DB code: T00007

CATH domain 1.10.540.10 : Butyryl-Coa Dehydrogenase, subunit A; domain 1
2.40.110.10 : Butyryl-CoA Dehydrogenase, subunit A; domain 2
1.20.140.10 : Butyryl-CoA Dehydrogenase, subunit A; domain 3 Catalytic domain
E.C. 1.3.8.1
CSA
M-CSA
MACiE

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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam RefSeq
Q06319 Acyl-CoA dehydrogenase, short-chain specific
EC 1.3.8.1
Butyryl-CoA dehydrogenase
BCAD
SCAD
PF00441 (Acyl-CoA_dh_1)
PF02770 (Acyl-CoA_dh_M)
PF02771 (Acyl-CoA_dh_N)
[Graphical View]
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial
SCAD
EC 1.3.8.1
Butyryl-CoA dehydrogenase
PF00441 (Acyl-CoA_dh_1)
PF02770 (Acyl-CoA_dh_M)
PF02771 (Acyl-CoA_dh_N)
[Graphical View]
NP_071957.1 (Protein)
NM_022512.2 (DNA/RNA sequence)

KEGG enzyme name
short-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)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P15651 ACADS_RAT Butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein. Homotetramer. Mitochondrion matrix. FAD.
Q06319 ACDS_MEGEL Butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein. Homotetramer. FAD.

KEGG Pathways
Map code Pathways E.C.
MAP00071 Fatty acid metabolism
MAP00280 Valine, leucine and isoleucine degradation
MAP00650 Butanoate metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00016 C00136 C04253 C00877 C04570
E.C.
Compound FAD Butanoyl-CoA Electron-transferring flavoprotein 2-Butenoyl-CoA Reduced electron-transferring flavoprotein
Type amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide amine group,carbohydrate,nucleotide ,peptide/protein,sulfide group amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,peptide/protein,phosphate group/phosphate ion amine group,carbohydrate,nucleotide ,peptide/protein,sulfide group amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,peptide/protein,phosphate group/phosphate ion
ChEBI 16238
15517
15473
PubChem 643975
122283
439173
5280381
5497143
1bucA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1bucB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1jqiA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1jqiB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1bucA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1bucB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1jqiA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1jqiB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1bucA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Analogue:CAA Unbound
1bucB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Analogue:CAA Unbound
1jqiA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Analogue:CAA Unbound
1jqiB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Analogue:CAA Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;Q06319 & literature [7]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1bucA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1bucB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jqiA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jqiB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1bucA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1bucB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jqiA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jqiB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1bucA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 367
1bucB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 367
1jqiA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 368
1jqiB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain GLU 768

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[9]
Scheme 5A, p.2161
[11]
[3]
Scheme III, p.3160
[6]
Fig.5
[7]
p.2166-2167, p.2170-2171
[8]
p.15361

References
[1]
Resource
Comments
Medline ID
PubMed ID 6639077
Journal Arch Biochem Biophys
Year 1983
Volume 227
Pages 21-30
Authors Reinsch J, Rojas C, McFarland JT
Title Kinetic methods for the study of the enzyme systems of beta-oxidation.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 6712628
Journal Biochem J
Year 1984
Volume 218
Pages 521-9
Authors Williamson G, Engel PC
Title Butyryl-CoA dehydrogenase from Megasphaera elsdenii. Specificity of the catalytic reaction.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 6466635
Journal Biochemistry
Year 1984
Volume 23
Pages 3154-61
Authors Ghisla S, Thorpe C, Massey V
Title Mechanistic 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.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 8399220
Journal Biochemistry
Year 1993
Volume 32
Pages 10736-42
Authors Becker DF, Fuchs JA, Banfield DK, Funk WD, MacGillivray RT, Stankovich MT
Title Characterization of wild-type and an active-site mutant in Escherichia coli of short-chain acyl-CoA dehydrogenase from Megasphaera elsdenii.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 8080271
Journal Arch Biochem Biophys
Year 1994
Volume 313
Pages 261-6
Authors Pace CP, Stankovich MT
Title Oxidation-reduction properties of short-chain acyl-CoA dehydrogenase: effects of substrate analogs.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8003473
Journal Biochemistry
Year 1994
Volume 33
Pages 7082-7
Authors Becker DF, Fuchs JA, Stankovich MT
Title Product binding modulates the thermodynamic properties of a Megasphaera elsdenii short-chain acyl-CoA dehydrogenase active-site mutant.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID 95161388
PubMed ID 7857927
Journal Biochemistry
Year 1995
Volume 34
Pages 2163-71
Authors Djordjevic S, Pace CP, Stankovich MT, Kim JJ
Title Three-dimensional structure of butyryl-CoA dehydrogenase from Megasphaera elsdenii.
Related PDB 1buc
Related UniProtKB Q06319
[8]
Resource
Comments
Medline ID
PubMed ID 8952487
Journal Biochemistry
Year 1996
Volume 35
Pages 15356-63
Authors Battaile KP, Mohsen AW, Vockley J
Title Functional role of the active site glutamate-368 in rat short chain acyl-CoA dehydrogenase.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 9459013
Journal Bioorg Med Chem
Year 1997
Volume 5
Pages 2157-64
Authors Dakoji S, Shin I, Battaile KP, Vockley J, Liu HW
Title Redesigning the active-site of an acyl-CoA dehydrogenase: new evidence supporting a one-base mechanism.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 10413528
Journal Biochemistry
Year 1999
Volume 38
Pages 9508-16
Authors Hofstein HA, Feng Y, Anderson VE, Tonge PJ
Title Role of glutamate 144 and glutamate 164 in the catalytic mechanism of enoyl-CoA hydratase.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11412126
Journal Biochemistry
Year 2001
Volume 40
Pages 7720-8
Authors Pellett JD, Becker DF, Saenger AK, Fuchs JA, Stankovich MT
Title Role 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.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 12220177
Journal Biochemistry
Year 2002
Volume 41
Pages 11126-33
Authors Nguyen TV, Riggs C, Babovic-Vuksanovic D, Kim YS, Carpenter JF, Burghardt TP, Gregersen N, Vockley J
Title Purification and characterization of two polymorphic variants of short chain acyl-CoA dehydrogenase reveal reduction of catalytic activity and stability of the Gly185Ser enzyme.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 11812788
Journal J Biol Chem
Year 2002
Volume 277
Pages 12200-7
Authors Battaile KP, Molin-Case J, Paschke R, Wang M, Bennett D, Vockley J, Kim JJ
Title Crystal structure of rat short chain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA: comparison with other acyl-CoA dehydrogenases.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 12504892
Journal Arch Biochem Biophys
Year 2003
Volume 409
Pages 251-61
Authors Lamm TR, Kohls TD, Saenger AK, Stankovich MT
Title Comparison of ligand polarization and enzyme activation in medium- and short-chain acyl-coenzyme A dehydrogenase-novel analog complexes.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 14506246
Journal J Biol Chem
Year 2003
Volume 278
Pages 47449-58
Authors Pedersen CB, Bross P, Winter VS, Corydon TJ, Bolund L, Bartlett K, Vockley J, Gregersen N
Title Misfolding, degradation, and aggregation of variant proteins. The molecular pathogenesis of short chain acyl-CoA dehydrogenase (SCAD) deficiency.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 14752098
Journal J Biol Chem
Year 2004
Volume 279
Pages 16526-34
Authors Battaile KP, Nguyen TV, Vockley J, Kim JJ
Title Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 14744856
Journal J Biol Chem
Year 2004
Volume 279
Pages 13786-91
Authors Hoard-Fruchey HM, Goetzman E, Benson L, Naylor S, Vockley J
Title Mammalian electron transferring flavoprotein.flavoprotein dehydrogenase complexes observed by microelectrospray ionization-mass spectrometry and surface plasmon resonance.
Related PDB
Related UniProtKB

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).

Created Updated
2005-04-27 2012-10-02