ID   BUTA_STAAC              Reviewed;         258 AA.
AC   Q5HJP2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Diacetyl reductase [(S)-acetoin forming];
DE            EC=1.1.1.304;
DE   AltName: Full=Acetoin(diacetyl) reductase;
DE            Short=AR;
DE   AltName: Full=Meso-2,3-butanediol dehydrogenase;
GN   Name=butA; OrderedLocusNames=SACOL0111;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
CC   -!- FUNCTION: Catalyzes the irreversible reduction of 2,3-butanediol to
CC       (S)-acetoin in the presence of NADH. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-acetoin + NAD(+) = diacetyl + H(+) + NADH;
CC         Xref=Rhea:RHEA:27286, ChEBI:CHEBI:15378, ChEBI:CHEBI:15687,
CC         ChEBI:CHEBI:16583, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.304;
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; CP000046; AAW38754.1; -; Genomic_DNA.
DR   RefSeq; WP_000183771.1; NC_002951.2.
DR   AlphaFoldDB; Q5HJP2; -.
DR   SMR; Q5HJP2; -.
DR   EnsemblBacteria; AAW38754; AAW38754; SACOL0111.
DR   KEGG; sac:SACOL0111; -.
DR   HOGENOM; CLU_010194_1_0_9; -.
DR   OMA; VYLCCKA; -.
DR   Proteomes; UP000000530; Chromosome.
DR   GO; GO:0052588; F:diacetyl reductase ((S)-acetoin forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0045150; P:acetoin catabolic process; IEA:InterPro.
DR   InterPro; IPR014007; 23BDH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR02415; 23BDH; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..258
FT                   /note="Diacetyl reductase [(S)-acetoin forming]"
FT                   /id="PRO_0000054539"
FT   ACT_SITE        154
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   ACT_SITE        158
FT                   /evidence="ECO:0000250"
FT   BINDING         8..32
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   258 AA;  27216 MW;  114AFD0DC5D780CF CRC64;
     MTNNKVALVT GGAQGIGFKI AERLVEDGFK VAVVDFNEEG AKAAALKLSS DGTKAIAIKA
     DVSNRDDVFN AVRQTAAQFG DFHVMVNNAG LGPTTPIDTI TEEQFKTVYG VNVAGVLWGI
     QAAHEQFKKF NHGGKIINAT SQAGVEGNPG LSLYCSTKFA VRGLTQVAAQ DLASEGITVN
     AFAPGIVQTP MMESIAVATA EEAGKPEAWG WEQFTSQIAL GRVSQPEDVS NVVSFLAGKD
     SDYITGQTII VDGGMRFR