[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=IAM 1063; Ui S.; Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=CG21; DOI=10.1038/sj/jim/7000179; PubMed=11687934 [NCBI, ExPASy, EBI, Israel, Japan] Wardwell S.A., Yang Y.T., Chang H.-Y., San K.Y., Rudolph F.B., Bennett G.N.; "Expression of the Klebsiella pneumoniae CG21 acetoin reductase gene in Clostridium acetobutylicum ATCC 824."; J. Ind. Microbiol. Biotechnol. 27:220-227(2001).
[3]	X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG. PubMed=11173520 [NCBI, ExPASy, EBI, Israel, Japan] 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. 129:205-208(2001).

Comments

FUNCTION: Catalyzes the reversible reduction of acetoin to 2,3-butanediol in the presence of NADH.
CATALYTIC ACTIVITY: Acetoin + NAD⁺ = diacetyl + NADH.
SUBUNIT: Homotetramer.
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D86412; BAA13085.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF098800; AAC78679.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1GEG; X-ray; 1.70 A; A/B/C/D/E/F/G/H=1-256.

[ExPASy / RCSB / EBI]

PDBsum

1GEG; -.

ModBase

Q48436.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-8762; -.

Family and domain databases

InterPro

IPR014007; 23BDH.
IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PRINTS

PR00081; GDHRDH.
PR00080; SDRFAMILY.

TIGRFAMs

TIGR02415; 23BDH; 1.

PROSITE

PS00061; ADH_SHORT; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 256`	`256`	`Acetoin(diacetyl) reductase.`	`PRO_0000054537`
`NP_BIND`	`6 33`	`28`	`NAD.`
`ACT_SITE`	`152 152`		`Proton acceptor.`
`BINDING`	`59 59`		`NAD.`
`BINDING`	`139 139`		`Substrate.`
`BINDING`	`156 156`		`NAD.`
`CONFLICT`	`52 54`		`RAM -> HAV (in Ref. 1; BAA13085).`
`STRAND`	`4 8`	`5`
`TURN`	`9 11`	`3`
`HELIX`	`13 24`	`12`
`STRAND`	`28 34`	`7`
`HELIX`	`36 48`	`13`
`STRAND`	`53 57`	`5`
`HELIX`	`63 76`	`14`
`STRAND`	`82 85`	`4`
`HELIX`	`95 97`	`3`
`HELIX`	`100 110`	`11`
`HELIX`	`112 128`	`17`
`STRAND`	`132 137`	`6`
`HELIX`	`140 142`	`3`
`HELIX`	`150 170`	`21`
`HELIX`	`171 173`	`3`
`STRAND`	`175 182`	`8`
`STRAND`	`184 187`	`4`
`HELIX`	`188 201`	`14`
`HELIX`	`207 213`	`7`
`HELIX`	`224 235`	`12`
`HELIX`	`237 239`	`3`
`STRAND`	`246 254`	`9`

Sequence information

Length: 256 AA [This is the length of the unprocessed precursor]

Molecular weight: 26642 Da [This is the MW of the unprocessed precursor]

CRC64: B250F184C665ACAF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKVALVTGA GQGIGKAIAL RLVKDGFAVA IADYNDATAK AVASEINQAG GRAMAVKVDV 

        70         80         90        100        110        120 
SDRDQVFAAV EQARKTLGGF DVIVNNAGVA PSTPIESITP EIVDKVYNIN VKGVIWGIQA 

       130        140        150        160        170        180 
AVEAFKKEGH GGKIINACSQ AGHVGNPELA VYSSSKFAVR GLTQTAARDL APLGITVNGY 

       190        200        210        220        230        240 
CPGIVKTPMW AEIDRQVSEA AGKPLGYGTA EFAKRITLGR LSEPEDVAAC VSYLASPDSD 

       250 
YMTGQSLLID GGMVFN

Q48436 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools