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Conserved domains on  [gi|119599702|gb|EAW79296|]
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acyl-Coenzyme A dehydrogenase family, member 9, isoform CRA_c [Homo sapiens]

Protein Classification

acyl-CoA dehydrogenase family protein( domain architecture ID 10100190)

acyl-CoA dehydrogenase (ACAD) family protein similar to mitochondrial very long-chain specific acyl-CoA dehydrogenase (VLCAD), which is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats

CATH:  1.10.540.10
EC:  1.3.8.-
Gene Ontology:  GO:0016627|GO:0006631|GO:0050660
PubMed:  10760462|12504675
SCOP:  3001580|3001701

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
38-445 0e+00

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: 747.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  38 AFAKELFLGKIKKKEVFPFPEVSQDELNE-INQFLGPVEKFFTEEVDSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYG 116
Cdd:cd01161    1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEeLNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 117 GLGFSNTMYSRLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRA 196
Cdd:cd01161   81 GLGLNNTQYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 197 TLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEVVDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFE 276
Cdd:cd01161  161 VLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 277 NTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVM 356
Cdd:cd01161  241 DVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYAT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 357 ESMTYLTAGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYI 436
Cdd:cd01161  321 ESMAYMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400

                 ....*....
gi 119599702 437 ALTGLQHAG 445
Cdd:cd01161  401 ALTGLQHAG 409
 
Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
38-445 0e+00

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: 747.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  38 AFAKELFLGKIKKKEVFPFPEVSQDELNE-INQFLGPVEKFFTEEVDSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYG 116
Cdd:cd01161    1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEeLNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 117 GLGFSNTMYSRLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRA 196
Cdd:cd01161   81 GLGLNNTQYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 197 TLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEVVDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFE 276
Cdd:cd01161  161 VLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 277 NTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVM 356
Cdd:cd01161  241 DVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYAT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 357 ESMTYLTAGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYI 436
Cdd:cd01161  321 ESMAYMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400

                 ....*....
gi 119599702 437 ALTGLQHAG 445
Cdd:cd01161  401 ALTGLQHAG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
66-437 7.92e-149

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: 435.04  E-value: 7.92e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  66 EINQFLGPVEKFFTEEVD--SRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISM-DGSITVTL 142
Cdd:COG1960    8 EQRALRDEVREFAEEEIApeAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARaDASLALPV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 143 AAHqAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANI 222
Cdd:COG1960   88 GVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGD--GYVLNGQKTFITNAPVADV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 223 FTVFAKTEvvDSDGSvkDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNS 302
Cdd:COG1960  165 ILVLARTD--PAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 303 GRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGfpDCSIEAAMV 382
Cdd:COG1960  241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE--DAALEAAMA 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119599702 383 KVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:COG1960  319 KLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
57-436 3.65e-80

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 259.04  E-value: 3.65e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  57 PEVSQDELNEinQFLGPVEKFFTEEV--DSRKIDQEGKIPDE-TLEKLK-SLGLFGLQVPEEYGGLGFSNTMYS-RLGEI 131
Cdd:PLN02519  22 SSLLFDDTQL--QFKESVQQFAQENIapHAAAIDATNSFPKDvNLWKLMgDFNLHGITAPEEYGGLGLGYLYHCiAMEEI 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 132 ISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEdkKHYILNGSK 211
Cdd:PLN02519 100 SRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVD--GGYVLNGNK 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 212 VWITNGGLANIFTVFAKTEVvdSDGSvkDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGD 291
Cdd:PLN02519 178 MWCTNGPVAQTLVVYAKTDV--AAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGK 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 292 GFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFA-----LMAQKAYVMESMTYLTAGM 366
Cdd:PLN02519 254 GVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLAdmytsLQSSRSYVYSVARDCDNGK 333
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 367 LDQpgfPDCsieaAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYI 436
Cdd:PLN02519 334 VDR---KDC----AGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
290-437 5.13e-44

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: 153.95  E-value: 5.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  290 GDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQ 369
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119599702  370 pGFPDcSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:pfam00441  81 -GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
 
Name Accession Description Interval E-value
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
38-445 0e+00

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: 747.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  38 AFAKELFLGKIKKKEVFPFPEVSQDELNE-INQFLGPVEKFFTEEVDSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYG 116
Cdd:cd01161    1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEeLNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 117 GLGFSNTMYSRLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRA 196
Cdd:cd01161   81 GLGLNNTQYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 197 TLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEVVDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFE 276
Cdd:cd01161  161 VLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 277 NTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVM 356
Cdd:cd01161  241 DVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYAT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 357 ESMTYLTAGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYI 436
Cdd:cd01161  321 ESMAYMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400

                 ....*....
gi 119599702 437 ALTGLQHAG 445
Cdd:cd01161  401 ALTGLQHAG 409
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
66-437 7.92e-149

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: 435.04  E-value: 7.92e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  66 EINQFLGPVEKFFTEEVD--SRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISM-DGSITVTL 142
Cdd:COG1960    8 EQRALRDEVREFAEEEIApeAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARaDASLALPV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 143 AAHqAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANI 222
Cdd:COG1960   88 GVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGD--GYVLNGQKTFITNAPVADV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 223 FTVFAKTEvvDSDGSvkDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNS 302
Cdd:COG1960  165 ILVLARTD--PAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 303 GRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGfpDCSIEAAMV 382
Cdd:COG1960  241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE--DAALEAAMA 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119599702 383 KVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:COG1960  319 KLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
69-437 5.49e-135

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: 399.34  E-value: 5.49e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  69 QFLGPVEKFFTEEVD--SRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSR-LGEIISMDGSITVTLAAH 145
Cdd:cd01158    5 MIRKTVRDFAEKEIAplAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIaIEELAKVDASVAVIVSVH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 146 QAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANIFTV 225
Cdd:cd01158   85 NSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD--DYVLNGSKMWITNGGEADFYIV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 226 FAKTevvdsDGSVKDK-ITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGR 304
Cdd:cd01158  163 FAVT-----DPSKGYRgITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 305 FSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYlTAGMLDQPGFPdCSIEAAMVKV 384
Cdd:cd01158  238 IGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTY-KAARLKDNGEP-FIKEAAMAKL 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119599702 385 FSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:cd01158  316 FASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIA 368
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
148-437 7.02e-121

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: 361.22  E-value: 7.02e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 148 IGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANIFTVFA 227
Cdd:cd00567   43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGD--GYVLNGRKIFISNGGDADLFIVLA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 228 KTevvDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSM 307
Cdd:cd00567  121 RT---DEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 308 GSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQpGFPDCSIEAAMVKVFSS 387
Cdd:cd00567  198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQ-GPDEARLEAAMAKLFAT 276
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 119599702 388 EAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:cd00567  277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
66-437 8.43e-106

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: 324.36  E-value: 8.43e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  66 EINQFLGPVEKFFTEEVDSR--KIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSntmYsrLGEIISMD------GS 137
Cdd:cd01156    5 EIEMLRQSVREFAQKEIAPLaaKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMG---Y--LAHVIIMEeisrasGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 138 ITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATlsEDKKHYILNGSKVWITNG 217
Cdd:cd01156   80 VALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAE--KKGDRYVLNGSKMWITNG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 218 GLANIFTVFAKTEVvdsdGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAM 297
Cdd:cd01156  158 PDADTLVVYAKTDP----SAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLM 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 298 NILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFA-----LMAQKAYVMESMTYLTAGMLDqpgf 372
Cdd:cd01156  234 SGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLAdmytrLNASRSYLYTVAKACDRGNMD---- 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119599702 373 pdcSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:cd01156  310 ---PKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
74-437 1.69e-87

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: 277.07  E-value: 1.69e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  74 VEKFFTEEVD--SRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISMDGSITVTLAAHQAIGLK 151
Cdd:cd01160   10 VRRFFAKEVApfHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGLSLHTDIVSP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 152 GIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLseDKKHYILNGSKVWITNGGLANIFTVFAKTev 231
Cdd:cd01160   90 YITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARK--DGDHYVLNGSKTFITNGMLADVVIVVART-- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 232 vDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVV 311
Cdd:cd01160  166 -GGEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGA 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 312 AGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPdcSIEAAMVKVFSSEAAW 391
Cdd:cd01160  245 LAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD--VAEASMAKYWATELQN 322
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 119599702 392 QCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:cd01160  323 RVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELIS 368
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
88-437 9.14e-87

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: 275.09  E-value: 9.14e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  88 DQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISM-DGSITVTLAAHQAIGLKgIILAGTEEQKAKYL 166
Cdd:cd01162   28 DQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTgCVSTAAYISIHNMCAWM-IDSFGNDEQRERFL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 167 PKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANIFTVFAKTevvdsDGSVKDKITAFI 246
Cdd:cd01162  107 PDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGD--HYVLNGSKAFISGAGDSDVYVVMART-----GGEGPKGISCFV 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 247 VERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYA 326
Cdd:cd01162  180 VEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYL 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 327 CTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQpGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGY 406
Cdd:cd01162  260 EERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDR-GDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGY 338
                        330       340       350
                 ....*....|....*....|....*....|.
gi 119599702 407 TRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:cd01162  339 LKDYPVEQYVRDLRVHQILEGTNEIMRLIIA 369
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
57-436 3.65e-80

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 259.04  E-value: 3.65e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  57 PEVSQDELNEinQFLGPVEKFFTEEV--DSRKIDQEGKIPDE-TLEKLK-SLGLFGLQVPEEYGGLGFSNTMYS-RLGEI 131
Cdd:PLN02519  22 SSLLFDDTQL--QFKESVQQFAQENIapHAAAIDATNSFPKDvNLWKLMgDFNLHGITAPEEYGGLGLGYLYHCiAMEEI 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 132 ISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEdkKHYILNGSK 211
Cdd:PLN02519 100 SRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVD--GGYVLNGNK 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 212 VWITNGGLANIFTVFAKTEVvdSDGSvkDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGD 291
Cdd:PLN02519 178 MWCTNGPVAQTLVVYAKTDV--AAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGK 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 292 GFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFA-----LMAQKAYVMESMTYLTAGM 366
Cdd:PLN02519 254 GVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLAdmytsLQSSRSYVYSVARDCDNGK 333
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 367 LDQpgfPDCsieaAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYI 436
Cdd:PLN02519 334 VDR---KDC----AGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
69-443 1.67e-74

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: 243.26  E-value: 1.67e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  69 QFLGPVEKFFTEEV--DSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISMDGSITVTLAAHQ 146
Cdd:cd01157    7 EFQETARKFAREEIipVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQTAIEAN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 147 AIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKkhYILNGSKVWITNGGLANIFTVF 226
Cdd:cd01157   87 SLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDE--YIINGQKMWITNGGKANWYFLL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 227 AKTEVvDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFS 306
Cdd:cd01157  165 ARSDP-DPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPP 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 307 MGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPgfPDCSIEAAMVKVFS 386
Cdd:cd01157  244 VAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSG--RRNTYYASIAKAFA 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119599702 387 SEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQH 443
Cdd:cd01157  322 ADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
74-430 2.18e-68

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 228.28  E-value: 2.18e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  74 VEKFFTEEVD--SRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLG-EIISMDGSITVTLAAHQAIGL 150
Cdd:PTZ00461  48 VAKFSREVVDkhAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHhELSKYDPGFCLAYLAHSMLFV 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 151 KGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKhYILNGSKVWITNGGLANIFTVFAKte 230
Cdd:PTZ00461 128 NNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGN-YVLNGSKIWITNGTVADVFLIYAK-- 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 231 vvdsdgsVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSV 310
Cdd:PTZ00461 205 -------VDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAM 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 311 VAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLdQPGFPDcSIEAAMVKVFSSEAA 390
Cdd:PTZ00461 278 AVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNV-HPGNKN-RLGSDAAKLFATPIA 355
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 119599702 391 WQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNE 430
Cdd:PTZ00461 356 KKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIE 395
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
74-442 2.56e-68

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: 227.24  E-value: 2.56e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  74 VEKFFTEEVDSRKID--QEGKIPDETLEKLKSLGLFGLQvPEEYGGLGFSNTMYSRLG-EIISMDGSITVTLAAHQAIGL 150
Cdd:cd01151   24 AREFCQEELAPRVLEayREEKFDRKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIArEVERVDSGYRSFMSVQSSLVM 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 151 KGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATlsEDKKHYILNGSKVWITNGGLANIFTVFAKTE 230
Cdd:cd01151  103 LPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRAR--KDGGGYKLNGSKTWITNSPIADVFVVWARND 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 231 vvdsdgsVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVgDGFKVAMNILNSGRFSMGSV 310
Cdd:cd01151  181 -------ETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGA-EGLRGPFKCLNNARYGIAWG 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 311 VAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGF-PDcsiEAAMVKVFSSEA 389
Cdd:cd01151  253 ALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKAtPE---QISLLKRNNCGK 329
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119599702 390 AWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEI--LRMYIALTGLQ 442
Cdd:cd01151  330 ALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIhaLILGRAITGIQ 384
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
85-431 1.23e-63

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: 215.33  E-value: 1.23e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  85 RKIDQEG--------KIPDETLEKLKSL---GLFGLQVPEEYGGLGFSNTMYSRLGEIISM-DGSITVTLAAHQAIglKG 152
Cdd:cd01153   18 ADGDREGpvfddgrvVVPPPFKEALDAFaeaGWMALGVPEEYGGQGLPITVYSALAEIFSRgDAPLMYASGTQGAA--AT 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 153 IILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYIlNGSKVWITNG---GLANIF-TVFAK 228
Cdd:cd01153   96 LLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRI-NGVKRFISAGehdMSENIVhLVLAR 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 229 TEVVDSDgsVKDkITAFIV-ERDFGGVTNG----KPEDKLGIRGSNTCEVHFENTKIPvenILGEVGDGFKVAMNILNSG 303
Cdd:cd01153  175 SEGAPPG--VKG-LSLFLVpKFLDDGERNGvtvaRIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGA 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 304 RFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQE------KFALMAQKAYVMES--MTYLTAGMLDQPGFPDC 375
Cdd:cd01153  249 RLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAVTIihhpdvRRSLMTQKAYAEGSraLDLYTATVQDLAERKAT 328
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119599702 376 SIEAA------------MVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEI 431
Cdd:cd01153  329 EGEDRkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
PRK12341 PRK12341
acyl-CoA dehydrogenase;
74-437 1.77e-53

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 187.24  E-value: 1.77e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  74 VEKFFTEEvDSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSN-TMYSRLGEIISMDGSITVTlaaHQAIGLKG 152
Cdd:PRK12341  20 ITRNFPEE-YFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYvTQMLVLEEVSKCGAPAFLI---TNGQCIHS 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 153 IILAGTEEQKAK-YLPKLASGEhiAAFCL--TEPASGSDAASIRSRATlSEDKKHYiLNGSKVWITNGGLANIFTVFAKt 229
Cdd:PRK12341  96 MRRFGSAEQLRKtAESTLETGD--PAYALalTEPGAGSDNNSATTTYT-RKNGKVY-LNGQKTFITGAKEYPYMLVLAR- 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 230 evvDSDGSVKDK-ITAFIVERDFGGVTNgKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMG 308
Cdd:PRK12341 171 ---DPQPKDPKKaFTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINA 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 309 SVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQpGFPdCSIEAAMVKVFSSE 388
Cdd:PRK12341 247 ARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADN-GQS-LRTSAALAKLYCAR 324
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 119599702 389 AAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILrMYIA 437
Cdd:PRK12341 325 TAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM-IYIA 372
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
100-442 2.03e-50

Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.


Pssm-ID: 173841 [Multi-domain]  Cd Length: 380  Bit Score: 179.08  E-value: 2.03e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 100 KLKSLGLFGLQVPEEYGGLGFS-------NTMYSRLGEIISMdGSITVTLAAHqaiglkgIILA-GTEEQKAKYLPKLAS 171
Cdd:cd01152   43 ALAAAGWAAPGWPKEYGGRGASlmeqlifREEMAAAGAPVPF-NQIGIDLAGP-------TILAyGTDEQKRRFLPPILS 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 172 GEHIaaFCL--TEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANIFTVFAKTevvdsDGSVK--DKITAFIV 247
Cdd:cd01152  115 GEEI--WCQgfSEPGAGSDLAGLRTRAVRDGD--DWVVNGQKIWTSGAHYADWAWLLVRT-----DPEAPkhRGISILLV 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 248 ERDFGGVT-------NGKPEdklgirgsnTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIe 320
Cdd:cd01152  186 DMDSPGVTvrpirsiNGGEF---------FNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLL- 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 321 mtaEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPDcsIEAAMVKVFSSEAAwQCVSE-ALQ 399
Cdd:cd01152  256 ---ARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPG--AEASIAKLFGSELA-QELAElALE 329
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119599702 400 ILGGLGYTRDYP--------YERILRDTRILLIFEGTNEILRMYIALTGLQ 442
Cdd:cd01152  330 LLGTAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIAERLLG 380
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
75-442 1.27e-49

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 176.95  E-value: 1.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  75 EKFFTEevdsrkIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISMDGSITVTLaaHQ-AIGLKGI 153
Cdd:PRK03354  26 EAYFAE------CDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVL--YQlPGGFNTF 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 154 ILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATlSEDKKHYiLNGSKVWITNGGLANIFTVFAKtevvD 233
Cdd:PRK03354  98 LREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYT-RRNGKVY-LNGSKCFITSSAYTPYIVVMAR----D 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 234 SDGSVKDKITAFIVERDFGGVTNGKPEdKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAG 313
Cdd:PRK03354 172 GASPDKPVYTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYG 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 314 LLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPdcSIEAAMVKVFSSEAAWQC 393
Cdd:PRK03354 251 TAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT--SGDAAMCKYFCANAAFEV 328
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 119599702 394 VSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEilrMYIALTGLQ 442
Cdd:PRK03354 329 VDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDE---MQILTLGRA 374
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
73-442 6.85e-46

Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). 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 ACAD 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. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.


Pssm-ID: 173844 [Multi-domain]  Cd Length: 394  Bit Score: 167.18  E-value: 6.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  73 PVEKFFTEEVdsRKIDQEGKIPDETLEKLK----SLGLFGLQVPEEYGGLGFSNTMYSRLGEII--SMDGSITVTLAAHQ 146
Cdd:cd01155   20 PAEQEFLEYY--AEGGDRWWTPPPIIEKLKakakAEGLWNLFLPEVSGLSGLTNLEYAYLAEETgrSFFAPEVFNCQAPD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 147 AIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPA-SGSDAASIRsrATLSEDKKHYILNGSKVWITNGG--LANIF 223
Cdd:cd01155   98 TGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIE--CSIERDGDDYVINGRKWWSSGAGdpRCKIA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 224 TVFAKTevvDSDGSVKDKITAFI-VERDFGGVTNGKPedkLGIRGSNT-----CEVHFENTKIPVENILGEVGDGFKVAM 297
Cdd:cd01155  176 IVMGRT---DPDGAPRHRQQSMIlVPMDTPGVTIIRP---LSVFGYDDaphghAEITFDNVRVPASNLILGEGRGFEIAQ 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 298 NILNSGRF--SMGSVvaGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFAlmaqKAYVMESMTYL----TAGMLDQPG 371
Cdd:cd01155  250 GRLGPGRIhhCMRLI--GAAERALELMCQRAVSREAFGKKLAQHGVVAHWIA----KSRIEIEQARLlvlkAAHMIDTVG 323
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119599702 372 FPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQ 442
Cdd:cd01155  324 NKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
290-437 5.13e-44

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: 153.95  E-value: 5.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  290 GDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQ 369
Cdd:pfam00441   1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119599702  370 pGFPDcSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:pfam00441  81 -GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
41-405 2.56e-43

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 166.15  E-value: 2.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  41 KELFLGK--IKKKEVFPFPEVSQDElneinQ-FL-GPVEKFfTEEVDSRKIDQE-GKIPDETLEKLKSLGLFGLQVPEEY 115
Cdd:PRK09463  59 GELFSGKpdWKKLLNYPKPTLTAEE-----QaFLdGPVEEL-CRMVNDWQITHElADLPPEVWQFIKEHGFFGMIIPKEY 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 116 GGLGFSNTMYSR-LGEIISMDGSITVTLAAHQAIGlKGIILA--GTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASI 192
Cdd:PRK09463 133 GGLEFSAYAHSRvLQKLASRSGTLAVTVMVPNSLG-PGELLLhyGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSI 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 193 RS-----RATLSEDKKHYI-LNGSKVWITnggLANIFTVFA---KteVVDSDGSVKDK----ITAFIVERDFGGVTNGKP 259
Cdd:PRK09463 212 PDtgvvcKGEWQGEEVLGMrLTWNKRYIT---LAPIATVLGlafK--LYDPDGLLGDKedlgITCALIPTDTPGVEIGRR 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 260 EDKLGirgsntceVHFEN--TK-----IPVENILGE---VGDGFKVAMNILNSGR-FSMGSVVAGLLKRLIEMTAEYACT 328
Cdd:PRK09463 287 HFPLN--------VPFQNgpTRgkdvfIPLDYIIGGpkmAGQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARI 358
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119599702 329 RKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPdcSIEAAMVKVFSSEAAWQCVSEALQILGGLG 405
Cdd:PRK09463 359 RRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLGEKP--SVLSAIAKYHLTERGRQVINDAMDIHGGKG 433
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
20-405 1.70e-39

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 154.73  E-value: 1.70e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  20 LVVSTANRRLLRTSPPVRAFAK-----------------------ELFLGK--IKKKEVFPFPEVSQDElneiNQFL-GP 73
Cdd:PRK13026  14 LVFAVKPLRRQFITRPVFKFFKkvlpplsdtereameagdvwwegELFSGKpdWQKLHSYPKPTLTAEE----QAFIdNE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  74 VEKFFTEeVDSRKIDQEGK-IPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRL-GEIISMDGSITVTLAAHQAIGlK 151
Cdd:PRK13026  90 VETLLTM-LDDWDIVQNRKdLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIvSKIATRSVSAAVTVMVPNSLG-P 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 152 GIILA--GTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSE---DKKHYI---LNGSKVWITnggLANIF 223
Cdd:PRK13026 168 GELLThyGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCRgefEGEEVLglrLTWDKRYIT---LAPVA 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 224 TV----FaktEVVDSDGSVKDK----ITAFIVERDFGGVTNGKPEDKLGIR---GSNTCEVHFentkIPVENILG---EV 289
Cdd:PRK13026 245 TVlglaF---KLRDPDGLLGDKkelgITCALIPTDHPGVEIGRRHNPLGMAfmnGTTRGKDVF----IPLDWIIGgpdYA 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 290 GDGFKVAMNILNSGR-FSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLD 368
Cdd:PRK13026 318 GRGWRMLVECLSAGRgISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLD 397
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 119599702 369 QPGFPdcSIEAAMVKVFSSEAAWQCVSEALQILGGLG 405
Cdd:PRK13026 398 LGVKP--SVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
PLN02526 PLN02526
acyl-coenzyme A oxidase
89-431 2.71e-37

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 143.45  E-value: 2.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  89 QEGKIPDETLEKLKSLGLFGLQVpEEYGGLGFSNTMYS-RLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLP 167
Cdd:PLN02526  57 EKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAiATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLP 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 168 KLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKkhYILNGSKVWITNGGLANIFTVFAKTevvdsdgSVKDKITAFIV 247
Cdd:PLN02526 136 SLAQLDTVACWALTEPDYGSDASSLNTTATKVEGG--WILNGQKRWIGNSTFADVLVIFARN-------TTTNQINGFIV 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 248 ERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVgDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYAC 327
Cdd:PLN02526 207 KKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLK 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 328 TRKQFNKRLSEFGLIQEKFALMAQKAYVMESM------TYLTAGMldQPGfpdcsiEAAMVKVFSSEAAWQCVSEALQIL 401
Cdd:PLN02526 286 ERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVgwrlckLYESGKM--TPG------HASLGKAWITKKARETVALGRELL 357
                        330       340       350
                 ....*....|....*....|....*....|
gi 119599702 402 GGLGYTRDYPYERILRDTRILLIFEGTNEI 431
Cdd:PLN02526 358 GGNGILADFLVAKAFCDLEPIYTYEGTYDI 387
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
138-432 1.00e-33

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: 133.65  E-value: 1.00e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 138 ITVTLAAhqaigLKGIILAGTEEQKaKYLPKLASGEH----IAAFCLTEPASGSDAASIRSRATLSEDKKhYILNGSKvW 213
Cdd:cd01154  113 LTMTDAA-----VYALRKYGPEELK-QYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSGGGV-YRLNGHK-W 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 214 ITNGGLANIFTVFAKTEvvDSDGSVKDkITAFIVER-DFGGVTNG----KPEDKLGIRGSNTCEVHFENTkipVENILGE 288
Cdd:cd01154  185 FASAPLADAALVLARPE--GAPAGARG-LSLFLVPRlLEDGTRNGyrirRLKDKLGTRSVATGEVEFDDA---EAYLIGD 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 289 VGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLD 368
Cdd:cd01154  259 EGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFD 338
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119599702 369 QPGfPDCSIEAAMVKVFS-------SEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEIL 432
Cdd:cd01154  339 RAA-ADKPVEAHMARLATpvakliaCKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
8-431 2.05e-31

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 129.60  E-value: 2.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702   8 LRTTAAARACRGLVVSTANRRLLRTSPPVR--AFAKELFLGKIKKKEVFPFPEVSQDELNEInqfLGPVEKFFTE----- 80
Cdd:PTZ00456   2 FRRVCSSAAASHAAAVSASARSLQYQPRIRdvQFLVEEVFNMYDHYEKLGKTDVTKELMDSL---LEEASKLATQtllpl 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  81 ----EVDSRKIDQEGKIP-----DETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISMdGSITVTLAAHQAIG-L 150
Cdd:PTZ00456  79 yessDSEGCVLLKDGNVTtpkgfKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMAT-ANWGFSMYPGLSIGaA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 151 KGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKhYILNGSKVWITNGG---LANI-FTVF 226
Cdd:PTZ00456 158 NTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADGS-YKITGTKIFISAGDhdlTENIvHIVL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 227 AKTEvvDSDGSVKDkITAFIVER----DFGGVTNGKP------EDKLGIRGSNTCEVHFENTkipVENILGEVGDGFKVA 296
Cdd:PTZ00456 237 ARLP--NSLPTTKG-LSLFLVPRhvvkPDGSLETAKNvkciglEKKMGIKGSSTCQLSFENS---VGYLIGEPNAGMKQM 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 297 MNILNSGRfsMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFA------------LMAQKAyVME---SMTY 361
Cdd:PTZ00456 311 FTFMNTAR--VGTALEGVCHAELAFQNALRYARERRSMRALSGTKEPEKPAdriichanvrqnILFAKA-VAEggrALLL 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 362 LTAGMLD-QPGFPDCSIEAAM----------VKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNE 430
Cdd:PTZ00456 388 DVGRLLDiHAAAKDAATREALdheigfytpiAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTG 467

                 .
gi 119599702 431 I 431
Cdd:PTZ00456 468 I 468
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
74-173 3.68e-29

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


Pssm-ID: 460686 [Multi-domain]  Cd Length: 113  Bit Score: 111.79  E-value: 3.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702   74 VEKFFTEEV--DSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISM-DGSITVTLAAHQAIGL 150
Cdd:pfam02771  11 VREFAEEEIapHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARaDASVALALSVHSSLGA 90
                          90       100
                  ....*....|....*....|...
gi 119599702  151 KGIILAGTEEQKAKYLPKLASGE 173
Cdd:pfam02771  91 PPILRFGTEEQKERYLPKLASGE 113
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
177-276 5.10e-28

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: 107.75  E-value: 5.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  177 AFCLTEPASGSDAASIRSRAtLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEvvdsDGSVKDKITAFIVERDFGGVTN 256
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLNGTKWWITNAGIADLFLVLARTG----GDDRHGGISLFLVPKDAPGVSV 75
                          90       100
                  ....*....|....*....|
gi 119599702  257 GKPEDKLGIRGSNTCEVHFE 276
Cdd:pfam02770  76 RRIETKLGVRGLPTGELVFD 95
PTZ00457 PTZ00457
acyl-CoA dehydrogenase; Provisional
27-571 2.17e-27

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185636 [Multi-domain]  Cd Length: 520  Bit Score: 116.52  E-value: 2.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  27 RRLLRTSP--PVR--AFAKELFLGKIKKKEVFPFPevsqdelneinqflgpvekffteevdSRKID-QEGKIPDETLEKL 101
Cdd:PTZ00457   2 RRRFSSAPrqYVRhaSYAAGLFNFKIVPEEMFPYP--------------------------CRKLDgDEAENLQSLLEQI 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 102 KSLG-----LFGLQVPEEYGGLGFSNTMYSRLGEIISMDGsITVTLAAHQAIGLKGIILA--GTEEQKAKYLPKLASGEH 174
Cdd:PTZ00457  56 RSNDkilgnLYGARIATEYGGLGLGHTAHALIYEEVGTNC-DSKLLSTIQHSGFCTYLLStvGSKELKGKYLTAMSDGTI 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 175 IAAFClTEPASGSDAASIRSRATLSEDKKhYILNGSKvWITNGGLANIFTVFAKT---EVVDSDGSVKDKITAFIVERDF 251
Cdd:PTZ00457 135 MMGWA-TEEGCGSDISMNTTKASLTDDGS-YVLTGQK-RCEFAASATHFLVLAKTltqTAAEEGATEVSRNSFFICAKDA 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 252 GGVTngkpedklgIRGSNtceVHFENTkiPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEmtaeyactrkQ 331
Cdd:PTZ00457 212 KGVS---------VNGDS---VVFENT--PAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQ----------E 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 332 FNKRLSEFGlIQEKFALMAQKAYVMESMTYLTAGMLDQPGfPDCSIEAAMVKVFSSEAawqcVSEALQILgGLGYTRDYP 411
Cdd:PTZ00457 268 LRGSNAEEG-ATDTVASFACAMYAMESTLYALTANLDLPT-EDSLLECTLVSAFVQST----TNQLLSIL-ETATPPSTT 340
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 412 YERILRDTRILLIFEGTNEILRMYIALTGLQHAG----RILTTRIHELKQAKVSTVMDTVG-RRLRDSlgrtvdlgltgn 486
Cdd:PTZ00457 341 LEKCFANARLFLSMMESRDFLYSSAVCCGVEDYGlffqRASTLQMMQARTLRSLGVRDRVPiKNLPDC------------ 408
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 487 hgvvhpSLADSAnkfeenTYCFGRTVETLLLRFGKTIMEEQLVLKRVANILINLYGMTAVLSRASRSIRIGLRNHDHEVL 566
Cdd:PTZ00457 409 ------SLIDEA------VVAFGNAVEATFVRSGSQVPYQQLLLNRLGEAASLLYAASAVASRASMCVSKGLPSAKVEGE 476

                 ....*
gi 119599702 567 LANTF 571
Cdd:PTZ00457 477 LASAF 481
PLN02876 PLN02876
acyl-CoA dehydrogenase
117-444 2.87e-20

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 95.25  E-value: 2.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 117 GLGFSNTMYSRLGEII--SMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEP-ASGSDAASIR 193
Cdd:PLN02876 491 GAGLSNLEYGYLCEIMgrSVWAPQVFNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPqVASSDATNIE 570
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 194 srATLSEDKKHYILNGSKvWITNGGL---ANIFTVFAKTevvDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGS-- 268
Cdd:PLN02876 571 --CSIRRQGDSYVINGTK-WWTSGAMdprCRVLIVMGKT---DFNAPKHKQQSMILVDIQTPGVQIKRPLLVFGFDDAph 644
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 269 NTCEVHFENTKIPVENI-LGEvGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGliqeKFA 347
Cdd:PLN02876 645 GHAEISFENVRVPAKNIlLGE-GRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHG----SFL 719
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 348 LMAQKAYVMESMTYL----TAGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILL 423
Cdd:PLN02876 720 SDLAKCRVELEQTRLlvleAADQLDRLGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLR 799
                        330       340
                 ....*....|....*....|.
gi 119599702 424 IFEGTNEILRMYIALTGLQHA 444
Cdd:PLN02876 800 IADGPDEVHLGTIAKLELQRA 820
AXO cd01150
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ...
99-462 1.67e-16

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: 83.15  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  99 EKLKSLGLFGLQVPEEYGGLGFSNTMYsrlgeiismDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAF 178
Cdd:cd01150   68 TDVERMGELMADDPEKMLALTNSLGGY---------DLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCF 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 179 CLTEPASGSDAASIRSRATLSEDKKHYILN-----GSKVWItnGGL---ANIFTVFAKTEVVDSDGSVKdkitAFIVE-R 249
Cdd:cd01150  139 AQTELGHGSNLQGLETTATYDPLTQEFVINtpdftATKWWP--GNLgktATHAVVFAQLITPGKNHGLH----AFIVPiR 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 250 DFG------GVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGD----------------GFKVAMNILNSGRFSM 307
Cdd:cd01150  213 DPKthqplpGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDvspdgtyvspfkdpnkRYGAMLGTRSGGRVGL 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 308 GSVVAGLLKRLIEMTAEYACTRKQFNKRLS-------EFGLIQEKFALMAQKAYV------------MESMTYLTAGMLD 368
Cdd:cd01150  293 IYDAAMSLKKAATIAIRYSAVRRQFGPKPSdpevqilDYQLQQYRLFPQLAAAYAfhfaakslvemyHEIIKELLQGNSE 372
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 369 QpgFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTrDYPYERILR-DTRILLIFEGTNEILrmyialtgLQHAGRI 447
Cdd:cd01150  373 L--LAELHALSAGLKAVATWTAAQGIQECREACGGHGYL-AMNRLPTLRdDNDPFCTYEGDNTVL--------LQQTANY 441
                        410
                 ....*....|....*
gi 119599702 448 LTTRIHELKQAKVST 462
Cdd:cd01150  442 LLKKYAQAFSLADYL 456
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
88-287 5.50e-15

Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.


Pssm-ID: 173852 [Multi-domain]  Cd Length: 377  Bit Score: 76.98  E-value: 5.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  88 DQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFS-NTMYSRLGEIISMDGSITVTLAAHQAIgLKGIILAGTEEQKAKYL 166
Cdd:cd01163   18 DRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASlPDLYEVVRELAAADSNIAQALRAHFGF-VEALLLAGPEQFRKRWF 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 167 PKLASGeHIAAFCLTEpaSGSDAASIRSRATLSEDkKHYILNGSKvWITNGGLaniFTVFAKTEVVDSDGsvkdKITAFI 246
Cdd:cd01163   97 GRVLNG-WIFGNAVSE--RGSVRPGTFLTATVRDG-GGYVLNGKK-FYSTGAL---FSDWVTVSALDEEG----KLVFAA 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 119599702 247 VERDFGGVTNGKPEDKLGIR--GSNTceVHFENTKIPVENILG 287
Cdd:cd01163  165 VPTDRPGITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLP 205
PLN02636 PLN02636
acyl-coenzyme A oxidase
133-437 1.47e-11

acyl-coenzyme A oxidase


Pssm-ID: 215342 [Multi-domain]  Cd Length: 686  Bit Score: 67.58  E-value: 1.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 133 SMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILN---- 208
Cdd:PLN02636 132 SVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINtpnd 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 209 -GSKVWITNGGLANIF-TVFAKTEVV--DSDGSVKDKITAFIVE-RDFG------GVTNGKPEDKLGIRGSNTCEVHFEN 277
Cdd:PLN02636 212 gAIKWWIGNAAVHGKFaTVFARLKLPthDSKGVSDMGVHAFIVPiRDMKthqvlpGVEIRDCGHKVGLNGVDNGALRFRS 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 278 TKIPVENILGEVGD----------------GFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFN-KRLSEFG 340
Cdd:PLN02636 292 VRIPRDNLLNRFGDvsrdgkytsslptinkRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGpPKQPEIS 371
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 341 LI-----QEKFALMAQKAYVMESMT-YLT---AGML---DQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTR 408
Cdd:PLN02636 372 ILdyqsqQHKLMPMLASTYAFHFATeYLVerySEMKkthDDQLVADVHALSAGLKAYITSYTAKALSTCREACGGHGYAA 451
                        330       340
                 ....*....|....*....|....*....
gi 119599702 409 DYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:PLN02636 452 VNRFGSLRNDHDIFQTFEGDNTVLLQQVA 480
PRK11561 PRK11561
isovaleryl CoA dehydrogenase; Provisional
180-432 1.80e-11

isovaleryl CoA dehydrogenase; Provisional


Pssm-ID: 183199 [Multi-domain]  Cd Length: 538  Bit Score: 66.70  E-value: 1.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 180 LTEPASGSDAASIRSRATLSEDKKhYILNGSKvWITNGGLANIFTVFAKTevvdsdgsvKDKITAFIVERDF-GGVTNG- 257
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERLADGS-YRLVGHK-WFFSVPQSDAHLVLAQA---------KGGLSCFFVPRFLpDGQRNAi 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 258 ---KPEDKLGIRGSNTCEVHFENTkipVENILGEVGDGFKvamNILNSG---RF--SMGSvvAGLLKRLIEMTAEYACTR 329
Cdd:PRK11561 253 rleRLKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIR---LILKMGgmtRFdcALGS--HGLMRRAFSVAIYHAHQR 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 330 KQFNKRLSEFGLIQEkfaLMAQKAYVMESMTYLT---AGMLDQPGFPDcsiEAAMVKVFSSEAAWQ-C------VSEALQ 399
Cdd:PRK11561 325 QVFGKPLIEQPLMRQ---VLSRMALQLEGQTALLfrlARAWDRRADAK---EALWARLFTPAAKFViCkrgipfVAEAME 398
                        250       260       270
                 ....*....|....*....|....*....|...
gi 119599702 400 ILGGLGYTRDYPYERILRDTRILLIFEGTNEIL 432
Cdd:PRK11561 399 VLGGIGYCEESELPRLYREMPVNSIWEGSGNIM 431
Acyl-CoA_dh_2 pfam08028
Acyl-CoA dehydrogenase, C-terminal domain;
306-430 4.42e-09

Acyl-CoA dehydrogenase, C-terminal domain;


Pssm-ID: 429790 [Multi-domain]  Cd Length: 133  Bit Score: 55.04  E-value: 4.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702  306 SMGSVVAGLLKRLIEMTAEYACTRKQ--FNKRLSEFGLIQEKFALMA----QKAYVMESMTYLTAGMLDQ--PGFPDCSI 377
Cdd:pfam08028   1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAaridAARLLLERAAARIEAAAAAgkPVTPALRA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 119599702  378 EAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNE 430
Cdd:pfam08028  81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
PTZ00460 PTZ00460
acyl-CoA dehydrogenase; Provisional
143-547 3.67e-07

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185639 [Multi-domain]  Cd Length: 646  Bit Score: 53.31  E-value: 3.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 143 AAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILN-----GSKVWITN- 216
Cdd:PTZ00460  96 TVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKFWPGEl 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 217 GGLANIFTVFAKTEVvdsDGSVKDkITAFIVE-RDFG------GVTNGKPEDKLGIRGSNTCEVHFENTKIPVENIL--- 286
Cdd:PTZ00460 176 GFLCNFALVYAKLIV---NGKNKG-VHPFMVRiRDKEthkplqGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLary 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 287 ------GEV---GDGfKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNK------RLSEFGLIQEK-FALMA 350
Cdd:PTZ00460 252 ikvsedGQVerqGNP-KVSYASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNdnkqenSVLEYQTQQQKlLPLLA 330
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 351 QkAYVMeSMTYLTAGMLDQPGF-----PDCSIEAAMVKVFSSEAAW--QCVSEALQ----ILGGLGYTRDYPYERILRDT 419
Cdd:PTZ00460 331 E-FYAC-IFGGLKIKELVDDNFnrvqkNDFSLLQLTHAILSAAKANytYFVSNCAEwcrlSCGGHGYAHYSGLPAIYFDM 408
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 420 RILLIFEGTNEILRMYIA---LTGLQHA-----------GRILT-----------TRIHELKQAKVSTVMDTVGRRLRDS 474
Cdd:PTZ00460 409 SPNITLEGENQIMYLQLArylLKQLQHAvqkpekvpeyfNFLSHitekladqttiESLGQLLGLNCTILTIYAAKKIMDH 488
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119599702 475 LGRTVDLGLTGNHgVVHPSLADSANKFEEN-TYcfgrtvetllLRFGKTIMEEQLVLKRVANILINLYGMTAVL 547
Cdd:PTZ00460 489 INTGKDFQQSWDT-KSGIALASAASRFIEYfNY----------LCFLDTINNANKSTKEILTQLADLYGITMLL 551
PLN02443 PLN02443
acyl-coenzyme A oxidase
157-406 9.33e-06

acyl-coenzyme A oxidase


Pssm-ID: 178062 [Multi-domain]  Cd Length: 664  Bit Score: 48.68  E-value: 9.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 157 GTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILN-----GSKVWitNGGLANIFT---VFAK 228
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHsptltSSKWW--PGGLGKVSThavVYAR 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 229 tevVDSDGsvKDK-ITAFIVE-------RDFGGVTNGKPEDKLGIRGSNTCE---VHFENTKIPVENILGEVG----DGF 293
Cdd:PLN02443 192 ---LITNG--KDHgIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRLSkvtrEGK 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 294 KVAMNI---LNSGR--FSMGSVVAG---LLKRLIEMTAEYACTRKQFNKRLS--EFGLIQEK------FALMAQkAY--- 354
Cdd:PLN02443 267 YVQSDVprqLVYGTmvYVRQTIVADastALSRAVCIATRYSAVRRQFGSQDGgpETQVIDYKtqqsrlFPLLAS-AYafr 345
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119599702 355 -VMESMTYLTAGML------DQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGY 406
Cdd:PLN02443 346 fVGEWLKWLYTDVTqrleanDFSTLPEAHACTAGLKSLTTSATADGIEECRKLCGGHGY 404
PLN02312 PLN02312
acyl-CoA oxidase
128-332 2.98e-05

acyl-CoA oxidase


Pssm-ID: 215178 [Multi-domain]  Cd Length: 680  Bit Score: 47.07  E-value: 2.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 128 LGEIISM-DGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYI 206
Cdd:PLN02312 138 LLEVIGIyDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFV 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 207 LN-----GSKVWItnGGLANIFT---VFAKTEVvdsDGsVKDKITAFIVE-RDFGGVT--NGKPED---KLGIRGSNTCE 272
Cdd:PLN02312 218 INtpcesAQKYWI--GGAANHAThtiVFSQLHI---NG-KNEGVHAFIAQiRDQDGNIcpNIRIADcghKIGLNGVDNGR 291
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119599702 273 VHFENTKIPVENILGEVGD----------------GFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQF 332
Cdd:PLN02312 292 IWFDNLRIPRENLLNSVADvspdgkyvsaikdpdqRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
 
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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