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Conserved domains on  [gi|21311885|ref|NP_083041|]
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acyl-coenzyme A oxidase-like protein [Mus musculus]

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 ...
 51-599 9.72e-153

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: 453.71  E-value: 9.72e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  51 MEEKRKSFISQILILGEVLCMVDVSMSIKCGILFLLFGGAISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGI 130
Cdd:cd01150  73 MGELMADDPEKMLALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGL 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 131 QTEATFDLDNQEFVIDMPCENAHKMYIGNAMH-GNYAAVFAQLIIEGKSQGPHCFIVPIRDENGNL-YPGVTAIDMMHKE 208
Cdd:cd01150 153 ETTATYDPLTQEFVINTPDFTATKWWPGNLGKtATHAVVFAQLITPGKNHGLHAFIVPIRDPKTHQpLPGVTVGDIGPKM 232

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 209 GMNGVDNGILIFDKVRIPRENLLDKFGSVTPDGQYHSPIQSKNARFNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSH 288
Cdd:cd01150 233 GLNGVDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSA 312

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 289 SRRQFGPKDKE-EVKIIEHQMQALRLMSHLATALAVTFTSRHADDILDE---DIFQGRAlTNSRSLQALMAGLKAYSTWE 364
Cdd:cd01150 313 VRRQFGPKPSDpEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEiikELLQGNS-ELLAELHALSAGLKAVATWT 391

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 365 TVSCLQDCRECTGGMGYMMETRISDLKCDTDVFVTFEGDNVVMLQVVARELLAQYSKQHKknlllgviqnwtatagdklr 444
Cdd:cd01150 392 AAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAFS-------------------- 451

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 445 tsflafntdtvgcLAFLLKAVNFRERVLQRSLVSRIYYKVVTKKGDFfSAWNSCMHHVTSLSLAHIHRVALEQFTTAVRQ 524
Cdd:cd01150 452 -------------LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSF-EARNNSQVHLRCAAKAHTEYTVLQRFHESVEE 517

                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21311885 525 CPNREDQALLMKFCLLYGTKLVFQERGWYLEHKYLTPKASMLIRAQLLNLCESVKDDALKVISAFNIPHITIRAP 599
Cdd:cd01150 518 IVDPSVRAVLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSP 592
 
Name Accession Description Interval E-value
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 51-599 9.72e-153

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: 453.71  E-value: 9.72e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  51 MEEKRKSFISQILILGEVLCMVDVSMSIKCGILFLLFGGAISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGI 130
Cdd:cd01150  73 MGELMADDPEKMLALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGL 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 131 QTEATFDLDNQEFVIDMPCENAHKMYIGNAMH-GNYAAVFAQLIIEGKSQGPHCFIVPIRDENGNL-YPGVTAIDMMHKE 208
Cdd:cd01150 153 ETTATYDPLTQEFVINTPDFTATKWWPGNLGKtATHAVVFAQLITPGKNHGLHAFIVPIRDPKTHQpLPGVTVGDIGPKM 232

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 209 GMNGVDNGILIFDKVRIPRENLLDKFGSVTPDGQYHSPIQSKNARFNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSH 288
Cdd:cd01150 233 GLNGVDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSA 312

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 289 SRRQFGPKDKE-EVKIIEHQMQALRLMSHLATALAVTFTSRHADDILDE---DIFQGRAlTNSRSLQALMAGLKAYSTWE 364
Cdd:cd01150 313 VRRQFGPKPSDpEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEiikELLQGNS-ELLAELHALSAGLKAVATWT 391

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 365 TVSCLQDCRECTGGMGYMMETRISDLKCDTDVFVTFEGDNVVMLQVVARELLAQYSKQHKknlllgviqnwtatagdklr 444
Cdd:cd01150 392 AAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAFS-------------------- 451

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 445 tsflafntdtvgcLAFLLKAVNFRERVLQRSLVSRIYYKVVTKKGDFfSAWNSCMHHVTSLSLAHIHRVALEQFTTAVRQ 524
Cdd:cd01150 452 -------------LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSF-EARNNSQVHLRCAAKAHTEYTVLQRFHESVEE 517

                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21311885 525 CPNREDQALLMKFCLLYGTKLVFQERGWYLEHKYLTPKASMLIRAQLLNLCESVKDDALKVISAFNIPHITIRAP 599
Cdd:cd01150 518 IVDPSVRAVLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSP 592
PLN02636 PLN02636
acyl-coenzyme A oxidase
 50-599 7.69e-124

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 381.90  E-value: 7.69e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885   50 IMEEKRKSFIsqiliLGEVLCMVDVSMSIKCGILFLLFGGAISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRG 129
Cdd:PLN02636 116 LVEDPAKYFA-----ITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQG 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  130 IQTEATFDLDNQEFVIDMPCENAHKMYIGNA-MHGNYAAVFAQLIIEG------KSQGPHCFIVPIRD-ENGNLYPGVTA 201
Cdd:PLN02636 191 LQTTATFDPLTDEFVINTPNDGAIKWWIGNAaVHGKFATVFARLKLPThdskgvSDMGVHAFIVPIRDmKTHQVLPGVEI 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  202 IDMMHKEGMNGVDNGILIFDKVRIPRENLLDKFGSVTPDGQYHSPIQSKNARFNAILATLTPSRLAVTFQALGAMKLGLM 281
Cdd:PLN02636 271 RDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGDVSRDGKYTSSLPTINKRFAATLGELVGGRVGLAYGSVGVLKASNT 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  282 IAIRYSHSRRQFGPKDKEEVKIIEHQMQALRLMSHLATALAVTFTSRHADDIL-------DEDIFQgraltnsrSLQALM 354
Cdd:PLN02636 351 IAIRYSLLRQQFGPPKQPEISILDYQSQQHKLMPMLASTYAFHFATEYLVERYsemkkthDDQLVA--------DVHALS 422

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  355 AGLKAYSTWETVSCLQDCRECTGGMGYMMETRISDLKCDTDVFVTFEGDNVVMLQVVARELLAQYsKQHKKNLLLGVIQN 434
Cdd:PLN02636 423 AGLKAYITSYTAKALSTCREACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQY-KEKFQGGTLSVTWN 501

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  435 WtatagdkLRTSFLAFNTDTVGCLA------------FLLKAVNFRERVLQRSLVSRIyyKVVTKKGDFFSAWNSCMHHV 502
Cdd:PLN02636 502 Y-------LRESMNTYLSQPNPVTTrwegeehlrdpkFQLDAFRYRTSRLLQTAALRL--RKHSKTLGSFGAWNRCLNHL 572

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  503 TSLSLAHIHRVALEQFTTAVRQCPNREDQALLMKFCLLYGTKLVFQERGWYLEHKYLTPKASMLIRAQLLNLCESVKDDA 582
Cdd:PLN02636 573 LTLAESHIESVILAKFIEAVERCPDRSTRAALKLVCDLYALDRIWKDIGTYRNVDYVAPNKAKAIHKLTEYLSFQVRNVA 652

                        570
                 ....*....|....*..
gi 21311885  583 LKVISAFNIPHITIRAP 599
Cdd:PLN02636 653 KELVDAFGLPDHVTRAP 669
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 57-420 1.42e-56

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: 195.83  E-value: 1.42e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  57 SFISQILILgEVLCMVDVSMSIKCGILFLlFGGAISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGIQTEATf 136
Cdd:COG1960  65 SLVELALVL-EELARADASLALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAV- 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 137 dLDNQEFVIdmpceNAHKMYIGNAMHGNYAAVFAQLIIEGKSQGPHCFIVPiRDEngnlyPGVTAIDMMHKEGMNGVDNG 216
Cdd:COG1960 142 -RDGDGYVL-----NGQKTFITNAPVADVILVLARTDPAAGHRGISLFLVP-KDT-----PGVTVGRIEDKMGLRGSDTG 209

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 217 ILIFDKVRIPRENLLdkfGSVtpdgqyhspiqskNARFNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQFGpk 296
Cdd:COG1960 210 ELFFDDVRVPAENLL---GEE-------------GKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFG-- 271

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 297 dkeeVKIIEHQMQALRLMSHLATALAVTFTSRHAddildedifqGRALTNSRSLQALMAGLKAYSTWETVSCLQDCRECT 376
Cdd:COG1960 272 ----RPIADFQAVQHRLADMAAELEAARALVYRA----------AWLLDAGEDAALEAAMAKLFATEAALEVADEALQIH 337

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 21311885 377 GGMGYMMETRISDLKCDTDVFVTFEGDNVVMLQVVARELLAQYS 420
Cdd:COG1960 338 GGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 116-221 6.47e-18

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: 79.25  E-value: 6.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885   116 FAMTERGHGSNVRGIQTEAtFDLDNQEFVIdmpceNAHKMYIGNAMHGNYAAVFAQLIIEGKSQGPHCFIVPIRDengnl 195
Cdd:pfam02770   2 FALTEPGAGSDVASLKTTA-ADGDGGGWVL-----NGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDA----- 70

                          90       100
                  ....*....|....*....|....*.
gi 21311885   196 yPGVTAIDMMHKEGMNGVDNGILIFD 221
Cdd:pfam02770  71 -PGVSVRRIETKLGVRGLPTGELVFD 95
 
Name Accession Description Interval E-value
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 51-599 9.72e-153

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: 453.71  E-value: 9.72e-153
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  51 MEEKRKSFISQILILGEVLCMVDVSMSIKCGILFLLFGGAISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGI 130
Cdd:cd01150  73 MGELMADDPEKMLALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGL 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 131 QTEATFDLDNQEFVIDMPCENAHKMYIGNAMH-GNYAAVFAQLIIEGKSQGPHCFIVPIRDENGNL-YPGVTAIDMMHKE 208
Cdd:cd01150 153 ETTATYDPLTQEFVINTPDFTATKWWPGNLGKtATHAVVFAQLITPGKNHGLHAFIVPIRDPKTHQpLPGVTVGDIGPKM 232

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 209 GMNGVDNGILIFDKVRIPRENLLDKFGSVTPDGQYHSPIQSKNARFNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSH 288
Cdd:cd01150 233 GLNGVDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSA 312

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 289 SRRQFGPKDKE-EVKIIEHQMQALRLMSHLATALAVTFTSRHADDILDE---DIFQGRAlTNSRSLQALMAGLKAYSTWE 364
Cdd:cd01150 313 VRRQFGPKPSDpEVQILDYQLQQYRLFPQLAAAYAFHFAAKSLVEMYHEiikELLQGNS-ELLAELHALSAGLKAVATWT 391

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 365 TVSCLQDCRECTGGMGYMMETRISDLKCDTDVFVTFEGDNVVMLQVVARELLAQYSKQHKknlllgviqnwtatagdklr 444
Cdd:cd01150 392 AAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYLLKKYAQAFS-------------------- 451

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 445 tsflafntdtvgcLAFLLKAVNFRERVLQRSLVSRIYYKVVTKKGDFfSAWNSCMHHVTSLSLAHIHRVALEQFTTAVRQ 524
Cdd:cd01150 452 -------------LADYLEAYEWLAAHLLRHAAAQLEKLKKSGSGSF-EARNNSQVHLRCAAKAHTEYTVLQRFHESVEE 517

                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21311885 525 CPNREDQALLMKFCLLYGTKLVFQERGWYLEHKYLTPKASMLIRAQLLNLCESVKDDALKVISAFNIPHITIRAP 599
Cdd:cd01150 518 IVDPSVRAVLKRLCDLYALWLLEEHIADFLEGGFLGGQDVKAVREALLALLPQLRPDAVALVDAFDLPDFVLNSP 592
PLN02636 PLN02636
acyl-coenzyme A oxidase
 50-599 7.69e-124

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 381.90  E-value: 7.69e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885   50 IMEEKRKSFIsqiliLGEVLCMVDVSMSIKCGILFLLFGGAISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRG 129
Cdd:PLN02636 116 LVEDPAKYFA-----ITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQG 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  130 IQTEATFDLDNQEFVIDMPCENAHKMYIGNA-MHGNYAAVFAQLIIEG------KSQGPHCFIVPIRD-ENGNLYPGVTA 201
Cdd:PLN02636 191 LQTTATFDPLTDEFVINTPNDGAIKWWIGNAaVHGKFATVFARLKLPThdskgvSDMGVHAFIVPIRDmKTHQVLPGVEI 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  202 IDMMHKEGMNGVDNGILIFDKVRIPRENLLDKFGSVTPDGQYHSPIQSKNARFNAILATLTPSRLAVTFQALGAMKLGLM 281
Cdd:PLN02636 271 RDCGHKVGLNGVDNGALRFRSVRIPRDNLLNRFGDVSRDGKYTSSLPTINKRFAATLGELVGGRVGLAYGSVGVLKASNT 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  282 IAIRYSHSRRQFGPKDKEEVKIIEHQMQALRLMSHLATALAVTFTSRHADDIL-------DEDIFQgraltnsrSLQALM 354
Cdd:PLN02636 351 IAIRYSLLRQQFGPPKQPEISILDYQSQQHKLMPMLASTYAFHFATEYLVERYsemkkthDDQLVA--------DVHALS 422

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  355 AGLKAYSTWETVSCLQDCRECTGGMGYMMETRISDLKCDTDVFVTFEGDNVVMLQVVARELLAQYsKQHKKNLLLGVIQN 434
Cdd:PLN02636 423 AGLKAYITSYTAKALSTCREACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQY-KEKFQGGTLSVTWN 501

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  435 WtatagdkLRTSFLAFNTDTVGCLA------------FLLKAVNFRERVLQRSLVSRIyyKVVTKKGDFFSAWNSCMHHV 502
Cdd:PLN02636 502 Y-------LRESMNTYLSQPNPVTTrwegeehlrdpkFQLDAFRYRTSRLLQTAALRL--RKHSKTLGSFGAWNRCLNHL 572

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  503 TSLSLAHIHRVALEQFTTAVRQCPNREDQALLMKFCLLYGTKLVFQERGWYLEHKYLTPKASMLIRAQLLNLCESVKDDA 582
Cdd:PLN02636 573 LTLAESHIESVILAKFIEAVERCPDRSTRAALKLVCDLYALDRIWKDIGTYRNVDYVAPNKAKAIHKLTEYLSFQVRNVA 652

                        570
                 ....*....|....*..
gi 21311885  583 LKVISAFNIPHITIRAP 599
Cdd:PLN02636 653 KELVDAFGLPDHVTRAP 669
PLN02312 PLN02312
acyl-CoA oxidase
 63-592 1.10e-118

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 368.33  E-value: 1.10e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885   63 LILGEVLCMVDVSMSIKCGILFLLFGGAISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGIQTEATFDLDNQE 142
Cdd:PLN02312 136 LALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEE 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  143 FVIDMPCENAHKMYIGNA-MHGNYAAVFAQLIIEGKSQGPHCFIVPIRDENGNLYPGVTAIDMMHKEGMNGVDNGILIFD 221
Cdd:PLN02312 216 FVINTPCESAQKYWIGGAaNHATHTIVFSQLHINGKNEGVHAFIAQIRDQDGNICPNIRIADCGHKIGLNGVDNGRIWFD 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  222 KVRIPRENLLDKFGSVTPDGQYHSPIQSKNARFNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQFG-PKDKEE 300
Cdd:PLN02312 296 NLRIPRENLLNSVADVSPDGKYVSAIKDPDQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAFSvTPNGPE 375

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  301 VKIIEHQMQALRLMSHLATALAVTFTsrhADDIldEDIFQGRALTNSRSLQALMAGLKAYSTWETVSCLQDCRECTGGMG 380
Cdd:PLN02312 376 VLLLDYPSHQRRLLPLLAKTYAMSFA---ANDL--KMIYVKRTPESNKAIHVVSSGFKAVLTWHNMRTLQECREACGGQG 450

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  381 YMMETRISDLKCDTDVFVTFEGDNVVMLQVVARELLAQYSKQHKKN-----LLLGVIQNWTATAGDKLRTSflafntdTV 455
Cdd:PLN02312 451 LKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAEYVSAKKRNkpfkgLGLEHMNGPRPVIPTQLTSS-------TL 523

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  456 GCLAFLLKAVNFRER-VLQR--SLVSRIYYKVVTKKGDFFSAWNScmhhVTSLSLAHIHRVALEQFTTAVRQCPNREDQA 532
Cdd:PLN02312 524 RDSQFQLNLFCLRERdLLERfaSEVSELQSKGESREFAFLLSYQL----AEDLGRAFSERAILQTFLDAEANLPTGSLKD 599

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  533 LLMKFCLLYgTKLVFQERGWYLEHKYLTPKASMLIRAQLLNLCESVKDDALKVISAFNIP 592
Cdd:PLN02312 600 VLGLLRSLY-VLISLDEDPSFLRYGYLSPDNVALVRKEVAKLCGELRPHALALVSSFGIP 658
PLN02443 PLN02443
acyl-coenzyme A oxidase
 86-590 3.23e-62

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 218.17  E-value: 3.23e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885   86 LFGGAISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGIQTEATFDLDNQEFVIDMPCENAHKMYIGN-AMHGN 164
Cdd:PLN02443 105 MFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHSPTLTSSKWWPGGlGKVST 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  165 YAAVFAQLIIEGKSQGPHCFIVPIRD-ENGNLYPGVTAIDMMHKEG---MNGVDNGILIFDKVRIPRENLLDKFGSVTPD 240
Cdd:PLN02443 185 HAVVYARLITNGKDHGIHGFIVQLRSlDDHSPLPGVTVGDIGMKFGngaYNTMDNGFLRFDHVRIPRDQMLMRLSKVTRE 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  241 GQYhspIQSKNARfNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQFGPKDKE-EVKIIEHQMQALRLMSHLAT 319
Cdd:PLN02443 265 GKY---VQSDVPR-QLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFGSQDGGpETQVIDYKTQQSRLFPLLAS 340

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  320 ALAVTFTSRHAdDILDEDIFQGRALTNSRSLQ---ALMAGLKAYSTWETVSCLQDCRECTGGMGYMMETRISDLKCdtdV 396
Cdd:PLN02443 341 AYAFRFVGEWL-KWLYTDVTQRLEANDFSTLPeahACTAGLKSLTTSATADGIEECRKLCGGHGYLCSSGLPELFA---V 416

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  397 FV---TFEGDNVVMLQVVARELLAQYSK--QHKKNL----LLGVIQNWT------ATAGDKLRTSFL--AFNTDT----V 455
Cdd:PLN02443 417 YVpacTYEGDNVVLLLQVARFLMKTVSQlgSGKKPVgttaYMGRVQHLLqcrcgvQTAEDWLNPSVVleAFEARAarmaV 496

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  456 GCLAFLLKAVNFRERVLQRSlvsriyykvvtkkGDFFSAwnscmhhvtslSLAHIHRVALEQFTTAVRQ-CPNREDQALL 534
Cdd:PLN02443 497 TCAQNLSKFENQEAGFQELS-------------ADLVEA-----------AVAHCQLIVVSKFIEKLQQdIPGKGVKKQL 552

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 21311885  535 MKFCLLYGTKLVFQERGWYLEHKYLTPKASMLIRAQLLNLCESVKDDALKVISAFN 590
Cdd:PLN02443 553 QNLCYIYALYLLHKHLGDFLSTGCITPKQASLANDQLRSLYSQVRPNAVALVDAFN 608
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 90-604 1.51e-60

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 213.55  E-value: 1.51e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885   90 AISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGIQTEATFDLDNQEFVIDMPCENAHKMYIGN-AMHGNYAAV 168
Cdd:PTZ00460 105 AFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHTPSVEAVKFWPGElGFLCNFALV 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  169 FAQLIIEGKSQGPHCFIVPIRDENGNL-YPGVTAIDMMHKEGMNGVDNGILIFDKVRIPRENLLDKFGSVTPDGQYhspi 247
Cdd:PTZ00460 185 YAKLIVNGKNKGVHPFMVRIRDKETHKpLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLARYIKVSEDGQV---- 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  248 qSKNARFNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQFGPKDKEEVKIIEHQMQALRLMSHLATALAVTFTS 327
Cdd:PTZ00460 261 -ERQGNPKVSYASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNDNKQENSVLEYQTQQQKLLPLLAEFYACIFGG 339

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  328 RHADDILDEDIfqGRALTNSRSL----QALMAGLKAYSTWETVSCLQDCRECTGGMGYMMETRISDLKCDTDVFVTFEGD 403
Cdd:PTZ00460 340 LKIKELVDDNF--NRVQKNDFSLlqltHAILSAAKANYTYFVSNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGE 417

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  404 NVVMLQVVARELLAQYSKQHKKNLLLGVIQNWTATAGDKLRtsflafNTDTVGCLAFLLKAvnfRERVLQRSLVSRIYYK 483
Cdd:PTZ00460 418 NQIMYLQLARYLLKQLQHAVQKPEKVPEYFNFLSHITEKLA------DQTTIESLGQLLGL---NCTILTIYAAKKIMDH 488

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  484 VVTKKgDFFSAWNScmhhVTSLSLAHIHRVALEQFTTAVRQ----CPNREDQALLMKFCLLYGTKLVFQERGWYLEHKYL 559
Cdd:PTZ00460 489 INTGK-DFQQSWDT----KSGIALASAASRFIEYFNYLCFLdtinNANKSTKEILTQLADLYGITMLLNNPQGLIEKGQI 563

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*...
gi 21311885  560 TPKASMLIRAQLLNLCESVKDDALKVISAFNIPHITIR---APKTGIP 604
Cdd:PTZ00460 564 TVEQIKLLQETREQLYPIIKPNALGLVEAFGLSDNSLRsliGCHDGDP 611
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 57-420 1.42e-56

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: 195.83  E-value: 1.42e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  57 SFISQILILgEVLCMVDVSMSIKCGILFLlFGGAISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGIQTEATf 136
Cdd:COG1960  65 SLVELALVL-EELARADASLALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAV- 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 137 dLDNQEFVIdmpceNAHKMYIGNAMHGNYAAVFAQLIIEGKSQGPHCFIVPiRDEngnlyPGVTAIDMMHKEGMNGVDNG 216
Cdd:COG1960 142 -RDGDGYVL-----NGQKTFITNAPVADVILVLARTDPAAGHRGISLFLVP-KDT-----PGVTVGRIEDKMGLRGSDTG 209

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 217 ILIFDKVRIPRENLLdkfGSVtpdgqyhspiqskNARFNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQFGpk 296
Cdd:COG1960 210 ELFFDDVRVPAENLL---GEE-------------GKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFG-- 271

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 297 dkeeVKIIEHQMQALRLMSHLATALAVTFTSRHAddildedifqGRALTNSRSLQALMAGLKAYSTWETVSCLQDCRECT 376
Cdd:COG1960 272 ----RPIADFQAVQHRLADMAAELEAARALVYRA----------AWLLDAGEDAALEAAMAKLFATEAALEVADEALQIH 337

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 21311885 377 GGMGYMMETRISDLKCDTDVFVTFEGDNVVMLQVVARELLAQYS 420
Cdd:COG1960 338 GGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 85-413 5.08e-46

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: 165.53  E-value: 5.08e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  85 LLFGGAISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGIQTEATfdLDNQEFVIdmpceNAHKMYIGNAMHGN 164
Cdd:cd00567  42 LLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTAR--KDGDGYVL-----NGRKIFISNGGDAD 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 165 YAAVFAQLIIEGK-SQGPHCFIVPIRDengnlyPGVTAIDMMHKEGMNGVDNGILIFDKVRIPRENLLDKFGSVtpdgqy 243
Cdd:cd00567 115 LFIVLARTDEEGPgHRGISAFLVPADT------PGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGG------ 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 244 hspiqsknarFNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQFGpkdkeeVKIIEHQMQALRL----MSHLAT 319
Cdd:cd00567 183 ----------FELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFG------KPLAEFQAVQFKLadmaAELEAA 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 320 ALAVTFTSRHADDILDEDifqgraltnsrSLQALMAglKAYSTWETVSCLQDCRECTGGMGYMMETRISDLKCDTDVFVT 399
Cdd:cd00567 247 RLLLYRAAWLLDQGPDEA-----------RLEAAMA--KLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARI 313

                       330
                ....*....|....
gi 21311885 400 FEGDNVVMLQVVAR 413
Cdd:cd00567 314 AEGTAEIQRLIIAR 327
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 91-416 4.90e-29

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: 119.14  E-value: 4.90e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  91 ISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGIQTEATfdLDNQEFVIdmpceNAHKMYIGNAMHGNYAAVFA 170
Cdd:cd01160  91 ITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTAR--KDGDHYVL-----NGSKTFITNGMLADVVIVVA 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 171 QLIIEGKSQ-GPHCFIVpirdENGNlyPGVTAIDMMHKEGMNGVDNGILIFDKVRIPRENLLdkfgsvtpdGQyhspiqs 249
Cdd:cd01160 164 RTGGEARGAgGISLFLV----ERGT--PGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLL---------GE------- 221

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 250 KNARFNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQFGpKDKEEVKIIEHQmqalrlMSHLATALAVTftsRH 329
Cdd:cd01160 222 ENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFG-KTLAQLQVVRHK------IAELATKVAVT---RA 291

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 330 ADDILDEDIFQGRaltnSRSLQALMAglKAYSTWETVSCLQDCRECTGGMGYMMETRISDLKCDTDVFVTFEGDNVVMLQ 409
Cdd:cd01160 292 FLDNCAWRHEQGR----LDVAEASMA--KYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKE 365


                ....*..
gi 21311885 410 VVARELL 416
Cdd:cd01160 366 LISRQMV 372
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 57-417 1.16e-28

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: 117.75  E-value: 1.16e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  57 SFISQILILGEvLCMVDVSMSIKCGILFLLFGGAISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGIQTEATF 136
Cdd:cd01158  59 DFLAYAIAIEE-LAKVDASVAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKK 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 137 DLDnqEFVIdmpceNAHKMYIGNAMHGNYAAVFAqliIEGKSQGPH---CFIVPiRDEngnlyPGVTAIDMMHKEGMNGV 213
Cdd:cd01158 138 DGD--DYVL-----NGSKMWITNGGEADFYIVFA---VTDPSKGYRgitAFIVE-RDT-----PGLSVGKKEDKLGIRGS 201

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 214 DNGILIFDKVRIPRENLLDKFGsvtpDGqyhspiqsknarFNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQF 293
Cdd:cd01158 202 STTELIFEDVRVPKENILGEEG----EG------------FKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQF 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 294 GpKDKEEVKIIEH-------QMQALRLMSHLATALAVtftsrhaddildedifQGRALTNsrslQALMAGLKAYSTWETV 366
Cdd:cd01158 266 G-KPIADFQGIQFkladmatEIEAARLLTYKAARLKD----------------NGEPFIK----EAAMAKLFASEVAMRV 324

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 21311885 367 SclQDCRECTGGMGYMMETRISDLKCDTDVFVTFEGDNVVMLQVVARELLA 417
Cdd:cd01158 325 T--TDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 60-419 1.64e-21

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: 97.15  E-value: 1.64e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  60 SQILILGEVLCM---VDVSMSIKCGILFLlfggAISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGIQTEATF 136
Cdd:cd01161  87 TQYARLAEIVGMdlgFSVTLGAHQSIGFK----GILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVL 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 137 DLDNQEFVIdmpceNAHKMYIGNAMHGNYAAVFAQLIIE----GKSQGPHCFIVPiRDengnlYPGVTAIDMMHKEGMNG 212
Cdd:cd01161 163 SEDGKHYVL-----NGSKIWITNGGIADIFTVFAKTEVKdatgSVKDKITAFIVE-RS-----FGGVTNGPPEKKMGIKG 231

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 213 VDNGILIFDKVRIPRENLLDKFGsvtpDGqyhspiqsknarFNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQ 292
Cdd:cd01161 232 SNTAEVYFEDVKIPVENVLGEVG----DG------------FKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQ 295

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 293 FGPKDKEEVKIIEHqmqalrlMSHLATALAVT-----FTSRHADdildedifqgRALTNSRSLQALMAglKAYSTWETVS 367
Cdd:cd01161 296 FGKKIHEFGLIQEK-------LANMAILQYATesmayMTSGNMD----------RGLKAEYQIEAAIS--KVFASEAAWL 356

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 21311885 368 CLQDCRECTGGMGYMMETRISDLKCDTDVFVTFEGDNVVMLQVVARELLAQY 419
Cdd:cd01161 357 VVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALTGLQHA 408
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 89-414 1.31e-20

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: 94.35  E-value: 1.31e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  89 GAISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGIQTEATFDldNQEFVIdmpceNAHKMYIGNAMHGNYAAV 168
Cdd:cd01151 103 LPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKD--GGGYKL-----NGSKTWITNSPIADVFVV 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 169 FAQLIIEGKSQGphcFIVPiRDengnlYPGVTAIDMMHKEGMNGVDNGILIFDKVRIPRENLLDkfgsvtpdgqyhspiq 248
Cdd:cd01151 176 WARNDETGKIRG---FILE-RG-----MKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLP---------------- 230

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 249 skNARFN-AILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQFGpkdkeeVKIIEHQMQALRLMSHLATALAVTFTS 327
Cdd:cd01151 231 --GAEGLrGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFG------RPLAAFQLVQKKLADMLTEIALGLLAC 302

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 328 RHADDILDedifQGRALTNSRSLqalmagLKAYSTWETVSCLQDCRECTGGMGYMMETRISDLKCDTDVFVTFEGDNVVM 407
Cdd:cd01151 303 LRVGRLKD----QGKATPEQISL------LKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIH 372


                ....*..
gi 21311885 408 LQVVARE 414
Cdd:cd01151 373 ALILGRA 379
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 89-296 5.26e-19

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: 89.39  E-value: 5.26e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  89 GAISNL--------GSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGIQTEATFDLDNqeFVIdmpceNAHKMYIGNA 160
Cdd:cd01156  85 GAHSNLcinqiyrnGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDR--YVL-----NGSKMWITNG 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 161 MHGNYAAVFAQLIIEGKSQGPHCFIVpirdENGnlYPGVTAIDMMHKEGMNGVDNGILIFDKVRIPRENLLDKFGSvtpd 240
Cdd:cd01156 158 PDADTLVVYAKTDPSAGAHGITAFIV----EKG--MPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENK---- 227

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21311885 241 GQYhspiqsknarfnAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQFGPK 296
Cdd:cd01156 228 GVY------------VLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQP 271
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 116-221 6.47e-18

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: 79.25  E-value: 6.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885   116 FAMTERGHGSNVRGIQTEAtFDLDNQEFVIdmpceNAHKMYIGNAMHGNYAAVFAQLIIEGKSQGPHCFIVPIRDengnl 195
Cdd:pfam02770   2 FALTEPGAGSDVASLKTTA-ADGDGGGWVL-----NGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDA----- 70

                          90       100
                  ....*....|....*....|....*.
gi 21311885   196 yPGVTAIDMMHKEGMNGVDNGILIFD 221
Cdd:pfam02770  71 -PGVSVRRIETKLGVRGLPTGELVFD 95
ACOX pfam01756
Acyl-CoA oxidase; This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts ...
 471-592 2.59e-17

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: 79.90  E-value: 2.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885   471 VLQRSLVSRIYYKVVT---------KKG-DFFSAWNSCMHHVTSLSLAHIHRVALEQFTTAVRQCPNREDQALLMKFCLL 540
Cdd:pfam01756   4 VLLKAFEWRAARLLREaaeklqallKSGkSQFEAWNNQSVELVRAAKAHAEYFVLRTFVERLSTSLDPPLKPVLKKLCKL 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21311885   541 YGTKLVFQERGWYLEHKYLTPKASMLIRAQLLNLCESVKDDALKVISAFNIP 592
Cdd:pfam01756  84 YALWTIEKHLGDFLQGGYLSPEQIDLIREAILELLAELRPNAVALVDAFDFP 135
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 91-418 1.68e-15

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: 78.64  E-value: 1.68e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  91 ISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGIQTEATFDLDnqEFVIdmpceNAHKMYIGNAMHGNYAAVFA 170
Cdd:cd01162  93 IDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGD--HYVL-----NGSKAFISGAGDSDVYVVMA 165

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 171 QLIIEGkSQGPHCFIVpirdENGNlyPGVTAIDMMHKEGMNGVDNGILIFDKVRIPRENLLdkfgsvTPDGQyhspiqsk 250
Cdd:cd01162 166 RTGGEG-PKGISCFVV----EKGT--PGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRL------GGEGQ-------- 224

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 251 naRFNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQFGPKDKEEvkiiehqmQALRL-MSHLATAL-AVTFTSR 328
Cdd:cd01162 225 --GFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADF--------QALQFkLADMATELvASRLMVR 294

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 329 HADDILDEDIFQGRALTNsrslqalMAglKAYSTWETVSCLQDCRECTGGMGYMMETRISDLKCDTDVFVTFEGDNVVML 408
Cdd:cd01162 295 RAASALDRGDPDAVKLCA-------MA--KRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMR 365

                       330
                ....*....|
gi 21311885 409 QVVARELLAQ 418
Cdd:cd01162 366 LIIARALLTR 375
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 97-411 1.94e-15

Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.


Pssm-ID: 173843 [Multi-domain]  Cd Length: 418  Bit Score: 78.95  E-value: 1.94e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  97 PEHVTKWFWPLKEQKY-TGMFA---MTERGHGSNVRGIQTEATFDLDnqefviDMPCENAHKMYIGNAMhGNYAAVFAQl 172
Cdd:cd01154 128 PEELKQYLPGLLSDRYkTGLLGgtwMTEKQGGSDLGANETTAERSGG------GVYRLNGHKWFASAPL-ADAALVLAR- 199

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 173 iIEGK---SQGPHCFIVPIRDENGNLypgvtaidmmhkegmngvdNGIlifdkvRIPRenLLDKFGS-------VTPDGQ 242
Cdd:cd01154 200 -PEGApagARGLSLFLVPRLLEDGTR-------------------NGY------RIRR--LKDKLGTrsvatgeVEFDDA 251

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 243 YHSPIQSKNARFNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQFGPkdkeevKIIEH---QMQALRLMSHLAT 319
Cdd:cd01154 252 EAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGK------PLIDHplmRRDLAEMEVDVEA 325

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 320 ALAVTFtsRHAddildeDIFQGRAltNSRSLQALMAGL-----KAYSTWETVSCLQDCRECTGGMGYMMETRISDLKCDT 394
Cdd:cd01154 326 ATALTF--RAA------RAFDRAA--ADKPVEAHMARLatpvaKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREA 395

                       330
                ....*....|....*...
gi 21311885 395 DVFVTFEG-DNVVMLQVV 411
Cdd:cd01154 396 QVTPIWEGtGNIQALDVL 413
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 95-416 2.15e-14

Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.


Pssm-ID: 173846 [Multi-domain]  Cd Length: 378  Bit Score: 75.31  E-value: 2.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  95 GSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGIQTEATFDLDnqEFVIdmpceNAHKMYIGNAMHGNYAAVFAQLII 174
Cdd:cd01157  97 GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD--EYII-----NGQKMWITNGGKANWYFLLARSDP 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 175 EGK---SQGPHCFIVPiRDENGnLYPGVTAIDMmhkeGMNGVDNGILIFDKVRIPRENLLDKFGsvtpdgqyhspiqskn 251
Cdd:cd01157 170 DPKcpaSKAFTGFIVE-ADTPG-IQPGRKELNM----GQRCSDTRGITFEDVRVPKENVLIGEG---------------- 227

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 252 ARFNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQFGpkdkeeVKIIEHQmqALRLMshLATALAVTFTSRHAD 331
Cdd:cd01157 228 AGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFG------KLIAEHQ--AVSFM--LADMAMKVELARLAY 297

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 332 DILDEDIFQGRALTNSRSLQalmaglKAYSTWETVSCLQDCRECTGGMGYMMETRISDLKCDTDVFVTFEGDNVVMLQVV 411
Cdd:cd01157 298 QRAAWEVDSGRRNTYYASIA------KAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLII 371


                ....*
gi 21311885 412 ARELL 416
Cdd:cd01157 372 SREHL 376
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 89-418 9.12e-13

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 70.29  E-value: 9.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885   89 GAISNL--------GSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGIQTEAtfDLDNQEFVIdmpceNAHKMYIGNA 160
Cdd:PLN02519 111 GAHSNLcinqlvrnGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKA--ERVDGGYVL-----NGNKMWCTNG 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  161 MHGNYAAVFAQLIIEGKSQGPHCFIVpirdENGnlYPGVTAIDMMHKEGMNGVDNGILIFDKVRIPRENLLDKFGSvtpd 240
Cdd:PLN02519 184 PVAQTLVVYAKTDVAAGSKGITAFII----EKG--MPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGK---- 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  241 GQYhspiqsknarfnAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQFGpKDKEEVKIIEHQMQAL--RLMSHLA 318
Cdd:PLN02519 254 GVY------------VMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFG-RPIGEFQFIQGKLADMytSLQSSRS 320

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  319 TALAVtftSRHADDildedifqGRALTNSRSLQALMAGLKAystweTVSCLQDCrECTGGMGYMMETRISDLKCDTDVFV 398
Cdd:PLN02519 321 YVYSV---ARDCDN--------GKVDRKDCAGVILCAAERA-----TQVALQAI-QCLGGNGYINEYPTGRLLRDAKLYE 383

                        330       340
                 ....*....|....*....|
gi 21311885  399 TFEGDNVVMLQVVARELLAQ 418
Cdd:PLN02519 384 IGAGTSEIRRMLIGRELFKE 403
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 88-412 6.15e-12

Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.


Pssm-ID: 173842 [Multi-domain]  Cd Length: 407  Bit Score: 67.80  E-value: 6.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  88 GGAISNL---GSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGIQTEATFDLDNQEFVidmpceNAHKMYI------- 157
Cdd:cd01153  90 QGAAATLlahGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRI------NGVKRFIsagehdm 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 158 -GNAMHgnyaAVFAQL--IIEGkSQGPHCFIVPIRDENGNlYPGVTAIDMMHKEGMNGVDNGILIFDKVRIPrenLLdkf 234
Cdd:cd01153 164 sENIVH----LVLARSegAPPG-VKGLSLFLVPKFLDDGE-RNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LI--- 231

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 235 gsvtpdGQYHSPIQsknarfnAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQFGP--KDKEEVKIIEH------ 306
Cdd:cd01153 232 ------GEEGMGLA-------QMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDliKAAPAVTIIHHpdvrrs 298

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885 307 -QMQALRLMSHLATALavtFTSRHADDILDEDIFQGRALTNSRSLQALMAGLKAYSTWETVSCLQDCRECTGGMGYMMET 385
Cdd:cd01153 299 lMTQKAYAEGSRALDL---YTATVQDLAERKATEGEDRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREY 375

                       330       340
                ....*....|....*....|....*..
gi 21311885 386 RISDLKCDTDVFVTFEGDNvvMLQVVA 412
Cdd:cd01153 376 PIEQYYRDARITTIYEGTT--GIQALD 400
PLN02526 PLN02526
acyl-coenzyme A oxidase
 64-415 1.55e-11

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 66.80  E-value: 1.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885   64 ILGEVLCM-----VDVSMSIKCGILFLLFGGAISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGIQTEAT--- 135
Cdd:PLN02526  89 ITASAIATaevarVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATkve 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  136 --FDLDNQefvidmpcenahKMYIGNAMHGNYAAVFAQLIIEGKSQGphcFIVpirdENGNlyPGVTAIDMMHKEGMNGV 213
Cdd:PLN02526 169 ggWILNGQ------------KRWIGNSTFADVLVIFARNTTTNQING---FIV----KKGA--PGLKATKIENKIGLRMV 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  214 DNGILIFDKVRIPRENLLDKFGSvtpdgqyhspiqsknarFNAILATLTPSRLAVTFQALGaMKLGLM-IAIRYSHSRRQ 292
Cdd:PLN02526 228 QNGDIVLKDVFVPDEDRLPGVNS-----------------FQDTNKVLAVSRVMVAWQPIG-ISMGVYdMCHRYLKERKQ 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  293 FGpkdkeeVKIIEHQMQALRLMSHLATALAVTFTSRHADDILDedifQGRALTNSRSLQALMAGLKAYstwETVSClqdC 372
Cdd:PLN02526 290 FG------APLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYE----SGKMTPGHASLGKAWITKKAR---ETVAL---G 353

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 21311885  373 RECTGGMGYMMETRISDLKCDTDVFVTFEGDNVVMLQVVAREL 415
Cdd:PLN02526 354 RELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 254-415 2.95e-10

Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.


Pssm-ID: 395354 [Multi-domain]  Cd Length: 149  Bit Score: 58.80  E-value: 2.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885   254 FNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQFGpkdkeeVKIIEHQMQALRLmSHLATAL-AVTFTSRHADD 332
Cdd:pfam00441   4 FRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFG------RPLIDFQLVRHKL-AEMAAEIeAARLLVYRAAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885   333 ILDEDIFQGraltnsrslqALMAGLKAYSTWETVSCLQDCRECTGGMGYMMETRISDLKCDTDVFVTFEGDNVVMLQVVA 412
Cdd:pfam00441  77 ALDAGGPDG----------AEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146


                  ...
gi 21311885   413 REL 415
Cdd:pfam00441 147 RRL 149
PRK12341 PRK12341
acyl-CoA dehydrogenase;
67-419 2.13e-08

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 56.66  E-value: 2.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885   67 EVLCMVDVSMSI-KCGILFLLFGGA-----ISNLGSPEHVTKWFwplKEQKYTG----MFAMTERGHGSNVRGIQTEATf 136
Cdd:PRK12341  66 DYVTQMLVLEEVsKCGAPAFLITNGqcihsMRRFGSAEQLRKTA---ESTLETGdpayALALTEPGAGSDNNSATTTYT- 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  137 dLDNQEFVIdmpceNAHKMYIGNAMHGNYAAVFAQliiEGKSQGPH-CF---IVPIRDengnlyPGVTaIDMMHKEGMNG 212
Cdd:PRK12341 142 -RKNGKVYL-----NGQKTFITGAKEYPYMLVLAR---DPQPKDPKkAFtlwWVDSSK------PGIK-INPLHKIGWHM 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  213 VDNGILIFDKVRIPRENLLDKFGsvtpDGqyhspiqsknarFNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQ 292
Cdd:PRK12341 206 LSTCEVYLDNVEVEESDLVGEEG----MG------------FLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQ 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  293 FGPKDKEEVKIIEH--QMQA-LRLMSHLatalaVTFTSRHADdildedifqgraltNSRSLQALMAGLKAYSTWETVSCL 369
Cdd:PRK12341 270 FGKPIGHNQLIQEKltLMAIkIENMRNM-----VYKVAWQAD--------------NGQSLRTSAALAKLYCARTAMEVI 330

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 21311885  370 QDCRECTGGMGYMMETRISDLKCDTDVFVTFEGDNVVMLQVVARELLAQY 419
Cdd:PRK12341 331 DDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDY 380
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 85-390 4.61e-07

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 52.63  E-value: 4.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885   85 LLFGGAISNLGSPEHVTKWFWPLKEQKYTGMFAMTERGHGSNVRGIQTEATFDlDNQEFVIdmpceNAHKMYIGNAMHGN 164
Cdd:PTZ00461 124 MLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKD-SNGNYVL-----NGSKIWITNGTVAD 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  165 YAAVFAQliIEGKSQGphcFIVpirdENGNlyPGVTAIDMMHKEGMNGVDNGILIFDKVRIPRENLLDKFGSvtpdgqyh 244
Cdd:PTZ00461 198 VFLIYAK--VDGKITA---FVV----ERGT--KGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGK-------- 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311885  245 spiqsknaRFNAILATLTPSRLAVTFQALGAMKLGLMIAIRYSHSRRQFGpkdkeevKIIEHQMQALRLmshlataLAVT 324
Cdd:PTZ00461 259 --------GMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFG-------KPISNFGQIQRY-------IAEG 316

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21311885  325 FTSRHADDILDEDIFQGRALTNSRSLQALMAGLKAYSTWETVSclQDCRECTGGMGYMMETRISDL 390
Cdd:PTZ00461 317 YADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFATPIAKKVA--DSAIQVMGGMGYSRDMPVERL 380
 
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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