P39714 (BDH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Diacetyl reductase [(R)-acetoin forming]
EC=1.1.1.303

Gene names

Name:	BDH1
Synonyms:	BDH
Ordered Locus Names:	YAL060W
ORF Names:	FUN49

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the irreversible reduction of 2,3-butanediol to (S)-acetoin in the presence of NADH By similarity.
Catalytic activity	(R)-acetoin + NAD+ = diacetyl + NADH.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm Ref.5.
Miscellaneous	Present with 8730 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	alcohol metabolic process Inferred from mutant phenotype Ref.4. Source: SGD butanediol biosynthetic process Inferred from mutant phenotype PubMed 19966022. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 11914276Ref.5. Source: SGD
Molecular_function	(R,R)-butanediol dehydrogenase activity Inferred from direct assay Ref.4. Source: SGD diacetyl reductase ((R)-acetoin forming) activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 382	382	Diacetyl reductase [(R)-acetoin forming]		PRO_0000160788
Sites
	Metal binding	39	1	Zinc 1; catalytic By similarity
	Metal binding	73	1	Zinc 1; catalytic By similarity
	Metal binding	103	1	Zinc 2 By similarity
	Metal binding	120	1	Zinc 2 By similarity
	Metal binding	123	1	Zinc 2 By similarity
	Metal binding	131	1	Zinc 2 By similarity
	Metal binding	173	1	Zinc 1; catalytic By similarity
Experimental info
	Sequence conflict	322	1	D → A in AAC04974. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P39714 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 1776FA5968EC1A12	FASTA	382	41,582
	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 EDFEEVVRAI HNGDIAMEDC KQLITGKQRI EDGWEKGFQE 370 380 LMDHKESNVK ILLTPNNHGE MK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae." 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. Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 322. Strain: ATCC 204508 / S288c.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Characterization of a (2R,3R)-2,3-butanediol dehydrogenase as the Saccharomyces cerevisiae YAL060W gene product. Disruption and induction of the gene." Gonzalez E., Fernandez M.R., Larroy C., Sola L., Pericas M.A., Pares X., Biosca J.A. J. Biol. Chem. 275:35876-35885(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: ATCC 90845 / FY834.
[5]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U12980 Genomic DNA. Translation: AAC04974.1. AY692922 Genomic DNA. Translation: AAT92941.1. BK006935 Genomic DNA. Translation: DAA06929.2.
PIR	S51962.
RefSeq	NP_009341.2. NM_001178202.2.
3D structure databases
ProteinModelPortal	P39714.
SMR	P39714. Positions 1-373.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5356N.
IntAct	P39714. 2 interactions.
MINT	MINT-487549.
STRING	4932.YAL060W.
Proteomic databases
PaxDb	P39714.
PeptideAtlas	P39714.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YAL060W; YAL060W; YAL060W.
GeneID	851239.
KEGG	sce:YAL060W.
Organism-specific databases
CYGD	YAL060w.
SGD	S000000056. BDH1.
Phylogenomic databases
eggNOG	COG1063.
GeneTree	ENSGT00550000075527.
HOGENOM	HOG000294670.
KO	K00004.
OMA	KALRWHA.
OrthoDB	EOG4H49CR.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14023. YEAST:YAL060W-MONOMER.
Gene expression databases
Genevestigator	P39714.
GermOnline	YAL060W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.50.720. 1 hit. 3.90.180.10. 1 hit.
InterPro	IPR013149. ADH_C. IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn-type. IPR002328. ADH_Zn_CS. IPR011032. GroES-like. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR11695. PTHR11695. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
SUPFAM	SSF50129. GroES_like. 1 hit.
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	968165.

Entry information

Entry name

BDH1_YEAST

Accession

Primary (citable) accession number: P39714
Secondary accession number(s): D6VPF9, E9P8Z3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	July 27, 2011
Last modified:	May 29, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program