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Protein

Alcohol dehydrogenase 4

Gene

ADH4

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

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.1 Publication

Catalytic activityi

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

Cofactori

Zn2+1 Publication, Fe2+1 PublicationNote: Zinc. May bind iron when zinc levels are limiting.1 Publication

Enzyme regulationi

Inhibited by EDTA.1 Publication

Kineticsi

  1. KM=59 mM for NAD1 Publication
  2. KM=122 µM for NADH1 Publication
  3. KM=2.83 mM for acetaldehyde1 Publication
  4. KM=16.7 mM for ethanol1 Publication

    pH dependencei

    Optimum pH is 8.3.1 Publication

    GO - Molecular functioni

    • alcohol dehydrogenase (NAD) activity Source: SGD
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    • amino acid catabolic process to alcohol via Ehrlich pathway Source: SGD
    • fermentation Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:YGL256W-MONOMER.
    YEAST:YGL256W-MONOMER.
    ReactomeiR-SCE-880009. Interconversion of 2-oxoglutarate and 2-hydroxyglutarate.
    SABIO-RKP10127.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alcohol dehydrogenase 4 (EC:1.1.1.1)
    Alternative name(s):
    Alcohol dehydrogenase IV
    Short name:
    ADHIV
    Gene namesi
    Name:ADH4
    Synonyms:ZRG5
    Ordered Locus Names:YGL256W
    ORF Names:NRC465
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome VII

    Organism-specific databases

    EuPathDBiFungiDB:YGL256W.
    SGDiS000003225. ADH4.

    Subcellular locationi

    GO - Cellular componenti

    • mitochondrion Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 382382Alcohol dehydrogenase 4PRO_0000087817Add
    BLAST

    Proteomic databases

    MaxQBiP10127.
    PeptideAtlasiP10127.

    Expressioni

    Inductioni

    Induced by transcription factor ZAP1 in response to zinc deficiency.5 Publications

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi33023. 58 interactions.
    DIPiDIP-4812N.
    IntActiP10127. 3 interactions.
    MINTiMINT-475922.

    Structurei

    3D structure databases

    ProteinModelPortaliP10127.
    SMRiP10127. Positions 7-380.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    GeneTreeiENSGT00390000003849.
    HOGENOMiHOG000243333.
    InParanoidiP10127.
    KOiK13954.
    OMAiNDGRKLG.
    OrthoDBiEOG7B31Z9.

    Family and domain databases

    InterProiIPR001670. ADH_Fe.
    IPR018211. ADH_Fe_CS.
    [Graphical view]
    PfamiPF00465. Fe-ADH. 1 hit.
    [Graphical view]
    PROSITEiPS00913. ADH_IRON_1. 1 hit.
    PS00060. ADH_IRON_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P10127-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSSVTGFYIP PISFFGEGAL EETADYIKNK DYKKALIVTD PGIAAIGLSG
    60 70 80 90 100
    RVQKMLEERD LNVAIYDKTQ PNPNIANVTA GLKVLKEQNS EIVVSIGGGS
    110 120 130 140 150
    AHDNAKAIAL LATNGGEIGD YEGVNQSKKA ALPLFAINTT AGTASEMTRF
    160 170 180 190 200
    TIISNEEKKI KMAIIDNNVT PAVAVNDPST MFGLPPALTA ATGLDALTHC
    210 220 230 240 250
    IEAYVSTASN PITDACALKG IDLINESLVA AYKDGKDKKA RTDMCYAEYL
    260 270 280 290 300
    AGMAFNNASL GYVHALAHQL GGFYHLPHGV CNAVLLPHVQ EANMQCPKAK
    310 320 330 340 350
    KRLGEIALHF GASQEDPEET IKALHVLNRT MNIPRNLKEL GVKTEDFEIL
    360 370 380
    AEHAMHDACH LTNPVQFTKE QVVAIIKKAY EY
    Length:382
    Mass (Da):41,142
    Last modified:July 22, 2008 - v3
    Checksum:i7DFFD43830FB269B
    GO

    Sequence cautioni

    The sequence CAA64131.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence CAA96976.1 differs from that shown. Reason: Erroneous initiation. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti60 – 601D → G in CAA29410 (PubMed:2823079).Curated
    Sequence conflicti88 – 881Q → E in CAA29410 (PubMed:2823079).Curated
    Sequence conflicti310 – 3101F → C in CAA29410 (PubMed:2823079).Curated
    Sequence conflicti339 – 3391E → D in CAA29410 (PubMed:2823079).Curated
    Sequence conflicti348 – 3481E → D in CAA29410 (PubMed:2823079).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    PIRiS61605. DEBY4.
    RefSeqiNP_011258.2. NM_001181122.1.

    Genome annotation databases

    EnsemblFungiiYGL256W; YGL256W; YGL256W.
    GeneIDi852636.
    KEGGisce:YGL256W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    PIRiS61605. DEBY4.
    RefSeqiNP_011258.2. NM_001181122.1.

    3D structure databases

    ProteinModelPortaliP10127.
    SMRiP10127. Positions 7-380.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi33023. 58 interactions.
    DIPiDIP-4812N.
    IntActiP10127. 3 interactions.
    MINTiMINT-475922.

    Proteomic databases

    MaxQBiP10127.
    PeptideAtlasiP10127.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYGL256W; YGL256W; YGL256W.
    GeneIDi852636.
    KEGGisce:YGL256W.

    Organism-specific databases

    EuPathDBiFungiDB:YGL256W.
    SGDiS000003225. ADH4.

    Phylogenomic databases

    GeneTreeiENSGT00390000003849.
    HOGENOMiHOG000243333.
    InParanoidiP10127.
    KOiK13954.
    OMAiNDGRKLG.
    OrthoDBiEOG7B31Z9.

    Enzyme and pathway databases

    BioCyciMetaCyc:YGL256W-MONOMER.
    YEAST:YGL256W-MONOMER.
    ReactomeiR-SCE-880009. Interconversion of 2-oxoglutarate and 2-hydroxyglutarate.
    SABIO-RKP10127.

    Miscellaneous databases

    NextBioi971879.
    PROiP10127.

    Family and domain databases

    InterProiIPR001670. ADH_Fe.
    IPR018211. ADH_Fe_CS.
    [Graphical view]
    PfamiPF00465. Fe-ADH. 1 hit.
    [Graphical view]
    PROSITEiPS00913. ADH_IRON_1. 1 hit.
    PS00060. ADH_IRON_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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] [Europe PMC] [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] [Europe PMC] [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.
      , 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: INDUCTION, IDENTIFICATION OF PROBABLE INITIATION SITE.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.

    Entry informationi

    Entry nameiADH4_YEAST
    AccessioniPrimary (citable) accession number: P10127
    Secondary accession number(s): D6VV79
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 22, 2008
    Last modified: May 11, 2016
    This is version 140 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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