ID   ADH4_YEAS7              Reviewed;         382 AA.
AC   A6ZTT5;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Alcohol dehydrogenase 4;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase IV;
DE            Short=ADHIV;
GN   Name=ADH4; Synonyms=ZRG5; ORFNames=SCY_1818;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Reduces acetaldehyde to ethanol during glucose fermentation.
CC       Specific for ethanol. Shows drastically reduced activity towards
CC       primary alcohols from 4 carbon atoms upward. Isomers of aliphatic
CC       alcohol, as well as secondary alcohols and glycerol are not used at all
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC         Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC         Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC         ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Zinc. May bind iron when zinc levels are limiting. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- INDUCTION: Induced by transcription factor ZAP1 in response to zinc
CC       deficiency. {ECO:0000250}.
CC   -!- MISCELLANEOUS: While ADH4 is expressed at only low levels in laboratory
CC       strains, it is often highly expressed in brewing strains.
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDN61873.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AAFW02000099; EDN61873.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A6ZTT5; -.
DR   SMR; A6ZTT5; -.
DR   EnsemblFungi; EDN61873; EDN61873; SCY_1818.
DR   HOGENOM; CLU_007207_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR018211; ADH_Fe_CS.
DR   InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR   PANTHER; PTHR11496; PTHR11496; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   PROSITE; PS00913; ADH_IRON_1; 1.
DR   PROSITE; PS00060; ADH_IRON_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Mitochondrion; NAD; Oxidoreductase; Zinc.
FT   CHAIN           1..382
FT                   /note="Alcohol dehydrogenase 4"
FT                   /id="PRO_0000345089"
SQ   SEQUENCE   382 AA;  41084 MW;  AC6E77B78D6B9AA8 CRC64;
     MSSVTGFYIP PISFFGEGAL EETADYIKNK DYKKALIVTD PGIAAIGLSG RVQKMLEERG
     LNVAIYDKTQ PNPNIANVTA GLKVLKEQNS EIVVSIGGGS AHDNAKAIAL LATNGGEIGD
     YEGVNQSKKA ALPLFAINTT AGTASEMTRF TIISNEEKKI KMAIIDNNVT PAVAVNDPST
     MFGLPPALTA ATGLDALTHC IEAYVSTASN PITDACALKG IDLINESLVA AYKDGKDKKA
     RTDMCYAEYL AGMAFNNASL GYVHALAHQL GGFYHLPHGV CNAVLLPHVQ EANMQCPKAK
     KRLGEIALHF GASQEDPEET IKALHVLNRT MNIPRNLKEL GVKTEDFEIL AEHAMHDACH
     LTNPVQFTKE QVVAIIKKAY EY