ID UDG_RICCN Reviewed; 432 AA. AC Q92GB1; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 122. 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=RC1212; OS Rickettsia conorii (strain ATCC VR-613 / Malish 7). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=272944; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-613 / Malish 7; RX PubMed=11557893; DOI=10.1126/science.1061471; RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.; RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii."; RL Science 293:2093-2098(2001). 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; AE006914; AAL03750.1; -; Genomic_DNA. DR PIR; D97851; D97851. DR RefSeq; WP_010977777.1; NC_003103.1. DR AlphaFoldDB; Q92GB1; -. DR SMR; Q92GB1; -. DR GeneID; 928375; -. DR KEGG; rco:RC1212; -. DR PATRIC; fig|272944.4.peg.1389; -. DR HOGENOM; CLU_023810_1_2_5; -. DR UniPathway; UPA00038; UER00491. DR Proteomes; UP000000816; 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..432 FT /note="UDP-glucose 6-dehydrogenase" FT /id="PRO_0000074051" FT ACT_SITE 258 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 202 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 206 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 247..251 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 255 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 261 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 319 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" FT BINDING 326 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q0P8H3" SQ SEQUENCE 432 AA; 47878 MW; B417A4117831C7ED CRC64; MNITFIGSGY VGLVSGIIMG YLGHNVTCLD NDEVKISKLN KQILPIYEAK LDEYLKQALE SDRLKFTNIY NNELQNADAI FITVGTPSKG LGEADLKYVY DAIDKVFEHI NKDCLIVIKS TVPPGSCSNI IAYLKSRGFS FNVASNPEFL REGSAVEDFL YPDRIVIGVN NKESEAILRK IYAPLQGVKF VVTDLVTSEL IKYASNSFLA TKIAFINEMA DLCEKIGGNI KDLSKGVGLD QRIGQNFLNA GPGFGGSCFP KDILALNNLV ENHHIDCRIL KAVIKSNKQR PSNMVDKIAT LLDGDLKGKN IAILGLTYKA GTDDVRASPA IAIVKILLNK DVYVKAFDPI GLENAKKNLE HKNLLYLDSA VDACKSVDII VIATEWSEFK ELNWQEIYDL VKSPIIIDFR NILDNETMKK IGFRYYAVGS KI //