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 24-JAN-2024, entry version 123.
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; Pseudomonadota; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 511145-b4266; -.
DR EnsemblBacteria; AAC77223; AAC77223; b4266.
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 OrthoDB; 286404at2; -.
DR PhylomeDB; P0A9P9; -.
DR BioCyc; EcoCyc:GLUCONREDUCT-MONOMER; -.
DR BioCyc; MetaCyc:GLUCONREDUCT-MONOMER; -.
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:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR GO; GO:0046183; P:L-idonate catabolic process; IEP:EcoCyc.
DR CDD; cd05347; Ga5DH-like_SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43669; 5-KETO-D-GLUCONATE 5-REDUCTASE; 1.
DR PANTHER; PTHR43669:SF9; 5-KETO-D-GLUCONATE 5-REDUCTASE; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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
//
