Alcohol dehydrogenase 2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P00331 (ADH2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 126. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alcohol dehydrogenase 2
EC=1.1.1.1

Alternative name(s):
Alcohol dehydrogenase II
YADH-2

Gene names

Name:	ADH2
Synonyms:	ADR2
Ordered Locus Names:	YMR303C
ORF Names:	YM9952.05C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This isozyme preferentially catalyzes the conversion of ethanol to acetaldehyde. Acts on a variety of primary unbranched aliphatic alcohols.
Catalytic activity	An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Induction	Repressed by glucose.
Miscellaneous	Present with 1620 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	NADH oxidation Inferred from direct assay. Source: SGD ethanol metabolic process Inferred from direct assay. Source: SGD
Cellular component	cytoplasm Inferred from direct assay. Source: SGD
Molecular function	alcohol dehydrogenase (NAD) activity Inferred from direct assay. Source: SGD nucleotide binding Inferred from electronic annotation. Source: InterPro 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

Initiator methionine

Removed

Chain

2 – 348

347

Alcohol dehydrogenase 2

PRO_0000160731

Regions

Nucleotide binding

178 – 184

NAD By similarity

Nucleotide binding

269 – 271

NAD By similarity

Sites

Metal binding

Zinc 1; catalytic

Metal binding

Zinc 1; catalytic

Metal binding

Zinc 2

Metal binding

101

Zinc 2

Metal binding

104

Zinc 2

Metal binding

112

Zinc 2

Metal binding

154

Zinc 1; catalytic

Binding site

202

NAD By similarity

Binding site

207

NAD By similarity

Binding site

341

NAD By similarity

Amino acid modifications

Modified residue

N-acetylserine Ref.6

Modified residue

288

Phosphoserine Ref.12

Modified residue

290

Phosphoserine Ref.9 Ref.11 Ref.12

Modified residue

294

Phosphoserine Ref.11

Modified residue

302

Phosphothreonine Ref.11

Modified residue

316

Phosphoserine Ref.10 Ref.12

Experimental info

Sequence conflict

N → H in AAA34411. Ref.2

Sequence conflict

P → A in AAA34411. Ref.2

Sequence conflict

233

V → K AA sequence Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P00331 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 54535FC3258B10EA
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FASTA

348

36,732

        10         20         30         40         50         60 
MSIPETQKAI IFYESNGKLE HKDIPVPKPK PNELLINVKY SGVCHTDLHA WHGDWPLPTK 

        70         80         90        100        110        120 
LPLVGGHEGA GVVVGMGENV KGWKIGDYAG IKWLNGSCMA CEYCELGNES NCPHADLSGY 

       130        140        150        160        170        180 
THDGSFQEYA TADAVQAAHI PQGTDLAEVA PILCAGITVY KALKSANLRA GHWAAISGAA 

       190        200        210        220        230        240 
GGLGSLAVQY AKAMGYRVLG IDGGPGKEEL FTSLGGEVFI DFTKEKDIVS AVVKATNGGA 

       250        260        270        280        290        300 
HGIINVSVSE AAIEASTRYC RANGTVVLVG LPAGAKCSSD VFNHVVKSIS IVGSYVGNRA 

       310        320        330        340 
DTREALDFFA RGLVKSPIKV VGLSSLPEIY EKMEKGQIAG RYVVDTSK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the yeast alcohol dehydrogenase II gene." Russell D.W., Smith M., Williamson V.M., Young E.T. J. Biol. Chem. 258:2674-2682(1983) [PubMed: 6337160] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The alcohol dehydrogenase genes of the yeast, Saccharomyces cerevisiae: isolation, structure, and regulation." Young E.T., Williamson V.M., Taguchi A., Smith M., Sledziewski A., Russell D.W., Osterman J., Denis C., Cox D., Beier D. Basic Life Sci. 19:335-361(1982) [PubMed: 6279086] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Protein identifications for a Saccharomyces cerevisiae protein database." Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S. Electrophoresis 15:1466-1486(1994) [PubMed: 7895733] [Abstract] Cited for: PROTEIN SEQUENCE OF 193-207 AND 227-234. Strain: ATCC 204508 / S288c.
[6]	"Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins." Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E. Electrophoresis 18:1347-1360(1997) [PubMed: 9298649] [Abstract] Cited for: ACETYLATION AT SER-2.
[7]	"The three zinc-containing alcohol dehydrogenases from baker's yeast, Saccharomyces cerevisiae." Leskovac V., Trivic S., Pericin D. FEMS Yeast Res. 2:481-494(2002) [PubMed: 12702265] [Abstract] Cited for: REVIEW.
[8]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, MASS SPECTROMETRY. Strain: YAL6B.
[10]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, MASS SPECTROMETRY. Strain: ADR376.
[11]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; SER-294 AND THR-302, MASS SPECTROMETRY.
[12]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-290 AND SER-316, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J01314 Genomic DNA. Translation: AAA34408.1. M38457 Genomic DNA. Translation: AAA34411.1. Z49212 Genomic DNA. Translation: CAA89136.1. BK006946 Genomic DNA. Translation: DAA10204.1.
PIR	DEBYA2. A00340.
RefSeq	NP_014032.1. NM_001182812.1.
3D structure databases
ProteinModelPortal	P00331.
SMR	P00331. Positions 2-348.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1181N.
IntAct	P00331. 18 interactions.
MINT	MINT-393329.
STRING	P00331.
Proteomic databases
PeptideAtlas	P00331.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR303C; YMR303C; YMR303C.
GeneID	855349.
KEGG	sce:YMR303C.
NMPDR	fig\|4932.3.peg.5090.
Organism-specific databases
SGD	S000004918. ADH2.
Phylogenomic databases
eggNOG	fuNOG04605.
GeneTree	EFGT00050000001793.
HOGENOM	HBG753318.
OMA	SFGIQYA.
OrthoDB	EOG4Q5CZM.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-11726.
Gene expression databases
ArrayExpress	P00331.
Genevestigator	P00331.
GermOnline	YMR303C. Saccharomyces cerevisiae.
Family and domain databases
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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K13953.
PANTHER	PTHR11695. ADH_Sf_Zn. 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	979103.

Entry information

Entry name

ADH2_YEAST

Accession

Primary (citable) accession number: P00331
Secondary accession number(s): D6W0D0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 126 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIII

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents