[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=7731988 [NCBI, ExPASy, EBI, Israel, Japan] Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K.; "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae."; Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
[2]	CHARACTERIZATION. STRAIN=ATCC 90845 / FY834; DOI=10.1074/jbc.M003035200; PubMed=10938079 [NCBI, ExPASy, EBI, Israel, Japan] Gonzalez E., Fernandez M.R., Larroy C., Sola L., Pericas M.A., Pares X., Biosca J.A.; "Characterization of a (2R,3R)-2,3-butanediol dehydrogenase as the Saccharomyces cerevisiae YAL060W gene product. Disruption and induction of the gene."; J. Biol. Chem. 275:35876-35885(2000).
[3]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).

Comments

CATALYTIC ACTIVITY: (R,R)-butane-2,3-diol + NAD⁺ = (R)-acetoin + NADH.
COFACTOR: Binds 2 zinc ions per subunit (By similarity).
SUBUNIT: Homodimer.
INTERACTION:
P40054:SER3; NbExp=1; IntAct=EBI-3501, EBI-16961;
MISCELLANEOUS: Present with 8730 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase 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

U12980; AAC04974.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S51962; S51962.

RefSeq

NP_009341.1; -.

3D structure databases

HSSP

O96496; 1E3J. [HSSP ENTRY / PDB]

ModBase

P39714.

Protein-protein interaction databases

DIP

DIP:5356N; -.

IntAct

P39714; -.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-14023; -.

Organism-specific databases

YAL060w; -.

S000000056; BDH1.

Gene expression databases

GermOnline

YAL060W; Saccharomyces cerevisiae.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0000721;	Molecular function: (R,R)-butanediol dehydrogenase activity (inferred from direct assay from SGD).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006066;	Biological process: cellular alcohol metabolic process (inferred from mutant phenotype from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.

PANTHER

PTHR11695; ADH_Sf_Zn; 1.

Pfam

PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00059; ADH_ZINC; 1.

BLOCKS

P39714.

Proteomic databases

PeptideAtlas

P39714; -.

Genome annotation databases

Ensembl

YAL060W; Saccharomyces cerevisiae. [Contig view]

851239; -.

U00091_GR; YAL060W.

sce:YAL060W; -.

fig|4932.3.peg.15; -.

Phylogenomic databases

HOGENOM

P39714; -.

Other

P39714; -.

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

Keywords

Complete proteome; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 382`	`382`	`(R,R)-butanediol dehydrogenase.`	`PRO_0000160788`
`METAL`	`39 39`		`Zinc 1; catalytic (By similarity).`
`METAL`	`73 73`		`Zinc 1; catalytic (By similarity).`
`METAL`	`103 103`		`Zinc 2 (By similarity).`
`METAL`	`120 120`		`Zinc 2 (By similarity).`
`METAL`	`123 123`		`Zinc 2 (By similarity).`
`METAL`	`131 131`		`Zinc 2 (By similarity).`
`METAL`	`173 173`		`Zinc 1; catalytic (By similarity).`

Sequence information

Length: 382 AA [This is the length of the unprocessed precursor]

Molecular weight: 41538 Da [This is the MW of the unprocessed precursor]

CRC64: 1006FA596DE91A17 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRALAYFKKG DIHFTNDIPR PEIQTDDEVI IDVSWCGICG SDLHEYLDGP IFMPKDGECH 

        70         80         90        100        110        120 
KLSNAALPLA MGHEMSGIVS KVGPKVTKVK VGDHVVVDAA SSCADLHCWP HSKFYNSKPC 

       130        140        150        160        170        180 
DACQRGSENL CTHAGFVGLG VISGGFAEQV VVSQHHIIPV PKEIPLDVAA LVEPLSVTWH 

       190        200        210        220        230        240 
AVKISGFKKG SSALVLGAGP IGLCTILVLK GMGASKIVVS EIAERRIEMA KKLGVEVFNP 

       250        260        270        280        290        300 
SKHGHKSIEI LRGLTKSHDG FDYSYDCSGI QVTFETSLKA LTFKGTATNI AVWGPKPVPF 

       310        320        330        340        350        360 
QPMDVTLQEK VMTGSIGYVV EAFEEVVRAI HNGDIAMEDC KQLITGKQRI EDGWEKGFQE 

       370        380 
LMDHKESNVK ILLTPNNHGE MK

P39714 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