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 27-MAR-2024, entry version 98.
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; Pseudomonadota; 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; NZ_CP051263.1.
DR AlphaFoldDB; P0A9Q0; -.
DR SMR; P0A9Q0; -.
DR STRING; 199310.c5367; -.
DR KEGG; ecc:c5367; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_1_6; -.
DR BioCyc; ECOL199310:C5367-MONOMER; -.
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 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 3: Inferred from homology;
KW Carbohydrate metabolism; NAD; NADP; Oxidoreductase; Reference proteome.
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
//
