ID   BDH1_YEAST              Reviewed;         382 AA.
AC   P39714; D6VPF9; E9P8Z3;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=(R,R)-butanediol dehydrogenase;
DE            EC=1.1.1.4;
GN   Name=BDH1; Synonyms=BDH; OrderedLocusNames=YAL060W; ORFNames=FUN49;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA   Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA   Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA   Storms R.K.;
RT   "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 322.
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   [3]
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   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 90845 / FY834;
RX   PubMed=10938079; DOI=10.1074/jbc.m003035200;
RA   Gonzalez E., Fernandez M.R., Larroy C., Sola L., Pericas M.A., Pares X.,
RA   Biosca J.A.;
RT   "Characterization of a (2R,3R)-2,3-butanediol dehydrogenase as the
RT   Saccharomyces cerevisiae YAL060W gene product. Disruption and induction of
RT   the gene.";
RL   J. Biol. Chem. 275:35876-35885(2000).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
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).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: NAD-dependent (R,R)-butanediol dehydrogenase which catalyzes
CC       oxidation of (R,R)-butane-2,3-diol to (3R)-acetoin, of meso-butanediol
CC       to (3S)-acetoin, and reduction of acetoin. Allows the use of 2,3-
CC       butanediol as an aerobic carbon source. {ECO:0000269|PubMed:10938079}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R,R)-butane-2,3-diol + NAD(+) = (R)-acetoin + H(+) + NADH;
CC         Xref=Rhea:RHEA:24340, ChEBI:CHEBI:15378, ChEBI:CHEBI:15686,
CC         ChEBI:CHEBI:16982, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.4;
CC         Evidence={ECO:0000269|PubMed:10938079};
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=14 mM for (R,R)-butane-2,3-diol {ECO:0000269|PubMed:10938079};
CC         KM=65 mM for meso-butanediol {ECO:0000269|PubMed:10938079};
CC         KM=57 mM for 1,2-Butanediol {ECO:0000269|PubMed:10938079};
CC         KM=4.5 mM for (3R/3S)-acetoin {ECO:0000269|PubMed:10938079};
CC         KM=0.55 mM for NAD {ECO:0000269|PubMed:10938079};
CC         KM=0.055 mM for NADH {ECO:0000269|PubMed:10938079};
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 8730 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; U12980; AAC04974.1; -; Genomic_DNA.
DR   EMBL; AY692922; AAT92941.1; -; Genomic_DNA.
DR   EMBL; BK006935; DAA06929.2; -; Genomic_DNA.
DR   PIR; S51962; S51962.
DR   RefSeq; NP_009341.2; NM_001178202.2.
DR   AlphaFoldDB; P39714; -.
DR   SMR; P39714; -.
DR   BioGRID; 31770; 52.
DR   DIP; DIP-5356N; -.
DR   IntAct; P39714; 1.
DR   MINT; P39714; -.
DR   STRING; 4932.YAL060W; -.
DR   CarbonylDB; P39714; -.
DR   iPTMnet; P39714; -.
DR   MaxQB; P39714; -.
DR   PaxDb; 4932-YAL060W; -.
DR   PeptideAtlas; P39714; -.
DR   EnsemblFungi; YAL060W_mRNA; YAL060W; YAL060W.
DR   GeneID; 851239; -.
DR   KEGG; sce:YAL060W; -.
DR   AGR; SGD:S000000056; -.
DR   SGD; S000000056; BDH1.
DR   VEuPathDB; FungiDB:YAL060W; -.
DR   eggNOG; KOG0024; Eukaryota.
DR   GeneTree; ENSGT00940000176805; -.
DR   HOGENOM; CLU_026673_11_0_1; -.
DR   InParanoid; P39714; -.
DR   OMA; AMGHEMS; -.
DR   OrthoDB; 1692576at2759; -.
DR   BioCyc; MetaCyc:YAL060W-MONOMER; -.
DR   BioCyc; YEAST:YAL060W-MONOMER; -.
DR   BRENDA; 1.1.1.303; 984.
DR   BRENDA; 1.1.1.4; 984.
DR   SABIO-RK; P39714; -.
DR   BioGRID-ORCS; 851239; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P39714; -.
DR   Proteomes; UP000002311; Chromosome I.
DR   RNAct; P39714; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0000721; F:(R,R)-butanediol dehydrogenase activity; IDA:SGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006066; P:alcohol metabolic process; IMP:SGD.
DR   GO; GO:0034079; P:butanediol biosynthetic process; IMP:SGD.
DR   CDD; cd08233; butanediol_DH_like; 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   PANTHER; PTHR43161:SF23; (R,R)-BUTANEDIOL DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Metal-binding; NAD; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Zinc.
FT   CHAIN           1..382
FT                   /note="(R,R)-butanediol dehydrogenase"
FT                   /id="PRO_0000160788"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         63
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        322
FT                   /note="D -> A (in Ref. 1; AAC04974)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   382 AA;  41582 MW;  1776FA5968EC1A12 CRC64;
     MRALAYFKKG DIHFTNDIPR PEIQTDDEVI IDVSWCGICG SDLHEYLDGP IFMPKDGECH
     KLSNAALPLA MGHEMSGIVS KVGPKVTKVK VGDHVVVDAA SSCADLHCWP HSKFYNSKPC
     DACQRGSENL CTHAGFVGLG VISGGFAEQV VVSQHHIIPV PKEIPLDVAA LVEPLSVTWH
     AVKISGFKKG SSALVLGAGP IGLCTILVLK GMGASKIVVS EIAERRIEMA KKLGVEVFNP
     SKHGHKSIEI LRGLTKSHDG FDYSYDCSGI QVTFETSLKA LTFKGTATNI AVWGPKPVPF
     QPMDVTLQEK VMTGSIGYVV EDFEEVVRAI HNGDIAMEDC KQLITGKQRI EDGWEKGFQE
     LMDHKESNVK ILLTPNNHGE MK
//