ADH2_YEAST
ID ADH2_YEAST Reviewed; 348 AA.
AC P00331; D6W0D0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Alcohol dehydrogenase 2;
DE EC=1.1.1.1;
DE AltName: Full=Alcohol dehydrogenase II;
DE AltName: Full=YADH-2;
GN Name=ADH2; Synonyms=ADR2; OrderedLocusNames=YMR303C; ORFNames=YM9952.05C;
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].
RX PubMed=6337160; DOI=10.1016/s0021-9258(18)32979-x;
RA Russell D.W., Smith M., Williamson V.M., Young E.T.;
RT "Nucleotide sequence of the yeast alcohol dehydrogenase II gene.";
RL J. Biol. Chem. 258:2674-2682(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6279086; DOI=10.1007/978-1-4684-4142-0_26;
RA Young E.T., Williamson V.M., Taguchi A., Smith M., Sledziewski A.,
RA Russell D.W., Osterman J., Denis C., Cox D., Beier D.;
RT "The alcohol dehydrogenase genes of the yeast, Saccharomyces cerevisiae:
RT isolation, structure, and regulation.";
RL Basic Life Sci. 19:335-361(1982).
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 PROTEIN SEQUENCE OF 193-207 AND 227-234.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
RN [6]
RP ACETYLATION AT SER-2.
RX PubMed=9298649; DOI=10.1002/elps.1150180810;
RA Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
RA Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R.,
RA Payne W.E.;
RT "Proteome studies of Saccharomyces cerevisiae: identification and
RT characterization of abundant proteins.";
RL Electrophoresis 18:1347-1360(1997).
RN [7]
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 [8]
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 -!- FUNCTION: This isozyme preferentially catalyzes the conversion of
CC ethanol to acetaldehyde. Acts on a variety of primary unbranched
CC aliphatic alcohols.
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: Cytoplasm.
CC -!- INDUCTION: Repressed by glucose.
CC -!- MISCELLANEOUS: Present with 1620 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; J01314; AAA34408.1; -; Genomic_DNA.
DR EMBL; M38457; AAA34411.1; -; Genomic_DNA.
DR EMBL; Z49212; CAA89136.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10204.1; -; Genomic_DNA.
DR PIR; A00340; DEBYA2.
DR RefSeq; NP_014032.1; NM_001182812.1.
DR AlphaFoldDB; P00331; -.
DR SMR; P00331; -.
DR BioGRID; 35483; 80.
DR DIP; DIP-1181N; -.
DR IntAct; P00331; 20.
DR MINT; P00331; -.
DR STRING; 4932.YMR303C; -.
DR CarbonylDB; P00331; -.
DR iPTMnet; P00331; -.
DR MaxQB; P00331; -.
DR PaxDb; P00331; -.
DR PRIDE; P00331; -.
DR EnsemblFungi; YMR303C_mRNA; YMR303C; YMR303C.
DR GeneID; 855349; -.
DR KEGG; sce:YMR303C; -.
DR SGD; S000004918; ADH2.
DR VEuPathDB; FungiDB:YMR303C; -.
DR eggNOG; KOG0023; Eukaryota.
DR GeneTree; ENSGT00940000171159; -.
DR HOGENOM; CLU_026673_20_1_1; -.
DR InParanoid; P00331; -.
DR OMA; ARPFNQA; -.
DR BioCyc; MetaCyc:YMR303C-MON; -.
DR BioCyc; YEAST:YMR303C-MON; -.
DR BRENDA; 1.1.1.1; 984.
DR PRO; PR:P00331; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P00331; protein.
DR GO; GO:0005737; C:cytoplasm; 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:0006067; P:ethanol metabolic process; IDA: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 Acetylation; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Metal-binding; NAD; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298649"
FT CHAIN 2..348
FT /note="Alcohol dehydrogenase 2"
FT /id="PRO_0000160731"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 178..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 269..271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:9298649"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00330"
FT MOD_RES 223
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00330"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00330"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00330"
FT CROSSLNK 226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P00330"
FT CROSSLNK 234
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P00330"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P00330"
FT CROSSLNK 319
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P00330"
FT CONFLICT 16
FT /note="N -> H (in Ref. 2; AAA34411)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="P -> A (in Ref. 2; AAA34411)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="V -> K (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 36732 MW; 54535FC3258B10EA CRC64;
MSIPETQKAI IFYESNGKLE HKDIPVPKPK PNELLINVKY SGVCHTDLHA WHGDWPLPTK
LPLVGGHEGA GVVVGMGENV KGWKIGDYAG IKWLNGSCMA CEYCELGNES NCPHADLSGY
THDGSFQEYA TADAVQAAHI PQGTDLAEVA PILCAGITVY KALKSANLRA GHWAAISGAA
GGLGSLAVQY AKAMGYRVLG IDGGPGKEEL FTSLGGEVFI DFTKEKDIVS AVVKATNGGA
HGIINVSVSE AAIEASTRYC RANGTVVLVG LPAGAKCSSD VFNHVVKSIS IVGSYVGNRA
DTREALDFFA RGLVKSPIKV VGLSSLPEIY EKMEKGQIAG RYVVDTSK
