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UniProtKB/Swiss-Prot entry P00330


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ADH1_YEAST
Primary accession number P00330
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 4)
Annotations were last modified on    November 25, 2008 (Entry version 105)
Name and origin of the protein
Protein name Alcohol dehydrogenase 1
Synonyms EC 1.1.1.1
Alcohol dehydrogenase I
YADH-1
Gene name
Name: ADH1
Synonyms: ADC1
OrderedLocusNames: YOL086C
ORFNames: O0947
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6277922 [NCBI, ExPASy, EBI, Israel, Japan]
Bennetzen J.L., Hall B.D.;
"The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase.";
J. Biol. Chem. 257:3018-3025(1982).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6279086 [NCBI, ExPASy, EBI, Israel, Japan]
Young E.T., Williamson V.M., Taguchi A., Smith M., Sledziewski A., Russell D.W., Osterman J., Denis C., Cox D., Beier D.;
"The alcohol dehydrogenase genes of the yeast, Saccharomyces cerevisiae: isolation, structure, and regulation.";
Basic Life Sci. 19:335-361(1982).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
DOI=10.1002/yea.320111009; PubMed=8533473 [NCBI, ExPASy, EBI, Israel, Japan]
Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.;
"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.";
Yeast 11:975-986(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169874 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[5]
PROTEIN SEQUENCE OF 2-348, ACETYLATION AT SER-2, AND VARIANT ILE-236.
DOI=10.1111/j.1432-1033.1977.tb11267.x; PubMed=320000 [NCBI, ExPASy, EBI, Israel, Japan]
Joernvall H.;
"The primary structure of yeast alcohol dehydrogenase.";
Eur. J. Biochem. 72:425-442(1977).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 214-333.
DOI=10.1038/283214a0; PubMed=6985717 [NCBI, ExPASy, EBI, Israel, Japan]
Williamson V.M., Bennetzen J.L., Young E.T., Nasmyth K., Hall B.D.;
"Isolation of the structural gene for alcohol dehydrogenase by genetic complementation in yeast.";
Nature 283:214-216(1980).
[7]
PROTEIN SEQUENCE OF 62-76; 320-332 AND 337-348.
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/elps.11501501210; PubMed=7895733 [NCBI, ExPASy, EBI, Israel, Japan]
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S.;
"Protein identifications for a Saccharomyces cerevisiae protein database.";
Electrophoresis 15:1466-1486(1994).
[8]
PROTEIN SEQUENCE OF 9-17; 40-48 AND 304-310.
STRAIN=ATCC 38531 / Y41;
DOI=10.1002/elps.1150160124; PubMed=7737086 [NCBI, ExPASy, EBI, Israel, Japan]
Norbeck J., Blomberg A.;
"Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides.";
Electrophoresis 16:149-156(1995).
[9]
REVIEW.
DOI=10.1016/S1567-1356(02)00157-5; PubMed=12702265 [NCBI, ExPASy, EBI, Israel, Japan]
Leskovac V., Trivic S., Pericin D.;
"The three zinc-containing alcohol dehydrogenases from baker's yeast, Saccharomyces cerevisiae.";
FEMS Yeast Res. 2:481-494(2002).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290 AND SER-316, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan]
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-213 AND THR-223, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND THR-325, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
V01292; CAA24601.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M38456; AAA34410.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X83121; CAA58193.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74828; CAA99098.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V01291; CAA24600.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S57383; DEBYA.
3D structure databases
PDB
2HCY; X-ray; 2.44 A; A/B/C/D=2-348.[ExPASy / RCSB / EBI]
PDBsum 2HCY; -.
ModBase P00330.
Protein-protein interaction databases
DIP DIP:1143N; -.
IntAct P00330; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-11724; -.
2D gel databases
SWISS-2DPAGE P00330; -.
COMPLUYEAST-2DPAGE P00330; -.
Organism-specific databases
CYGD YOL086c; -.
SGD S000005446; ADH1.
Yeast-GFP YOL086C.
Gene expression databases
GermOnline YOL086C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004022; Molecular function: alcohol dehydrogenase activity (inferred from electronic annotation from EC).
GO:0019170; Molecular function: methylglyoxal reductase (NADH-dependent) activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0000947; Biological process: amino acid catabolic process to alcohol via Ehrlich pathway (inferred from genetic interaction from SGD).
GO:0043458; Biological process: ethanol biosynthetic process during fermentation (inferred from mutant phenotype from SGD).
GO:0006116; Biological process: NADH oxidation (inferred from direct assay from SGD).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.
PROSITE PS00059; ADH_ZINC; 1.
ProtoNet P00330.
Proteomic databases
PeptideAtlas P00330; -.
Genome annotation databases
Ensembl YOL086C; Saccharomyces cerevisiae. [Contig view]
GenomeReviews Y13140_GR; YOL086C.
Phylogenomic databases
HOGENOM P00330; -.
Other
LinkHub P00330; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Phosphoprotein; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   348  347     Alcohol dehydrogenase 1. PRO_0000160730
METAL   44    44        Zinc 1; catalytic. 
METAL   67    67        Zinc 1; catalytic. 
METAL   98    98        Zinc 2. 
METAL   101   101        Zinc 2. 
METAL   104   104        Zinc 2. 
METAL   112   112        Zinc 2. 
METAL   154   154        Zinc 1; catalytic. 
MOD_RES   2     2        N-acetylserine. 
MOD_RES   15    15        Phosphoserine. 
MOD_RES   213   213        Phosphoserine. 
MOD_RES   223   223        Phosphothreonine. 
MOD_RES   290   290        Phosphoserine. 
MOD_RES   316   316        Phosphoserine. 
MOD_RES   325   325        Phosphothreonine. 
VARIANT   236   236  1     T -> I. 
CONFLICT   21    21        H -> Y (in Ref. 1; CAA99098 and 3; CAA58193). 
CONFLICT   59    59        V -> T (in Ref. 5; AA sequence). 
CONFLICT   148   148        Q -> E (in Ref. 5; AA sequence). 
CONFLICT   152   152        I -> V (in Ref. 5; AA sequence). 
CONFLICT   237   237        D -> N (in Ref. 5; AA sequence). 
CONFLICT   314   314        V -> I (in Ref. 5; AA sequence). 
CONFLICT   338   338        I -> V (in Ref. 5; AA sequence). 
STRAND   5    14  10      
STRAND   20    25  6      
STRAND   33    43  11      
HELIX   45    52  8      
STRAND   55    57  3      
STRAND   61    64  4      
STRAND   68    76  9      
STRAND   88    91  4      
STRAND   93    96  4      
STRAND   99   101  3      
TURN   102   107  6      
HELIX   109   111  3      
STRAND   116   118  3      
TURN   119   121  3      
STRAND   125   133  9      
TURN   134   136  3      
STRAND   137   140  4      
HELIX   146   149  4      
HELIX   150   153  4      
HELIX   155   164  10      
TURN   165   167  3      
STRAND   173   177  5      
TURN   178   180  3      
HELIX   182   193  12      
STRAND   197   202  6      
HELIX   207   213  7      
STRAND   218   221  4      
TURN   222   224  3      
HELIX   228   236  9      
STRAND   240   245  6      
HELIX   250   256  7      
STRAND   259   268  10      
STRAND   276   280  5      
HELIX   281   286  6      
STRAND   290   293  4      
HELIX   299   310  12      
STRAND   318   322  5      
HELIX   323   325  3      
HELIX   326   334  9      
STRAND   339   346  8      
Sequence information
Length: 348 AA [This is the length of the unprocessed precursor] Molecular weight: 36823 Da [This is the MW of the unprocessed precursor] CRC64: 5C3EE64328856BD3 [This is a checksum on the sequence]
        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 

P00330 in FASTA format

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