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Conserved domains on  [gi|767918731|ref|XP_011509730|]
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acyl-coenzyme A oxidase-like protein isoform X14 [Homo sapiens]

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 ...
 2-396 2.44e-122

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: 370.12  E-value: 2.44e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731   2 RALTVQRV--KFAMDLPLLKRAGQDLAEKTknfvsrsLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQ 79
Cdd:cd01150   55 REELYEELkrKAKTDVERMGELMADDPEKM-------LALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQ 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  80 PLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGN-AMYGNYAAVFAQLIIDGRSQGPHCF 158
Cdd:cd01150  128 GANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFVINTPDFTATKWWPGNlGKTATHAVVFAQLITPGKNHGLHAF 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 159 IVPVRDENG-SLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTP 237
Cdd:cd01150  208 IVPIRDPKThQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSG 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 238 SRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKE-EVKIIEHQTQTLRLMPHLATALALTFVSRY-------AGALLD 309
Cdd:cd01150  288 GRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKPSDpEVQILDYQLQQYRLFPQLAAAYAFHFAAKSlvemyheIIKELL 367

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 310 EDVFQgkelvNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGREL 389
Cdd:cd01150  368 QGNSE-----LLAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYL 442


                 ....*..
gi 767918731 390 LAQYTKQ 396
Cdd:cd01150  443 LKKYAQA 449
 
Name Accession Description Interval E-value
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
 2-396 2.44e-122

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: 370.12  E-value: 2.44e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731   2 RALTVQRV--KFAMDLPLLKRAGQDLAEKTknfvsrsLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQ 79
Cdd:cd01150   55 REELYEELkrKAKTDVERMGELMADDPEKM-------LALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQ 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  80 PLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGN-AMYGNYAAVFAQLIIDGRSQGPHCF 158
Cdd:cd01150  128 GANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFVINTPDFTATKWWPGNlGKTATHAVVFAQLITPGKNHGLHAF 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 159 IVPVRDENG-SLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTP 237
Cdd:cd01150  208 IVPIRDPKThQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSG 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 238 SRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKE-EVKIIEHQTQTLRLMPHLATALALTFVSRY-------AGALLD 309
Cdd:cd01150  288 GRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKPSDpEVQILDYQLQQYRLFPQLAAAYAFHFAAKSlvemyheIIKELL 367

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 310 EDVFQgkelvNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGREL 389
Cdd:cd01150  368 QGNSE-----LLAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYL 442


                 ....*..
gi 767918731 390 LAQYTKQ 396
Cdd:cd01150  443 LKKYAQA 449
PLN02312 PLN02312
acyl-CoA oxidase
 2-446 1.64e-112

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 346.76  E-value: 1.64e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731   2 RALTVQRVKFamdlpLLKRAGQD--LAEKTKNFVSRSLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQ 79
Cdd:PLN02312 104 REITMKRILY-----LLERGVFRgwLTETGPEAELRKLALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLK 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  80 PLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGNA-MYGNYAAVFAQLIIDGRSQGPHCF 158
Cdd:PLN02312 179 DTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINTPCESAQKYWIGGAaNHATHTIVFSQLHINGKNEGVHAF 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 159 IVPVRDENGSLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTPS 238
Cdd:PLN02312 259 IAQIRDQDGNICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPDQRFGAFLAPLTSG 338

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 239 RLAVAFQAMGAMKLGLTIAIRYSHSRRQF-----GPktkeEVKIIEHQTQTLRLMPHLATALALTFVSRYAgalldEDVF 313
Cdd:PLN02312 339 RVTIAVSAIYSSKVGLAIAIRYSLSRRAFsvtpnGP----EVLLLDYPSHQRRLLPLLAKTYAMSFAANDL-----KMIY 409

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 314 QGKELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQY 393
Cdd:PLN02312 410 VKRTPESNKAIHVVSSGFKAVLTWHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAEY 489

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767918731 394 -TKQYEEKPLFGL----LQNWAESVGDKLRTSflafnmdTVDDLAFLLKAVKFRERVL 446
Cdd:PLN02312 490 vSAKKRNKPFKGLglehMNGPRPVIPTQLTSS-------TLRDSQFQLNLFCLRERDL 540
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 37-393 1.80e-58

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: 197.37  E-value: 1.80e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  37 LVIGEVLSMADMATGVKCGIiYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQE 116
Cdd:COG1960   70 ALVLEELARADASLALPVGV-HNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRD--GDG 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 117 FVIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPvRDEngslyPGVTAIDMMYKEGLHGVDNGILIFDK 196
Cdd:COG1960  147 YVL-----NGQKTFITNAPVADVILVLARTDPAAGHRGISLFLVP-KDT-----PGVTVGRIEDKMGLRGSDTGELFFDD 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 197 VRIPRENLLDKFGsvapdgqyhspirnksARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpktkeeVK 276
Cdd:COG1960  216 VRVPAENLLGEEG----------------KGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFG------RP 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 277 IIEHQTQTLRLMPHLATALALTFVSRYAGALLDEDvfqgkelvnsRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYM 356
Cdd:COG1960  274 IADFQAVQHRLADMAAELEAARALVYRAAWLLDAG----------EDAALEAAMAKLFATEAALEVADEALQIHGGYGYT 343

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 767918731 357 MENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQY 393
Cdd:COG1960  344 REYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRP 380
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 90-195 7.19e-16

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: 72.70  E-value: 7.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731   90 FAMTERGHGSNARGIQTEAtFDLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPVRDengsl 169
Cdd:pfam02770   2 FALTEPGAGSDVASLKTTA-ADGDGGGWVL-----NGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDA----- 70

                          90       100
                  ....*....|....*....|....*.
gi 767918731  170 yPGVTAIDMMYKEGLHGVDNGILIFD 195
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 ...
 2-396 2.44e-122

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: 370.12  E-value: 2.44e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731   2 RALTVQRV--KFAMDLPLLKRAGQDLAEKTknfvsrsLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQ 79
Cdd:cd01150   55 REELYEELkrKAKTDVERMGELMADDPEKM-------LALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQ 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  80 PLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGN-AMYGNYAAVFAQLIIDGRSQGPHCF 158
Cdd:cd01150  128 GANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFVINTPDFTATKWWPGNlGKTATHAVVFAQLITPGKNHGLHAF 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 159 IVPVRDENG-SLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTP 237
Cdd:cd01150  208 IVPIRDPKThQPLPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDVSPDGTYVSPFKDPNKRYGAMLGTRSG 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 238 SRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKE-EVKIIEHQTQTLRLMPHLATALALTFVSRY-------AGALLD 309
Cdd:cd01150  288 GRVGLIYDAAMSLKKAATIAIRYSAVRRQFGPKPSDpEVQILDYQLQQYRLFPQLAAAYAFHFAAKSlvemyheIIKELL 367

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 310 EDVFQgkelvNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGREL 389
Cdd:cd01150  368 QGNSE-----LLAELHALSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTANYL 442


                 ....*..
gi 767918731 390 LAQYTKQ 396
Cdd:cd01150  443 LKKYAQA 449
PLN02312 PLN02312
acyl-CoA oxidase
 2-446 1.64e-112

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 346.76  E-value: 1.64e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731   2 RALTVQRVKFamdlpLLKRAGQD--LAEKTKNFVSRSLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQ 79
Cdd:PLN02312 104 REITMKRILY-----LLERGVFRgwLTETGPEAELRKLALLEVIGIYDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLK 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  80 PLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGNA-MYGNYAAVFAQLIIDGRSQGPHCF 158
Cdd:PLN02312 179 DTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINTPCESAQKYWIGGAaNHATHTIVFSQLHINGKNEGVHAF 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 159 IVPVRDENGSLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTPS 238
Cdd:PLN02312 259 IAQIRDQDGNICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSVADVSPDGKYVSAIKDPDQRFGAFLAPLTSG 338

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 239 RLAVAFQAMGAMKLGLTIAIRYSHSRRQF-----GPktkeEVKIIEHQTQTLRLMPHLATALALTFVSRYAgalldEDVF 313
Cdd:PLN02312 339 RVTIAVSAIYSSKVGLAIAIRYSLSRRAFsvtpnGP----EVLLLDYPSHQRRLLPLLAKTYAMSFAANDL-----KMIY 409

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 314 QGKELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQY 393
Cdd:PLN02312 410 VKRTPESNKAIHVVSSGFKAVLTWHNMRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDNNVLMQQVSKALLAEY 489

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767918731 394 -TKQYEEKPLFGL----LQNWAESVGDKLRTSflafnmdTVDDLAFLLKAVKFRERVL 446
Cdd:PLN02312 490 vSAKKRNKPFKGLglehMNGPRPVIPTQLTSS-------TLRDSQFQLNLFCLRERDL 540
PLN02636 PLN02636
acyl-coenzyme A oxidase
 34-398 6.99e-105

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 327.20  E-value: 6.99e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  34 SRSLVIGEVLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLS 113
Cdd:PLN02636 121 AKYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPL 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 114 AQEFVIDTPCENAEKMYIGNA-MYGNYAAVFAQLIIDG------RSQGPHCFIVPVRD-ENGSLYPGVTAIDMMYKEGLH 185
Cdd:PLN02636 201 TDEFVINTPNDGAIKWWIGNAaVHGKFATVFARLKLPThdskgvSDMGVHAFIVPIRDmKTHQVLPGVEIRDCGHKVGLN 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 186 GVDNGILIFDKVRIPRENLLDKFGSVAPDGQYHSPIRNKSARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRR 265
Cdd:PLN02636 281 GVDNGALRFRSVRIPRDNLLNRFGDVSRDGKYTSSLPTINKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQ 360

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 266 QFGPKTKEEVKIIEHQTQTLRLMPHLATALALTFVSRYAGALLDE-DVFQGKELVNsrSLQALVAGLKAYSTWENIRCLQ 344
Cdd:PLN02636 361 QFGPPKQPEISILDYQSQQHKLMPMLASTYAFHFATEYLVERYSEmKKTHDDQLVA--DVHALSAGLKAYITSYTAKALS 438

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767918731 345 DCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQYTKQYE 398
Cdd:PLN02636 439 TCREACGGHGYAAVNRFGSLRNDHDIFQTFEGDNTVLLQQVAADLLKQYKEKFQ 492
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
 64-437 2.36e-61

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 211.63  E-value: 2.36e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  64 AIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGN-AMYGNYAAV 142
Cdd:PTZ00460 105 AFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHTPSVEAVKFWPGElGFLCNFALV 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 143 FAQLIIDGRSQGPHCFIVPVRDENG-SLYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVAPDGQYhspI 221
Cdd:PTZ00460 185 YAKLIVNGKNKGVHPFMVRIRDKEThKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLARYIKVSEDGQV---E 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 222 R--NKSARFNAMLAaltpSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKEEVKIIEHQTQTLRLMPHLATALALTF 299
Cdd:PTZ00460 262 RqgNPKVSYASMMY----MRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNDNKQENSVLEYQTQQQKLLPLLAEFYACIF 337

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 300 VSRYAGALLDEDV--FQGKELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGD 377
Cdd:PTZ00460 338 GGLKIKELVDDNFnrVQKNDFSLLQLTHAILSAAKANYTYFVSNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGE 417

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767918731 378 DVVMLQVVGRELLAQYtKQYEEKP-----LFGLLQNWAESVGDKlrtsflafnmDTVDDLAFLLK 437
Cdd:PTZ00460 418 NQIMYLQLARYLLKQL-QHAVQKPekvpeYFNFLSHITEKLADQ----------TTIESLGQLLG 471
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 37-393 1.80e-58

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: 197.37  E-value: 1.80e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  37 LVIGEVLSMADMATGVKCGIiYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQE 116
Cdd:COG1960   70 ALVLEELARADASLALPVGV-HNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRD--GDG 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 117 FVIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPvRDEngslyPGVTAIDMMYKEGLHGVDNGILIFDK 196
Cdd:COG1960  147 YVL-----NGQKTFITNAPVADVILVLARTDPAAGHRGISLFLVP-KDT-----PGVTVGRIEDKMGLRGSDTGELFFDD 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 197 VRIPRENLLDKFGsvapdgqyhspirnksARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpktkeeVK 276
Cdd:COG1960  216 VRVPAENLLGEEG----------------KGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFG------RP 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 277 IIEHQTQTLRLMPHLATALALTFVSRYAGALLDEDvfqgkelvnsRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYM 356
Cdd:COG1960  274 IADFQAVQHRLADMAAELEAARALVYRAAWLLDAG----------EDAALEAAMAKLFATEAALEVADEALQIHGGYGYT 343

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 767918731 357 MENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQY 393
Cdd:COG1960  344 REYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRP 380
PLN02443 PLN02443
acyl-coenzyme A oxidase
 57-390 2.12e-57

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 201.22  E-value: 2.12e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  57 IYW-LFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVIDTPCENAEKMYIGN-A 134
Cdd:PLN02443 101 LHWgMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHSPTLTSSKWWPGGlG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 135 MYGNYAAVFAQLIIDGRSQGPHCFIVPVRD-ENGSLYPGVTAIDMMYKEGLHG---VDNGILIFDKVRIPRENLLDKFGS 210
Cdd:PLN02443 181 KVSTHAVVYARLITNGKDHGIHGFIVQLRSlDDHSPLPGVTVGDIGMKFGNGAyntMDNGFLRFDHVRIPRDQMLMRLSK 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 211 VAPDGQYHSPIRNKSARFNAMLAAltpsRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKE-EVKIIEHQTQTLRLMP 289
Cdd:PLN02443 261 VTREGKYVQSDVPRQLVYGTMVYV----RQTIVADASTALSRAVCIATRYSAVRRQFGSQDGGpETQVIDYKTQQSRLFP 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 290 HLATALALTFVSRYAGALLdEDVFQGKELVNSRSLQ---ALVAGLKAYSTWENIRCLQDCRECTGGMGYMMEnriSGLKc 366
Cdd:PLN02443 337 LLASAYAFRFVGEWLKWLY-TDVTQRLEANDFSTLPeahACTAGLKSLTTSATADGIEECRKLCGGHGYLCS---SGLP- 411

                        330       340       350
                 ....*....|....*....|....*....|
gi 767918731 367 dtDVFA------TFEGDDVVMLQVVGRELL 390
Cdd:PLN02443 412 --ELFAvyvpacTYEGDNVVLLLQVARFLM 439
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 58-387 2.43e-44

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: 158.22  E-value: 2.43e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  58 YWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQEFVIdtpceNAEKMYIGNAMYG 137
Cdd:cd00567   41 LLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKD--GDGYVL-----NGRKIFISNGGDA 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 138 NYAAVFAQLIIDG-RSQGPHCFIVPvRDEngslyPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSVapdgq 216
Cdd:cd00567  114 DLFIVLARTDEEGpGHRGISAFLVP-ADT-----PGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGG----- 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 217 yhspirnksarFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpktkeeVKIIEHQTQTLRLMPHLATALA 296
Cdd:cd00567  183 -----------FELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFG------KPLAEFQAVQFKLADMAAELEA 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 297 LTFVSRYAGALLDEDvfqgkelvnSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEG 376
Cdd:cd00567  246 ARLLLYRAAWLLDQG---------PDEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEG 316

                        330
                 ....*....|.
gi 767918731 377 DDVVMLQVVGR 387
Cdd:cd00567  317 TAEIQRLIIAR 327
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 31-391 1.72e-29

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: 118.91  E-value: 1.72e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  31 NFVSRSLVIGEvLSMADMATGVKCGIIYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATF 110
Cdd:cd01158   59 DFLAYAIAIEE-LAKVDASVAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKK 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 111 DlsAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPvRDEngslyPGVTAIDMMYKEGLHGVDNG 190
Cdd:cd01158  138 D--GDDYVL-----NGSKMWITNGGEADFYIVFAVTDPSKGYRGITAFIVE-RDT-----PGLSVGKKEDKLGIRGSSTT 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 191 ILIFDKVRIPRENLLDKFGsvapDGqyhspirnksarFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpK 270
Cdd:cd01158  205 ELIFEDVRVPKENILGEEG----EG------------FKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFG-K 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 271 TKEEVKIIEHQTQTLRLMphLATALALTFVsryAGALLDedvfQGKELVNSRSLQALVAGLKAystwenIRCLQDCRECT 350
Cdd:cd01158  268 PIADFQGIQFKLADMATE--IEAARLLTYK---AARLKD----NGEPFIKEAAMAKLFASEVA------MRVTTDAVQIF 332

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 767918731 351 GGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLA 391
Cdd:cd01158  333 GGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 65-390 1.99e-27

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: 112.98  E-value: 1.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  65 IRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQEFVIdtpceNAEKMYIGNAMYGNYAAVFA 144
Cdd:cd01160   91 ITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKD--GDHYVL-----NGSKTFITNGMLADVVIVVA 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 145 QLIIDGRSQ-GPHCFIVpvrdENGSlyPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLdkfgsvapdGQyhspiRN 223
Cdd:cd01160  164 RTGGEARGAgGISLFLV----ERGT--PGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLL---------GE-----EN 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 224 KSarFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpKTKEEVKIIEHQtqtlrlMPHLATALAltfVSRy 303
Cdd:cd01160  224 KG--FYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFG-KTLAQLQVVRHK------IAELATKVA---VTR- 290

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 304 agALLDEDVfqgKELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQ 383
Cdd:cd01160  291 --AFLDNCA---WRHEQGRLDVAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKE 365


                 ....*..
gi 767918731 384 VVGRELL 390
Cdd:cd01160  366 LISRQMV 372
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 63-388 9.13e-23

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: 99.74  E-value: 9.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  63 GAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQEFVIdtpceNAEKMYIGNAMYGNYAAV 142
Cdd:cd01151  103 LPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKD--GGGYKL-----NGSKTWITNSPIADVFVV 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 143 FAQLIIDGRSQGphcFIVPvRDengslYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLdkfgsvapdgqyhspir 222
Cdd:cd01151  176 WARNDETGKIRG---FILE-RG-----MKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL----------------- 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 223 NKSARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFG-PKTKEEV---KIIEHQTQTlrlmpHLATALALT 298
Cdd:cd01151  230 PGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGrPLAAFQLvqkKLADMLTEI-----ALGLLACLR 304

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 299 fVSRyagaLLDedvfQGKELVNSRSLqalvagLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDD 378
Cdd:cd01151  305 -VGR----LKD----QGKATPEQISL------LKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTH 369

                        330
                 ....*....|
gi 767918731 379 VVMLQVVGRE 388
Cdd:cd01151  370 DIHALILGRA 379
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 25-376 1.45e-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: 96.38  E-value: 1.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  25 LAEKtknfVSRSLVIGEVLSmADMATGVKcGIIYWlfggairnlGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGI 104
Cdd:cd01161   92 LAEI----VGMDLGFSVTLG-AHQSIGFK-GILLF---------GTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASI 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 105 QTEATFDLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQliidgrsqgphcfiVPVRDENGSLYPGVTAidMMYKEGL 184
Cdd:cd01161  157 RTTAVLSEDGKHYVL-----NGSKIWITNGGIADIFTVFAK--------------TEVKDATGSVKDKITA--FIVERSF 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 185 HGVDNGI--------------LIFDKVRIPRENLLDKFGsvapDGqyhspirnksarFNAMLAALTPSRLAVAFQAMGAM 250
Cdd:cd01161  216 GGVTNGPpekkmgikgsntaeVYFEDVKIPVENVLGEVG----DG------------FKVAMNILNNGRFGMGAALIGTM 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 251 KLGLTIAIRYSHSRRQFGPKTKEEVKIIEHqtqtlrlmphLATALALTFVSR----YAGALLDedvfqgKELVNSRSLQA 326
Cdd:cd01161  280 KRCIEKAVDYANNRKQFGKKIHEFGLIQEK----------LANMAILQYATEsmayMTSGNMD------RGLKAEYQIEA 343

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 767918731 327 LVAglKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEG 376
Cdd:cd01161  344 AIS--KVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEG 391
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 66-391 9.57e-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: 87.85  E-value: 9.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  66 RNlGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlsAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQ 145
Cdd:cd01156   97 RN-GSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKK--GDRYVL-----NGSKMWITNGPDADTLVVYAK 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 146 LIIDGRSQGPHCFIVpvrdENGslYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSvapdGQYhspirnks 225
Cdd:cd01156  169 TDPSAGAHGITAFIV----EKG--MPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENK----GVY-------- 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 226 arfnAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKeEVKIIEHQtqtlrlMPHLATAL--ALTFVSRY 303
Cdd:cd01156  231 ----VLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIG-EFQLVQGK------LADMYTRLnaSRSYLYTV 299

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 304 AGAlLDEDVFQGKElvnsrslqalVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQ 383
Cdd:cd01156  300 AKA-CDRGNMDPKD----------AAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRM 368


                 ....*...
gi 767918731 384 VVGRELLA 391
Cdd:cd01156  369 VIGRELFK 376
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 38-392 4.12e-17

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: 82.88  E-value: 4.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  38 VIGEVLSMADMATGVKCGIiYWLFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATfdLSAQEF 117
Cdd:cd01162   67 IIFEALSTGCVSTAAYISI-HNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAV--REGDHY 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 118 VIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGrSQGPHCFIVpvrdENGSlyPGVTAIDMMYKEGLHGVDNGILIFDKV 197
Cdd:cd01162  144 VL-----NGSKAFISGAGDSDVYVVMARTGGEG-PKGISCFVV----EKGT--PGLSFGANEKKMGWNAQPTRAVIFEDC 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 198 RIPRENLLdkfgsvAPDGQyhspirnksaRFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKEEvki 277
Cdd:cd01162  212 RVPVENRL------GGEGQ----------GFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADF--- 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 278 iehqtQTLRL-MPHLATAL--ALTFVSRYAGALLDEDvfqgKELVnsrslqALVAGLKAYSTwenIRCLQDCRECT---G 351
Cdd:cd01162  273 -----QALQFkLADMATELvaSRLMVRRAASALDRGD----PDAV------KLCAMAKRFAT---DECFDVANQALqlhG 334

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 767918731 352 GMGYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQ 392
Cdd:cd01162  335 GYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 90-195 7.19e-16

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: 72.70  E-value: 7.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731   90 FAMTERGHGSNARGIQTEAtFDLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQLIIDGRSQGPHCFIVPVRDengsl 169
Cdd:pfam02770   2 FALTEPGAGSDVASLKTTA-ADGDGGGWVL-----NGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDA----- 70

                          90       100
                  ....*....|....*....|....*.
gi 767918731  170 yPGVTAIDMMYKEGLHGVDNGILIFD 195
Cdd:pfam02770  71 -PGVSVRRIETKLGVRGLPTGELVFD 95
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 59-376 5.00e-15

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: 76.66  E-value: 5.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  59 WLFGGAIRNL---GSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDLSAQEFVidtpceNAEKMYIGN-- 133
Cdd:cd01153   87 SGTQGAAATLlahGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRI------NGVKRFISAge 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 134 -AMYGNyaavfAQLIIDGRSQGP-------HCFIVPVRDENGSlYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPrenLL 205
Cdd:cd01153  161 hDMSEN-----IVHLVLARSEGAppgvkglSLFLVPKFLDDGE-RNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LI 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 206 dkfgsvapdGQYHSPIRnksarfnAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGP--KTKEEVKIIEHQTQ 283
Cdd:cd01153  232 ---------GEEGMGLA-------QMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDliKAAPAVTIIHHPDV 295

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 284 TLRLMPHLATALALTFVSRYAGALLDEDVFQGKELVNSRSLQALVAGL----KAYSTWENIRCLQDCRECTGGMGYMMEN 359
Cdd:cd01153  296 RRSLMTQKAYAEGSRALDLYTATVQDLAERKATEGEDRKALSALADLLtpvvKGFGSEAALEAVSDAIQVHGGSGYTREY 375

                        330
                 ....*....|....*..
gi 767918731 360 RISGLKCDTDVFATFEG 376
Cdd:cd01153  376 PIEQYYRDARITTIYEG 392
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 63-387 6.31e-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: 76.64  E-value: 6.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  63 GAIRNLGsPEHVTKWFQPLQEQKY-TGMFA---MTERGHGSNARGIQTEATFDLSaqefviDTPCENAEKMYIGNAMyGN 138
Cdd:cd01154  121 YALRKYG-PEELKQYLPGLLSDRYkTGLLGgtwMTEKQGGSDLGANETTAERSGG------GVYRLNGHKWFASAPL-AD 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 139 YAAVFAQLI-IDGRSQGPHCFIVPVRDENGSLypgvtaidmmykeglhgvdNGILIfdkvriprENLLDKFG--SVAP-- 213
Cdd:cd01154  193 AALVLARPEgAPAGARGLSLFLVPRLLEDGTR-------------------NGYRI--------RRLKDKLGtrSVATge 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 214 ---DGQYHSPIRNKSARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpKTkeevkIIEH---QTQTLRL 287
Cdd:cd01154  246 vefDDAEAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFG-KP-----LIDHplmRRDLAEM 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 288 MPHLATALALTFvsRYAGALldeDVFQGKELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCD 367
Cdd:cd01154  320 EVDVEAATALTF--RAARAF---DRAAADKPVEAHMARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHRE 394

                        330       340
                 ....*....|....*....|....
gi 767918731 368 TDVFATFEGDDVV----MLQVVGR 387
Cdd:cd01154  395 AQVTPIWEGTGNIqaldVLRVLVK 418
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 69-390 1.54e-13

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: 71.85  E-value: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  69 GSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEAtfDLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFAQLII 148
Cdd:cd01157   97 GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYII-----NGQKMWITNGGKANWYFLLARSDP 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 149 DGR---SQGPHCFIVPvRDENGsLYPGVTAIDMmykeGLHGVDNGILIFDKVRIPRENLLDKFGsvapdgqyhspirnks 225
Cdd:cd01157  170 DPKcpaSKAFTGFIVE-ADTPG-IQPGRKELNM----GQRCSDTRGITFEDVRVPKENVLIGEG---------------- 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 226 ARFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpktkeeVKIIEHQTQTLrLMPHLATALALTFVSRYAG 305
Cdd:cd01157  228 AGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFG------KLIAEHQAVSF-MLADMAMKVELARLAYQRA 300

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 306 AlldEDVFQGKElvnsRSLQALVAglKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQVV 385
Cdd:cd01157  301 A---WEVDSGRR----NTYYASIA--KAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLII 371


                 ....*
gi 767918731 386 GRELL 390
Cdd:cd01157  372 SREHL 376
PLN02526 PLN02526
acyl-coenzyme A oxidase
 65-389 3.10e-13

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 71.42  E-value: 3.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  65 IRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATfdLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFA 144
Cdd:PLN02526 121 IALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTAT--KVEGGWIL-----NGQKRWIGNSTFADVLVIFA 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 145 QLIIDGRSQGphcFIVpvrdENGSlyPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLdkfgsvapdgqyhsPIRNK 224
Cdd:PLN02526 194 RNTTTNQING---FIV----KKGA--PGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRL--------------PGVNS 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 225 SARFNAMLAAltpSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpktkeeVKIIEHQTQTLRLMPHLATALALTFVSRYA 304
Cdd:PLN02526 251 FQDTNKVLAV---SRVMVAWQPIGISMGVYDMCHRYLKERKQFG------APLAAFQINQEKLVRMLGNIQAMFLVGWRL 321

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 305 GALLDedvfQGKELVNSRSLQalvaglKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQV 384
Cdd:PLN02526 322 CKLYE----SGKMTPGHASLG------KAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALV 391


                 ....*
gi 767918731 385 VGREL 389
Cdd:PLN02526 392 TGREI 396
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 228-389 7.28e-12

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: 63.04  E-value: 7.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  228 FNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpktkeeVKIIEHqtQTLRLMphLATALALTFVSRY---- 303
Cdd:pfam00441   4 FRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFG------RPLIDF--QLVRHK--LAEMAAEIEAARLlvyr 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  304 AGALLDEDVFQGKElvnsrslqalVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQ 383
Cdd:pfam00441  74 AAEALDAGGPDGAE----------ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRN 143


                  ....*.
gi 767918731  384 VVGREL 389
Cdd:pfam00441 144 IIARRL 149
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 65-392 1.60e-11

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 66.05  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  65 IRNlGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEAtfDLSAQEFVIdtpceNAEKMYIGNAMYGNYAAVFA 144
Cdd:PLN02519 122 VRN-GTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKA--ERVDGGYVL-----NGNKMWCTNGPVAQTLVVYA 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 145 QLIIDGRSQGPHCFIVpvrdENGslYPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSvapdGQYhspirnk 224
Cdd:PLN02519 194 KTDVAAGSKGITAFII----EKG--MPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGK----GVY------- 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 225 sarfnAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGpKTKEEVKIIehQTQTLRLMPHLATALALTF-VSRY 303
Cdd:PLN02519 257 -----VMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFG-RPIGEFQFI--QGKLADMYTSLQSSRSYVYsVARD 328

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 304 AgallDEDVFQGKElvnsrslqalVAGLKAYSTWENIRCLQDCRECTGGMGYMMENRISGLKCDTDVFATFEGDDVVMLQ 383
Cdd:PLN02519 329 C----DNGKVDRKD----------CAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRM 394


                 ....*....
gi 767918731 384 VVGRELLAQ 392
Cdd:PLN02519 395 LIGRELFKE 403
PRK12341 PRK12341
acyl-CoA dehydrogenase;
53-393 9.25e-08

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 53.96  E-value: 9.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  53 KCGIIYWLFGGA-----IRNLGSPEHVTKWFQplqEQKYTG----MFAMTERGHGSNARGIQTEATFDlSAQEFVidtpc 123
Cdd:PRK12341  79 KCGAPAFLITNGqcihsMRRFGSAEQLRKTAE---STLETGdpayALALTEPGAGSDNNSATTTYTRK-NGKVYL----- 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 124 eNAEKMYIGNAMYGNYAAVFAQliiDGRSQGPH-CF---IVPVRDengslyPGVTaIDMMYKEGLHGVDNGILIFDKVRI 199
Cdd:PRK12341 150 -NGQKTFITGAKEYPYMLVLAR---DPQPKDPKkAFtlwWVDSSK------PGIK-INPLHKIGWHMLSTCEVYLDNVEV 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 200 PRENLLDKFGsvapDGqyhspirnksarFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFGPKTKEEVKIIE 279
Cdd:PRK12341 219 EESDLVGEEG----MG------------FLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQE 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 280 HQT------QTLRLMphlatalaltfvsRYAGALldedvfqgkELVNSRSLQALVAGLKAYSTWENIRCLQDCRECTGGM 353
Cdd:PRK12341 283 KLTlmaikiENMRNM-------------VYKVAW---------QADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGL 340

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 767918731 354 GYMMENRISGLKCDTDVFATFEGDDVVMLQVVGRELLAQY 393
Cdd:PRK12341 341 GYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDY 380
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 60-268 3.04e-07

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 52.63  E-value: 3.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731  60 LFGGAIRNLGSPEHVTKWFQPLQEQKYTGMFAMTERGHGSNARGIQTEATFDlSAQEFVIdtpceNAEKMYIGNAMYGNY 139
Cdd:PTZ00461 125 LFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKD-SNGNYVL-----NGSKIWITNGTVADV 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918731 140 AAVFAQliIDGRSQGphcFIVpvrdENGSlyPGVTAIDMMYKEGLHGVDNGILIFDKVRIPRENLLDKFGSvapdgqyhs 219
Cdd:PTZ00461 199 FLIYAK--VDGKITA---FVV----ERGT--KGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGK--------- 258

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767918731 220 pirnksaRFNAMLAALTPSRLAVAFQAMGAMKLGLTIAIRYSHSRRQFG 268
Cdd:PTZ00461 259 -------GMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFG 300
 
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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