ID UDG_RICTY Reviewed; 434 AA. AC Q68VX0; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 106. 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=udg; OrderedLocusNames=RT0766; OS Rickettsia typhi (strain ATCC VR-144 / Wilmington). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=257363; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-144 / Wilmington; RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004; RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C., RA Yu X.-J., Walker D.H., Weinstock G.M.; RT "Complete genome sequence of Rickettsia typhi and comparison with sequences RT of other Rickettsiae."; RL J. Bacteriol. 186:5842-5855(2004). 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 -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017197; AAU04222.1; -; Genomic_DNA. DR RefSeq; WP_011191197.1; NC_006142.1. DR AlphaFoldDB; Q68VX0; -. DR SMR; Q68VX0; -. DR KEGG; rty:RT0766; -. DR eggNOG; COG1004; Bacteria. DR HOGENOM; CLU_023810_1_2_5; -. DR OrthoDB; 9803238at2; -. DR UniPathway; UPA00038; UER00491. DR Proteomes; UP000000604; Chromosome. DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB. DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro. DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. 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 NCBIfam; TIGR03026; NDP-sugDHase; 1. DR PANTHER; PTHR43750; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 1. DR PANTHER; PTHR43750:SF3; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 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 PIRSF; PIRSF500134; UDPglc_DH_bac; 1. DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1. DR SMART; SM00984; UDPG_MGDP_dh_C; 1. DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR SUPFAM; SSF52413; UDP-glucose/GDP-mannose dehydrogenase C-terminal domain; 1. PE 3: Inferred from homology; KW NAD; Oxidoreductase. FT CHAIN 1..434 FT /note="UDP-glucose 6-dehydrogenase" FT /id="PRO_0000281046" FT ACT_SITE 260 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 30 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 35 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 121 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 148..152 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 152 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 204 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 208 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 249..253 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 257 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 263 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 321 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 328 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" SQ SEQUENCE 434 AA; 48146 MW; 6BB8BA50CE45464D CRC64; MNITFIGSGY VGLVSGIIMG YLGHNVTCFD NDDVKISKLN KKILPIYEAK LDEYLKQALE SDRLKFTNIY SNDFRNVDAV FITVGTPSKE LGEADLKYVY DAVDKVSKHI NKDCLIVIKS TVPPGSCNNI IAYLKAKGFS FNVASNPEFL REGSAVEDFL YPDRIVVGVN NQESEALLRT IYAPLIEQGV KFLVTNLVTS ELIKYASNSF LATKIAFINE MADLCEKIGA NIKDLSQGVG LDQRIGRNFL NAGPGFGGSC FPKDILALNN LVENYKIDCK ILKSVIKSNK LRPGNMVAKI ATLLDGDLKG RNIAILGLTY KAGTDDVRAS PAIEIITILL NKDVYVKAFD PIGLENAKKN LEHKNLLYFA SAVEACESVD IIVIATEWSE FKELNWQEIY DLVKSPMIID LRNILDNEVM KKIGFRYYAV GSKI //