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 1.3.99.2 SCAD Butyryl-CoA dehydrogenase BCAD	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 1.3.99.2 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)

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
Q06319	ACDS_MEGEL	Butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein.	Homotetramer.		FAD.
P15651	ACADS_RAT	Butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein.	Homotetramer.	Mitochondrion matrix.	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 16238	15517 15517		15473 15473
PubChem	643975 643975	122283 439173 122283 439173		5280381 5497143 5280381 5497143

1bucA01	Unbound	Unbound	Unbound	Unbound	Unbound
1bucB01	Unbound	Unbound	Unbound	Unbound	Unbound
1jqiA01	Unbound	Unbound	Unbound	Unbound	Unbound
1jqiB01	Unbound	Unbound	Unbound	Unbound	Unbound
1bucA02	Bound:FAD	Unbound	Unbound	Unbound	Unbound
1bucB02	Bound:FAD	Unbound	Unbound	Unbound	Unbound
1jqiA02	Bound:FAD	Unbound	Unbound	Unbound	Unbound
1jqiB02	Bound:FAD	Unbound	Unbound	Unbound	Unbound
1bucA03	Unbound	Unbound	Unbound	Analogue:CAA	Unbound
1bucB03	Unbound	Unbound	Unbound	Analogue:CAA	Unbound
1jqiA03	Unbound	Unbound	Unbound	Analogue:CAA	Unbound
1jqiB03	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
1bucB01
1jqiA01
1jqiB01
1bucA02
1bucB02
1jqiA02
1jqiB02
1bucA03	GLU 367
1bucB03	GLU 367
1jqiA03	GLU 368
1jqiB03	GLU 768

References for Catalytic Mechanism
References	Sections	No. 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]
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