DLGD_SHIFL
ID DLGD_SHIFL Reviewed; 332 AA.
AC Q83PQ6; Q7BZ08;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=SF3619, S4150;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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; AE005674; AAN45067.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP19122.1; -; Genomic_DNA.
DR RefSeq; NP_709360.1; NC_004337.2.
DR RefSeq; WP_000869039.1; NZ_WPGW01000060.1.
DR AlphaFoldDB; Q83PQ6; -.
DR SMR; Q83PQ6; -.
DR STRING; 198214.SF3619; -.
DR EnsemblBacteria; AAN45067; AAN45067; SF3619.
DR EnsemblBacteria; AAP19122; AAP19122; S4150.
DR GeneID; 1026304; -.
DR GeneID; 66672536; -.
DR KEGG; sfl:SF3619; -.
DR KEGG; sfx:S4150; -.
DR PATRIC; fig|198214.7.peg.4272; -.
DR HOGENOM; CLU_040452_4_0_6; -.
DR OMA; ISHMAPH; -.
DR OrthoDB; 1374098at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome.
FT CHAIN 1..332
FT /note="2,3-diketo-L-gulonate reductase"
FT /id="PRO_0000083839"
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; 36587 MW; A411EDA20EAB3DF7 CRC64;
MKVTFEQLKA AFNRVLISRG VDSETADACA EMFARTTESG VYSHGVNRFP RFIQQLENGD
IIPDAQPKRI TSLGAIEQWD AQRSIGNLTA KKMMDRAIEL AADHGIGLVA LRNANHWMRG
GSYGWQAAEK GYIGICWTNS IAVMPPWGAK ECRIGTNPLI VAIPSTPITM VDMSMSMFSY
GMLEVNRLAG RQLPVDGGFD DEGNLTKEPG VIEKNRRILP MGYWKGSGMS IVLDMIATLL
SDGASVAEVT QDNSDEYGIS QIFIAIEVDK LIDGPTRDAK LQRIMDYVTT AERADENQAI
RLPGHEFTTL LAENRRNGIT VDDSVWAKIQ AL
