(data stored in ACNUC7421 zone)

SWISSPROT: DKGB_ECO57

ID   DKGB_ECO57              Reviewed;         267 AA.
AC   Q8X7Z7;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 93.
DE   RecName: Full=2,5-diketo-D-gluconic acid reductase B;
DE            Short=2,5-DKG reductase B;
DE            Short=2,5-DKGR B;
DE            Short=25DKGR-B;
DE            EC=1.1.1.346;
DE   AltName: Full=AKR5D;
GN   Name=dkgB; OrderedLocusNames=Z0229, ECs0203;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-206.
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11108008;
RA   Ohnishi M., Murata T., Nakayama K., Kuhara S., Hattori M.,
RA   Kurokawa K., Yasunaga T., Yokoyama K., Makino K., Shinagawa H.,
RA   Hayashi T.;
RT   "Comparative analysis of the whole set of rRNA operons between an
RT   enterohemorrhagic Escherichia coli O157:H7 Sakai strain and an
RT   Escherichia coli K-12 strain MG1655.";
RL   Syst. Appl. Microbiol. 23:315-324(2000).
CC   -!- FUNCTION: Catalyzes the reduction of 2,5-diketo-D-gluconic acid
CC       (25DKG) to 2-keto-L-gulonic acid (2KLG). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: 2-dehydro-L-gulonate + NADP(+) = 2,5-
CC       didehydro-D-gluconate + NADPH.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: 2-keto-L-gulonic acid is a key intermediate in the
CC       production of L-ascorbic acid (vitamin C).
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family.
CC       {ECO:0000305}.
DR   EMBL; AE005174; AAG54503.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33626.1; -; Genomic_DNA.
DR   EMBL; AB035926; BAA93569.1; -; Genomic_DNA.
DR   PIR; C85505; C85505.
DR   PIR; C90654; C90654.
DR   RefSeq; NP_308230.1; NC_002695.1.
DR   RefSeq; WP_000997018.1; NZ_MWVM01000070.1.
DR   ProteinModelPortal; Q8X7Z7; -.
DR   SMR; Q8X7Z7; -.
DR   STRING; 155864.Z0229; -.
DR   EnsemblBacteria; AAG54503; AAG54503; Z0229.
DR   EnsemblBacteria; BAB33626; BAB33626; BAB33626.
DR   GeneID; 914031; -.
DR   KEGG; ece:Z0229; -.
DR   KEGG; ecs:ECs0203; -.
DR   PATRIC; fig|386585.9.peg.307; -.
DR   eggNOG; ENOG4105CV8; Bacteria.
DR   eggNOG; COG0656; LUCA.
DR   HOGENOM; HOG000250272; -.
DR   KO; K06222; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd06660; Aldo_ket_red; 1.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR020471; Aldo/keto_reductase.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8X7Z7.
DR   SWISS-2DPAGE; Q8X7Z7.
KW   Ascorbate biosynthesis; Complete proteome; Cytoplasm; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    267       2,5-diketo-D-gluconic acid reductase B.
FT                                /FTId=PRO_0000124605.
FT   NP_BIND     179    231       NADP. {ECO:0000250}.
FT   ACT_SITE     39     39       Proton donor. {ECO:0000250}.
FT   BINDING      97     97       Substrate. {ECO:0000250}.
SQ   SEQUENCE   267 AA;  29439 MW;  C03126A69D94CED4 CRC64;
     MAIPAFGLGT FRLKDDVVIS SVKTALELGY RAIDTAQIYD NEAAVGLAIA ESGVPRHELY
     ITTKIWIENL SKDKLIPSLK ESLQKLRTDY VDLTLIHWPS PNDEVSVEEF MQALLEAKKE
     GLTREIGISN FTIPLMEKAI AAVGAENIAT NQIELSPYLQ NRKVVAWAKQ HGIHITSYMT
     LAYGKALKDE VIARIAAKHN ATPAQVILAW AMGEGYSVIP SSTKRENLES NLKAQNLQLD
     AEDKKAIAAL DCNDRLVSPE GLAPEWD
//

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