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Protein

Alcohol dehydrogenase 1

Gene

ADH1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This isozyme preferentially catalyzes the conversion of primary unbranched alcohols to their corresponding aldehydes. Also also shows activity toward secondary alcohols.

Catalytic activityi

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Cofactori

Zn2+Note: Binds 2 Zn2+ ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi44 – 441Zinc 1; catalytic
Metal bindingi67 – 671Zinc 1; catalytic
Metal bindingi98 – 981Zinc 2
Metal bindingi101 – 1011Zinc 2
Metal bindingi104 – 1041Zinc 2
Metal bindingi112 – 1121Zinc 2
Metal bindingi154 – 1541Zinc 1; catalytic
Binding sitei202 – 2021NADBy similarity
Binding sitei207 – 2071NADBy similarity
Binding sitei341 – 3411NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi178 – 1847NADBy similarity
Nucleotide bindingi269 – 2713NADBy similarity

GO - Molecular functioni

  • alcohol dehydrogenase (NAD) activity Source: SGD
  • methylglyoxal reductase (NADH-dependent) activity Source: SGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • amino acid catabolic process to alcohol via Ehrlich pathway Source: SGD
  • ethanol biosynthetic process involved in glucose fermentation to ethanol Source: SGD
  • NADH oxidation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:YOL086C-MONOMER.
YEAST:YOL086C-MONOMER.
BRENDAi1.1.1.1. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase 1 (EC:1.1.1.1)
Alternative name(s):
Alcohol dehydrogenase I
YADH-1
Gene namesi
Name:ADH1
Synonyms:ADC1
Ordered Locus Names:YOL086C
ORF Names:O0947
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL086C.
SGDiS000005446. ADH1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 348347Alcohol dehydrogenase 1PRO_0000160730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei213 – 2131PhosphoserineCombined sources
Modified residuei223 – 2231PhosphothreonineCombined sources
Modified residuei279 – 2791PhosphoserineCombined sources
Modified residuei316 – 3161PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP00330.
PeptideAtlasiP00330.
PRIDEiP00330.
TopDownProteomicsiP00330.

2D gel databases

COMPLUYEAST-2DPAGEP00330.
SWISS-2DPAGEP00330.

PTM databases

iPTMnetiP00330.
SwissPalmiP00330.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi34317. 139 interactions.
DIPiDIP-1143N.
IntActiP00330. 213 interactions.
MINTiMINT-642403.

Structurei

Secondary structure

1
348
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 1410Combined sources
Beta strandi20 – 256Combined sources
Beta strandi33 – 4210Combined sources
Helixi45 – 528Combined sources
Beta strandi55 – 573Combined sources
Beta strandi61 – 644Combined sources
Beta strandi68 – 769Combined sources
Beta strandi88 – 914Combined sources
Beta strandi93 – 964Combined sources
Beta strandi99 – 1013Combined sources
Helixi102 – 1054Combined sources
Helixi109 – 1113Combined sources
Beta strandi116 – 1183Combined sources
Turni119 – 1213Combined sources
Beta strandi125 – 1339Combined sources
Turni134 – 1363Combined sources
Beta strandi137 – 1404Combined sources
Helixi146 – 1494Combined sources
Helixi150 – 1534Combined sources
Helixi155 – 16410Combined sources
Beta strandi173 – 1775Combined sources
Turni178 – 1803Combined sources
Helixi184 – 19411Combined sources
Beta strandi197 – 2026Combined sources
Helixi207 – 2137Combined sources
Beta strandi218 – 2214Combined sources
Turni222 – 2243Combined sources
Helixi228 – 2358Combined sources
Beta strandi240 – 2456Combined sources
Helixi250 – 25910Combined sources
Beta strandi260 – 2689Combined sources
Beta strandi276 – 2805Combined sources
Helixi281 – 2866Combined sources
Beta strandi290 – 2934Combined sources
Helixi299 – 31012Combined sources
Beta strandi318 – 3225Combined sources
Helixi323 – 3253Combined sources
Helixi326 – 3349Combined sources
Beta strandi339 – 3468Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4W6ZX-ray2.40A/B/C/D2-348[»]
5ENVX-ray3.00A/B2-348[»]
ProteinModelPortaliP00330.
SMRiP00330. Positions 2-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00330.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000075207.
HOGENOMiHOG000294685.
InParanoidiP00330.
KOiK13953.
OMAiNAPLGAN.
OrthoDBiEOG7JDR73.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00330-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIPETQKGV IFYESHGKLE YKDIPVPKPK ANELLINVKY SGVCHTDLHA
60 70 80 90 100
WHGDWPLPVK LPLVGGHEGA GVVVGMGENV KGWKIGDYAG IKWLNGSCMA
110 120 130 140 150
CEYCELGNES NCPHADLSGY THDGSFQQYA TADAVQAAHI PQGTDLAQVA
160 170 180 190 200
PILCAGITVY KALKSANLMA GHWVAISGAA GGLGSLAVQY AKAMGYRVLG
210 220 230 240 250
IDGGEGKEEL FRSIGGEVFI DFTKEKDIVG AVLKATDGGA HGVINVSVSE
260 270 280 290 300
AAIEASTRYV RANGTTVLVG MPAGAKCCSD VFNQVVKSIS IVGSYVGNRA
310 320 330 340
DTREALDFFA RGLVKSPIKV VGLSTLPEIY EKMEKGQIVG RYVVDTSK
Length:348
Mass (Da):36,849
Last modified:October 5, 2010 - v5
Checksum:iF14AE24B5D8D12A5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211Y → H in CAA24601 (PubMed:6277922).Curated
Sequence conflicti21 – 211Y → H in AAA34410 (PubMed:6279086).Curated
Sequence conflicti59 – 591V → T AA sequence (PubMed:320000).Curated
Sequence conflicti148 – 1481Q → E AA sequence (PubMed:320000).Curated
Sequence conflicti152 – 1521I → V AA sequence (PubMed:320000).Curated
Sequence conflicti237 – 2371D → N AA sequence (PubMed:320000).Curated
Sequence conflicti314 – 3141V → I AA sequence (PubMed:320000).Curated
Sequence conflicti338 – 3381I → V AA sequence (PubMed:320000).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti236 – 2361T → I.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BK006948 Genomic DNA. Translation: DAA10699.1.
PIRiS57383. DEBYA.
RefSeqiNP_014555.1. NM_001183340.1.

Genome annotation databases

EnsemblFungiiYOL086C; YOL086C; YOL086C.
GeneIDi854068.
KEGGisce:YOL086C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BK006948 Genomic DNA. Translation: DAA10699.1.
PIRiS57383. DEBYA.
RefSeqiNP_014555.1. NM_001183340.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4W6ZX-ray2.40A/B/C/D2-348[»]
5ENVX-ray3.00A/B2-348[»]
ProteinModelPortaliP00330.
SMRiP00330. Positions 2-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34317. 139 interactions.
DIPiDIP-1143N.
IntActiP00330. 213 interactions.
MINTiMINT-642403.

PTM databases

iPTMnetiP00330.
SwissPalmiP00330.

2D gel databases

COMPLUYEAST-2DPAGEP00330.
SWISS-2DPAGEP00330.

Proteomic databases

MaxQBiP00330.
PeptideAtlasiP00330.
PRIDEiP00330.
TopDownProteomicsiP00330.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL086C; YOL086C; YOL086C.
GeneIDi854068.
KEGGisce:YOL086C.

Organism-specific databases

EuPathDBiFungiDB:YOL086C.
SGDiS000005446. ADH1.

Phylogenomic databases

GeneTreeiENSGT00550000075207.
HOGENOMiHOG000294685.
InParanoidiP00330.
KOiK13953.
OMAiNAPLGAN.
OrthoDBiEOG7JDR73.

Enzyme and pathway databases

BioCyciMetaCyc:YOL086C-MONOMER.
YEAST:YOL086C-MONOMER.
BRENDAi1.1.1.1. 984.

Miscellaneous databases

EvolutionaryTraceiP00330.
PROiP00330.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "The primary structure of yeast alcohol dehydrogenase."
    Joernvall H.
    Eur. J. Biochem. 72:425-442(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-348, ACETYLATION AT SER-2, VARIANT ILE-236.
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 214-333.
  8. Cited for: PROTEIN SEQUENCE OF 62-76; 320-332 AND 337-348.
    Strain: ATCC 204508 / S288c.
  9. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 9-17; 40-48 AND 304-310.
    Strain: ATCC 38531 / Y41.
  10. "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] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  11. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  12. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  13. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213 AND THR-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279 AND SER-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiADH1_YEAST
AccessioniPrimary (citable) accession number: P00330
Secondary accession number(s): D6W1Y3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 5, 2010
Last modified: June 8, 2016
This is version 177 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

PubMed:320000 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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.