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 25-NOV-2008, entry version 52. 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; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=168927; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=O111:H- / M92 / EPEC; RX MEDLINE=93225815; PubMed=7682279; 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: UDP-glucose + 2 NAD(+) + H(2)O = UDP- CC glucuronate + 2 NADH. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-glucuronate CC biosynthesis; UDP-glucuronate 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z17241; CAA78939.1; -; Genomic_DNA. DR PIR; S33668; S33668. DR HSSP; Q07172; 1DLJ. DR GO; GO:0051287; F:NAD 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. DR InterPro; IPR017476; Nucleotide_sugar_DH. DR InterPro; IPR014027; UDP-Glc/GDP-Man_DHase_C. DR InterPro; IPR014026; UDP-Glc/GDP-Man_DHase_dimer. DR InterPro; IPR001732; UDP-Glc/GDP-Man_DHase_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 Pfam; PF00984; UDPG_MGDP_dh; 1. DR Pfam; PF03720; UDPG_MGDP_dh_C; 1. DR Pfam; PF03721; UDPG_MGDP_dh_N; 1. PE 3: Inferred from homology; KW NAD; Oxidoreductase; Phosphoprotein. FT CHAIN 1 388 UDP-glucose 6-dehydrogenase. FT /FTId=PRO_0000074044. FT NP_BIND 2 19 NAD (Potential). FT ACT_SITE 253 253 By similarity. 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 //