ID   DKGA_SALTI              Reviewed;         275 AA.
AC   P58744;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Putative 2,5-diketo-D-gluconic acid reductase A;
DE            Short=2,5-DKG reductase A;
DE            Short=2,5-DKGR A;
DE            Short=25DKGR-A;
DE            EC=1.1.1.346;
DE   AltName: Full=AKR5C;
GN   Name=dkgA; OrderedLocusNames=STY3338, t3085;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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}.
CC   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AE014613; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=AL513382; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL513382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AE014613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P58744; -.
DR   SMR; P58744; -.
DR   OMA; AFKPGNE; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE   5: Uncertain;
KW   Ascorbate biosynthesis; Cytoplasm; NADP; Oxidoreductase.
FT   CHAIN           1..275
FT                   /note="Putative 2,5-diketo-D-gluconic acid reductase A"
FT                   /id="PRO_0000124601"
FT   ACT_SITE        51
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         187..241
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   275 AA;  30931 MW;  8620FEB8901540AE CRC64;
     MANPTIIRLQ DGNVMPQLGL GVWKASNEEV IAAIHKALEV GYRSIDTATA YQNEEGVGKA
     LKAASVAREE LFITTKLWND DQKRPREALQ ESLKKLQLDY LDLYLMHWPV PAIDHYVDAW
     KGMIALQKEG LVKSIGVCNF QIHHLQRLID ETGVPPVINQ IELHPLMQQR QLHAWNATHK
     IQTESWSPLA QGGEGVFDQK VIRELADKYG KTPAQIVIRW HLDCGLVVIP KSVTPSRIAE
     NFAVWDFRLD KDELGEIAKL DQGKRLGPDP DQSGG