UDG_ECOLI
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 03-AUG-2022, entry version 165.
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; Proteobacteria; 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; BAA15860.1; -; 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; P76373; -.
DR PRIDE; P76373; -.
DR EnsemblBacteria; AAC75089; AAC75089; b2028.
DR EnsemblBacteria; BAA15860; BAA15860; BAA15860.
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; EDFTRPD; -.
DR PhylomeDB; P76373; -.
DR BioCyc; EcoCyc:UGD-MON; -.
DR BioCyc; MetaCyc:UGD-MON; -.
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; 1.10.1040.10; -; 1.
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 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; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52413; SSF52413; 1.
DR TIGRFAMs; TIGR03026; NDP-sugDHase; 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 2..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
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
