ID   UDG_ECOL6               Reviewed;         388 AA.
AC   Q8FG45;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 48.
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; OrderedLocusNames=c2555;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN81010.1; -; Genomic_DNA.
DR   RefSeq; NP_754443.1; -.
DR   HSSP; Q07172; 1DLJ.
DR   GeneID; 1037832; -.
DR   GenomeReviews; AE014075_GR; c2555.
DR   KEGG; ecc:c2555; -.
DR   HOGENOM; Q8FG45; -.
DR   OMA; Q8FG45; ILFTDST.
DR   BRENDA; 1.1.1.22; 292881.
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   Complete proteome; NAD; Oxidoreductase; Phosphoprotein.
FT   CHAIN         1    388       UDP-glucose 6-dehydrogenase.
FT                                /FTId=PRO_0000074043.
FT   NP_BIND       2     19       NAD (Potential).
FT   ACT_SITE    253    253       By similarity.
SQ   SEQUENCE   388 AA;  43655 MW;  9CFB8471E9CEF8E2 CRC64;
     MKITISGTGY VGLSNGLLIA QNHEVVALDI LPSRVAMLND RISPIVDKEI QQFLQSDKIH
     FNATLDKNEA YRDADYVIIA TPTDYDPKTN YFNTSSVESV IKDVVEINPY AVMVIKSTVP
     VGFTAAMHKK YRTENIIFSP EFLREGKALY DNLHPSRIVI GERSERAERF AALLQEGAIK
     QNIPTLFTDS TEAEAIKLFA NTYLAMRVAY FNELDSYAES LGLNTRQIIE GVCLDPRIGN
     HYNNPSFGYG GYCLPKDTKQ LLANYQSVPN NLISAIVDAN RTRKDFIADA ILSRKPQVVG
     IYRLIMKSGS DNFRASSIQG IMKRIKAKGV EVIIYEPVMK EDSFFNSRLE RDLATFKQQA
     DIIISNRMAE ELKDVADKVY TRDLFGSD
//