ID C0R367_WOLWR Unreviewed; 435 AA. AC C0R367; DT 05-MAY-2009, integrated into UniProtKB/TrEMBL. DT 05-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 97. DE RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00015132, ECO:0000256|PIRNR:PIRNR000124}; DE EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954, ECO:0000256|PIRNR:PIRNR000124}; GN OrderedLocusNames=WRi_005820 {ECO:0000313|EMBL:ACN95359.1}, WRi_010480 GN {ECO:0000313|EMBL:ACN95753.1}; OS Wolbachia sp. subsp. Drosophila simulans (strain wRi). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Wolbachieae; Wolbachia. OX NCBI_TaxID=66084 {ECO:0000313|EMBL:ACN95359.1, ECO:0000313|Proteomes:UP000001293}; RN [1] {ECO:0000313|EMBL:ACN95359.1, ECO:0000313|Proteomes:UP000001293} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=wRi {ECO:0000313|Proteomes:UP000001293}, and WRi RC {ECO:0000313|EMBL:ACN95359.1}; RX PubMed=19307581; DOI=10.1073/pnas.0810753106; RA Klasson L., Westberg J., Sapountzis P., Naeslund K., Lutnaes Y., RA Darby A.C., Veneti Z., Chen L., Braig H.R., Garrett R., Bourtzis K., RA Andersson S.G.; RT "The mosaic genome structure of the Wolbachia wRi strain infecting RT Drosophila simulans."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5725-5730(2009). 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 Evidence={ECO:0000256|ARBA:ARBA00000874, CC ECO:0000256|PIRNR:PIRNR000124}; CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate CC biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step CC 1/1. {ECO:0000256|ARBA:ARBA00004701}. CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase CC family. {ECO:0000256|ARBA:ARBA00006601, ECO:0000256|PIRNR:PIRNR000124}. 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; CP001391; ACN95359.1; -; Genomic_DNA. DR EMBL; CP001391; ACN95753.1; -; Genomic_DNA. DR RefSeq; WP_006280072.1; NZ_MKIF01000142.1. DR AlphaFoldDB; C0R367; -. DR STRING; 66084.WRi_005820; -. DR GeneID; 70036101; -. DR KEGG; wri:WRi_005820; -. DR KEGG; wri:WRi_010480; -. DR HOGENOM; CLU_023810_1_2_5; -. DR UniPathway; UPA00038; UER00491. DR Proteomes; UP000001293; Chromosome. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:UniProtKB-EC. 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 {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000124}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000124}. FT DOMAIN 313..414 FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal" FT /evidence="ECO:0000259|SMART:SM00984" FT ACT_SITE 260 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-1" FT BINDING 30 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3" FT BINDING 35 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3" FT BINDING 86 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3" FT BINDING 121 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3" FT BINDING 204 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2" FT BINDING 249..253 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2" FT BINDING 257 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2" FT BINDING 263 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3" FT BINDING 320 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2" FT BINDING 327 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3" SQ SEQUENCE 435 AA; 48327 MW; 18165E39C9F50802 CRC64; MYITIIGIGY VGLVSCAMLS EQGHNVDCID INTKKIELLK LGKIPIYEPG LADYLENNIK LQRIRFFDSY SQINPNTEVV FVTVDTPSDS LGNANLQNVY NAVSEVSERV NQDCLIVIKS TVPPGTAENI YNYLSNKGYN FDLGVNPEFL KQGSAVSDFL YPDRIIIGVK TKLARAKLEV IYRSFIDKNI PLIVTDTVTA EMIKYASNAF LATKVAFINE MAGLCELLGA DIDLLANSMG MDHRIGKEFL KAGPGFGGSC FPKDLSALIR LAEDHNVKLQ ILNSVKESNY NHITNIAKKV EYVLNGVQNK KIAIWGLTFK SGTDDVRNSP AIDIAQLLVN NKAKITAYDP MGMDNARQVL KDIEYADNAI GAARDAEALL LLTEWKEFKN QDFASLKSIM AAPNVFDFRN LLDSELLLRY GYHVYSLGKK SIYKV //