ID   DLGD_SALPA              Reviewed;         332 AA.
AC   Q5PLN6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=2,3-diketo-L-gulonate reductase {ECO:0000255|HAMAP-Rule:MF_00820};
DE            Short=2,3-DKG reductase {ECO:0000255|HAMAP-Rule:MF_00820};
DE            EC=1.1.1.130 {ECO:0000255|HAMAP-Rule:MF_00820};
DE   AltName: Full=3-dehydro-L-gulonate 2-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00820};
GN   Name=dlgD {ECO:0000255|HAMAP-Rule:MF_00820}; OrderedLocusNames=SPA3519;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
CC   -!- FUNCTION: Catalyzes the reduction of 2,3-diketo-L-gulonate in the
CC       presence of NADH, to form 3-keto-L-gulonate. {ECO:0000255|HAMAP-
CC       Rule:MF_00820}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydro-L-gulonate + NAD(+) = 2,3-dioxo-L-gulonate + H(+) +
CC         NADH; Xref=Rhea:RHEA:21924, ChEBI:CHEBI:15378, ChEBI:CHEBI:57441,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57655, ChEBI:CHEBI:57945;
CC         EC=1.1.1.130; Evidence={ECO:0000255|HAMAP-Rule:MF_00820};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydro-L-gulonate + NADP(+) = 2,3-dioxo-L-gulonate + H(+) +
CC         NADPH; Xref=Rhea:RHEA:21928, ChEBI:CHEBI:15378, ChEBI:CHEBI:57441,
CC         ChEBI:CHEBI:57655, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.130; Evidence={ECO:0000255|HAMAP-Rule:MF_00820};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00820}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00820}.
CC   -!- SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family. DlgD
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00820}.
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DR   EMBL; CP000026; AAV79324.1; -; Genomic_DNA.
DR   RefSeq; WP_000869009.1; NC_006511.1.
DR   AlphaFoldDB; Q5PLN6; -.
DR   SMR; Q5PLN6; -.
DR   PRIDE; Q5PLN6; -.
DR   EnsemblBacteria; AAV79324; AAV79324; SPA3519.
DR   KEGG; spt:SPA3519; -.
DR   HOGENOM; CLU_040452_4_0_6; -.
DR   OMA; DKELQHM; -.
DR   Proteomes; UP000008185; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047559; F:3-dehydro-L-gulonate 2-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   Gene3D; 1.10.1530.10; -; 1.
DR   Gene3D; 3.30.1370.60; -; 1.
DR   HAMAP; MF_00820; Diketo_gul_reduc; 1.
DR   InterPro; IPR023689; Diketo_gul_Rdtase.
DR   InterPro; IPR043144; Mal/L-sulf/L-lact_DH-like_ah.
DR   InterPro; IPR043143; Mal/L-sulf/L-lact_DH-like_NADP.
DR   InterPro; IPR036111; Mal/L-sulfo/L-lacto_DH-like_sf.
DR   InterPro; IPR003767; Malate/L-lactate_DH-like.
DR   PANTHER; PTHR11091; PTHR11091; 1.
DR   Pfam; PF02615; Ldh_2; 1.
DR   SUPFAM; SSF89733; SSF89733; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; Oxidoreductase.
FT   CHAIN           1..332
FT                   /note="2,3-diketo-L-gulonate reductase"
FT                   /id="PRO_0000083836"
FT   ACT_SITE        44
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00820"
FT   BINDING         168..174
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00820"
FT   BINDING         224..225
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00820"
FT   BINDING         304..306
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00820"
SQ   SEQUENCE   332 AA;  36699 MW;  F78537D320CC8A48 CRC64;
     MKVTFEELKG AFYRVLRSRN IAEDTADACA EMFARTTESG VYSHGVNRFP RFIQQLDNGD
     IIPDAKPQRV TSLGAIEQWD AQRAIGNLTA KKMMDRAIEL ASDHGIGLVA LRNANHWMRG
     GSYGWQAAEK GYIGICWTNS IAVMPPWGAK ECRIGTNPLI VAIPSTPITM VDMSMSMFSY
     GMLEVNRLAG RELPVDGGFD DNGQLTKEPG VIEKNRRILP MGYWKGSGLS IVLDMIATLL
     SNGSSVAEVT QENSDEYGVS QIFIAIEVDK LIDGATRDAK LQRIMDFITT AERADDNVAI
     RLPGHEFTKL LDDNRRHGIT VDDSVWAKIQ AL