DLGD_ECOL5
ID DLGD_ECOL5 Reviewed; 332 AA.
AC Q0TBM6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=ECP_3679;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000247; ABG71653.1; -; Genomic_DNA.
DR RefSeq; WP_000869044.1; NC_008253.1.
DR AlphaFoldDB; Q0TBM6; -.
DR SMR; Q0TBM6; -.
DR STRING; 362663.ECP_3679; -.
DR EnsemblBacteria; ABG71653; ABG71653; ECP_3679.
DR KEGG; ecp:ECP_3679; -.
DR HOGENOM; CLU_040452_4_0_6; -.
DR OMA; DKELQHM; -.
DR Proteomes; UP000009182; 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_1000062442"
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; 36574 MW; A05A6E1E4E072740 CRC64;
MKVTFEQLKA AFNRVLISRG VDSETADACA EMFARTTESG VYSHGVNRFP RFIQQLENGD
IIPDAQPKRI TSLGAIEQWD AQRSIGNLTA KKMMDRAIEL AADHGIGLVA LRNANHWMRG
GSYGWQAAEK GYIGICWTNS IAVMPPWGAK ECRIGTNPLI VAIPSTPITM VDMSMSMFSY
GMLEVNRLAG RQLPVDGGFD DEGNLTKEPG VIEKNRRILP MGYWKGSGMS LVLDMIATLL
SDGASVAEVT EDNSDEYGIS QIFIAIEVDK LIDGPTRDAK LQRIMDYVTS AERADENQAI
RLPGHEFTTL LAENRRNGIT VDDSVWAKIQ AL