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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
 
 
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