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Conserved domains on  [gi|30089974|ref|NP_009223|]
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peroxisomal acyl-coenzyme A oxidase 1 isoform b [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: 870.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974   3 PDLRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHE-DLNFLTRSQRYEVAVRKSAIMVKKMREFGIAD 81
Cdd:cd01150   1 PDLDKERASATFDWKALTHILEGGEENLRRKREVERELESDPLFQRElPSKHLSREELYEELKRKAKTDVERMGELMADD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  82 PDEIMWFKKLHLVNFV---EPVGLNYSMFIPTLLNQGTTAQKEKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDP 158
Cdd:cd01150  81 PEKMLALTNSLGGYDLslgAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 159 ETQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNG 238
Cdd:cd01150 161 LTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPGKNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMGLNGVDNG 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 239 YLKMDNHRIPRENMLMKYAQVKPDGTYVKPLSN-KLTYGTMVFVRS----FLVGEAARALSKACTIAIRYSAVRHQSEIK 313
Cdd:cd01150 241 FLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDpNKRYGAMLGTRSggrvGLIYDAAMSLKKAATIAIRYSAVRRQFGPK 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 314 PGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIGQGDLSELPELHALTAGLKAFTSWTANTGIEACR 393
Cdd:cd01150 321 PSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGNSELLAELHALSAGLKAVATWTAAQGIQECR 400

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 394 MACGGHGYSHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSYDQvhsgklvcgmvsylndlpsqriqpqqvavwpt 473
Cdd:cd01150 401 EACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQ-------------------------------- 448

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 474 mvdINSPESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFSEKLLKIQDKAIQA 553
Cdd:cd01150 449 ---AFSLADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQVHLRCAAKAHTEYTVLQRFHESVEEIVDPSVRA 525

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 554 VLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLF 633
Cdd:cd01150 526 VLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSPIGRYDGDVYENLF 605


                ....
gi 30089974 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: 870.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974   3 PDLRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHE-DLNFLTRSQRYEVAVRKSAIMVKKMREFGIAD 81
Cdd:cd01150   1 PDLDKERASATFDWKALTHILEGGEENLRRKREVERELESDPLFQRElPSKHLSREELYEELKRKAKTDVERMGELMADD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  82 PDEIMWFKKLHLVNFV---EPVGLNYSMFIPTLLNQGTTAQKEKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDP 158
Cdd:cd01150  81 PEKMLALTNSLGGYDLslgAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 159 ETQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNG 238
Cdd:cd01150 161 LTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPGKNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMGLNGVDNG 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 239 YLKMDNHRIPRENMLMKYAQVKPDGTYVKPLSN-KLTYGTMVFVRS----FLVGEAARALSKACTIAIRYSAVRHQSEIK 313
Cdd:cd01150 241 FLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDpNKRYGAMLGTRSggrvGLIYDAAMSLKKAATIAIRYSAVRRQFGPK 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 314 PGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIGQGDLSELPELHALTAGLKAFTSWTANTGIEACR 393
Cdd:cd01150 321 PSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGNSELLAELHALSAGLKAVATWTAAQGIQECR 400

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 394 MACGGHGYSHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSYDQvhsgklvcgmvsylndlpsqriqpqqvavwpt 473
Cdd:cd01150 401 EACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQ-------------------------------- 448

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 474 mvdINSPESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFSEKLLKIQDKAIQA 553
Cdd:cd01150 449 ---AFSLADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQVHLRCAAKAHTEYTVLQRFHESVEEIVDPSVRA 525

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 554 VLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLF 633
Cdd:cd01150 526 VLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSPIGRYDGDVYENLF 605


                ....
gi 30089974 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: 639.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974    5 LRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHEDLNFLTRSQRYEVAVRKSAIMVKKMREFGIADpDE 84
Cdd:PLN02443   7 LAGERNKAQFDVDAMKIVWAGSRHAFEVSDRMARLVASDPVFSKDNRTRLSRKELFKNTLRKAAHAWKRIIELRLTE-EE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974   85 IMWFKklHLVNfvEP--VGLNYSMFIPTLLNQGTTAQKEKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPETQE 162
Cdd:PLN02443  86 AGKLR--SFVD--EPgyTDLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  163 FILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFG---YDEIDNGY 239
Cdd:PLN02443 162 FVIHSPTLTSSKWWPGGLGKVSTHAVVYARLITNGKDHGIHGFIVQLRSLDDHSPLPGVTVGDIGMKFGngaYNTMDNGF 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  240 LKMDNHRIPRENMLMKYAQVKPDGTYVKP-LSNKLTYGTMVFVRSFLVGEAARALSKACTIAIRYSAVRHQSEIKPGEPE 318
Cdd:PLN02443 242 LRFDHVRIPRDQMLMRLSKVTREGKYVQSdVPRQLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFGSQDGGPE 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  319 PQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIGQGDLSELPELHALTAGLKAFTSWTANTGIEACRMACGG 398
Cdd:PLN02443 322 TQVIDYKTQQSRLFPLLASAYAFRFVGEWLKWLYTDVTQRLEANDFSTLPEAHACTAGLKSLTTSATADGIEECRKLCGG 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  399 HGYSHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSYDQVHSGKLVCGMVSYL---NDLPSQRIQPQQVAVWPtmv 475
Cdd:PLN02443 402 HGYLCSSGLPELFAVYVPACTYEGDNVVLLLQVARFLMKTVSQLGSGKKPVGTTAYMgrvQHLLQCRCGVQTAEDWL--- 478

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  476 dinSPESLTEAYKLRAARLVEIAAKNLQKevihRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFSEKLLK-IQDKAIQAV 554
Cdd:PLN02443 479 ---NPSVVLEAFEARAARMAVTCAQNLSK----FENQEAGFQELSADLVEAAVAHCQLIVVSKFIEKLQQdIPGKGVKKQ 551

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  555 LRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFE 634
Cdd:PLN02443 552 LQNLCYIYALYLLHKHLGDFLSTGCITPKQASLANDQLRSLYSQVRPNAVALVDAFNYTDHYLGSVLGRYDGNVYPKLYE 631

                        650
                 ....*....|....*..
gi 30089974  635 WAKNSPLNKAEVHESYK 651
Cdd:PLN02443 632 EAWKDPLNDSVVPDGYE 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 5.39e-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: 5.39e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974   479 SPESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFSEKLLKIQDKAIQAVLRSL 558
Cdd:pfam01756   1 DPEVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNNQSVELVRAAKAHAEYFVLRTFVERLSTSLDPPLKPVLKKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974   559 CLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFEWAKN 638
Cdd:pfam01756  81 CKLYALWTIEKHLGDFLQGGYLSPEQIDLIREAILELLAELRPNAVALVDAFDFPDFILNSALGRYDGNVYENLFEWAKK 160

                         170
                  ....*....|....*....
gi 30089974   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 3.35e-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: 125.72  E-value: 3.35e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  99 PVGLNYSM---FIPTLLNQGTTAQKEKWLlssKGL---QIIGTYAQTEMGHGTHLRGLETTATYDPEtqEFILN-Sptvt 171
Cdd:COG1960  82 SLALPVGVhngAAEALLRFGTEEQKERYL---PRLasgEWIGAFALTEPGAGSDAAALRTTAVRDGD--GYVLNgQ---- 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 172 siKWWPGGlGKTSNHAIVLAQLITKGKCYGLHAFIVPireigthKPLPGITVGDIGPKFGYDEIDNGYLKMDNHRIPREN 251
Cdd:COG1960 153 --KTFITN-APVADVILVLARTDPAAGHRGISLFLVP-------KDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAEN 222

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 252 ML------MKYAQvkpdgtyvkplsnkltyGTMVFVRSFL----VGEAARALskacTIAIRYSAVRHQseikPGEPepqI 321
Cdd:COG1960 223 LLgeegkgFKIAM-----------------STLNAGRLGLaaqaLGIAEAAL----ELAVAYAREREQ----FGRP---I 274

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 322 LDFQTQQYKLFPLLATAYAfqfvgayMKETYHRINEGIGQGDlselpELHALTAGLKAFTSWTANTGIEACRMACGGHGY 401
Cdd:COG1960 275 ADFQAVQHRLADMAAELEA-------ARALVYRAAWLLDAGE-----DAALEAAMAKLFATEAALEVADEALQIHGGYGY 342

                       330       340       350
                ....*....|....*....|....*....|....*...
gi 30089974 402 SHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSY 439
Cdd:COG1960 343 TREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRP 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: 870.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974   3 PDLRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHE-DLNFLTRSQRYEVAVRKSAIMVKKMREFGIAD 81
Cdd:cd01150   1 PDLDKERASATFDWKALTHILEGGEENLRRKREVERELESDPLFQRElPSKHLSREELYEELKRKAKTDVERMGELMADD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  82 PDEIMWFKKLHLVNFV---EPVGLNYSMFIPTLLNQGTTAQKEKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDP 158
Cdd:cd01150  81 PEKMLALTNSLGGYDLslgAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 159 ETQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNG 238
Cdd:cd01150 161 LTQEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITPGKNHGLHAFIVPIRDPKTHQPLPGVTVGDIGPKMGLNGVDNG 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 239 YLKMDNHRIPRENMLMKYAQVKPDGTYVKPLSN-KLTYGTMVFVRS----FLVGEAARALSKACTIAIRYSAVRHQSEIK 313
Cdd:cd01150 241 FLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDpNKRYGAMLGTRSggrvGLIYDAAMSLKKAATIAIRYSAVRRQFGPK 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 314 PGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIGQGDLSELPELHALTAGLKAFTSWTANTGIEACR 393
Cdd:cd01150 321 PSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGNSELLAELHALSAGLKAVATWTAAQGIQECR 400

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 394 MACGGHGYSHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSYDQvhsgklvcgmvsylndlpsqriqpqqvavwpt 473
Cdd:cd01150 401 EACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQ-------------------------------- 448

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 474 mvdINSPESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFSEKLLKIQDKAIQA 553
Cdd:cd01150 449 ---AFSLADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSFEARNNSQVHLRCAAKAHTEYTVLQRFHESVEEIVDPSVRA 525

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 554 VLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLF 633
Cdd:cd01150 526 VLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSPIGRYDGDVYENLF 605


                ....
gi 30089974 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: 639.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974    5 LRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHEDLNFLTRSQRYEVAVRKSAIMVKKMREFGIADpDE 84
Cdd:PLN02443   7 LAGERNKAQFDVDAMKIVWAGSRHAFEVSDRMARLVASDPVFSKDNRTRLSRKELFKNTLRKAAHAWKRIIELRLTE-EE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974   85 IMWFKklHLVNfvEP--VGLNYSMFIPTLLNQGTTAQKEKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPETQE 162
Cdd:PLN02443  86 AGKLR--SFVD--EPgyTDLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  163 FILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFG---YDEIDNGY 239
Cdd:PLN02443 162 FVIHSPTLTSSKWWPGGLGKVSTHAVVYARLITNGKDHGIHGFIVQLRSLDDHSPLPGVTVGDIGMKFGngaYNTMDNGF 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  240 LKMDNHRIPRENMLMKYAQVKPDGTYVKP-LSNKLTYGTMVFVRSFLVGEAARALSKACTIAIRYSAVRHQSEIKPGEPE 318
Cdd:PLN02443 242 LRFDHVRIPRDQMLMRLSKVTREGKYVQSdVPRQLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFGSQDGGPE 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  319 PQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIGQGDLSELPELHALTAGLKAFTSWTANTGIEACRMACGG 398
Cdd:PLN02443 322 TQVIDYKTQQSRLFPLLASAYAFRFVGEWLKWLYTDVTQRLEANDFSTLPEAHACTAGLKSLTTSATADGIEECRKLCGG 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  399 HGYSHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSYDQVHSGKLVCGMVSYL---NDLPSQRIQPQQVAVWPtmv 475
Cdd:PLN02443 402 HGYLCSSGLPELFAVYVPACTYEGDNVVLLLQVARFLMKTVSQLGSGKKPVGTTAYMgrvQHLLQCRCGVQTAEDWL--- 478

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  476 dinSPESLTEAYKLRAARLVEIAAKNLQKevihRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFSEKLLK-IQDKAIQAV 554
Cdd:PLN02443 479 ---NPSVVLEAFEARAARMAVTCAQNLSK----FENQEAGFQELSADLVEAAVAHCQLIVVSKFIEKLQQdIPGKGVKKQ 551

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  555 LRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFE 634
Cdd:PLN02443 552 LQNLCYIYALYLLHKHLGDFLSTGCITPKQASLANDQLRSLYSQVRPNAVALVDAFNYTDHYLGSVLGRYDGNVYPKLYE 631

                        650
                 ....*....|....*..
gi 30089974  635 WAKNSPLNKAEVHESYK 651
Cdd:PLN02443 632 EAWKDPLNDSVVPDGYE 648
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 5-659 3.05e-158

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 470.10  E-value: 3.05e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974    5 LRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQ-HEDLNFLTRSQRYEVAVRKSAIMVKKmreFGIADPd 83
Cdd:PTZ00460   4 LEEARKQVQFPVLEMTHLLYGNKEQFETFLERQKFIDNEPMFKvHPDYYNWSRQDQILLNAEKTREAHKH---LNLANP- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974   84 eIMWFKKLHLVNFVEPVGLNYSMFIPTLLNQGTTAQKEKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPETQEF 163
Cdd:PTZ00460  80 -NYYTPNLLCPQGTFISTVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  164 ILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNGYLKMD 243
Cdd:PTZ00460 159 VIHTPSVEAVKFWPGELGFLCNFALVYAKLIVNGKNKGVHPFMVRIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  244 NHRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGEAARALSKACTIAIRYSAVRHQSEIKPGEpEPQILD 323
Cdd:PTZ00460 239 HYRIPLDSLLARYIKVSEDGQVERQGNPKVSYASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNDNKQ-ENSVLE 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  324 FQTQQYKLFPLLATAYAFQFVGAYMKE----TYHRINegigQGDLSELPELHALTAGLKA-FTSWTANTGiEACRMACGG 398
Cdd:PTZ00460 318 YQTQQQKLLPLLAEFYACIFGGLKIKElvddNFNRVQ----KNDFSLLQLTHAILSAAKAnYTYFVSNCA-EWCRLSCGG 392

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  399 HGYSHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSYDQVhsgklvcgmVSYLNDLPS--QRIQPQQVavwpTMVD 476
Cdd:PTZ00460 393 HGYAHYSGLPAIYFDMSPNITLEGENQIMYLQLARYLLKQLQHA---------VQKPEKVPEyfNFLSHITE----KLAD 459

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  477 INSPESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTS-VDLVRASEAHCHYVVVKLFSEkllKIQDKA--IQA 553
Cdd:PTZ00460 460 QTTIESLGQLLGLNCTILTIYAAKKIMDHINTGKDFQQSWDTKSgIALASAASRFIEYFNYLCFLD---TINNANksTKE 536

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  554 VLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLF 633
Cdd:PTZ00460 537 ILTQLADLYGITMLLNNPQGLIEKGQITVEQIKLLQETREQLYPIIKPNALGLVEAFGLSDNSLRSLIGCHDGDPYENMY 616

                        650       660
                 ....*....|....*....|....*..
gi 30089974  634 EWA-KNSPLNKAEVHESYKHLKSLQSK 659
Cdd:PTZ00460 617 NWAsKENSLNKQQVHQGVNYLMKMEIK 643
PLN02636 PLN02636
acyl-coenzyme A oxidase
 13-622 1.95e-97

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 313.72  E-value: 1.95e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974   13 SFNPELLTHILDGSPEKTRRRreIENMILNDPDFQH--EdlnfLTRSQRYEVAVRKSAIMVKK--MREFGIADPDEIMWF 88
Cdd:PLN02636  51 SVNTEKLSLYMRGKHRDIQEK--IYEFFNSRPDLQTpvE----ISKDEHRELCMRQLTGLVREagIRPMKYLVEDPAKYF 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974   89 KKLHLVNFVE-----PVGLNYSMFIPTLLNQGTTAQKEKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPETQEF 163
Cdd:PLN02636 125 AITEAVGSVDmslgiKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEF 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  164 ILNSPTVTSIKWWPGGLGKTSNHAIVLAQLI-----TKG-KCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDN 237
Cdd:PLN02636 205 VINTPNDGAIKWWIGNAAVHGKFATVFARLKlpthdSKGvSDMGVHAFIVPIRDMKTHQVLPGVEIRDCGHKVGLNGVDN 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  238 GYLKMDNHRIPRENMLMKYAQVKPDGTYVK--PLSNK---LTYGTMVFVRSFLVGEAARALSKACTIAIRYSAVRHQSEi 312
Cdd:PLN02636 285 GALRFRSVRIPRDNLLNRFGDVSRDGKYTSslPTINKrfaATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFG- 363

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  313 KPGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEgigQGDLSELPELHALTAGLKAF-TSWTANTgIEA 391
Cdd:PLN02636 364 PPKQPEISILDYQSQQHKLMPMLASTYAFHFATEYLVERYSEMKK---THDDQLVADVHALSAGLKAYiTSYTAKA-LST 439

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  392 CRMACGGHGYSHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSYDQVHSGKLVCGMVSYLNDLPSQRI-QPQQVAV 470
Cdd:PLN02636 440 CREACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQYKEKFQGGTLSVTWNYLRESMNTYLsQPNPVTT 519

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  471 -WPTMVDINSPESLTEAYKLRAARLVEIAAKNLQKEvihrkSKEV----AWNLTSVDLVRASEAHCHYVVVKLFSEKLLK 545
Cdd:PLN02636 520 rWEGEEHLRDPKFQLDAFRYRTSRLLQTAALRLRKH-----SKTLgsfgAWNRCLNHLLTLAESHIESVILAKFIEAVER 594

                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30089974  546 IQDKAIQAVLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLG 622
Cdd:PLN02636 595 CPDRSTRAALKLVCDLYALDRIWKDIGTYRNVDYVAPNKAKAIHKLTEYLSFQVRNVAKELVDAFGLPDHVTRAPIA 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 5.39e-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: 5.39e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974   479 SPESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFSEKLLKIQDKAIQAVLRSL 558
Cdd:pfam01756   1 DPEVLLKAFEWRAARLLREAAEKLQALLKSGKSQFEAWNNQSVELVRAAKAHAEYFVLRTFVERLSTSLDPPLKPVLKKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974   559 CLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFEWAKN 638
Cdd:pfam01756  81 CKLYALWTIEKHLGDFLQGGYLSPEQIDLIREAILELLAELRPNAVALVDAFDFPDFILNSALGRYDGNVYENLFEWAKK 160

                         170
                  ....*....|....*....
gi 30089974   639 SPLNKaEVHESY-KHLKSL 656
Cdd:pfam01756 161 NPLNT-EVPPSYhEYLKPL 178
PLN02312 PLN02312
acyl-CoA oxidase
 115-620 3.60e-75

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 254.70  E-value: 3.60e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  115 GTTAQKEKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPETQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLI 194
Cdd:PLN02312 168 GTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINTPCESAQKYWIGGAANHATHTIVFSQLH 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  195 TKGKCYGLHAFIVPIREIGTHKpLPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENMLMKYAQVKPDGTYVKPLSNK-- 272
Cdd:PLN02312 248 INGKNEGVHAFIAQIRDQDGNI-CPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPdq 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  273 --------LTYGTMVFVRSflvgeaARALSK-ACTIAIRYSAVRHQSEIKPGEPEPQILDFQTQQYKLFPLLATAYAFQF 343
Cdd:PLN02312 327 rfgaflapLTSGRVTIAVS------AIYSSKvGLAIAIRYSLSRRAFSVTPNGPEVLLLDYPSHQRRLLPLLAKTYAMSF 400

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  344 VGAYMKETYhrinegigqgdLSELPE----LHALTAGLKAFTSWTANTGIEACRMACGGHGYSHCSGLPNIYVNFTPSCT 419
Cdd:PLN02312 401 AANDLKMIY-----------VKRTPEsnkaIHVVSSGFKAVLTWHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQST 469

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  420 FEGENTVMMLQTARFLMKSYDQVHS-GKLVCGM-VSYLNDlpSQRIQPQQVavwpTMVDINSPESLTEAYKLRAARLVEI 497
Cdd:PLN02312 470 FEGDNNVLMQQVSKALLAEYVSAKKrNKPFKGLgLEHMNG--PRPVIPTQL----TSSTLRDSQFQLNLFCLRERDLLER 543

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  498 AAKNLQKEVIHRKSKEVAWNLT---SVDLVRAseahchyvvvklFSEK-----LLKIQDKAIQAVLRS-LCLLYSLYGIS 568
Cdd:PLN02312 544 FASEVSELQSKGESREFAFLLSyqlAEDLGRA------------FSERailqtFLDAEANLPTGSLKDvLGLLRSLYVLI 611

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 30089974  569 QNAGD--FLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSV 620
Cdd:PLN02312 612 SLDEDpsFLRYGYLSPDNVALVRKEVAKLCGELRPHALALVSSFGIPDAFLSPI 665
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 106-433 1.38e-52

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: 184.02  E-value: 1.38e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 106 MFIPTLLNQGTTAQKEKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPEtqEFILNsptvtSIKWWPGGlGKTSN 185
Cdd:cd00567  43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGD--GYVLN-----GRKIFISN-GGDAD 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 186 HAIVLAQLITKGK-CYGLHAFIVPIREigthkplPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENMLMKYAQVKpdgt 264
Cdd:cd00567 115 LFIVLARTDEEGPgHRGISAFLVPADT-------PGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGF---- 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 265 yvkplsnKLTYGTMVFVRSFLVGEAARALSKACTIAIRYSAVRHQseikPGEPepqILDFQTQQYKLFPLLATAYAFQFV 344
Cdd:cd00567 184 -------ELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQ----FGKP---LAEFQAVQFKLADMAAELEAARLL 249

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 345 GAYMKETYHRinegigqgdlsELPELHALTAGLKAFTSWTANTGIEACRMACGGHGYSHCSGLPNIYVNFTPSCTFEGEN 424
Cdd:cd00567 250 LYRAAWLLDQ-----------GPDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTA 318


                ....*....
gi 30089974 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 1.40e-43

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: 152.37  E-value: 1.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974    15 NPELLTHILDGSPEKTRRRREIENMILNDPDFQH-EDLNFLTRSQRYEVAVRKSAIMVKKMREFGIADPDEIMWFKKLHL 93
Cdd:pfam14749   1 DVEELTALLYGGEEKLERRREIESLIESDPEFSKpEDYYFLSREERYERALRKAKRLVKKLRELQIEDPEETLLLYLRGL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 30089974    94 VNFVEPVGLNYSMFIPTLLNQGTTAQKEKWLLSSKGLQII 133
Cdd:pfam14749  81 LDEGLPLGLHFGMFIPTLKGQGTDEQQAKWLPLAENFEII 120
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 99-439 3.35e-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: 125.72  E-value: 3.35e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  99 PVGLNYSM---FIPTLLNQGTTAQKEKWLlssKGL---QIIGTYAQTEMGHGTHLRGLETTATYDPEtqEFILN-Sptvt 171
Cdd:COG1960  82 SLALPVGVhngAAEALLRFGTEEQKERYL---PRLasgEWIGAFALTEPGAGSDAAALRTTAVRDGD--GYVLNgQ---- 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 172 siKWWPGGlGKTSNHAIVLAQLITKGKCYGLHAFIVPireigthKPLPGITVGDIGPKFGYDEIDNGYLKMDNHRIPREN 251
Cdd:COG1960 153 --KTFITN-APVADVILVLARTDPAAGHRGISLFLVP-------KDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAEN 222

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 252 ML------MKYAQvkpdgtyvkplsnkltyGTMVFVRSFL----VGEAARALskacTIAIRYSAVRHQseikPGEPepqI 321
Cdd:COG1960 223 LLgeegkgFKIAM-----------------STLNAGRLGLaaqaLGIAEAAL----ELAVAYAREREQ----FGRP---I 274

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 322 LDFQTQQYKLFPLLATAYAfqfvgayMKETYHRINEGIGQGDlselpELHALTAGLKAFTSWTANTGIEACRMACGGHGY 401
Cdd:COG1960 275 ADFQAVQHRLADMAAELEA-------ARALVYRAAWLLDAGE-----DAALEAAMAKLFATEAALEVADEALQIHGGYGY 342

                       330       340       350
                ....*....|....*....|....*....|....*...
gi 30089974 402 SHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSY 439
Cdd:COG1960 343 TREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRP 380
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 115-253 2.67e-13

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: 72.01  E-value: 2.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 115 GTTAQKEKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDpeTQEFILNSPtvtsiKWWPGGlGKTSNHAIVLAQLI 194
Cdd:cd01151 109 GSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKD--GGGYKLNGS-----KTWITN-SPIADVFVVWARND 180

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30089974 195 TKGKcygLHAFIVPireigthKPLPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENML 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 8.06e-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 30089974   135 TYAQTEMGHGTHLRGLETTAtYDPETQEFILNSptvtsIKWWPGGlGKTSNHAIVLAQLITKGKCYGLHAFIVPireigt 214
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLNG-----TKWWITN-AGIADLFLVLARTGGDDRHGGISLFLVP------ 67

                          90       100
                  ....*....|....*....|....*....
gi 30089974   215 hKPLPGITVGDIGPKFGYDEIDNGYLKMD 243
Cdd:pfam02770  68 -KDAPGVSVRRIETKLGVRGLPTGELVFD 95
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 115-436 1.21e-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: 60.53  E-value: 1.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 115 GTTAQKEKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPEtqEFILNSptvtsIKWWPGGLGKTSNHaIVLAQLI 194
Cdd:cd01162  97 GNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGD--HYVLNG-----SKAFISGAGDSDVY-VVMARTG 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 195 TKGKcYGLHAFIVPireigthKPLPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENMLMKYAQvkPDGTYVKPLSnklt 274
Cdd:cd01162 169 GEGP-KGISCFVVE-------KGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQ--GFGIAMAGLN---- 234

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 275 yGTMVFVRSFLVGEAARALSKactiAIRYSAVRHQSeikpGEPepqILDFQTQQYKLFPL---LATAYAFQFVGAymket 351
Cdd:cd01162 235 -GGRLNIASCSLGAAQAALDL----ARAYLEERKQF----GKP---LADFQALQFKLADMateLVASRLMVRRAA----- 297

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 352 yHRINEGIgqgdlselPELHALTAGLKAFTSwtaNTGIEACRMAC---GGHGYSHCSGLPNIYVNFTPSCTFEGENTVMM 428
Cdd:cd01162 298 -SALDRGD--------PDAVKLCAMAKRFAT---DECFDVANQALqlhGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMR 365


                ....*...
gi 30089974 429 LQTARFLM 436
Cdd:cd01162 366 LIIARALL 373
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 100-331 1.31e-08

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: 57.28  E-value: 1.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 100 VGLNYSMFIPTLLNQGTTAQKEKWL--LSSKGLqiIGTYAQTEMGHGTHLRGLETTATYDPEtqEFILNSPtvtsiKWWP 177
Cdd:cd01158  81 VSVHNSLGANPIIKFGTEEQKKKYLppLATGEK--IGAFALSEPGAGSDAAALKTTAKKDGD--DYVLNGS-----KMWI 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 178 GGlGKTSNHAIVLAQLITKGKCYGLHAFIVPireigthKPLPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENML---- 253
Cdd:cd01158 152 TN-GGEADFYIVFAVTDPSKGYRGITAFIVE-------RDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILgeeg 223

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 254 --MKYAqvkpdgtyvkplsnkltygtMVFVRSFLVGEAARAL---SKACTIAIRYSAVRHQSeikpGEPepqILDFQTQQ 328
Cdd:cd01158 224 egFKIA--------------------MQTLDGGRIGIAAQALgiaQAALDAAVDYAKERKQF----GKP---IADFQGIQ 276


                ...
gi 30089974 329 YKL 331
Cdd:cd01158 277 FKL 279
PLN02526 PLN02526
acyl-coenzyme A oxidase
 115-433 8.69e-08

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 54.86  E-value: 8.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  115 GTTAQKEKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPETqeFILNSPtvtsiKWWPGglgkTSNHAIVLAQLI 194
Cdd:PLN02526 125 GSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGG--WILNGQ-----KRWIG----NSTFADVLVIFA 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  195 TKGKCYGLHAFIVpireigtHKPLPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENMLmkyaqvkpDGTYVKPLSNKLT 274
Cdd:PLN02526 194 RNTTTNQINGFIV-------KKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL--------PGVNSFQDTNKVL 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  275 YGTMVFVRSFLVGeAARALSKACTiaiRYSAVRHQSeikpGEPepqILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHR 354
Cdd:PLN02526 259 AVSRVMVAWQPIG-ISMGVYDMCH---RYLKERKQF----GAP---LAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYES 327

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30089974  355 INEGIGQGDLSelpelhaltaglKAFTSWTANTGIEACRMACGGHGYSHCSGLPNIYVNFTPSCTFEGENTVMMLQTAR 433
Cdd:PLN02526 328 GKMTPGHASLG------------KAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGR 394
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 106-433 1.61e-07

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: 54.04  E-value: 1.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 106 MFIPTLLNQGTTAQKEKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPEtqEFILNSPTV--TSikwwpgglGKT 183
Cdd:cd01160  86 IVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGD--HYVLNGSKTfiTN--------GML 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 184 SNHAIVLAQliTKGKCYGLHAFIVPIREIGThkplPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENMLMKYAQvkpdG 263
Cdd:cd01160 156 ADVVIVVAR--TGGEARGAGGISLFLVERGT----PGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENK----G 225

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 264 TY--VKPLSNKltygtmvfvRSFLVGEAARALSKACTIAIRYSAVRHQSeikpGEPepqILDFQTQQYKLFPLLATAYAF 341
Cdd:cd01160 226 FYylMQNLPQE---------RLLIAAGALAAAEFMLEETRNYVKQRKAF----GKT---LAQLQVVRHKIAELATKVAVT 289

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974 342 QfvgAYMKETYHRINEGigqgdlsELPELHALTAglKAFTSWTANTGIEACRMACGGHGYSHCSGLPNIYVNFTPSCTFE 421
Cdd:cd01160 290 R---AFLDNCAWRHEQG-------RLDVAEASMA--KYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYG 357

                       330
                ....*....|..
gi 30089974 422 GENTVMMLQTAR 433
Cdd:cd01160 358 GTTEIMKELISR 369
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 102-253 5.89e-04

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 42.62  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30089974  102 LNYSM-FIPTLLNQGTTAQKEKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPEtQEFILNSPtvtsiKWWPGGl 180
Cdd:PTZ00461 120 LAHSMlFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSN-GNYVLNGS-----KIWITN- 192

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30089974  181 GKTSNHAIVLAQLitKGKcygLHAFIVpirEIGThkplPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENML 253
Cdd:PTZ00461 193 GTVADVFLIYAKV--DGK---ITAFVV---ERGT----KGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLL 253
 
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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