ID   DKGA_SALTY              Reviewed;         275 AA.
AC   Q8ZM06;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=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=STM3165;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL22039.1; -; Genomic_DNA.
DR   RefSeq; NP_462080.1; NC_003197.2.
DR   RefSeq; WP_000013100.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZM06; -.
DR   SMR; Q8ZM06; -.
DR   STRING; 99287.STM3165; -.
DR   PaxDb; Q8ZM06; -.
DR   EnsemblBacteria; AAL22039; AAL22039; STM3165.
DR   GeneID; 1254688; -.
DR   KEGG; stm:STM3165; -.
DR   PATRIC; fig|99287.12.peg.3355; -.
DR   HOGENOM; CLU_023205_0_1_6; -.
DR   OMA; AFKPGNE; -.
DR   PhylomeDB; Q8ZM06; -.
DR   BioCyc; SENT99287:STM3165-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0051596; P:methylglyoxal catabolic process; IBA:GO_Central.
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   3: Inferred from homology;
KW   Ascorbate biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..275
FT                   /note="2,5-diketo-D-gluconic acid reductase A"
FT                   /id="PRO_0000124602"
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;  30996 MW;  84E0E6C8901544AE CRC64;
     MANPTIIRLQ DGNVMPQLGL GVWKASNEEV IAAIHKALEV GYRSIDTATA YQNEEGVGKA
     LKAASVAREE LFITTKLWND DQKRPREALQ ESLKKLQLDY LDLYLMHWPV PAIDHYVDAW
     KGMIALQKEG LVKSIGVCNF QIHHLQRLID ETGVTPVINQ IELHPLMQQR QLHAWNATHK
     IQTESWSPLA QGGEGVFDQK VIRELADKYG KTPAQIVIRW HLDCGLVVIP KSVTPSRIAE
     NFAVWDFRLD KDELGEIAKL DQGKRLGPDP DQFGG