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   16-JUN-2009, entry version 30.
DE   RecName: Full=Gluconate 5-dehydrogenase;
DE            EC=1.1.1.69;
DE   AltName: Full=5-keto-D-gluconate 5-reductase;
GN   Name=idnO; OrderedLocusNames=c5367;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes a reversible reduction of 5-ketoglutanate to
CC       form D-gluconate. Dependent on NADP, almost inactive with NAD (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: D-gluconate + NAD(P)(+) = 5-dehydro-D-
CC       gluconate + NAD(P)H.
CC   -!- PATHWAY: Carbohydrate acid metabolism; L-idonic acid degradation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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DR   EMBL; AE014075; AAN83789.1; -; Genomic_DNA.
DR   RefSeq; NP_757215.1; -.
DR   HSSP; P25529; 1AHH.
DR   GeneID; 1037302; -.
DR   GenomeReviews; AE014075_GR; c5367.
DR   KEGG; ecc:c5367; -.
DR   HOGENOM; P0A9Q0; -.
DR   OMA; P0A9Q0; RYMIKRQ.
DR   BRENDA; 1.1.1.69; 292881.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0008874; F:gluconate 5-dehydrogenase activity; IEA:EC.
DR   GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Gluconate utilization; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    254       Gluconate 5-dehydrogenase.
FT                                /FTId=PRO_0000054703.
FT   NP_BIND      13     37       NADP (By similarity).
FT   ACT_SITE    158    158       Proton acceptor (By similarity).
FT   BINDING     145    145       Substrate (By similarity).
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
//