DKGB_SALTI
ID DKGB_SALTI Reviewed; 267 AA.
AC Q8Z988;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=STY0276, t2610;
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}.
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DR EMBL; AL513382; CAD08709.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70186.1; -; Genomic_DNA.
DR RefSeq; NP_454858.1; NC_003198.1.
DR RefSeq; WP_000154870.1; NZ_WSUR01000037.1.
DR AlphaFoldDB; Q8Z988; -.
DR SMR; Q8Z988; -.
DR STRING; 220341.16501532; -.
DR EnsemblBacteria; AAO70186; AAO70186; t2610.
DR KEGG; stt:t2610; -.
DR KEGG; sty:STY0276; -.
DR PATRIC; fig|220341.7.peg.278; -.
DR eggNOG; COG0656; Bacteria.
DR HOGENOM; CLU_023205_0_1_6; -.
DR OMA; WRHPDEP; -.
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; 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;
KW Ascorbate biosynthesis; Cytoplasm; NADP; Oxidoreductase.
FT CHAIN 1..267
FT /note="2,5-diketo-D-gluconic acid reductase B"
FT /id="PRO_0000124606"
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; 29260 MW; 29E47E48555F9F9E CRC64;
MTIPAFGLGT FRLKDDVVIA SVKTALELGY RAVDTAQIYD NEAAVGQAIA ESGVPRNELY
ITTKIWIENL SKDKLIPSLK ESLKKLRTDY VDLTLIHWPS PGDAVSVEEF MQALLEAKKQ
GLTREIGISN FTIPLMEKAI AAVGADHIAT NQIELSPYLQ NRKVVDWAKA HGIHITSYMT
LAYGKALKDE VIARIAVKHN ATPVQVILAW AMGEGYSVIP SSTRRENLAS NLLAQDLHLD
AEDKNAIAAL DCNDRLVSPE GLAPAWD
