cdd:COG1960 281 QHRLADMAAELEA-------ARALVYRAAWLLDAGE-----DAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPL 348
                       330       340       350
                ....*....|....*....|....*....|..
gi 30089972 408 PNIYVNFTPSCTFEGENTVMMLQTARFLMKSY 439
Cdd:COG1960 349 ERLYRDARILTIYEGTNEIQRLIIARRLLGRP 380
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
118-253 2.13e-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: 66.23  E-value: 2.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 118 EQQERFFMPAW-NLEIIGTYAQTEMGHGTHLRGLETTATYDpeTQEFILNSPtvtsiKWWPGGlGKTSNHAIVLAQLITK 196
Cdd:cd01151 111 EEQKQKYLPKLaSGELIGCFGLTEPNHGSDPGGMETRARKD--GGGYKLNGS-----KTWITN-SPIADVFVVWARNDET 182
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30089972 197 GKcygLHAFIVPireigthKPLPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENML 253
Cdd:cd01151 183 GK---IRGFILE-------RGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL 229
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
135-243 8.06e-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: 58.83  E-value: 8.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972   135 TYAQTEMGHGTHLRGLETTAtYDPETQEFILNSptvtsIKWWPGGlGKTSNHAIVLAQLITKGKCYGLHAFIVPireigt 214
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLNG-----TKWWITN-AGIADLFLVLARTGGDDRHGGISLFLVP------ 67
                          90       100
                  ....*....|....*....|....*....
gi 30089972   215 hKPLPGITVGDIGPKFGYDEIDNGYLKMD 243
Cdd:pfam02770  68 -KDAPGVSVRRIETKLGVRGLPTGELVFD 95
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
100-331 2.41e-09

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: 59.59  E-value: 2.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 100 LDLHLGMFLPTLLHQATAEQQERFFMPAWNLEIIGTYAQTEMGHGTHLRGLETTATYDPEtqEFILNSPtvtsiKWWPGG 179
Cdd:cd01158  81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD--DYVLNGS-----KMWITN 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 180 lGKTSNHAIVLAQLITKGKCYGLHAFIVPireigthKPLPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENML------ 253
Cdd:cd01158 154 -GGEADFYIVFAVTDPSKGYRGITAFIVE-------RDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILgeegeg 225
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 254 MKYAqvkpdgtyvkplsnkltygtMVFVRSFLVGEAARAL---SKACTIAIRYSAVRHQSeikpGEPepqILDFQTQQYK 330
Cdd:cd01158 226 FKIA--------------------MQTLDGGRIGIAAQALgiaQAALDAAVDYAKERKQF----GKP---IADFQGIQFK 278

                .
gi 30089972 331 L 331
Cdd:cd01158 279 L 279
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
116-436 3.29e-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: 59.38  E-value: 3.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 116 TAEQQERFFMPAWNLEIIGTYAQTEMGHGTHLRGLETTATYDPEtqEFILNsptvtSIKWWPGGLGKTSNHaIVLAQLIT 195
Cdd:cd01162  98 NDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGD--HYVLN-----GSKAFISGAGDSDVY-VVMARTGG 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 196 KGKcYGLHAFIVPireigthKPLPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENMLMKYAQvkPDGTYVKPLSnklty 275
Cdd:cd01162 170 EGP-KGISCFVVE-------KGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQ--GFGIAMAGLN----- 234
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 276 GTMVFVRSFLVGEAARALSKactiAIRYSAVRHQSeikpGEPepqILDFQTQQYKLFPL---LATAYAFQFVGAymkety 352
Cdd:cd01162 235 GGRLNIASCSLGAAQAALDL----ARAYLEERKQF----GKP---LADFQALQFKLADMateLVASRLMVRRAA------ 297
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 353 HRINEGIgqgdlselPELHALTAGLKAFTSwtaNTGIEACRMAC---GGHGYSHCSGLPNIYVNFTPSCTFEGENTVMML 429
Cdd:cd01162 298 SALDRGD--------PDAVKLCAMAKRFAT---DECFDVANQALqlhGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRL 366

                ....*..
gi 30089972 430 QTARFLM 436
Cdd:cd01162 367 IIARALL 373
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
100-433 7.44e-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: 58.28  E-value: 7.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 100 LDLHLGMFLPTLLHQATAEQQERFFMPAWNLEIIGTYAQTEMGHGTHLRGLETTATYDPEtqEFILNSPTV--TSikwwp 177
Cdd:cd01160  80 LSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGD--HYVLNGSKTfiTN----- 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 178 gglGKTSNHAIVLAQliTKGKCYGLHAFIVPIREIGThkplPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENMLMKYA 257
Cdd:cd01160 153 ---GMLADVVIVVAR--TGGEARGAGGISLFLVERGT----PGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEEN 223
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 258 QvkpdGTY--VKPLSNKltygtmvfvRSFLVGEAARALSKACTIAIRYSAVRHQSeikpGEPepqILDFQTQQYKLFPLL 335
Cdd:cd01160 224 K----GFYylMQNLPQE---------RLLIAAGALAAAEFMLEETRNYVKQRKAF----GKT---LAQLQVVRHKIAELA 283
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 336 ATAYAFQfvgAYMKETYHRINEGigqgdlsELPELHALTAglKAFTSWTANTGIEACRMACGGHGYSHCSGLPNIYVNFT 415
Cdd:cd01160 284 TKVAVTR---AFLDNCAWRHEQG-------RLDVAEASMA--KYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDAR 351
                       330
                ....*....|....*...
gi 30089972 416 PSCTFEGENTVMMLQTAR 433
Cdd:cd01160 352 VQPIYGGTTEIMKELISR 369
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
95-253 2.51e-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: 2.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972  95 GRPEPlDLHLGMFL--PTLLHQATAEQQERFFMPAWNLEIIGTYAQTEMGHGTHLRGLETTATYDPEtqEFILNSPtvts 172
Cdd:cd01152  79 GAPVP-FNQIGIDLagPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGD--DWVVNGQ---- 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089972 173 iKWWPGGlGKTSNHAIVLAQLITKG-KCYGLHAFIVPIREigthkplPGITVGDIGPKFGYDEIDNGYLkmDNHRIPREN 251
Cdd:cd01152 152 -KIWTSG-AHYADWAWLLVRTDPEApKHRGISILLVDMDS-------PGVTVRPIRSINGGEFFNEVFL--DDVRVPDAN 220

                ..
gi 30089972 252 ML 253
Cdd:cd01152 221 RV 222
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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