ID   DLGD_ECOLI              Reviewed;         332 AA.
AC   P37672; P76716; Q2M7N8;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   10-JUN-2026, entry version 166.
DE   RecName: Full=2,3-diketo-L-gulonate reductase;
DE            Short=2,3-DKG reductase;
DE            EC=1.1.1.130;
DE   AltName: Full=3-dehydro-L-gulonate 2-dehydrogenase;
GN   Name=dlgD; Synonyms=yiaK; OrderedLocusNames=b3575, JW3547;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA   Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT   from 76.0 to 81.5 minutes.";
RL   Nucleic Acids Res. 22:2576-2586(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
RX   PubMed=9525947; DOI=10.1074/jbc.273.14.8376;
RA   Badia J., Ibanez E., Sabate M., Baldoma L., Aguilar J.;
RT   "A rare 920-kilobase chromosomal inversion mediated by IS1 transposition
RT   causes constitutive expression of the yiaK-S operon for carbohydrate
RT   utilization in Escherichia coli.";
RL   J. Biol. Chem. 273:8376-8381(1998).
RN   [5]
RP   FUNCTION.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=11741871; DOI=10.1128/jb.184.1.302-306.2002;
RA   Yew W.S., Gerlt J.A.;
RT   "Utilization of L-ascorbate by Escherichia coli K-12: assignments of
RT   functions to products of the yjf-sga and yia-sgb operons.";
RL   J. Bacteriol. 184:302-306(2002).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH
RP   NAD AND TARTRATE, AND SUBUNIT.
RX   PubMed=14718529; DOI=10.1074/jbc.m313580200;
RA   Forouhar F., Lee I., Benach J., Kulkarni K., Xiao R., Acton T.B.,
RA   Montelione G.T., Tong L.;
RT   "A novel NAD-binding protein revealed by the crystal structure of 2,3-
RT   diketo-L-gulonate reductase (YiaK).";
RL   J. Biol. Chem. 279:13148-13155(2004).
CC   -!- FUNCTION: Catalyzes the reduction of 2,3-diketo-L-gulonate in the
CC       presence of NADH, to form 3-keto-L-gulonate.
CC       {ECO:0000269|PubMed:11741871}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydro-L-gulonate + NAD(+) = 2,3-dioxo-L-gulonate + NADH +
CC         H(+); 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;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydro-L-gulonate + NADP(+) = 2,3-dioxo-L-gulonate + NADPH
CC         + H(+); 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;
CC   -!- ACTIVITY REGULATION: The enzyme is inhibited by tartrate and D-malate.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14718529}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- MISCELLANEOUS: NAD is bound in an unusual conformation, at the
CC       interface of a dimer of the enzyme.
CC   -!- SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family. DlgD
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U00039; AAB18552.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76599.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77718.1; -; Genomic_DNA.
DR   EMBL; AJ223475; CAA11398.1; -; Genomic_DNA.
DR   PIR; A65157; A65157.
DR   RefSeq; NP_418032.1; NC_000913.3.
DR   RefSeq; WP_000869037.1; NZ_CP009789.1.
DR   PDB; 1NXU; X-ray; 1.80 A; A/B=1-332.
DR   PDB; 1S20; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-332.
DR   AlphaFoldDB; P37672; -.
DR   SMR; P37672; -.
DR   BioGRID; 4262546; 12.
DR   FunCoup; P37672; 117.
DR   STRING; 511145.b3575; -.
DR   DrugBank; DB01694; D-tartaric acid.
DR   PaxDb; 511145-b3575; -.
DR   DNASU; 948096; -.
DR   EnsemblBacteria; AAC76599; AAC76599; b3575.
DR   GeneID; 948096; -.
DR   KEGG; ecj:JW3547; -.
DR   KEGG; eco:b3575; -.
DR   KEGG; ecoc:C3026_19385; -.
DR   PATRIC; fig|1411691.4.peg.3137; -.
DR   EchoBASE; EB2187; -.
DR   eggNOG; COG2055; Bacteria.
DR   HOGENOM; CLU_040452_4_0_6; -.
DR   InParanoid; P37672; -.
DR   OMA; GEVGDQY; -.
DR   OrthoDB; 9811519at2; -.
DR   PhylomeDB; P37672; -.
DR   BioCyc; EcoCyc:EG12279-MONOMER; -.
DR   BioCyc; MetaCyc:EG12279-MONOMER; -.
DR   EvolutionaryTrace; P37672; -.
DR   PRO; PR:P37672; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P37672; -.
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   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:EcoCyc.
DR   FunFam; 1.10.1530.10:FF:000001; 2,3-diketo-L-gulonate reductase; 1.
DR   Gene3D; 1.10.1530.10; -; 1.
DR   Gene3D; 3.30.1370.60; Hypothetical oxidoreductase yiak, domain 2; 1.
DR   Gene3D; 3.30.60.50; Hypothetical oxidoreductase yiak, domain 3; 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   NCBIfam; NF009750; PRK13260.1; 1.
DR   PANTHER; PTHR11091:SF3; 2,3-DIKETO-L-GULONATE REDUCTASE; 1.
DR   PANTHER; PTHR11091; OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF02615; Ldh_2; 1.
DR   SUPFAM; SSF89733; L-sulfolactate dehydrogenase-like; 1.
DR   PDBsum; 1NXU; -.
DR   PDBsum; 1S20; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..332
FT                   /note="2,3-diketo-L-gulonate reductase"
FT                   /id="PRO_0000083830"
FT   ACT_SITE        44
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305"
FT   BINDING         168..174
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   BINDING         224..225
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   BINDING         304..306
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   HELIX           5..18
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   HELIX           23..38
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   TURN            43..45
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   HELIX           46..48
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   HELIX           49..57
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   STRAND          76..80
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   HELIX           86..104
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   STRAND          105..114
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   HELIX           121..129
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   STRAND          133..138
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   STRAND          149..151
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   STRAND          159..163
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   STRAND          169..173
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   STRAND          175..178
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   HELIX           180..188
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   STRAND          203..206
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   HELIX           209..215
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   TURN            221..223
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   HELIX           224..241
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   HELIX           246..252
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   STRAND          254..256
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   STRAND          258..266
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   TURN            269..271
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   HELIX           274..289
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   STRAND          293..295
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   TURN            303..305
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   HELIX           306..317
FT                   /evidence="ECO:0007829|PDB:1NXU"
FT   HELIX           323..331
FT                   /evidence="ECO:0007829|PDB:1NXU"
SQ   SEQUENCE   332 AA;  36573 MW;  A411EB14D5C03DF7 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 LQRIMDYVTS AERADENQAI
     RLPGHEFTTL LAENRRNGIT VDDSVWAKIQ AL
//