UDG_ECO11
ID UDG_ECO11 Reviewed; 388 AA.
AC Q04872;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 110.
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;
GN Name=ugd;
OS Escherichia coli O111:H-.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=168927;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O111:H- / M92 / EPEC;
RX PubMed=7682279; DOI=10.1111/j.1365-2958.1993.tb01163.x;
RA Bastin D.A., Stevenson G., Brown P.K., Haase A., Reeves P.R.;
RT "Repeat unit polysaccharides of bacteria: a model for polymerization
RT resembling that of ribosomes and fatty acid synthetase, with a novel
RT mechanism for determining chain length.";
RL Mol. Microbiol. 7:725-734(1993).
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 -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate
CC biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step
CC 1/1.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis.
CC -!- PTM: Phosphorylated on a tyrosine residue. It results in a significant
CC increase of the dehydrogenase activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; Z17241; CAA78939.1; -; Genomic_DNA.
DR PIR; S33668; S33668.
DR AlphaFoldDB; Q04872; -.
DR SMR; Q04872; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00038; UER00491.
DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; ISS:UniProtKB.
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; 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 3: Inferred from homology;
KW NAD; Oxidoreductase; Phosphoprotein.
FT CHAIN 1..388
FT /note="UDP-glucose 6-dehydrogenase"
FT /id="PRO_0000074044"
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 34
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; 43289 MW; E85B4550BB1FA02F CRC64;
MKITISGTGY VGLSNGILIA QHHEVVALDI VPTKVEMLNQ KKSPIVDKEI EEYLATKQLN
FRATTDKYDA YRDGTYVIIA TPTDYDPKTN YFNTSSVESV IRDVVDINPN AVMVIKSTIP
VGFTNLLKER LGIDNIFFSP EFLREGRALY DNLHPSRIVI GERSERAGRF AALLQEGAVK
KDIPTLFTDS TEAEAIKLFA NTYLALRVAY FNELDSYAES LGLNSRQIIE GVCLDPRIGN
HYNNPSFGYG GYCLPKDTKQ LLANYASVPN NIIGAIVDAN RTRKDFIADS ILARKPKVVG
VYRLIMKSGS DNFRASSIQG IMKRIKAKGV PVIIYEPVMV EDEFFHSRVV RDLTAFKNEA
DIIISNRMTS ELADVADKVY TRGLFGSD
