ID   DLGD_ECOK1              Reviewed;         332 AA.
AC   A1AHB7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Ecok1_35630;
GN   ORFNames=APECO1_2875;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ03057.1; -; Genomic_DNA.
DR   RefSeq; WP_000869018.1; NC_008563.1.
DR   AlphaFoldDB; A1AHB7; -.
DR   SMR; A1AHB7; -.
DR   EnsemblBacteria; ABJ03057; ABJ03057; APECO1_2875.
DR   KEGG; ecv:APECO1_2875; -.
DR   HOGENOM; CLU_040452_4_0_6; -.
DR   OMA; DKELQHM; -.
DR   Proteomes; UP000008216; 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_1000062441"
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;  36601 MW;  F329FEFE03F9B01C CRC64;
     MKVTFEQLKA AFNRVLISRG VDNETADACA EMFARTTESG VYSHGVNRFP RFIQQLENGD
     IIPDAQPKRI TSLGAIEQWD AQRSIGNLTA KKMMDRAIEL AADHGIGLVA LRNANHWMRG
     GSYGWQAAEK GYIGICWTNS IAVMPPWGAK ECRIGTNPLI VAIPSTPITM VDMSMSMFSY
     GMLEVNRLAG RQLPVDGGFD DEGNLTKEPG VIEKNRRILP MGYWKGSGMS IVLDMIATLL
     SDGASVAEVT EDNSDEYGIS QIFIAIEVDK LIDGPTRDAK LQRIMDYVTS AERADENQAI
     RLPGHEFTTL LAENRRNGIT VDDSVWAKIQ AL