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Conserved domains on  [gi|67541190|ref|XP_664369|]
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acyl-CoA oxidase aoxB [Aspergillus nidulans FGSC A4]

Protein Classification

acyl-CoA dehydrogenase family protein( domain architecture ID 550)

acyl-CoA dehydrogenase (ACAD) family protein similar to acyl-CoA dehydrogenase that catalyzes the alpha,beta dehydrogenation of an acyl-CoA to form 2,3-dehydroacyl-CoA; requires an acceptor such as FAD, which becomes reduced

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ACAD super family cl09933
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 19-657 1.85e-132

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)


The actual alignment was detected with superfamily member cd01150:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 610  Bit Score: 403.63  E-value: 1.85e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  19 LASERARSNLSIDELSTHLHSHDGFLALQDKVLPILQSEPLLNKSTQHN-LSRPDRFKLALARAKLVRRLADKHGWTPAE 97
Cdd:cd01150   3 LDKERASATFDWKALTHILEGGEENLRRKREVERELESDPLFQRELPSKhLSREELYEELKRKAKTDVERMGELMADDPE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  98 HEMAEYLVDEV------SPYMLHMGMFITTIQEQGSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQARWDGTR 171
Cdd:cd01150  83 KMLALTNSLGGydlslgAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLT 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 172 KGFVLHSPTLTASKWWNGTLGRTANHAVVVAQLMLPdpvqtsegdsgDQRgtkyisYGPHPFIVQVRDMKTHQPFEGIVI 251
Cdd:cd01150 163 QEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITP-----------GKN------HGLHAFIVPIRDPKTHQPLPGVTV 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 252 GDIGPKYG-------------IRIPHSALLSRYCSVNPEtGRYSKP-SQPTLVYGTLTYMRSK----IVQHARLVLARAV 313
Cdd:cd01150 226 GDIGPKMGlngvdngflqfrnVRIPRENLLNRFGDVSPD-GTYVSPfKDPNKRYGAMLGTRSGgrvgLIYDAAMSLKKAA 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 314 TVAVRYTAIRRQFKDRddasKNSPELPVLDYPTVQIRILPLLATAFALHYTGLAMQNVYSRTRRQIESGDFSSLAYMH-- 391
Cdd:cd01150 305 TIAIRYSAVRRQFGPK----PSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGNSELLAELHal 380

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 392 ------------TDGIETCRRALGGHGYGGGSGLVQLNADYLSKVTVEGDNWMITQQTAAYLIKKmgsvvsasvakvekd 459
Cdd:cd01150 381 saglkavatwtaAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKK--------------- 445

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 460 eidvqfttyfpkiqggetdrgdrqcdYDILRNDGDLVQAFQHRATALAYDVYRE-------RVVRKRGWTSIMTQLHRLS 532
Cdd:cd01150 446 --------------------------YAQAFSLADYLEAYEWLAAHLLRHAAAQleklkksGSGSFEARNNSQVHLRCAA 499

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 533 KgtesllveqeltssAQSQSILVTQFYNALSSDTElsAAVKDVLWDLYRLFSLSTLETEKYEFFSHNAASKHDLDAVLER 612
Cdd:cd01150 500 K--------------AHTEYTVLQRFHESVEEIVD--PSVRAVLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREA 563

                       650       660       670       680
                ....*....|....*....|....*....|....*....|....*
gi 67541190 613 INELTSRIRPHAVRLVDAWQIPDYLLDSALGRYDGRVYEDLFHRA 657
Cdd:cd01150 564 LLALLPQLRPDAVALVDAFDLPDFVLNSPIGRYDGDVYENLFEEA 608
 
Name Accession Description Interval E-value
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 19-657 1.85e-132

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: 403.63  E-value: 1.85e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  19 LASERARSNLSIDELSTHLHSHDGFLALQDKVLPILQSEPLLNKSTQHN-LSRPDRFKLALARAKLVRRLADKHGWTPAE 97
Cdd:cd01150   3 LDKERASATFDWKALTHILEGGEENLRRKREVERELESDPLFQRELPSKhLSREELYEELKRKAKTDVERMGELMADDPE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  98 HEMAEYLVDEV------SPYMLHMGMFITTIQEQGSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQARWDGTR 171
Cdd:cd01150  83 KMLALTNSLGGydlslgAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLT 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 172 KGFVLHSPTLTASKWWNGTLGRTANHAVVVAQLMLPdpvqtsegdsgDQRgtkyisYGPHPFIVQVRDMKTHQPFEGIVI 251
Cdd:cd01150 163 QEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITP-----------GKN------HGLHAFIVPIRDPKTHQPLPGVTV 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 252 GDIGPKYG-------------IRIPHSALLSRYCSVNPEtGRYSKP-SQPTLVYGTLTYMRSK----IVQHARLVLARAV 313
Cdd:cd01150 226 GDIGPKMGlngvdngflqfrnVRIPRENLLNRFGDVSPD-GTYVSPfKDPNKRYGAMLGTRSGgrvgLIYDAAMSLKKAA 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 314 TVAVRYTAIRRQFKDRddasKNSPELPVLDYPTVQIRILPLLATAFALHYTGLAMQNVYSRTRRQIESGDFSSLAYMH-- 391
Cdd:cd01150 305 TIAIRYSAVRRQFGPK----PSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGNSELLAELHal 380

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 392 ------------TDGIETCRRALGGHGYGGGSGLVQLNADYLSKVTVEGDNWMITQQTAAYLIKKmgsvvsasvakvekd 459
Cdd:cd01150 381 saglkavatwtaAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKK--------------- 445

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 460 eidvqfttyfpkiqggetdrgdrqcdYDILRNDGDLVQAFQHRATALAYDVYRE-------RVVRKRGWTSIMTQLHRLS 532
Cdd:cd01150 446 --------------------------YAQAFSLADYLEAYEWLAAHLLRHAAAQleklkksGSGSFEARNNSQVHLRCAA 499

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 533 KgtesllveqeltssAQSQSILVTQFYNALSSDTElsAAVKDVLWDLYRLFSLSTLETEKYEFFSHNAASKHDLDAVLER 612
Cdd:cd01150 500 K--------------AHTEYTVLQRFHESVEEIVD--PSVRAVLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREA 563

                       650       660       670       680
                ....*....|....*....|....*....|....*....|....*
gi 67541190 613 INELTSRIRPHAVRLVDAWQIPDYLLDSALGRYDGRVYEDLFHRA 657
Cdd:cd01150 564 LLALLPQLRPDAVALVDAFDLPDFVLNSPIGRYDGDVYENLFEEA 608
PLN02443 PLN02443
acyl-coenzyme A oxidase
 15-674 1.06e-124

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 385.34  E-value: 1.06e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190   15 GASVLASERARSNLSIDELSTHLHSHDGFLALQDKVLPILQSEPLLNKSTQHNLSRPDRFKLALARAKLVRRLADKHGWT 94
Cdd:PLN02443   3 GVDHLAGERNKAQFDVDAMKIVWAGSRHAFEVSDRMARLVASDPVFSKDNRTRLSRKELFKNTLRKAAHAWKRIIELRLT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190   95 PAEHEMAEYLVDEVSPYMLHMGMFITTIQEQGSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQARWDGTRKGF 174
Cdd:PLN02443  83 EEEAGKLRSFVDEPGYTDLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  175 VLHSPTLTASKWWNGTLGRTANHAVVVAQLMlpdpvqtsegdsgdqrgTKYISYGPHPFIVQVRDMKTHQPFEGIVIGDI 254
Cdd:PLN02443 163 VIHSPTLTSSKWWPGGLGKVSTHAVVYARLI-----------------TNGKDHGIHGFIVQLRSLDDHSPLPGVTVGDI 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  255 GPKYG----------------IRIPHSALLSRYCSVNPEtGRYSKPSQP-TLVYGTLTYMRSKIVQHARLVLARAVTVAV 317
Cdd:PLN02443 226 GMKFGngayntmdngflrfdhVRIPRDQMLMRLSKVTRE-GKYVQSDVPrQLVYGTMVYVRQTIVADASTALSRAVCIAT 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  318 RYTAIRRQFKDRDdaskNSPELPVLDYPTVQIRILPLLATAFALHYTGLAMQNVYSRTRRQIESGDFSSLAYMH------ 391
Cdd:PLN02443 305 RYSAVRRQFGSQD----GGPETQVIDYKTQQSRLFPLLASAYAFRFVGEWLKWLYTDVTQRLEANDFSTLPEAHactagl 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  392 --------TDGIETCRRALGGHGYGGGSGLVQLNADYLSKVTVEGDNWMITQQTAAYLIKkmgsvvsaSVAKVEKDEIDV 463
Cdd:PLN02443 381 kslttsatADGIEECRKLCGGHGYLCSSGLPELFAVYVPACTYEGDNVVLLLQVARFLMK--------TVSQLGSGKKPV 452

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  464 QFTTYFPKIQGGETDRGDRQCDYDILrNDGDLVQAFQHRATALAYDVYRErvvrkrgwtsiMTQLHRLSKGTESLLVEQE 543
Cdd:PLN02443 453 GTTAYMGRVQHLLQCRCGVQTAEDWL-NPSVVLEAFEARAARMAVTCAQN-----------LSKFENQEAGFQELSADLV 520

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  544 LTSSAQSQSILVTQFYNALSSDTElSAAVKDVLWDLYRLFSLSTLETEKYEFFSHNAASKHDLDAVLERINELTSRIRPH 623
Cdd:PLN02443 521 EAAVAHCQLIVVSKFIEKLQQDIP-GKGVKKQLQNLCYIYALYLLHKHLGDFLSTGCITPKQASLANDQLRSLYSQVRPN 599

                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|.
gi 67541190  624 AVRLVDAWQIPDYLLDSALGRYDGRVYEDLFHRAHRvNPLNKTTVNPNYWE 674
Cdd:PLN02443 600 AVALVDAFNYTDHYLGSVLGRYDGNVYPKLYEEAWK-DPLNDSVVPDGYEE 649
ACOX pfam01756
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ...
 494-677 2.14e-38

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: 140.37  E-value: 2.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190   494 DLVQAFQHRATAL---AYDVYRERVVRKRG----WTSIMTQLHRLSKgtesllveqeltssAQSQSILVTQFYNALSsdT 566
Cdd:pfam01756   4 VLLKAFEWRAARLlreAAEKLQALLKSGKSqfeaWNNQSVELVRAAK--------------AHAEYFVLRTFVERLS--T 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190   567 ELSAAVKDVLWDLYRLFSLSTLETEKYEFFSHNAASKHDLDAVLERINELTSRIRPHAVRLVDAWQIPDYLLDSALGRYD 646
Cdd:pfam01756  68 SLDPPLKPVLKKLCKLYALWTIEKHLGDFLQGGYLSPEQIDLIREAILELLAELRPNAVALVDAFDFPDFILNSALGRYD 147

                         170       180       190
                  ....*....|....*....|....*....|.
gi 67541190   647 GRVYEDLFHRAHRvNPLNkTTVNPnYWEDEI 677
Cdd:pfam01756 148 GNVYENLFEWAKK-NPLN-TEVPP-SYHEYL 175
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 83-360 3.18e-24

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: 105.31  E-value: 3.18e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  83 LVRRLADkHGWT----PAEH---------------EMAEYLVDEVSPYMLHMGmFITTIQEQGSDEQRQEWLPKIEKWEI 143
Cdd:COG1960  41 LWRKLAE-LGLLgltiPEEYgglglslvelalvleELARADASLALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEW 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 144 IGAYAQTELGHGSNVRGLETQARWDGtrKGFVLhsptlTASKWWNgTLGRTANHAVVVAQLmlpdpvqtsegdsGDQRGT 223
Cdd:COG1960 119 IGAFALTEPGAGSDAAALRTTAVRDG--DGYVL-----NGQKTFI-TNAPVADVILVLART-------------DPAAGH 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 224 KYISYgphpFIVqvrDMKThqpfEGIVIGDIGPKYGIR-------------IPHSALLsrycsvnPETGRyskpsqptlv 290
Cdd:COG1960 178 RGISL----FLV---PKDT----PGVTVGRIEDKMGLRgsdtgelffddvrVPAENLL-------GEEGK---------- 229

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67541190 291 ygTLTYMRSkIVQHARLVLA--------RAVTVAVRYTAIRRQFKDrddasknspelPVLDYPTVQIRILPLLATAFA 360
Cdd:COG1960 230 --GFKIAMS-TLNAGRLGLAaqalgiaeAALELAVAYAREREQFGR-----------PIADFQAVQHRLADMAAELEA 293
 
Name Accession Description Interval E-value
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 19-657 1.85e-132

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: 403.63  E-value: 1.85e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  19 LASERARSNLSIDELSTHLHSHDGFLALQDKVLPILQSEPLLNKSTQHN-LSRPDRFKLALARAKLVRRLADKHGWTPAE 97
Cdd:cd01150   3 LDKERASATFDWKALTHILEGGEENLRRKREVERELESDPLFQRELPSKhLSREELYEELKRKAKTDVERMGELMADDPE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  98 HEMAEYLVDEV------SPYMLHMGMFITTIQEQGSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQARWDGTR 171
Cdd:cd01150  83 KMLALTNSLGGydlslgAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLT 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 172 KGFVLHSPTLTASKWWNGTLGRTANHAVVVAQLMLPdpvqtsegdsgDQRgtkyisYGPHPFIVQVRDMKTHQPFEGIVI 251
Cdd:cd01150 163 QEFVINTPDFTATKWWPGNLGKTATHAVVFAQLITP-----------GKN------HGLHAFIVPIRDPKTHQPLPGVTV 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 252 GDIGPKYG-------------IRIPHSALLSRYCSVNPEtGRYSKP-SQPTLVYGTLTYMRSK----IVQHARLVLARAV 313
Cdd:cd01150 226 GDIGPKMGlngvdngflqfrnVRIPRENLLNRFGDVSPD-GTYVSPfKDPNKRYGAMLGTRSGgrvgLIYDAAMSLKKAA 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 314 TVAVRYTAIRRQFKDRddasKNSPELPVLDYPTVQIRILPLLATAFALHYTGLAMQNVYSRTRRQIESGDFSSLAYMH-- 391
Cdd:cd01150 305 TIAIRYSAVRRQFGPK----PSDPEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEIIKELLQGNSELLAELHal 380

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 392 ------------TDGIETCRRALGGHGYGGGSGLVQLNADYLSKVTVEGDNWMITQQTAAYLIKKmgsvvsasvakvekd 459
Cdd:cd01150 381 saglkavatwtaAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKK--------------- 445

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 460 eidvqfttyfpkiqggetdrgdrqcdYDILRNDGDLVQAFQHRATALAYDVYRE-------RVVRKRGWTSIMTQLHRLS 532
Cdd:cd01150 446 --------------------------YAQAFSLADYLEAYEWLAAHLLRHAAAQleklkksGSGSFEARNNSQVHLRCAA 499

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 533 KgtesllveqeltssAQSQSILVTQFYNALSSDTElsAAVKDVLWDLYRLFSLSTLETEKYEFFSHNAASKHDLDAVLER 612
Cdd:cd01150 500 K--------------AHTEYTVLQRFHESVEEIVD--PSVRAVLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREA 563

                       650       660       670       680
                ....*....|....*....|....*....|....*....|....*
gi 67541190 613 INELTSRIRPHAVRLVDAWQIPDYLLDSALGRYDGRVYEDLFHRA 657
Cdd:cd01150 564 LLALLPQLRPDAVALVDAFDLPDFVLNSPIGRYDGDVYENLFEEA 608
PLN02443 PLN02443
acyl-coenzyme A oxidase
 15-674 1.06e-124

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 385.34  E-value: 1.06e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190   15 GASVLASERARSNLSIDELSTHLHSHDGFLALQDKVLPILQSEPLLNKSTQHNLSRPDRFKLALARAKLVRRLADKHGWT 94
Cdd:PLN02443   3 GVDHLAGERNKAQFDVDAMKIVWAGSRHAFEVSDRMARLVASDPVFSKDNRTRLSRKELFKNTLRKAAHAWKRIIELRLT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190   95 PAEHEMAEYLVDEVSPYMLHMGMFITTIQEQGSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQARWDGTRKGF 174
Cdd:PLN02443  83 EEEAGKLRSFVDEPGYTDLHWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  175 VLHSPTLTASKWWNGTLGRTANHAVVVAQLMlpdpvqtsegdsgdqrgTKYISYGPHPFIVQVRDMKTHQPFEGIVIGDI 254
Cdd:PLN02443 163 VIHSPTLTSSKWWPGGLGKVSTHAVVYARLI-----------------TNGKDHGIHGFIVQLRSLDDHSPLPGVTVGDI 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  255 GPKYG----------------IRIPHSALLSRYCSVNPEtGRYSKPSQP-TLVYGTLTYMRSKIVQHARLVLARAVTVAV 317
Cdd:PLN02443 226 GMKFGngayntmdngflrfdhVRIPRDQMLMRLSKVTRE-GKYVQSDVPrQLVYGTMVYVRQTIVADASTALSRAVCIAT 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  318 RYTAIRRQFKDRDdaskNSPELPVLDYPTVQIRILPLLATAFALHYTGLAMQNVYSRTRRQIESGDFSSLAYMH------ 391
Cdd:PLN02443 305 RYSAVRRQFGSQD----GGPETQVIDYKTQQSRLFPLLASAYAFRFVGEWLKWLYTDVTQRLEANDFSTLPEAHactagl 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  392 --------TDGIETCRRALGGHGYGGGSGLVQLNADYLSKVTVEGDNWMITQQTAAYLIKkmgsvvsaSVAKVEKDEIDV 463
Cdd:PLN02443 381 kslttsatADGIEECRKLCGGHGYLCSSGLPELFAVYVPACTYEGDNVVLLLQVARFLMK--------TVSQLGSGKKPV 452

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  464 QFTTYFPKIQGGETDRGDRQCDYDILrNDGDLVQAFQHRATALAYDVYRErvvrkrgwtsiMTQLHRLSKGTESLLVEQE 543
Cdd:PLN02443 453 GTTAYMGRVQHLLQCRCGVQTAEDWL-NPSVVLEAFEARAARMAVTCAQN-----------LSKFENQEAGFQELSADLV 520

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  544 LTSSAQSQSILVTQFYNALSSDTElSAAVKDVLWDLYRLFSLSTLETEKYEFFSHNAASKHDLDAVLERINELTSRIRPH 623
Cdd:PLN02443 521 EAAVAHCQLIVVSKFIEKLQQDIP-GKGVKKQLQNLCYIYALYLLHKHLGDFLSTGCITPKQASLANDQLRSLYSQVRPN 599

                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|.
gi 67541190  624 AVRLVDAWQIPDYLLDSALGRYDGRVYEDLFHRAHRvNPLNKTTVNPNYWE 674
Cdd:PLN02443 600 AVALVDAFNYTDHYLGSVLGRYDGNVYPKLYEEAWK-DPLNDSVVPDGYEE 649
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 17-670 1.92e-88

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 290.21  E-value: 1.92e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190   17 SVLASERARSNLSIDELSTHLHS----HDGFLALQDkvlpILQSEPLL-NKSTQHNLSRPDRFKLALARAKLVRR---LA 88
Cdd:PTZ00460   2 QMLEEARKQVQFPVLEMTHLLYGnkeqFETFLERQK----FIDNEPMFkVHPDYYNWSRQDQILLNAEKTREAHKhlnLA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190   89 DKHGWTPAEhemaeYLVDEVSPYMLHMGMFITTIQEQGSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQARWD 168
Cdd:PTZ00460  78 NPNYYTPNL-----LCPQGTFISTVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  169 GTRKGFVLHSPTLTASKWWNGTLGRTANHAVVVAQLMLPDPvqtsegdsgdqrgtkyiSYGPHPFIVQVRDMKTHQPFEG 248
Cdd:PTZ00460 153 KQTNEFVIHTPSVEAVKFWPGELGFLCNFALVYAKLIVNGK-----------------NKGVHPFMVRIRDKETHKPLQG 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  249 IVIGDIGPKYG-------------IRIPHSALLSRYCSVNpETGRYSKPSQPTLVYGTLTYMRSKIV-QHARLVlARAVT 314
Cdd:PTZ00460 216 VEVGDIGPKMGyavkdngflsfdhYRIPLDSLLARYIKVS-EDGQVERQGNPKVSYASMMYMRNLIIdQYPRFA-AQALT 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  315 VAVRYTAIRRQFKDrDDASKNSpelpVLDYPTVQIRILPLLATAFALHYTGLAMQNVYSRTRRQIESGDFSSLAYMH--- 391
Cdd:PTZ00460 294 VAIRYSIYRQQFTN-DNKQENS----VLEYQTQQQKLLPLLAEFYACIFGGLKIKELVDDNFNRVQKNDFSLLQLTHail 368

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  392 -----------TDGIETCRRALGGHGYGGGSGLVQLNADYLSKVTVEGDNWMITQQTAAYLIKKMGSVVSASVAKVEkde 460
Cdd:PTZ00460 369 saakanytyfvSNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQLARYLLKQLQHAVQKPEKVPE--- 445

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  461 idvqfttYFPKIQgGETdrgDRQCDYDILRNDGDLVQ---AFQHRATAlaydvyrERVVRKRGWTSIMTQLHRLSKGTes 537
Cdd:PTZ00460 446 -------YFNFLS-HIT---EKLADQTTIESLGQLLGlncTILTIYAA-------KKIMDHINTGKDFQQSWDTKSGI-- 505

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  538 llveqELTSSAQSqsilVTQFYNALS-SDTELSAA--VKDVLWDLYRLFSLSTLETEKYEFFSHNAASKHDLDAVLERIN 614
Cdd:PTZ00460 506 -----ALASAASR----FIEYFNYLCfLDTINNANksTKEILTQLADLYGITMLLNNPQGLIEKGQITVEQIKLLQETRE 576

                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 67541190  615 ELTSRIRPHAVRLVDAWQIPDYLLDSALGRYDGRVYEDLFHRAHRVNPLNKTTVNP 670
Cdd:PTZ00460 577 QLYPIIKPNALGLVEAFGLSDNSLRSLIGCHDGDPYENMYNWASKENSLNKQQVHQ 632
PLN02636 PLN02636
acyl-coenzyme A oxidase
 126-643 4.60e-45

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 171.58  E-value: 4.60e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  126 GSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQARWDGTRKGFVLHSPTLTASKWWNGTLGRTANHAVVVAQLM 205
Cdd:PLN02636 156 GTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINTPNDGAIKWWIGNAAVHGKFATVFARLK 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  206 LPDPvqTSEGDSgdqrgtkyiSYGPHPFIVQVRDMKTHQPFEGIVIGDIGPKYG-------------IRIPHSALLSRYC 272
Cdd:PLN02636 236 LPTH--DSKGVS---------DMGVHAFIVPIRDMKTHQVLPGVEIRDCGHKVGlngvdngalrfrsVRIPRDNLLNRFG 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  273 SVNPEtGRYSKpSQPTL------VYGTLTYMRSKIVQHARLVLARAVTVAVRYTAIRRQFkdrddASKNSPELPVLDYPT 346
Cdd:PLN02636 305 DVSRD-GKYTS-SLPTInkrfaaTLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQF-----GPPKQPEISILDYQS 377

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  347 VQIRILPLLATAFALHYTGLAMQNVYSRTRRQIES---GDFSSL-----AYMHT---DGIETCRRALGGHGYGGGSGLVQ 415
Cdd:PLN02636 378 QQHKLMPMLASTYAFHFATEYLVERYSEMKKTHDDqlvADVHALsaglkAYITSytaKALSTCREACGGHGYAAVNRFGS 457

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  416 LNADYLSKVTVEGDNWMITQQTAAYLIKKMGSVVSASVAKVEKDEIDVQFTTYFPKIQGGETdrgdRQCDYDILRNDGDL 495
Cdd:PLN02636 458 LRNDHDIFQTFEGDNTVLLQQVAADLLKQYKEKFQGGTLSVTWNYLRESMNTYLSQPNPVTT----RWEGEEHLRDPKFQ 533

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  496 VQAFQHRATALAYDVyrerVVRKRGWTSIMTQLHRLSKGTESLLVEQEltssAQSQSILVTQFYNALSS--DTELSAAVK 573
Cdd:PLN02636 534 LDAFRYRTSRLLQTA----ALRLRKHSKTLGSFGAWNRCLNHLLTLAE----SHIESVILAKFIEAVERcpDRSTRAALK 605

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 67541190  574 dVLWDLYRL----FSLSTLETEKYefFSHNAASkhdldAVLERINELTSRIRPHAVRLVDAWQIPDYLLDSALG 643
Cdd:PLN02636 606 -LVCDLYALdriwKDIGTYRNVDY--VAPNKAK-----AIHKLTEYLSFQVRNVAKELVDAFGLPDHVTRAPIA 671
PLN02312 PLN02312
acyl-CoA oxidase
 113-638 9.20e-45

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 170.72  E-value: 9.20e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  113 LHMGMFITTIQEQGSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQARWDGTRKGFVLHSPTLTASKWWNGTLG 192
Cdd:PLN02312 155 VHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINTPCESAQKYWIGGAA 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  193 RTANHAVVVAQLMLpdpvqtsegdsgdqRGTkyiSYGPHPFIVQVRDMKTHQpFEGIVIGDIGPKYG------------- 259
Cdd:PLN02312 235 NHATHTIVFSQLHI--------------NGK---NEGVHAFIAQIRDQDGNI-CPNIRIADCGHKIGlngvdngriwfdn 296

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  260 IRIPHSALLSRYCSVNPEtGRY-SKPSQPTLVYGT----LTYMRSKIVQHARLVLARAVTVAVRYTAIRRQFKdrddASK 334
Cdd:PLN02312 297 LRIPRENLLNSVADVSPD-GKYvSAIKDPDQRFGAflapLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAFS----VTP 371

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  335 NSPELPVLDYPTVQIRILPLLATAFALHYTGLAMQNVY-------SRTRRQIESGDFSSLAYMHTDGIETCRRALGGHGY 407
Cdd:PLN02312 372 NGPEVLLLDYPSHQRRLLPLLAKTYAMSFAANDLKMIYvkrtpesNKAIHVVSSGFKAVLTWHNMRTLQECREACGGQGL 451

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  408 GGGSGLVQLNADYLSKVTVEGDNWMITQQTAAYLIKKMgsvvsASVAKVEKdeidvqfttyfP-KIQGGETDRGDR---- 482
Cdd:PLN02312 452 KTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAEY-----VSAKKRNK-----------PfKGLGLEHMNGPRpvip 515

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  483 -QCDYDILRNdgdlvQAFQHRATALaydvyRERVVRKRgWTSIMTQLhrLSKGTE-------SLLVEQELTSSAQSQSIL 554
Cdd:PLN02312 516 tQLTSSTLRD-----SQFQLNLFCL-----RERDLLER-FASEVSEL--QSKGESrefafllSYQLAEDLGRAFSERAIL 582

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  555 VTqfynALSSDTELSA-AVKDVLWDLYRLFSLSTLEtEKYEFFSHNAASKHDLDAVLERINELTSRIRPHAVRLVDAWQI 633
Cdd:PLN02312 583 QT----FLDAEANLPTgSLKDVLGLLRSLYVLISLD-EDPSFLRYGYLSPDNVALVRKEVAKLCGELRPHALALVSSFGI 657


                 ....*
gi 67541190  634 PDYLL 638
Cdd:PLN02312 658 PDAFL 662
ACOX pfam01756
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ...
 494-677 2.14e-38

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: 140.37  E-value: 2.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190   494 DLVQAFQHRATAL---AYDVYRERVVRKRG----WTSIMTQLHRLSKgtesllveqeltssAQSQSILVTQFYNALSsdT 566
Cdd:pfam01756   4 VLLKAFEWRAARLlreAAEKLQALLKSGKSqfeaWNNQSVELVRAAK--------------AHAEYFVLRTFVERLS--T 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190   567 ELSAAVKDVLWDLYRLFSLSTLETEKYEFFSHNAASKHDLDAVLERINELTSRIRPHAVRLVDAWQIPDYLLDSALGRYD 646
Cdd:pfam01756  68 SLDPPLKPVLKKLCKLYALWTIEKHLGDFLQGGYLSPEQIDLIREAILELLAELRPNAVALVDAFDFPDFILNSALGRYD 147

                         170       180       190
                  ....*....|....*....|....*....|.
gi 67541190   647 GRVYEDLFHRAHRvNPLNkTTVNPnYWEDEI 677
Cdd:pfam01756 148 GNVYENLFEWAKK-NPLN-TEVPP-SYHEYL 175
Acyl-CoA_ox_N pfam14749
Acyl-coenzyme A oxidase N-terminal; Acyl-coenzyme A oxidase consists of three domains. An ...
 29-144 2.34e-34

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: 126.94  E-value: 2.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190    29 SIDELSTHLHSHDGFLALQDKVLPILQSEPLLNKSTQ-HNLSRPDRFKLALARAKLVRRLADKHGWTP---AEHEMAEYL 104
Cdd:pfam14749   1 DVEELTALLYGGEEKLERRREIESLIESDPEFSKPEDyYFLSREERYERALRKAKRLVKKLRELQIEDpeeTLLLYLRGL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 67541190   105 VDEVSPYMLHMGMFITTIQEQGSDEQRQEWLPKIEKWEII 144
Cdd:pfam14749  81 LDEGLPLGLHFGMFIPTLKGQGTDEQQAKWLPLAENFEII 120
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 83-360 3.18e-24

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: 105.31  E-value: 3.18e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  83 LVRRLADkHGWT----PAEH---------------EMAEYLVDEVSPYMLHMGmFITTIQEQGSDEQRQEWLPKIEKWEI 143
Cdd:COG1960  41 LWRKLAE-LGLLgltiPEEYgglglslvelalvleELARADASLALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEW 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 144 IGAYAQTELGHGSNVRGLETQARWDGtrKGFVLhsptlTASKWWNgTLGRTANHAVVVAQLmlpdpvqtsegdsGDQRGT 223
Cdd:COG1960 119 IGAFALTEPGAGSDAAALRTTAVRDG--DGYVL-----NGQKTFI-TNAPVADVILVLART-------------DPAAGH 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 224 KYISYgphpFIVqvrDMKThqpfEGIVIGDIGPKYGIR-------------IPHSALLsrycsvnPETGRyskpsqptlv 290
Cdd:COG1960 178 RGISL----FLV---PKDT----PGVTVGRIEDKMGLRgsdtgelffddvrVPAENLL-------GEEGK---------- 229

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67541190 291 ygTLTYMRSkIVQHARLVLA--------RAVTVAVRYTAIRRQFKDrddasknspelPVLDYPTVQIRILPLLATAFA 360
Cdd:COG1960 230 --GFKIAMS-TLNAGRLGLAaqalgiaeAALELAVAYAREREQFGR-----------PIADFQAVQHRLADMAAELEA 293
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 81-368 5.64e-24

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: 103.52  E-value: 5.64e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  81 AKLVRRLADKHGWtPAEHEMAEYLVDEVsPYMLHMG--MFITTIQEQGSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNV 158
Cdd:cd00567   7 RDSAREFAAEELE-PYARERRETPEEPW-ELLAELGllLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 159 RGLETQARWDGtrKGFVLHSptltaSKWWNgTLGRTANHAVVVAqlmlpdpvQTSEGDSGDQRgtkyISYgphpFIVqVR 238
Cdd:cd00567  85 AGIRTTARKDG--DGYVLNG-----RKIFI-SNGGDADLFIVLA--------RTDEEGPGHRG----ISA----FLV-PA 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 239 DMKthqpfeGIVIGDIGPKYGIR-------------IPHSALLsrycsvnPETGRYSKpsqptLVYGTLTYMRSKIVQHA 305
Cdd:cd00567 140 DTP------GVTVGRIWDKMGMRgsgtgelvfddvrVPEDNLL-------GEEGGGFE-----LAMKGLNVGRLLLAAVA 201

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 67541190 306 RLVLARAVTVAVRYTAIRRQFkdrddasknspELPVLDYPTVQIRilplLATAFALHYTGLAM 368
Cdd:cd00567 202 LGAARAALDEAVEYAKQRKQF-----------GKPLAEFQAVQFK----LADMAAELEAARLL 249
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 109-261 6.61e-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: 70.85  E-value: 6.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 109 SPYMLHMGMFITTIQEQGSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQARWDGtrKGFVlhsptLTASKWW- 187
Cdd:cd01151  92 SFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDG--GGYK-----LNGSKTWi 164

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 67541190 188 -NGTLgrtANHAVVVAQLMlpdpvqtsegDSGDQRGtkyisygphpFIVQvRDMKthqpfeGIVIGDIGPKYGIR 261
Cdd:cd01151 165 tNSPI---ADVFVVWARND----------ETGKIRG----------FILE-RGMK------GLSAPKIQGKFSLR 209
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 114-261 7.43e-10

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: 61.52  E-value: 7.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 114 HMGMFITTIQEQGSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQARWDGTRkgFVlhsptLTASKWWNgTLGR 193
Cdd:cd01158  84 HNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDD--YV-----LNGSKMWI-TNGG 155

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 67541190 194 TANHAVVVAQLmlpDPvqtsegdsgdQRGTKYISygphPFIVqvrdmktHQPFEGIVIGDIGPKYGIR 261
Cdd:cd01158 156 EADFYIVFAVT---DP----------SKGYRGIT----AFIV-------ERDTPGLSVGKKEDKLGIR 199
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 111-170 3.12e-08

Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.


Pssm-ID: 173849 [Multi-domain]  Cd Length: 372  Bit Score: 56.35  E-value: 3.12e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 111 YMLHMGMFITTIQEQGSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQARWDGT 170
Cdd:cd01160  80 LSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGD 139
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 126-261 9.79e-08

Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer.


Pssm-ID: 173850 [Multi-domain]  Cd Length: 409  Bit Score: 54.78  E-value: 9.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 126 GSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQARWDGTRKGFVLHsptltASKWWNgTLGRTANHAVVVAQLm 205
Cdd:cd01161 121 GTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKHYVLN-----GSKIWI-TNGGIADIFTVFAKT- 193

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 67541190 206 lpdPVQTSEGDSGDQrgtkyISygphPFIVQvRDmkthqpFEGIVIGDIGPKYGIR 261
Cdd:cd01161 194 ---EVKDATGSVKDK-----IT----AFIVE-RS------FGGVTNGPPEKKMGIK 230
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 98-191 1.00e-07

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 54.94  E-value: 1.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190   98 HEMAEYLVDEVSPYMLHMGMFITTIQEQGSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQARWDGTRKgFVLH 177
Cdd:PTZ00461 106 HELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGN-YVLN 184

                         90
                 ....*....|....*.
gi 67541190  178 sptltASKWW--NGTL 191
Cdd:PTZ00461 185 -----GSKIWitNGTV 195
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 146-267 3.92e-07

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: 48.43  E-value: 3.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190   146 AYAQTELGHGSNVRGLETQARwDGTRKGFVLHsptltASKWWNgTLGRTANHAVVVAQlmlpdpvqtSEGDSGDQrgtky 225
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAA-DGDGGGWVLN-----GTKWWI-TNAGIADLFLVLAR---------TGGDDRHG----- 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 67541190   226 isyGPHPFIVqvrdmKTHQPfeGIVIGDIGPKYGIR-IPHSAL 267
Cdd:pfam02770  60 ---GISLFLV-----PKDAP--GVSVRRIETKLGVRgLPTGEL 92
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 91-251 1.50e-06

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: 50.81  E-value: 1.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  91 HGWTPAEH-----EMAEYLVDEVSPyMLHMGMFITTIQEQGSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQA 165
Cdd:cd01152  61 RGASLMEQlifreEMAAAGAPVPFN-QIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRA 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 166 RWDGtrKGFVlhsptLTASKWWNgTLGRTANHAVVVAQlmlPDPvqtsegDSGDQRGtkyISYgphpFIVqvrDMKThqp 245
Cdd:cd01152 140 VRDG--DDWV-----VNGQKIWT-SGAHYADWAWLLVR---TDP------EAPKHRG---ISI----LLV---DMDS--- 189


                ....*.
gi 67541190 246 fEGIVI 251
Cdd:cd01152 190 -PGVTV 194
PLN02526 PLN02526
acyl-coenzyme A oxidase
 112-166 9.38e-06

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 48.70  E-value: 9.38e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 67541190  112 MLHMGMFITTIQEQGSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQAR 166
Cdd:PLN02526 111 LVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTAT 165
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 111-215 5.04e-05

Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.


Pssm-ID: 173845 [Multi-domain]  Cd Length: 376  Bit Score: 46.25  E-value: 5.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190 111 YMLHMGMFITTIQEQGSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQARWDGTRkgFVLHsptltASKWWNgT 190
Cdd:cd01156  84 YGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDR--YVLN-----GSKMWI-T 155

                        90       100
                ....*....|....*....|....*
gi 67541190 191 LGRTANHAVVVAQlmlPDPVQTSEG 215
Cdd:cd01156 156 NGPDADTLVVYAK---TDPSAGAHG 177
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 126-169 6.18e-05

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: 45.90  E-value: 6.18e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 67541190 126 GSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQARWDG 169
Cdd:cd01162  97 GNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREG 140
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 111-215 1.13e-04

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 45.25  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67541190  111 YMLHMGMFITTIQEQGSDEQRQEWLPKIEKWEIIGAYAQTELGHGSNVRGLETQArwDGTRKGFVLHsptltASKWWnGT 190
Cdd:PLN02519 110 YGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKA--ERVDGGYVLN-----GNKMW-CT 181

                         90       100
                 ....*....|....*....|....*
gi 67541190  191 LGRTANHAVVVAQlmlPDPVQTSEG 215
Cdd:PLN02519 182 NGPVAQTLVVYAK---TDVAAGSKG 203
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 111-138 3.87e-04

Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.


Pssm-ID: 460686 [Multi-domain]  Cd Length: 113  Bit Score: 40.52  E-value: 3.87e-04
                          10        20
                  ....*....|....*....|....*...
gi 67541190   111 YMLHMGMFITTIQEQGSDEQRQEWLPKI 138
Cdd:pfam02771  82 LSVHSSLGAPPILRFGTEEQKERYLPKL 109
 
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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