ID   UDG_ECOLI               Reviewed;         388 AA.
AC   P76373;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=UDP-glucose 6-dehydrogenase;
DE            Short=UDP-Glc dehydrogenase;
DE            Short=UDP-GlcDH;
DE            Short=UDPGDH;
DE            EC=1.1.1.22 {ECO:0000269|PubMed:12851388};
GN   Name=ugd; Synonyms=pmrE, udg, yefA; OrderedLocusNames=b2028, JW2010;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
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   PHOSPHORYLATION AT A TYROSINE, AND CATALYTIC ACTIVITY.
RX   PubMed=12851388; DOI=10.1074/jbc.m305134200;
RA   Grangeasse C., Obadia B., Mijakovic I., Deutscher J., Cozzone A.J.,
RA   Doublet P.;
RT   "Autophosphorylation of the Escherichia coli protein kinase Wzc regulates
RT   tyrosine phosphorylation of Ugd, a UDP-glucose dehydrogenase.";
RL   J. Biol. Chem. 278:39323-39329(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-
CC         alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22;
CC         Evidence={ECO:0000269|PubMed:12851388};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate
CC       biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step
CC       1/1. {ECO:0000305|PubMed:12851388}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis.
CC   -!- INTERACTION:
CC       P76373; P0A8F8: uvrB; NbExp=2; IntAct=EBI-1120497, EBI-552176;
CC   -!- PTM: Phosphorylated on a tyrosine residue. It results in a significant
CC       increase of the dehydrogenase activity. {ECO:0000269|PubMed:12851388}.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; U00096; AAC75089.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15860.2; -; Genomic_DNA.
DR   PIR; C64968; C64968.
DR   RefSeq; NP_416532.1; NC_000913.3.
DR   RefSeq; WP_000704857.1; NZ_LN832404.1.
DR   AlphaFoldDB; P76373; -.
DR   SMR; P76373; -.
DR   BioGRID; 4261356; 256.
DR   BioGRID; 850918; 1.
DR   IntAct; P76373; 4.
DR   STRING; 511145.b2028; -.
DR   PaxDb; 511145-b2028; -.
DR   EnsemblBacteria; AAC75089; AAC75089; b2028.
DR   GeneID; 946571; -.
DR   KEGG; ecj:JW2010; -.
DR   KEGG; eco:b2028; -.
DR   PATRIC; fig|1411691.4.peg.224; -.
DR   EchoBASE; EB3183; -.
DR   eggNOG; COG1004; Bacteria.
DR   InParanoid; P76373; -.
DR   OMA; LFMGFTE; -.
DR   OrthoDB; 9803238at2; -.
DR   PhylomeDB; P76373; -.
DR   BioCyc; EcoCyc:UGD-MONOMER; -.
DR   BioCyc; MetaCyc:UGD-MONOMER; -.
DR   SABIO-RK; P76373; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00038; UER00491.
DR   PRO; PR:P76373; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR   GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IDA:EcoCyc.
DR   GO; GO:0009242; P:colanic acid biosynthetic process; IDA:EcoCyc.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR017476; UDP-Glc/GDP-Man.
DR   InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
DR   InterPro; IPR036220; UDP-Glc/GDP-Man_DH_C_sf.
DR   InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer.
DR   InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N.
DR   InterPro; IPR028357; UDPglc_DH_bac.
DR   NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR   PANTHER; PTHR43750:SF2; UDP-GLUCOSE 6-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43750; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 1.
DR   Pfam; PF00984; UDPG_MGDP_dh; 1.
DR   Pfam; PF03720; UDPG_MGDP_dh_C; 1.
DR   Pfam; PF03721; UDPG_MGDP_dh_N; 1.
DR   PIRSF; PIRSF500134; UDPglc_DH_bac; 1.
DR   PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR   SMART; SM00984; UDPG_MGDP_dh_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52413; UDP-glucose/GDP-mannose dehydrogenase C-terminal domain; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..388
FT                   /note="UDP-glucose 6-dehydrogenase"
FT                   /id="PRO_0000074041"
FT   ACT_SITE        253
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         11
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         29
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         83
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         118
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         141..145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         145
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         242..246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         252
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         256
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         307
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
FT   BINDING         314
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q0P8H3"
SQ   SEQUENCE   388 AA;  43657 MW;  DA33CEE3EF944AED CRC64;
     MKITISGTGY VGLSNGLLIA QNHEVVALDI LPSRVAMLND RISPIVDKEI QQFLQSDKIH
     FNATLDKNEA YRDADYVIIA TPTDYDPKTN YFNTSSVESV IKDVVEINPY AVMVIKSTVP
     VGFTAAMHKK YRTENIIFSP EFLREGKALY DNLHPSRIVI GERSERAERF AALLQEGAIK
     QNIPMLFTDS TEAEAIKLFA NTYLAMRVAY FNELDSYAES LGLNSRQIIE GVCLDPRIGN
     HYNNPSFGYG GYCLPKDTKQ LLANYQSVPN NLISAIVDAN RTRKDFIADA ILSRKPQVVG
     IYRLIMKSGS DNFRASSIQG IMKRIKAKGV EVIIYEPVMK EDSFFNSRLE RDLATFKQQA
     DVIISNRMAE ELKDVADKVY TRDLFGSD
//