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Alcohol dehydrogenase 4 (EC 1.1.1.1) (Alcohol dehydrogenase IV) (ADHIV)

 ADH4_YEAS7              Reviewed;         382 AA.
A6ZTT5;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 2.
22-NOV-2017, entry version 39.
RecName: Full=Alcohol dehydrogenase 4;
EC=1.1.1.1;
AltName: Full=Alcohol dehydrogenase IV;
Short=ADHIV;
Name=ADH4; Synonyms=ZRG5; ORFNames=SCY_1818;
Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=307796;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=YJM789;
PubMed=17652520; DOI=10.1073/pnas.0701291104;
Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R.,
Wang X., Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S.,
Li Y., Davis R.W., Steinmetz L.M.;
"Genome sequencing and comparative analysis of Saccharomyces
cerevisiae strain YJM789.";
Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
-!- 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 (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: A primary alcohol + NAD(+) = an aldehyde +
NADH.
-!- CATALYTIC ACTIVITY: A secondary alcohol + NAD(+) = a ketone +
NADH.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
Note=Zinc. May bind iron when zinc levels are limiting.
{ECO:0000250};
-!- ENZYME REGULATION: Inhibited by EDTA. {ECO:0000250}.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
-!- INDUCTION: Induced by transcription factor ZAP1 in response to
zinc deficiency. {ECO:0000250}.
-!- MISCELLANEOUS: While ADH4 is expressed at only low levels in
laboratory strains, it is often highly expressed in brewing
strains.
-!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=EDN61873.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AAFW02000099; EDN61873.1; ALT_INIT; Genomic_DNA.
ProteinModelPortal; A6ZTT5; -.
SMR; A6ZTT5; -.
PRIDE; A6ZTT5; -.
EnsemblFungi; EDN61873; EDN61873; SCY_1818.
OrthoDB; EOG092C28AS; -.
Proteomes; UP000007060; Unassembled WGS sequence.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
InterPro; IPR001670; ADH_Fe/gldA.
InterPro; IPR018211; ADH_Fe_CS.
Pfam; PF00465; Fe-ADH; 1.
PROSITE; PS00913; ADH_IRON_1; 1.
PROSITE; PS00060; ADH_IRON_2; 1.
3: Inferred from homology;
Complete proteome; Metal-binding; Mitochondrion; NAD; Oxidoreductase;
Zinc.
CHAIN 1 382 Alcohol dehydrogenase 4.
/FTId=PRO_0000345089.
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


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