ID   DKGB_YERPE              Reviewed;         267 AA.
AC   Q8ZH36; Q0WHW9;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 125.
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; Synonyms=ara13; OrderedLocusNames=YPO1075, y3101, YP_2774;
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(2004).
CC   -!- FUNCTION: Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG)
CC       to 2-keto-L-gulonic acid (2KLG). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-dehydro-L-idonate + NADP(+) = 2,5-didehydro-D-gluconate +
CC         H(+) + NADPH; Xref=Rhea:RHEA:35111, ChEBI:CHEBI:11449,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:36602, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.346;
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. {ECO:0000305}.
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DR   EMBL; AL590842; CAL19741.1; -; Genomic_DNA.
DR   EMBL; AE009952; AAM86651.1; -; Genomic_DNA.
DR   EMBL; AE017042; AAS62958.1; -; Genomic_DNA.
DR   PIR; AC0132; AC0132.
DR   RefSeq; WP_002210693.1; NZ_WUCM01000115.1.
DR   RefSeq; YP_002346119.1; NC_003143.1.
DR   AlphaFoldDB; Q8ZH36; -.
DR   SMR; Q8ZH36; -.
DR   STRING; 214092.YPO1075; -.
DR   PaxDb; Q8ZH36; -.
DR   DNASU; 1148048; -.
DR   EnsemblBacteria; AAM86651; AAM86651; y3101.
DR   EnsemblBacteria; AAS62958; AAS62958; YP_2774.
DR   GeneID; 57977480; -.
DR   KEGG; ype:YPO1075; -.
DR   KEGG; ypk:y3101; -.
DR   KEGG; ypm:YP_2774; -.
DR   PATRIC; fig|214092.21.peg.1366; -.
DR   eggNOG; COG0656; Bacteria.
DR   HOGENOM; CLU_023205_0_1_6; -.
DR   OMA; WRHPDEP; -.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; 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   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   PANTHER; PTHR43827; PTHR43827; 1.
DR   Pfam; PF00248; Aldo_ket_red; 2.
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;
KW   Ascorbate biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..267
FT                   /note="2,5-diketo-D-gluconic acid reductase B"
FT                   /id="PRO_0000124608"
FT   ACT_SITE        39
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         179..231
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   267 AA;  29035 MW;  1E5AC57827C31AF5 CRC64;
     MSIPVFGLGT FRLQDQIVID SVSQALTLGY RAIDTAQIYE NEAPVGQAIQ ESGINRDELF
     ITTKIWIANL SKDKLIPSLR ESIQKLKTDY VDLTLIHWPS PNDEVSVAEF MSELLKAKGL
     GLTRQIGISN FTIDLMKQAI AAVGAEEIAT NQIELSPLLQ NRNVVDFAKQ NGIAVTSYMT
     LAYGKALAEP VIKTIAEQHG ATPAQVILSW AMQLGYGVIP SSTKAANLAS NLLAQKLCLN
     AADMALIATL DRNERLVSPD GLAPKWD