BDH1_YEAST
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 03-AUG-2022, entry version 179.
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; 51.
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; P39714; -.
DR PRIDE; P39714; -.
DR EnsemblFungi; YAL060W_mRNA; YAL060W; YAL060W.
DR GeneID; 851239; -.
DR KEGG; sce:YAL060W; -.
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; FMGHEFS; -.
DR BioCyc; MetaCyc:YAL060W-MON; -.
DR BioCyc; YEAST:YAL060W-MON; -.
DR BRENDA; 1.1.1.303; 984.
DR BRENDA; 1.1.1.4; 984.
DR SABIO-RK; P39714; -.
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 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 Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 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
