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P10127 (ADH4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alcohol dehydrogenase 4

EC=1.1.1.1
Alternative name(s):
Alcohol dehydrogenase IV
Short name=ADHIV
Gene names
Name:ADH4
Synonyms:ZRG5
Ordered Locus Names:YGL256W
ORF Names:NRC465
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reduces acetaldehyde to ethanol during glucose fermentation. Specific for ethanol. Shows drastically reduced activity towards primary alcohols from 4 carbon atoms upward. Isomers of aliphatic alcohol, as well as secondary alcohols and glycerol are not used at all. Ref.13

Catalytic activity

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

Cofactor

Zinc. May bind iron when zinc levels are limiting. Ref.5

Enzyme regulation

Inhibited by EDTA. Ref.5

Subunit structure

Homodimer. Ref.5

Subcellular location

Mitochondrion Ref.8.

Induction

Induced by transcription factor ZAP1 in response to zinc deficiency. Ref.5 Ref.6 Ref.7 Ref.10 Ref.12 Ref.13

Miscellaneous

While ADH4 is expressed at only low levels in laboratory strains, it is often highly expressed in brewing strains.

Present with 125 molecules/cell in log phase SD medium. Ref.9

Sequence similarities

Belongs to the iron-containing alcohol dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=59 mM for NAD Ref.5

KM=122 µM for NADH

KM=2.83 mM for acetaldehyde

KM=16.7 mM for ethanol

pH dependence:

Optimum pH is 8.3.

Sequence caution

The sequence CAA64131.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA96976.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentMitochondrion
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processfermentation

Inferred from mutant phenotype. Source: SGD

   Cellular componentmitochondrion

Inferred from direct assay Ref.8. Source: SGD

   Molecular functionalcohol dehydrogenase (NAD) activity

Inferred from direct assay Ref.5. Source: SGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 382382Alcohol dehydrogenase 4
PRO_0000087817

Experimental info

Sequence conflict601D → G in CAA29410. Ref.1
Sequence conflict881Q → E in CAA29410. Ref.1
Sequence conflict3101F → C in CAA29410. Ref.1
Sequence conflict3391E → D in CAA29410. Ref.1
Sequence conflict3481E → D in CAA29410. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P10127 [UniParc].

Last modified July 22, 2008. Version 3.
Checksum: 7DFFD43830FB269B

FASTA38241,142
        10         20         30         40         50         60 
MSSVTGFYIP PISFFGEGAL EETADYIKNK DYKKALIVTD PGIAAIGLSG RVQKMLEERD 

        70         80         90        100        110        120 
LNVAIYDKTQ PNPNIANVTA GLKVLKEQNS EIVVSIGGGS AHDNAKAIAL LATNGGEIGD 

       130        140        150        160        170        180 
YEGVNQSKKA ALPLFAINTT AGTASEMTRF TIISNEEKKI KMAIIDNNVT PAVAVNDPST 

       190        200        210        220        230        240 
MFGLPPALTA ATGLDALTHC IEAYVSTASN PITDACALKG IDLINESLVA AYKDGKDKKA 

       250        260        270        280        290        300 
RTDMCYAEYL AGMAFNNASL GYVHALAHQL GGFYHLPHGV CNAVLLPHVQ EANMQCPKAK 

       310        320        330        340        350        360 
KRLGEIALHF GASQEDPEET IKALHVLNRT MNIPRNLKEL GVKTEDFEIL AEHAMHDACH 

       370        380 
LTNPVQFTKE QVVAIIKKAY EY 

« Hide

References

« Hide 'large scale' references
[1]"Homology of Saccharomyces cerevisiae ADH4 to an iron-activated alcohol dehydrogenase from Zymomonas mobilis."
Williamson V.M., Paquin C.E.
Mol. Gen. Genet. 209:374-381(1987) [PubMed: 2823079] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence of a 39,411 bp DNA fragment covering the left end of chromosome VII of Saccharomyces cerevisiae."
Coissac E., Maillier E., Robineau S., Netter P.
Yeast 12:1555-1562(1996) [PubMed: 8972578] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed: 9169869] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Overexpression, purification and properties of alcohol dehydrogenase IV from Saccharomyces cerevisiae."
Drewke C., Ciriacy M.
Biochim. Biophys. Acta 950:54-60(1988) [PubMed: 3282541] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR, ENZYME REGULATION.
[6]"Zinc-regulated genes in Saccharomyces cerevisiae revealed by transposon tagging."
Yuan D.S.
Genetics 156:45-58(2000) [PubMed: 10978274] [Abstract]
Cited for: INDUCTION.
[7]"Genome-wide characterization of the Zap1p zinc-responsive regulon in yeast."
Lyons T.J., Gasch A.P., Gaither L.A., Botstein D., Brown P.O., Eide D.J.
Proc. Natl. Acad. Sci. U.S.A. 97:7957-7962(2000) [PubMed: 10884426] [Abstract]
Cited for: INDUCTION, IDENTIFICATION OF PROBABLE INITIATION SITE.
[8]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]"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].
[10]"Repression of ADH1 and ADH3 during zinc deficiency by Zap1-induced intergenic RNA transcripts."
Bird A.J., Gordon M., Eide D.J., Winge D.R.
EMBO J. 25:5726-5734(2006) [PubMed: 17139254] [Abstract]
Cited for: INDUCTION.
[11]"Characterization of low-acetic-acid-producing yeast isolated from 2-deoxyglucose-resistant mutants and its application to high-gravity brewing."
Mizuno A., Tabei H., Iwahuti M.
J. Biosci. Bioeng. 101:31-37(2006) [PubMed: 16503288] [Abstract]
Cited for: EXPRESSION LEVEL IN BREWING STRAINS.
[12]"Physiological and transcriptional responses of Saccharomyces cerevisiae to zinc limitation in chemostat cultures."
De Nicola R., Hazelwood L.A., De Hulster E.A.F., Walsh M.C., Knijnenburg T.A., Reinders M.J.T., Walker G.M., Pronk J.T., Daran J.-M., Daran-Lapujade P.
Appl. Environ. Microbiol. 73:7680-7692(2007) [PubMed: 17933919] [Abstract]
Cited for: INDUCTION.
[13]"Acetaldehyde addition throughout the growth phase alleviates the phenotypic effect of zinc deficiency in Saccharomyces cerevisiae."
Cheraiti N., Sauvage F.-X., Salmon J.-M.
Appl. Microbiol. Biotechnol. 77:1093-1109(2008) [PubMed: 17938904] [Abstract]
Cited for: FUNCTION, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05992 Genomic DNA. Translation: CAA29410.1.
X94357 Genomic DNA. Translation: CAA64131.1. Different initiation.
Z72778 Genomic DNA. Translation: CAA96976.1. Different initiation.
BK006941 Genomic DNA. Translation: DAA07863.1.
PIRDEBY4. S61605.
RefSeqNP_011258.2. NM_001181122.1.

3D structure databases

ProteinModelPortalP10127.
SMRP10127. Positions 5-380.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4812N.
IntActP10127. 11 interactions.
MINTMINT-475922.
STRINGP10127.

Proteomic databases

PeptideAtlasP10127.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL256W; YGL256W; YGL256W.
GeneID852636.
KEGGsce:YGL256W.
NMPDRfig|4932.3.peg.2361.

Organism-specific databases

CYGDYGL256w.
SGDS000003225. ADH4.

Phylogenomic databases

eggNOGfuNOG07707.
GeneTreeEFGT00050000001042.
HOGENOMHBG742415.
OMASAHDNAK.
OrthoDBEOG4SXRN9.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11725.

Gene expression databases

ArrayExpressP10127.
GenevestigatorP10127.
GermOnlineYGL256W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR001670. ADH_Fe.
IPR018211. ADH_Fe_CS.
[Graphical view]
KOK13954.
PfamPF00465. Fe-ADH. 1 hit.
[Graphical view]
PROSITEPS00913. ADH_IRON_1. 1 hit.
PS00060. ADH_IRON_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADH4_YEAST
AccessionPrimary (citable) accession number: P10127
Secondary accession number(s): D6VV79
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 22, 2008
Last modified: November 16, 2011
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

SIMILARITY comments

Index of protein domains and families