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P39714 (BDH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
(R,R)-butanediol dehydrogenase

EC=1.1.1.4
Gene names
Name:BDH1
Synonyms:BDH
Ordered Locus Names:YAL060W
ORF Names:FUN49
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

NAD-dependent (R,R)-butanediol dehydrogenase which catalyzes oxidation of (R,R)-butane-2,3-diol to (3R)-acetoin, of meso-butanediol to (3S)-acetoin, and reduction of acetoin. Allows the use of 2,3-butanediol as an aerobic carbon source. Ref.4

Catalytic activity

(R,R)-butane-2,3-diol + NAD+ = (R)-acetoin + NADH. Ref.4

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.

Biophysicochemical properties

Kinetic parameters:

KM=14 mM for (R,R)-butane-2,3-diol Ref.4

KM=65 mM for meso-butanediol

KM=57 mM for 1,2-Butanediol

KM=4.5 mM for (3R/3S)-acetoin

KM=0.55 mM for NAD

KM=0.055 mM for NADH

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 382382(R,R)-butanediol dehydrogenase
PRO_0000160788

Sites

Metal binding391Zinc 1; catalytic By similarity
Metal binding731Zinc 1; catalytic By similarity
Metal binding1031Zinc 2 By similarity
Metal binding1201Zinc 2 By similarity
Metal binding1231Zinc 2 By similarity
Metal binding1311Zinc 2 By similarity
Metal binding1731Zinc 1; catalytic By similarity

Amino acid modifications

Modified residue631Phosphoserine Ref.7

Experimental info

Sequence conflict3221D → A in AAC04974. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P39714 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 1776FA5968EC1A12

FASTA38241,582
        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 

« Hide

References

« Hide '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 204508 / S288c.
[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. expand/collapse author list , 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: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
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].
[7]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, IDENTIFICATION BY MASS SPECTROMETRY [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.
PIRS51962.
RefSeqNP_009341.2. NM_001178202.2.

3D structure databases

ProteinModelPortalP39714.
SMRP39714. Positions 1-373.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31770. 33 interactions.
DIPDIP-5356N.
IntActP39714. 2 interactions.
MINTMINT-487549.
STRING4932.YAL060W.

Proteomic databases

PaxDbP39714.
PeptideAtlasP39714.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYAL060W; YAL060W; YAL060W.
GeneID851239.
KEGGsce:YAL060W.

Organism-specific databases

CYGDYAL060w.
SGDS000000056. BDH1.

Phylogenomic databases

eggNOGCOG1063.
GeneTreeENSGT00750000118226.
HOGENOMHOG000294670.
KOK00004.
OMACSEYLVT.
OrthoDBEOG7DVDNZ.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14023.
YEAST:YAL060W-MONOMER.

Gene expression databases

GenevestigatorP39714.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProIPR013149. 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]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. SSF50129. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968165.

Entry information

Entry nameBDH1_YEAST
AccessionPrimary (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: April 16, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome I

Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families