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: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alcohol dehydrogenase activity Ref.6 Inferred from electronic annotation. Source: EC 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: InterPro
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

Chain

2 – 348

347

Alcohol dehydrogenase 1

PRO_0000160730

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

Amino acid modifications

Modified residue

2

1

N-acetylserine

Modified residue

15

1

Phosphoserine

Modified residue

213

1

Phosphoserine

Modified residue

223

1

Phosphothreonine

Modified residue

290

1

Phosphoserine

Modified residue

316

1

Phosphoserine

Modified residue

325

1

Phosphothreonine

Natural variations

Natural variant

236

1

T → I

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." <