ID Q6XQ76_SACBA Unreviewed; 375 AA.
AC Q6XQ76;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN Name=ADH3 {ECO:0000313|EMBL:AAP51044.1};
OS Saccharomyces bayanus (Yeast) (Saccharomyces uvarum x Saccharomyces
OS eubayanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4931 {ECO:0000313|EMBL:AAP51044.1};
RN [1] {ECO:0000313|EMBL:AAP51044.1}
RP NUCLEOTIDE SEQUENCE.
RA Thomson J.M.;
RT "Interpretive Proteomics: Experimental paleogenetics as a tool to analyze
RT function and discover pathways in yeast.";
RL Thesis (2002), University of Florida.
RN [2] {ECO:0000313|EMBL:AAP51044.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15864308; DOI=10.1038/ng1553;
RA Thomson J.M., Gaucher E.A., Burgan M.F., De Kee D.W., Li T., Aris J.P.,
RA Benner S.A.;
RT "Resurrecting ancestral alcohol dehydrogenases from yeast.";
RL Nat. Genet. 37:630-635(2005).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; AY216994; AAP51044.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6XQ76; -.
DR SMR; Q6XQ76; -.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08297; CAD3; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_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 PANTHER; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR42940:SF3; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AAP51044.1}; Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 41..371
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 375 AA; 40329 MW; C5B93C86FC3FA3C6 CRC64;
MLRTSTLFTR RVQPSLFARN ILRLQSTIAI PQTQKGVIFY ENNGKLHYKD IPVPEPKPNE
ILINVKYSGV CHTDLHAWHG DWPLPVKLPL VGGHEGAGVV VKLGSNVKGW KVGDLAGIKW
LNGSCMTCEF CESGHESNCP DADLSGYTHD GSFQQFATAD AIQAAKIQQG TDLAEVAPIL
CAGVTVYKAL KEANLKAGDW VAISGAAGGL GSLAVQYATA MGYRVLGIDA GAEKEKLFKQ
LGGEVFIDFT KTKDMVSDIQ EATKGGPQGV INVSVSEAAI SLSTEYVRPT GTVVLVGLPA
NAYVKSEVFS HVIKSINIKG SYVGNRADTR EALDFFSRGL IKSPIKIVGL SELPMVYDLM
EKGKILGRYV VDTSK
//