EzCatDB: T00007
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeT00007
CATH domainDomain 11.10.540.10 : Butyryl-Coa Dehydrogenase, subunit A; domain 1
Domain 22.40.110.10 : Butyryl-CoA Dehydrogenase, subunit A; domain 2
Domain 31.20.140.10 : Butyryl-CoA Dehydrogenase, subunit A; domain 3Catalytic domain
E.C.1.3.8.1

CATH domainRelated DB codes (homologues)
1.10.540.10 : Butyryl-Coa Dehydrogenase, subunit A; domain 1T00008,T00009
1.20.140.10 : Butyryl-CoA Dehydrogenase, subunit A; domain 3T00008,T00009
2.40.110.10 : Butyryl-CoA Dehydrogenase, subunit A; domain 2T00008,T00009

Enzyme Name
UniProtKBKEGG

Q06319P15651
Protein nameAcyl-CoA dehydrogenase, short-chain specificShort-chain specific acyl-CoA dehydrogenase, mitochondrialshort-chain acyl-CoA dehydrogenase
butyryl-CoA dehydrogenase
butanoyl-CoA dehydrogenase
butyryl dehydrogenase
unsaturated acyl-CoA reductase
ethylene reductase
enoyl-coenzyme A reductase
unsaturated acyl coenzyme A reductase
butyryl coenzyme A dehydrogenase
short-chain acyl CoA dehydrogenase
short-chain acyl-coenzyme A dehydrogenase
3-hydroxyacyl CoA reductase
butanoyl-CoA:(acceptor) 2,3-oxidoreductase
ACADS (gene name)
SynonymsEC 1.3.8.1
Butyryl-CoA dehydrogenase
BCAD
SCAD
SCAD
EC 1.3.8.1
Butyryl-CoA dehydrogenase
RefSeq
NP_071957.1 (Protein)
NM_022512.2 (DNA/RNA sequence)
PfamPF00441 (Acyl-CoA_dh_1)
PF02770 (Acyl-CoA_dh_M)
PF02771 (Acyl-CoA_dh_N)
[Graphical view]
PF00441 (Acyl-CoA_dh_1)
PF02770 (Acyl-CoA_dh_M)
PF02771 (Acyl-CoA_dh_N)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00071Fatty acid metabolism
MAP00280Valine, leucine and isoleucine degradation
MAP00650Butanoate metabolism

UniProtKB:Accession NumberQ06319P15651
Entry nameACDS_MEGELACADS_RAT
ActivityButanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein.Butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein.
SubunitHomotetramer.Homotetramer.
Subcellular location
Mitochondrion matrix.
CofactorFAD.FAD.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00016C00136C04253C00877C04570
CompoundFADButanoyl-CoAElectron-transferring flavoprotein2-Butenoyl-CoAReduced electron-transferring flavoprotein
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotideamine group,carbohydrate,nucleotide,peptide/protein,sulfide groupamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,peptide/protein,phosphate group/phosphate ionamine group,carbohydrate,nucleotide,peptide/protein,sulfide groupamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,peptide/protein,phosphate group/phosphate ion
ChEBI16238
15517

15473

PubChem643975
122283
439173

5280381
5497143

             
1bucA01UnboundUnboundUnboundUnboundUnbound
1bucB01UnboundUnboundUnboundUnboundUnbound
1jqiA01UnboundUnboundUnboundUnboundUnbound
1jqiB01UnboundUnboundUnboundUnboundUnbound
1bucA02Bound:FADUnboundUnboundUnboundUnbound
1bucB02Bound:FADUnboundUnboundUnboundUnbound
1jqiA02Bound:FADUnboundUnboundUnboundUnbound
1jqiB02Bound:FADUnboundUnboundUnboundUnbound
1bucA03UnboundUnboundUnboundAnalogue:CAAUnbound
1bucB03UnboundUnboundUnboundAnalogue:CAAUnbound
1jqiA03UnboundUnboundUnboundAnalogue:CAAUnbound
1jqiB03UnboundUnboundUnboundAnalogue:CAAUnbound

Active-site residues
resource
Swiss-prot;Q06319 & literature [7]
pdbCatalytic residues
         
1bucA01 
1bucB01 
1jqiA01 
1jqiB01 
1bucA02 
1bucB02 
1jqiA02 
1jqiB02 
1bucA03GLU 367
1bucB03GLU 367
1jqiA03GLU 368
1jqiB03GLU 768

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Scheme III, p.3160
[6]Fig.5
[7]p.2166-2167, p.2170-2171
[8]p.15361
[9]Scheme 5A, p.2161
[11]


references
[1]
PubMed ID6639077
JournalArch Biochem Biophys
Year1983
Volume227
Pages21-30
AuthorsReinsch J, Rojas C, McFarland JT
TitleKinetic methods for the study of the enzyme systems of beta-oxidation.
[2]
PubMed ID6712628
JournalBiochem J
Year1984
Volume218
Pages521-9
AuthorsWilliamson G, Engel PC
TitleButyryl-CoA dehydrogenase from Megasphaera elsdenii. Specificity of the catalytic reaction.
[3]
PubMed ID6466635
JournalBiochemistry
Year1984
Volume23
Pages3154-61
AuthorsGhisla S, Thorpe C, Massey V
TitleMechanistic studies with general acyl-CoA dehydrogenase and butyryl-CoA dehydrogenase: evidence for the transfer of the beta-hydrogen to the flavin N(5)-position as a hydride.
[4]
PubMed ID8399220
JournalBiochemistry
Year1993
Volume32
Pages10736-42
AuthorsBecker DF, Fuchs JA, Banfield DK, Funk WD, MacGillivray RT, Stankovich MT
TitleCharacterization of wild-type and an active-site mutant in Escherichia coli of short-chain acyl-CoA dehydrogenase from Megasphaera elsdenii.
[5]
PubMed ID8080271
JournalArch Biochem Biophys
Year1994
Volume313
Pages261-6
AuthorsPace CP, Stankovich MT
TitleOxidation-reduction properties of short-chain acyl-CoA dehydrogenase: effects of substrate analogs.
[6]
PubMed ID8003473
JournalBiochemistry
Year1994
Volume33
Pages7082-7
AuthorsBecker DF, Fuchs JA, Stankovich MT
TitleProduct binding modulates the thermodynamic properties of a Megasphaera elsdenii short-chain acyl-CoA dehydrogenase active-site mutant.
[7]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID95161388
PubMed ID7857927
JournalBiochemistry
Year1995
Volume34
Pages2163-71
AuthorsDjordjevic S, Pace CP, Stankovich MT, Kim JJ
TitleThree-dimensional structure of butyryl-CoA dehydrogenase from Megasphaera elsdenii.
Related PDB1buc
Related UniProtKBQ06319
[8]
PubMed ID8952487
JournalBiochemistry
Year1996
Volume35
Pages15356-63
AuthorsBattaile KP, Mohsen AW, Vockley J
TitleFunctional role of the active site glutamate-368 in rat short chain acyl-CoA dehydrogenase.
[9]
PubMed ID9459013
JournalBioorg Med Chem
Year1997
Volume5
Pages2157-64
AuthorsDakoji S, Shin I, Battaile KP, Vockley J, Liu HW
TitleRedesigning the active-site of an acyl-CoA dehydrogenase: new evidence supporting a one-base mechanism.
[10]
PubMed ID10413528
JournalBiochemistry
Year1999
Volume38
Pages9508-16
AuthorsHofstein HA, Feng Y, Anderson VE, Tonge PJ
TitleRole of glutamate 144 and glutamate 164 in the catalytic mechanism of enoyl-CoA hydratase.
[11]
PubMed ID11412126
JournalBiochemistry
Year2001
Volume40
Pages7720-8
AuthorsPellett JD, Becker DF, Saenger AK, Fuchs JA, Stankovich MT
TitleRole of aromatic stacking interactions in the modulation of the two-electron reduction potentials of flavin and substrate/product in Megasphaera elsdenii short-chain acyl-coenzyme A dehydrogenase.
[12]
PubMed ID12220177
JournalBiochemistry
Year2002
Volume41
Pages11126-33
AuthorsNguyen TV, Riggs C, Babovic-Vuksanovic D, Kim YS, Carpenter JF, Burghardt TP, Gregersen N, Vockley J
TitlePurification and characterization of two polymorphic variants of short chain acyl-CoA dehydrogenase reveal reduction of catalytic activity and stability of the Gly185Ser enzyme.
[13]
PubMed ID11812788
JournalJ Biol Chem
Year2002
Volume277
Pages12200-7
AuthorsBattaile KP, Molin-Case J, Paschke R, Wang M, Bennett D, Vockley J, Kim JJ
TitleCrystal structure of rat short chain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA: comparison with other acyl-CoA dehydrogenases.
[14]
PubMed ID12504892
JournalArch Biochem Biophys
Year2003
Volume409
Pages251-61
AuthorsLamm TR, Kohls TD, Saenger AK, Stankovich MT
TitleComparison of ligand polarization and enzyme activation in medium- and short-chain acyl-coenzyme A dehydrogenase-novel analog complexes.
[15]
PubMed ID14506246
JournalJ Biol Chem
Year2003
Volume278
Pages47449-58
AuthorsPedersen CB, Bross P, Winter VS, Corydon TJ, Bolund L, Bartlett K, Vockley J, Gregersen N
TitleMisfolding, degradation, and aggregation of variant proteins. The molecular pathogenesis of short chain acyl-CoA dehydrogenase (SCAD) deficiency.
[16]
PubMed ID14752098
JournalJ Biol Chem
Year2004
Volume279
Pages16526-34
AuthorsBattaile KP, Nguyen TV, Vockley J, Kim JJ
TitleStructures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases.
[17]
PubMed ID14744856
JournalJ Biol Chem
Year2004
Volume279
Pages13786-91
AuthorsHoard-Fruchey HM, Goetzman E, Benson L, Naylor S, Vockley J
TitleMammalian electron transferring flavoprotein.flavoprotein dehydrogenase complexes observed by microelectrospray ionization-mass spectrometry and surface plasmon resonance.

comments
This enzyme is a member of short-chain acyl-CoA dehydrogenases.
FAD is bound to PHE 126;LEU 128;THR 129;THR 135;THR 162;GLN 283;THR 369;GLU 371 in the PDB entry (1buc).

createdupdated
2005-04-272012-10-02
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.