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InterPro: IPR014007 Acetoin reductase

Protein matches Help

UniProtKB

Matches:

188 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR014007 23BDH

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR02415	23BDH	188
Signatures in BioMart

InterPro Relationships Help

Parent

IPR002347 Glucose/ribitol dehydrogenase

Contains

IPR016040 NAD(P)-binding domain
IPR020904 Short-chain dehydrogenase/reductase, conserved site

GO Term annotation Help

Process

GO:0045150 acetoin catabolic process
GO:0055114 oxidation reduction

Function

GO:0019152 acetoin dehydrogenase activity

InterPro annotation

Entry Details in BioMart

Abstract

One member of this family, as characterised in Klebsiella terrigena [1], is able to interconvert acetoin + NADH with meso-2,3-butanediol + NAD(+). It is also capable of irreversible reduction of diacetyl with NADH to acetoin. There has been a reuctance to classify the enzyme as either EC:1.1.1.4, which is (R,R)-butanediol dehydrogenase, or EC:1.1.1.5, which is acetoin dehydrogenase without a specified stereochemistry [1]. Another member of this family, from Corynebacterium glutamicum (Brevibacterium flavum), is called L-2,3-butanediol dehydrogenase [2].

This enzyme is a homotetramer in the family of short chain dehydrogenases (IPR002198).

Structural links Help

PDB - click here

SCOP: c.2.1.2

CATH: 3.40.50.720

Database links Help

Enzyme: EC:1.1.1.5

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR014007

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

Q48436 Acetoin(diacetyl) reductase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR020904	Short-chain dehydrogenase/reductase, conserved site
IPR016040	NAD(P)-binding domain
IPR002347	Glucose/ribitol dehydrogenase
IPR014007	Acetoin reductase
IPR002198	Short-chain dehydrogenase/reductase SDR
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Blomqvist K, Nikkola M, Lehtovaara P, Suihko ML, Airaksinen U, Straby KB, Knowles JK, Penttila ME. Characterization of the genes of the 2,3-butanediol operons from Klebsiella terrigena and Enterobacter aerogenes. J. Bacteriol. 175 1392-404 1993 [PubMed: 8444801] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=8444801
2.	Takusagawa Y, Otagiri M, Ui S, Ohtsuki T, Mimura A, Ohkuma M, Kudo T. Purification and characterization of L-2,3-butanediol dehydrogenase of Brevibacterium saccharolyticum C-1012 expressed in Escherichia coli. Biosci. Biotechnol. Biochem. 65 1876-8 2001 [PubMed: 11577733] http://dx.doi.org/10.1271/bbb.65.1876

Additional Reading Open in usermanual
	Otagiri M, Kurisu G, Ui S, Takusagawa Y, Ohkuma M, Kudo T, Kusunoki M. Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with NAD+ and inhibitor mercaptoethanol at 1.7 A resolution for understanding of chiral substrate recognition mechanisms. J. Biochem. 129 2001 205-8 [PubMed: 11173520] http://jb.oxfordjournals.org/cgi/content/abstract/129/2/205
	Smania AM, Argarana CE. Molecular cloning and characterization of a cDNA encoding a bovine butanediol dehydrogenase. Gene 197 1997 231-8 [PubMed: 9332371] http://dx.doi.org/10.1016/S0378-1119(97)00267-9

InterPro 23.1