BUDC_KLEPN
ID BUDC_KLEPN Reviewed; 256 AA.
AC Q48436; Q9R878;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 126.
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 Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IAM 1063;
RA Ui S.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CG21;
RX PubMed=11687934; DOI=10.1038/sj/jim/7000179;
RA Wardwell S.A., Yang Y.T., Chang H.-Y., San K.Y., Rudolph F.B.,
RA Bennett G.N.;
RT "Expression of the Klebsiella pneumoniae CG21 acetoin reductase gene in
RT Clostridium acetobutylicum ATCC 824.";
RL J. Ind. Microbiol. Biotechnol. 27:220-227(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE
RP ANALOG.
RX PubMed=11173520; DOI=10.1093/oxfordjournals.jbchem.a002845;
RA Otagiri M., Kurisu G., Ui S., Takusagawa Y., Ohkuma M., Kudo T.,
RA Kusunoki M.;
RT "Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with
RT NAD+ and inhibitor mercaptoethanol at 1.7 A resolution for understanding of
RT chiral substrate recognition mechanisms.";
RL J. Biochem. 129:205-208(2001).
CC -!- FUNCTION: Catalyzes the reversible reduction of (S)-acetoin to 2,3-
CC butanediol 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. {ECO:0000269|PubMed:11173520}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; D86412; BAA13085.1; -; Genomic_DNA.
DR EMBL; AF098800; AAC78679.1; -; Genomic_DNA.
DR RefSeq; WP_004151179.1; NZ_WYAM01000009.1.
DR PDB; 1GEG; X-ray; 1.70 A; A/B/C/D/E/F/G/H=1-256.
DR PDB; 3WYE; X-ray; 1.58 A; A/B=1-83, A/B=119-134, A/B=162-181, A/B=237-256.
DR PDBsum; 1GEG; -.
DR PDBsum; 3WYE; -.
DR AlphaFoldDB; Q48436; -.
DR SMR; Q48436; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR GeneID; 64294969; -.
DR OrthoDB; 1601931at2; -.
DR BioCyc; MetaCyc:MON-8762; -.
DR BRENDA; 1.1.1.304; 2814.
DR BRENDA; 1.1.1.76; 2814.
DR BRENDA; 1.1.1.B20; 2814.
DR EvolutionaryTrace; Q48436; -.
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 Pfam; PF00106; adh_short; 1.
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 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase.
FT CHAIN 1..256
FT /note="Diacetyl reductase [(S)-acetoin forming]"
FT /id="PRO_0000054537"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT BINDING 6..33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11173520"
FT BINDING 59
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11173520"
FT BINDING 139
FT /ligand="substrate"
FT BINDING 156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:11173520"
FT CONFLICT 52..54
FT /note="RAM -> HAV (in Ref. 1; BAA13085)"
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3WYE"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:3WYE"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:3WYE"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:3WYE"
FT HELIX 36..47
FT /evidence="ECO:0007829|PDB:3WYE"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:3WYE"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:3WYE"
FT HELIX 63..77
FT /evidence="ECO:0007829|PDB:3WYE"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:3WYE"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1GEG"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:1GEG"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:3WYE"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:3WYE"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1GEG"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:3WYE"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:3WYE"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:3WYE"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:1GEG"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:1GEG"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:1GEG"
FT HELIX 224..235
FT /evidence="ECO:0007829|PDB:1GEG"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:3WYE"
FT STRAND 246..254
FT /evidence="ECO:0007829|PDB:3WYE"
SQ SEQUENCE 256 AA; 26642 MW; B250F184C665ACAF CRC64;
MKKVALVTGA GQGIGKAIAL RLVKDGFAVA IADYNDATAK AVASEINQAG GRAMAVKVDV
SDRDQVFAAV EQARKTLGGF DVIVNNAGVA PSTPIESITP EIVDKVYNIN VKGVIWGIQA
AVEAFKKEGH GGKIINACSQ AGHVGNPELA VYSSSKFAVR GLTQTAARDL APLGITVNGY
CPGIVKTPMW AEIDRQVSEA AGKPLGYGTA EFAKRITLGR LSEPEDVAAC VSYLASPDSD
YMTGQSLLID GGMVFN
