Reviewed, UniProtKB/Swiss-Prot P00330 (ADH1_YEAST)

Names and origin

Protein names

Recommended name:
    Alcohol dehydrogenase 1
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase I
    YADH-1

Gene names

Name:	ADH1
Synonyms:	ADC1
Ordered Locus Names:	YOL086C
ORF Names:	O0947

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 primary unbranched alcohols to their corresponding aldehydes. Also also shows activity toward secondary alcohols.
Catalytic activity	An alcohol + NAD+ = an aldehyde or ketone + NADH.
Cofactor	Binds 2 zinc ions per subunit.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Miscellaneous	Ref.5 sequence has several conflicting residues and reports microheterogeneities at additional postitions. Analysis of the sequence suggests that the sequenced protein was a mixture of at least 3 of the different isoforms of alcohol dehydrogenases found in yeast.
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	3D-structure 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 biosynthetic process during fermentation Inferred from mutant phenotype. Source: SGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane enriched fraction Inferred from direct assay. Source: SGD
Molecular function	alcohol dehydrogenase activity Ref.6 Inferred from direct assay. Source: SGD methylglyoxal reductase (NADH-dependent) 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
	Q12298	1	EBI-2218,EBI-34580
KHA1	P40309	1	EBI-2218,EBI-25993
LEM3	P42838	1	EBI-2218,EBI-28396
PHM8	P40025	1	EBI-2218,EBI-22502
PRC1	P00729	1	EBI-2218,EBI-4153

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 348

347

Alcohol dehydrogenase 1

PRO_0000160730

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

15

1

Phosphoserine Ref.12

Modified residue

213

1

Phosphoserine Ref.12

Modified residue

223

1

Phosphothreonine Ref.12

Modified residue

290

1

Phosphoserine Ref.10

Modified residue

316

1

Phosphoserine Ref.10 Ref.11 Ref.13 Ref.14

Modified residue

325

1

Phosphothreonine Ref.14

Natural variations

Natural variant

236

1

T → I Ref.5

Experimental info

Sequence conflict

21

1

H → Y in CAA99098. Ref.1

Sequence conflict

21

1

H → Y in CAA58193. Ref.3

Sequence conflict

59

1

V → T AA sequence Ref.5

Sequence conflict

148

1

Q → E AA sequence Ref.5

Sequence conflict

152

1

I → V AA sequence Ref.5

Sequence conflict

237

1

D → N AA sequence Ref.5

Sequence conflict

314

1

V → I AA sequence Ref.5

Sequence conflict

338

1

I → V AA sequence Ref.5

Secondary structure

1

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348

Helix Strand Turn

Details...

Beta strand

5 – 14

10

Beta strand

20 – 25

6

Beta strand

33 – 43

11

Helix

45 – 52

8

Beta strand

55 – 57

3

Beta strand

61 – 64

4

Beta strand

68 – 76

9

Beta strand

88 – 91

4

Beta strand

93 – 96

4

Beta strand

99 – 101

3

Turn

102 – 107

6

Helix

109 – 111

3

Beta strand

116 – 118

3

Turn

119 – 121

3

Beta strand

125 – 133

9

Turn

134 – 136

3

Beta strand

137 – 140

4

Helix

146 – 149

4

Helix

150 – 153

4

Helix

155 – 164

10

Turn

165 – 167

3

Beta strand

173 – 177

5

Turn

178 – 180

3

Helix

182 – 193

12

Beta strand

197 – 202

6

Helix

207 – 213

7

Beta strand

218 – 221

4

Turn

222 – 224

3

Helix

228 – 236

9

Beta strand

240 – 245

6

Helix

250 – 256

7

Beta strand

259 – 268

10

Beta strand

276 – 280

5

Helix

281 – 286

6

Beta strand

290 – 293

4

Helix

299 – 310

12

Beta strand

318 – 322

5

Helix

323 – 325

3

Helix

326 – 334

9

Beta strand

339 – 346

8

Sequences

	Sequence		Length	Mass (Da)
	P00330-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 5C3EE64328856BD3	FASTA	348	36,823
	10 20 30 40 50 60 MSIPETQKGV IFYESHGKLE HKDIPVPKPK ANELLINVKY SGVCHTDLHA WHGDWPLPVK 70 80 90 100 110 120 LPLVGGHEGA GVVVGMGENV KGWKIGDYAG IKWLNGSCMA CEYCELGNES NCPHADLSGY 130 140 150 160 170 180 THDGSFQQYA TADAVQAAHI PQGTDLAQVA PILCAGITVY KALKSANLMA GHWVAISGAA 190 200 210 220 230 240 GGLGSLAVQY AKAMGYRVLG IDGGEGKEEL FRSIGGEVFI DFTKEKDIVG AVLKATDGGA 250 260 270 280 290 300 HGVINVSVSE AAIEASTRYV RANGTTVLVG MPAGAKCCSD VFNQVVKSIS IVGSYVGNRA 310 320 330 340 DTREALDFFA RGLVKSPIKV VGLSTLPEIY EKMEKGQIVG RYVVDTSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase." Bennetzen J.L., Hall B.D. J. Biol. Chem. 257:3018-3025(1982) [PubMed: 6277922] [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]	"A 29.425 kb segment on the left arm of yeast chromosome XV contains more than twice as many unknown as known open reading frames." Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M. Yeast 11:975-986(1995) [PubMed: 8533473] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	"The primary structure of yeast alcohol dehydrogenase." Joernvall H. Eur. J. Biochem. 72:425-442(1977) [PubMed: 320000] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-348, ACETYLATION AT SER-2, VARIANT ILE-236.
[6]	"Isolation of the structural gene for alcohol dehydrogenase by genetic complementation in yeast." Williamson V.M., Bennetzen J.L., Young E.T., Nasmyth K., Hall B.D. Nature 283:214-216(1980) [PubMed: 6985717] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 214-333.
[7]	"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 62-76; 320-332 AND 337-348. Strain: ATCC 204508 / S288c.
[8]	"Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides." Norbeck J., Blomberg A. Electrophoresis 16:149-156(1995) [PubMed: 7737086] [Abstract] Cited for: PROTEIN SEQUENCE OF 9-17; 40-48 AND 304-310. Strain: ATCC 38531 / Y41.
[9]	"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.
[10]	"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 AND SER-316, MASS SPECTROMETRY.
[11]	"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.
[12]	"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-15; SER-213 AND THR-223, MASS SPECTROMETRY.
[13]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, MASS SPECTROMETRY.
[14]	"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-316 AND THR-325, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

V01292 Genomic DNA. Translation: CAA24601.1.
M38456 Genomic DNA. Translation: AAA34410.1.
X83121 Genomic DNA. Translation: CAA58193.1.
Z74828 Genomic DNA. Translation: CAA99098.1.
V01291 Genomic DNA. Translation: CAA24600.1.

PIR

DEBYA. S57383.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HCY	X-ray	2.44	A/B/C/D	2-347	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1143N.

IntAct

P00330. 221 interactions.

2-D gel databases

SWISS-2DPAGE

P00330.

COMPLUYEAST-2DPAGE

P00330.

Proteomic databases

PeptideAtlas

P00330.

PRIDE

P00330.

Genome annotation databases

Ensembl

YOL086C. Saccharomyces cerevisiae. [Contig view]

GenomeReviews

Gene locus YOL086C in contig Y13140_GR.

KEGG

sce:YOL086C.

Organism-specific databases

CYGD

YOL086c.

SGD

S000005446. ADH1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P00330.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-11724.

BRENDA

1.1.1.1. 250.

Gene expression databases

GermOnline

YOL086C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
[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...

Entry information

Entry name

ADH1_YEAST

Accession

Primary (citable) accession number: P00330

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 110 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)