ID   BUTA_STAAS              Reviewed;         258 AA.
AC   Q6GCZ8;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-NOV-2008, entry version 26.
DE   RecName: Full=Acetoin(diacetyl) reductase;
DE            Short=AR;
DE            EC=1.1.1.5;
DE   AltName: Full=Acetoin dehydrogenase;
DE   AltName: Full=Meso-2,3-butanediol dehydrogenase;
GN   Name=butA; OrderedLocusNames=SAS0101;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Catalyzes the reversible reduction of acetoin to 2,3-
CC       butanediol in the presence of NADH (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acetoin + NAD(+) = diacetyl + NADH.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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DR   EMBL; BX571857; CAG41868.1; -; Genomic_DNA.
DR   RefSeq; YP_042225.1; -.
DR   GeneID; 2862349; -.
DR   GenomeReviews; BX571857_GR; SAS0101.
DR   KEGG; sas:SAS0101; -.
DR   HOGENOM; Q6GCZ8; -.
DR   BioCyc; SAUR282459:SAS0101-MON; -.
DR   GO; GO:0019152; F:acetoin dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0045150; P:acetoin catabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR014007; 23BDH.
DR   InterPro; IPR002198; DHase_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DHase.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR19410; ADH_short_C2; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   TIGRFAMs; TIGR02415; 23BDH; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    258       Acetoin(diacetyl) reductase.
FT                                /FTId=PRO_0000054543.
FT   NP_BIND       8     32       NAD (By similarity).
FT   ACT_SITE    154    154       Proton acceptor (By similarity).
FT   ACT_SITE    158    158       By similarity.
FT   BINDING     141    141       Substrate (By similarity).
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
//