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 16-JUN-2009, entry version 36. DE RecName: Full=Gluconate 5-dehydrogenase; DE EC=1.1.1.69; DE AltName: Full=5-keto-D-gluconate 5-reductase; GN Name=idnO; Synonyms=yjgU; OrderedLocusNames=b4266, JW4223; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=95334362; PubMed=7610040; DOI=10.1093/nar/23.12.2105; RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., RA Blattner F.R.; RT "Analysis of the Escherichia coli genome VI: DNA sequence of the RT region 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 MEDLINE=97426617; 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., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(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 RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP FUNCTION. RX MEDLINE=98324983; PubMed=9658018; RA Bausch C., Peekhaus N., Utz C., Blais T., Murray E., Lowary T., RA 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 a reversible reduction of 5-ketoglutanate to CC form D-gluconate. Dependent on NADP, almost inactive with NAD. 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 (Probable). CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases CC (SDR) family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs 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; AP_004762.1; -. DR RefSeq; NP_418687.1; -. DR HSSP; P25529; 1AHH. DR GeneID; 947109; -. DR GenomeReviews; AP009048_GR; JW4223. DR GenomeReviews; U00096_GR; b4266. DR KEGG; ecj:JW4223; -. DR KEGG; eco:b4266; -. DR EchoBASE; EB2429; -. DR EcoGene; EG12540; idnO. DR HOGENOM; P0A9P9; -. DR OMA; P0A9P9; RYMIKRQ. DR BioCyc; EcoCyc:GLUCONREDUCT-MON; -. DR BioCyc; MetaCyc:GLUCONREDUCT-MON; -. 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_0000054702. 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 //