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IDNO_ECOLI
ID   IDNO_ECOLI              Reviewed;         254 AA.
AC   P0A9P9; P39345; Q2M643;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=5-keto-D-gluconate 5-reductase {ECO:0000303|PubMed:9658018};
DE            EC=1.1.1.69 {ECO:0000269|PubMed:9658018};
GN   Name=idnO {ECO:0000303|PubMed:9658018}; Synonyms=yjgU;
GN   OrderedLocusNames=b4266, JW4223;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP   INDUCTION.
RC   STRAIN=K12 / ATCC 12435 / DSM 5695 / NBRC 3302 / NCIMB 9481 / W1485;
RX   PubMed=9658018; DOI=10.1128/jb.180.14.3704-3710.1998;
RA   Bausch C., Peekhaus N., Utz C., Blais T., Murray E., Lowary T., Conway T.;
RT   "Sequence analysis of the GntII (subsidiary) system for gluconate
RT   metabolism reveals a novel pathway for L-idonic acid catabolism in
RT   Escherichia coli.";
RL   J. Bacteriol. 180:3704-3710(1998).
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:0000269|PubMed:9658018}.
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:0000269|PubMed:9658018};
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:0000269|PubMed:9658018};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.5 mM for 5-keto-D-gluconate {ECO:0000269|PubMed:9658018};
CC         KM=2 mM for D-gluconate {ECO:0000269|PubMed:9658018};
CC   -!- PATHWAY: Carbohydrate acid metabolism; L-idonate degradation.
CC       {ECO:0000305|PubMed:9658018}.
CC   -!- INDUCTION: Is up-regulated by L-idonate (15-fold) and by 5-
CC       ketogluconate (80-fold). Seems to be catabolite repressed. Is probably
CC       under the control of the positive regulator IdnR. Is part of the
CC       idnDOTR operon. {ECO:0000269|PubMed:9658018}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; U14003; AAA97163.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77223.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78263.1; -; Genomic_DNA.
DR   PIR; S56492; S56492.
DR   RefSeq; NP_418687.1; NC_000913.3.
DR   RefSeq; WP_000998695.1; NZ_SSUV01000014.1.
DR   AlphaFoldDB; P0A9P9; -.
DR   SMR; P0A9P9; -.
DR   BioGRID; 4262730; 8.
DR   BioGRID; 851444; 2.
DR   IntAct; P0A9P9; 7.
DR   STRING; 511145.b4266; -.
DR   jPOST; P0A9P9; -.
DR   PaxDb; P0A9P9; -.
DR   PRIDE; P0A9P9; -.
DR   EnsemblBacteria; AAC77223; AAC77223; b4266.
DR   EnsemblBacteria; BAE78263; BAE78263; BAE78263.
DR   GeneID; 947109; -.
DR   KEGG; ecj:JW4223; -.
DR   KEGG; eco:b4266; -.
DR   PATRIC; fig|1411691.4.peg.2437; -.
DR   EchoBASE; EB2429; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_1_1_6; -.
DR   InParanoid; P0A9P9; -.
DR   OMA; FPQWGAY; -.
DR   PhylomeDB; P0A9P9; -.
DR   BioCyc; EcoCyc:GLUCONREDUCT-MON; -.
DR   BioCyc; MetaCyc:GLUCONREDUCT-MON; -.
DR   UniPathway; UPA00793; -.
DR   PRO; PR:P0A9P9; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0008874; F:gluconate 5-dehydrogenase activity; IDA:EcoCyc.
DR   GO; GO:0046183; P:L-idonate catabolic process; IEP:EcoCyc.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..254
FT                   /note="5-keto-D-gluconate 5-reductase"
FT                   /id="PRO_0000054702"
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
 
 
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