Reviewed, UniProtKB/Swiss-Prot P00331 (ADH2_YEAST)

Names and origin

Protein names

Recommended name:
    Alcohol dehydrogenase 2
    EC=1.1.1.1
Alternative name(s):
    YADH-2
    Alcohol dehydrogenase II

Gene names

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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [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.7
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
Gene Ontology (GO)
Biological process	NADH oxidation Inferred from direct assay. Source: SGD amino acid catabolic process to alcohol via Ehrlich pathway Inferred from genetic interaction. Source: SGD ethanol metabolic process Inferred from direct assay. Source: SGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: SGD
Molecular function	alcohol dehydrogenase (NAD) activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC42	P19073	1	EBI-2222,EBI-4274
RSP5	P39940	1	EBI-2222,EBI-16219
SSM4	P40318	1	EBI-2222,EBI-18208

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 348	347	Alcohol dehydrogenase 2		PRO_0000160731
Regions
	Nucleotide binding	178 – 184	7	NAD By similarity
	Nucleotide binding	269 – 271	3	NAD By similarity
Sites
	Metal binding	44	1	Zinc 1; catalytic
	Metal binding	67	1	Zinc 1; catalytic
	Metal binding	98	1	Zinc 2
	Metal binding	101	1	Zinc 2
	Metal binding	104	1	Zinc 2
	Metal binding	112	1	Zinc 2
	Metal binding	154	1	Zinc 1; catalytic
	Binding site	202	1	NAD By similarity
	Binding site	207	1	NAD By similarity
	Binding site	341	1	NAD By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.5
	Modified residue	288	1	Phosphoserine Ref.11
	Modified residue	290	1	Phosphoserine Ref.11 Ref.8 Ref.10
	Modified residue	294	1	Phosphoserine Ref.10
	Modified residue	302	1	Phosphothreonine Ref.10
	Modified residue	316	1	Phosphoserine Ref.11 Ref.9
Experimental info
	Sequence conflict	16	1	N → H in AAA34411. Ref.2
	Sequence conflict	31	1	P → A in AAA34411. Ref.2
	Sequence conflict	233	1	V → K AA sequence Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P00331-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 54535FC3258B10EA	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

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. , Skelton J., Walsh S.V., Whitehead S., 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]	"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.
[5]	"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.
[6]	"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.
[7]	"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].
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
PIR	DEBYA2. A00340.
RefSeq	NP_014032.1.
3D structure databases
SMR	P00331. Positions 2-348.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1181N.
IntAct	P00331. 19 interactions.
STRING	P00331.
Proteomic databases
PeptideAtlas	P00331.
PRIDE	P00331.
Genome annotation databases
Ensembl	YMR303C; YMR303C; YMR303C; Saccharomyces cerevisiae. [Genome view]
GeneID	855349.
KEGG	sce:YMR303C.
NMPDR	fig|4932.3.peg.5090.
Organism-specific databases
CYGD	YMR303c.
SGD	S000004918. ADH2.
Phylogenomic databases
eggNOG	fuNOG04605.
HOGENOM	HBG753318.
OMA	SELASIY.
OrthoDB	EOG95HTDV.
PhylomeDB	P00331.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-11726.
BRENDA	1.1.1.1. 250.
Gene expression databases
ArrayExpress	P00331.
Genevestigator	P00331.
GermOnline	YMR303C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002328. ADH_Zn_CS. IPR011032. GroES-like. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	979103.

Entry information

Entry name

ADH2_YEAST

Accession

Primary (citable) accession number: P00331

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 106 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)