ID   BUTA_STAAW              Reviewed;         258 AA.
AC   P66776; Q99X89;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=MW0100;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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; BA000033; BAB93965.1; -; Genomic_DNA.
DR   RefSeq; WP_000183771.1; NC_003923.1.
DR   AlphaFoldDB; P66776; -.
DR   SMR; P66776; -.
DR   EnsemblBacteria; BAB93965; BAB93965; BAB93965.
DR   KEGG; sam:MW0100; -.
DR   HOGENOM; CLU_010194_1_0_9; -.
DR   OMA; VYLCCKA; -.
DR   Proteomes; UP000000418; 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_0000054544"
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