ID   BUDC_RAOTE              Reviewed;         241 AA.
AC   Q04520;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=budC;
OS   Raoultella terrigena (Klebsiella terrigena).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Raoultella.
OX   NCBI_TaxID=577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VTT-E-74023;
RX   PubMed=8444801; DOI=10.1128/jb.175.5.1392-1404.1993;
RA   Blomqvist K., Nikkola M., Lehtovaara P., Suihko M.-L., Airaksinen U.,
RA   Straby K.B., Knowles J.K.C., Penttilae M.E.;
RT   "Characterization of the genes of the 2,3-butanediol operons from
RT   Klebsiella terrigena and Enterobacter aerogenes.";
RL   J. Bacteriol. 175:1392-1404(1993).
CC   -!- FUNCTION: Catalyzes the irreversible reduction of 2,3-butanediol to
CC       (S)-acetoin in the presence of NADH.
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   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; L04507; AAA25056.1; -; Genomic_DNA.
DR   PIR; E47069; E47069.
DR   AlphaFoldDB; Q04520; -.
DR   SMR; Q04520; -.
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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   NCBIfam; TIGR02415; 23BDH; 1.
DR   PANTHER; PTHR24321:SF17; DEHYDROGENASE; 1.
DR   PANTHER; PTHR24321; DEHYDROGENASES, SHORT CHAIN; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..241
FT                   /note="Diacetyl reductase [(S)-acetoin forming]"
FT                   /id="PRO_0000054538"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   ACT_SITE        156
FT                   /evidence="ECO:0000250"
FT   BINDING         6..30
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   241 AA;  25313 MW;  D85801C56931BF04 CRC64;
     MQKVALVTGA GQGIGKAIAL RLVKDGFAVA IADYNDATAT AVAAEINQAG GRAVAIKVDV
     SRRDQVFAAV EQARKALGGF NVIVNNAGIA PSTPIESITE EIVDRVYNIN VKGVIWGMQA
     AVEAFKKEGH GGKIVNACSQ AGHVGNPELA VYSSSKFAVR GLTQTAARDL APLGITVNGF
     CPGIVKTPMW AEIDRQCRKR RANRWATARL NLPNASPLAA CRSLKTSPPA CRSSPARIPT
     I
//