DLGD_SALTI
ID DLGD_SALTI Reviewed; 332 AA.
AC Q8Z2C5; Q7C644;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
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};
GN OrderedLocusNames=STY4130, t3851;
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 2,3-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; AL513382; CAD07960.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO71331.1; -; Genomic_DNA.
DR RefSeq; NP_458259.1; NC_003198.1.
DR RefSeq; WP_000869006.1; NZ_WSUR01000001.1.
DR AlphaFoldDB; Q8Z2C5; -.
DR SMR; Q8Z2C5; -.
DR STRING; 220341.16504948; -.
DR EnsemblBacteria; AAO71331; AAO71331; t3851.
DR KEGG; stt:t3851; -.
DR KEGG; sty:STY4130; -.
DR PATRIC; fig|220341.7.peg.4217; -.
DR eggNOG; COG2055; Bacteria.
DR HOGENOM; CLU_040452_4_0_6; -.
DR OMA; DKELQHM; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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_0000083837"
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; 36591 MW; 80C94811B80B87F9 CRC64;
MKVTFEELKG AFYRVLRSRN IAEDTADACA EMFARTTESG VYSHGVNRFP RFIQQLDNGD
IIPDAKPQRV TSLGAIEQWD AQRAIGNLTA KKMMDRAIEL ASDHGIGLVA LRNANHWMRG
GSYGWQAAEK GYIGICWTNS IAVMPPWGAK ECRIGTNPLI VAIPSTPITM VDMSMSMFSY
GMLEVNRLAG RELPVDGGFD DNGQLTKEPG VIEKNHRILP MGYWKGSGLS IVLDMIATLL
SNGSSVAEVT QENSDEYGVS QIFIAIEVDK LIDGATRDAK LQRIMDFITT AERADDNVAI
RLPGHEFTKL LDDSRCNGIT IDDSVWAKIQ AL
