BDH2_YEAST
ID BDH2_YEAST Reviewed; 417 AA.
AC P39713; D6VPF8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Probable diacetyl reductase [(R)-acetoin forming] 2;
DE EC=1.1.1.303;
GN Name=BDH2; OrderedLocusNames=YAL061W; ORFNames=FUN50;
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.
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 INDUCTION.
RX PubMed=11470516; DOI=10.1016/s0378-1119(01)00558-3;
RA do Valle Matta M.A., Jonniaux J.-L., Balzi E., Goffeau A.,
RA van den Hazel B.;
RT "Novel target genes of the yeast regulator Pdr1p: a contribution of the
RT TPO1 gene in resistance to quinidine and other drugs.";
RL Gene 272:111-119(2001).
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 INDUCTION.
RX PubMed=14871952; DOI=10.1128/ec.3.1.221-231.2004;
RA Kaniak A., Xue Z., Macool D., Kim J.-H., Johnston M.;
RT "Regulatory network connecting two glucose signal transduction pathways in
RT Saccharomyces cerevisiae.";
RL Eukaryot. Cell 3:221-231(2004).
CC -!- FUNCTION: Catalyzes the irreversible reduction of 2,3-butanediol to
CC (S)-acetoin in the presence of NADH. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-acetoin + NAD(+) = diacetyl + H(+) + NADH;
CC Xref=Rhea:RHEA:22900, ChEBI:CHEBI:15378, ChEBI:CHEBI:15686,
CC ChEBI:CHEBI:16583, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.303;
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Expression is controlled by the PDR1 transcription factor
CC and the glucose-responsive transcription factor RGT1.
CC {ECO:0000269|PubMed:11470516, ECO:0000269|PubMed:14871952}.
CC -!- MISCELLANEOUS: Present with 3090 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; AAC04973.1; -; Genomic_DNA.
DR EMBL; AY692730; AAT92749.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06928.1; -; Genomic_DNA.
DR PIR; S51961; S51961.
DR RefSeq; NP_009340.1; NM_001178203.1.
DR AlphaFoldDB; P39713; -.
DR SMR; P39713; -.
DR BioGRID; 31769; 131.
DR DIP; DIP-6734N; -.
DR IntAct; P39713; 2.
DR MINT; P39713; -.
DR STRING; 4932.YAL061W; -.
DR MaxQB; P39713; -.
DR PaxDb; P39713; -.
DR PRIDE; P39713; -.
DR EnsemblFungi; YAL061W_mRNA; YAL061W; YAL061W.
DR GeneID; 851238; -.
DR KEGG; sce:YAL061W; -.
DR SGD; S000000057; BDH2.
DR VEuPathDB; FungiDB:YAL061W; -.
DR eggNOG; KOG0024; Eukaryota.
DR GeneTree; ENSGT00940000176805; -.
DR HOGENOM; CLU_026673_11_0_1; -.
DR InParanoid; P39713; -.
DR OMA; RSAACKV; -.
DR BioCyc; YEAST:G3O-28863-MON; -.
DR PRO; PR:P39713; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39713; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000721; F:(R,R)-butanediol dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0052587; F:diacetyl reductase ((R)-acetoin forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; ISS:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034079; P:butanediol biosynthetic process; IBA:GO_Central.
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; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..417
FT /note="Probable diacetyl reductase [(R)-acetoin forming] 2"
FT /id="PRO_0000160897"
FT REGION 380..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
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:0000250|UniProtKB:P39714"
SQ SEQUENCE 417 AA; 46099 MW; D921CEDBE61D0151 CRC64;
MRALAYFGKG NIRFTNHLKE PHIVAPDELV IDIEWCGICG TDLHEYTDGP IFFPEDGHTH
EISHNPLPQA MGHEMAGTVL EVGPGVKNLK VGDKVVVEPT GTCRDRYRWP LSPNVDKEWC
AACKKGYYNI CSYLGLCGAG VQSGGFAERV VMNESHCYKV PDFVPLDVAA LIQPLAVCWH
AIRVCEFKAG STALIIGAGP IGLGTILALN AAGCKDIVVS EPAKVRRELA EKMGARVYDP
TAHAAKESID YLRSIADGGD GFDYTFDCSG LEVTLNAAIQ CLTFRGTAVN LAMWGHHKIQ
FSPMDITLHE RKYTGSMCYT HHDFEAVIEA LEEGRIDIDR ARHMITGRVN IEDGLDGAIM
KLINEKESTI KIILTPNNHG ELNREADNEK KEISELSSRK DQERLRESIN EAKLRHT
