DLGD_ECOLI
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 03-AUG-2022, entry version 151.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 + 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;
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;
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_SSZK01000041.1.
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 PDBsum; 1NXU; -.
DR PDBsum; 1S20; -.
DR AlphaFoldDB; P37672; -.
DR SMR; P37672; -.
DR BioGRID; 4262546; 12.
DR STRING; 511145.b3575; -.
DR DrugBank; DB01694; D-tartaric acid.
DR PaxDb; P37672; -.
DR PRIDE; P37672; -.
DR DNASU; 948096; -.
DR EnsemblBacteria; AAC76599; AAC76599; b3575.
DR EnsemblBacteria; BAE77718; BAE77718; BAE77718.
DR GeneID; 948096; -.
DR KEGG; ecj:JW3547; -.
DR KEGG; eco:b3575; -.
DR PATRIC; fig|1411691.4.peg.3137; -.
DR EchoBASE; EB2187; -.
DR eggNOG; COG2055; Bacteria.
DR HOGENOM; CLU_040452_4_0_6; -.
DR OMA; ISHMAPH; -.
DR PhylomeDB; P37672; -.
DR BioCyc; EcoCyc:EG12279-MON; -.
DR BioCyc; MetaCyc:EG12279-MON; -.
DR EvolutionaryTrace; P37672; -.
DR PRO; PR:P37672; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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 GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:EcoCyc.
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 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
