ADH3_YEAST
ID ADH3_YEAST Reviewed; 375 AA.
AC P07246; D6VZQ6;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Alcohol dehydrogenase 3, mitochondrial;
DE EC=1.1.1.1;
DE AltName: Full=Alcohol dehydrogenase III;
DE AltName: Full=YADH-3;
DE Flags: Precursor;
GN Name=ADH3; OrderedLocusNames=YMR083W; ORFNames=YM9582.08;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Pilgrim D., Ciriacy M.;
RL Submitted (OCT-1985) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2943982; DOI=10.1128/mcb.5.11.3024-3034.1985;
RA Young E.T., Pilgrim D.;
RT "Isolation and DNA sequence of ADH3, a nuclear gene encoding the
RT mitochondrial isozyme of alcohol dehydrogenase in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 5:3024-3034(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP REVIEW.
RX PubMed=12702265; DOI=10.1111/j.1567-1364.2002.tb00116.x;
RA Leskovac V., Trivic S., Pericin D.;
RT "The three zinc-containing alcohol dehydrogenases from baker's yeast,
RT Saccharomyces cerevisiae.";
RL FEMS Yeast Res. 2:481-494(2002).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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 Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- MISCELLANEOUS: Present with 11600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; K03292; AAA34409.1; -; Genomic_DNA.
DR EMBL; Z49259; CAA89229.1; -; Genomic_DNA.
DR EMBL; AY692988; AAT93007.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09980.1; -; Genomic_DNA.
DR PIR; S54458; S54458.
DR RefSeq; NP_013800.1; NM_001182582.1.
DR AlphaFoldDB; P07246; -.
DR SMR; P07246; -.
DR BioGRID; 35258; 176.
DR DIP; DIP-4445N; -.
DR IntAct; P07246; 25.
DR MINT; P07246; -.
DR STRING; 4932.YMR083W; -.
DR CarbonylDB; P07246; -.
DR iPTMnet; P07246; -.
DR MaxQB; P07246; -.
DR PaxDb; P07246; -.
DR PRIDE; P07246; -.
DR EnsemblFungi; YMR083W_mRNA; YMR083W; YMR083W.
DR GeneID; 855107; -.
DR KEGG; sce:YMR083W; -.
DR SGD; S000004688; ADH3.
DR VEuPathDB; FungiDB:YMR083W; -.
DR eggNOG; KOG0023; Eukaryota.
DR GeneTree; ENSGT00940000171159; -.
DR HOGENOM; CLU_026673_20_1_1; -.
DR InParanoid; P07246; -.
DR OMA; GLKMTDT; -.
DR BioCyc; MetaCyc:YMR083W-MON; -.
DR BioCyc; YEAST:YMR083W-MON; -.
DR PRO; PR:P07246; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P07246; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000947; P:amino acid catabolic process to alcohol via Ehrlich pathway; IGI:SGD.
DR GO; GO:0006116; P:NADH oxidation; IDA:SGD.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW Transit peptide; Zinc.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT CHAIN 28..375
FT /note="Alcohol dehydrogenase 3, mitochondrial"
FT /id="PRO_0000000879"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 205..211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 296..298
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 10
FT /note="R -> K (in Ref. 1; AAA34409)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="K -> N (in Ref. 1; AAA34409)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 40370 MW; AB849BC4E9D4EB8A CRC64;
MLRTSTLFTR RVQPSLFSRN ILRLQSTAAI PKTQKGVIFY ENKGKLHYKD IPVPEPKPNE
ILINVKYSGV CHTDLHAWHG DWPLPVKLPL VGGHEGAGVV VKLGSNVKGW KVGDLAGIKW
LNGSCMTCEF CESGHESNCP DADLSGYTHD GSFQQFATAD AIQAAKIQQG TDLAEVAPIL
CAGVTVYKAL KEADLKAGDW VAISGAAGGL GSLAVQYATA MGYRVLGIDA GEEKEKLFKK
LGGEVFIDFT KTKNMVSDIQ EATKGGPHGV INVSVSEAAI SLSTEYVRPC GTVVLVGLPA
NAYVKSEVFS HVVKSINIKG SYVGNRADTR EALDFFSRGL IKSPIKIVGL SELPKVYDLM
EKGKILGRYV VDTSK
