ID   UDG8_ECOLX              Reviewed;         388 AA.
AC   O33952;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 53.
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.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O8:K40 / 2775;
RX   MEDLINE=98043545; PubMed=9383197;
RX   DOI=10.1046/j.1365-2958.1997.5631930.x;
RA   Amor P.A., Whitfield C.;
RT   "Molecular and functional analysis of genes required for expression of
RT   group IB K antigens in Escherichia coli: characterization of the his-
RT   region containing gene clusters for multiple cell-surface
RT   polysaccharides.";
RL   Mol. Microbiol. 26:145-161(1997).
CC   -!- CATALYTIC ACTIVITY: UDP-glucose + 2 NAD(+) + H(2)O = UDP-
CC       glucuronate + 2 NADH.
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-glucuronic acid
CC       biosynthesis; UDP-glucuronic acid from UDP-glucose: step 1/1.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis.
CC   -!- PTM: Phosphorylated on a tyrosine residue. It results in a
CC       significant increase of the dehydrogenase activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family.
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DR   EMBL; U78086; AAC45829.1; -; Genomic_DNA.
DR   HSSP; Q07172; 1DLI.
DR   BRENDA; 1.1.1.22; 246.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR017476; Nucleotide_sugar_DH.
DR   InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
DR   InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer.
DR   InterPro; IPR014028; UDP-Glc/GDP-Man_DH_dimer-bd.
DR   InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:3.40.50.1870; UDP-Glc/GDP-Man_DH_C; 1.
DR   PANTHER; PTHR11374; UDPG_MGDP_DH_Creg; 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   TIGRFAMs; TIGR03026; NDP-sugDHase; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Phosphoprotein.
FT   CHAIN         1    388       UDP-glucose 6-dehydrogenase.
FT                                /FTId=PRO_0000074046.
FT   NP_BIND       2     19       NAD (Potential).
FT   ACT_SITE    253    253       By similarity.
SQ   SEQUENCE   388 AA;  43549 MW;  D30E622AA6489AC9 CRC64;
     MKITISGTGY VGLSNGILIA QNHEVVALDI VQAKVDMLNK KQSPIVDKEI EEYLATKDLN
     FRATTDKYDA YKNADYVIIA TPTDYDPKTN YFNTSSVEAV IRDVTEINPN AVMVIKSTIP
     VGFTKSIKER LGIDNLIFSP EFLREGKALY DNLHPSRIVI GERSERAERF AALLQEGAIK
     QNIPTLFTDS TEAEAIKLFA NTYLAMRVAY FNELDSYAES LGLNTRQIIE GVCLDPRIGN
     HYNNPSFGYG GYCLPKDTKQ LLANYQSVPN NLISAIVDAN RTRKDFIADA ILSRKPQVVG
     IYRLIMKSGS DNFRASSIQG IMKRIKAKGV EVIIYEPVMK EDSFFNSRLE RDLATFKQQA
     DVIISNRMAE ELKDVADKVY TRDLFGSD
//