ID   IDNO_ECOL6              Reviewed;         254 AA.
AC   P0A9Q0; P39345;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=5-keto-D-gluconate 5-reductase {ECO:0000250|UniProtKB:P0A9P9};
DE            EC=1.1.1.69 {ECO:0000250|UniProtKB:P0A9P9};
GN   Name=idnO {ECO:0000312|EMBL:AAN83789.1}; OrderedLocusNames=c5367;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the reduction of 5-keto-D-gluconate to D-gluconate,
CC       using either NADH or NADPH. Is likely involved in an L-idonate
CC       degradation pathway that allows E.coli to utilize L-idonate as the sole
CC       carbon and energy source. Is also able to catalyze the reverse reaction
CC       in vitro, but the D-gluconate oxidation by the enzyme can only proceed
CC       with NAD. {ECO:0000250|UniProtKB:P0A9P9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-gluconate + NAD(+) = 5-dehydro-D-gluconate + H(+) + NADH;
CC         Xref=Rhea:RHEA:23940, ChEBI:CHEBI:15378, ChEBI:CHEBI:18391,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58143; EC=1.1.1.69;
CC         Evidence={ECO:0000250|UniProtKB:P0A9P9};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-gluconate + NADP(+) = 5-dehydro-D-gluconate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:23936, ChEBI:CHEBI:15378, ChEBI:CHEBI:18391,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58143, ChEBI:CHEBI:58349; EC=1.1.1.69;
CC         Evidence={ECO:0000250|UniProtKB:P0A9P9};
CC   -!- PATHWAY: Carbohydrate acid metabolism; L-idonate degradation.
CC       {ECO:0000250|UniProtKB:P0A9P9}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN83789.1; -; Genomic_DNA.
DR   RefSeq; WP_000998695.1; NC_004431.1.
DR   AlphaFoldDB; P0A9Q0; -.
DR   SMR; P0A9Q0; -.
DR   STRING; 199310.c5367; -.
DR   EnsemblBacteria; AAN83789; AAN83789; c5367.
DR   KEGG; ecc:c5367; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_1_1_6; -.
DR   OMA; FPQWGAY; -.
DR   BioCyc; ECOL199310:C5367-MON; -.
DR   UniPathway; UPA00793; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0008874; F:gluconate 5-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046183; P:L-idonate catabolic process; IEA:UniProtKB-UniPathway.
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   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; NAD; NADP; Oxidoreductase.
FT   CHAIN           1..254
FT                   /note="5-keto-D-gluconate 5-reductase"
FT                   /id="PRO_0000054703"
FT   ACT_SITE        158
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         13..37
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   254 AA;  27563 MW;  C5AA4A044CEC1E6E CRC64;
     MNDLFSLAGK NILITGSAQG IGFLLATGLG KYGAQIIIND ITAERAELAV EKLHQEGIQA
     VAAPFNVTHK HEIDAAVEHI EKDIGPIDVL VNNAGIQRRH PFTEFPEQEW NDVIAVNQTA
     VFLVSQAVTR HMVERKAGKV INICSMQSEL GRDTITPYAA SKGAVKMLTR GMCVELARHN
     IQVNGIAPGY FKTEMTKALV EDEAFTAWLC KRTPAARWGD PQELIGAAVF LSSKASDFVN
     GHLLFVDGGM LVAV