ID   BUTA_STAAM              Reviewed;         258 AA.
AC   P66775; Q99X89;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=SAV0126;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000017; BAB56288.1; -; Genomic_DNA.
DR   RefSeq; WP_000183771.1; NC_002758.2.
DR   AlphaFoldDB; P66775; -.
DR   SMR; P66775; -.
DR   PaxDb; P66775; -.
DR   EnsemblBacteria; BAB56288; BAB56288; SAV0126.
DR   KEGG; sav:SAV0126; -.
DR   HOGENOM; CLU_010194_1_0_9; -.
DR   OMA; VYLCCKA; -.
DR   PhylomeDB; P66775; -.
DR   BioCyc; SAUR158878:SAV_RS00770-MON; -.
DR   Proteomes; UP000002481; 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_0000054540"
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