DKGB_SALTY
ID DKGB_SALTY Reviewed; 267 AA.
AC Q8ZRM7;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=STM0255;
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; AAL19212.1; -; Genomic_DNA.
DR RefSeq; NP_459253.1; NC_003197.2.
DR RefSeq; WP_000154872.1; NC_003197.2.
DR AlphaFoldDB; Q8ZRM7; -.
DR SMR; Q8ZRM7; -.
DR STRING; 99287.STM0255; -.
DR PaxDb; Q8ZRM7; -.
DR EnsemblBacteria; AAL19212; AAL19212; STM0255.
DR GeneID; 1251773; -.
DR KEGG; stm:STM0255; -.
DR PATRIC; fig|99287.12.peg.264; -.
DR HOGENOM; CLU_023205_0_1_6; -.
DR PhylomeDB; Q8ZRM7; -.
DR BioCyc; SENT99287:STM0255-MON; -.
DR Proteomes; UP000001014; 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;
KW Reference proteome.
FT CHAIN 1..267
FT /note="2,5-diketo-D-gluconic acid reductase B"
FT /id="PRO_0000124607"
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; 29153 MW; 2E46FECC55B18876 CRC64;
MTIPAFGLGT FRLKDDVVIA SVKTALELGY RAVDTAQIYD NEAAVGQAIA ESGVPRNELY
ITTKIWIENL SKDKLIPSLK ESLKKLRTDY VDLTLIHWPS PGDAVSVEEF MQALLEAKKQ
GLTREIGISN FTIPLMEKAI AAVGADNIAT NQIELSPYLQ NRKVVDWAKA HGIHITSYMT
LAYGKALKDE VIARIAAKHN ATPAQVILAW AMGEGYSVIP SSTRRENLAS SLLAQDLHLD
AEDKNAIAAL DCNDRLVSPE GLAPAWD
