ID   DLGD_SALHS              Reviewed;         332 AA.
AC   B4T959;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=SeHA_C3991;
OS   Salmonella heidelberg (strain SL476).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL476;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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; CP001120; ACF66975.1; -; Genomic_DNA.
DR   RefSeq; WP_000869010.1; NC_011083.1.
DR   AlphaFoldDB; B4T959; -.
DR   SMR; B4T959; -.
DR   KEGG; seh:SeHA_C3991; -.
DR   HOGENOM; CLU_040452_4_0_6; -.
DR   OMA; DKELQHM; -.
DR   Proteomes; UP000001866; 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_1000134349"
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;  36741 MW;  49678DAE4354C02D CRC64;
     MKVTFEELKG AFYRVLRSRN IAEDTADACA EMFARTTESG VYSHGVNRFP RFIQQLDNGD
     IIPDAKPQRV TSLGAIEQWD AQRAIGNLTA KKMMDRAIEL ASDHGIGLVA LRNANHWMRG
     GSYGWQAAER GYIGICWTNS IAVMPPWGAK ECRIGTNPLI VAIPSTPITM VDMSMSMFSY
     GMLEVNRLAG RELPVDGGFD DNGQLTKEPG VIEKNRRILP MGYWKGSGLS IVLDMIATLL
     SNGSSVAEVT QENSDEYGVS QIFIAIEVDK LIDGATRDAK LQRIMDFITT AERADDNVAI
     RLPGHEFTKL LDDNRRHGIT IDDSVWAKIQ AL