ID UDG_RICPR Reviewed; 434 AA. AC O05973; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 27-MAR-2024, entry version 128. 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=RP779; OS Rickettsia prowazekii (strain Madrid E). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=272947; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Madrid E; RX PubMed=9274032; DOI=10.1099/00221287-143-8-2783; RA Andersson J.O., Andersson S.G.E.; RT "Genomic rearrangements during evolution of the obligate intracellular RT parasite Rickettsia prowazekii as inferred from an analysis of 52015 bp RT nucleotide sequence."; RL Microbiology 143:2783-2795(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Madrid E; RX PubMed=9823893; DOI=10.1038/24094; RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., RA Kurland C.G.; RT "The genome sequence of Rickettsia prowazekii and the origin of RT mitochondria."; RL Nature 396:133-140(1998). 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; Y11785; CAA72478.1; -; Genomic_DNA. DR EMBL; AJ235273; CAA15205.1; -; Genomic_DNA. DR PIR; E71638; E71638. DR RefSeq; NP_221129.1; NC_000963.1. DR RefSeq; WP_004596947.1; NC_000963.1. DR AlphaFoldDB; O05973; -. DR SMR; O05973; -. DR STRING; 272947.gene:17555848; -. DR EnsemblBacteria; CAA15205; CAA15205; CAA15205. DR GeneID; 57569902; -. DR KEGG; rpr:RP779; -. DR PATRIC; fig|272947.5.peg.815; -. DR eggNOG; COG1004; Bacteria. DR HOGENOM; CLU_023810_1_2_5; -. DR OrthoDB; 9803238at2; -. DR UniPathway; UPA00038; UER00491. DR Proteomes; UP000002480; 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; Reference proteome. FT CHAIN 1..434 FT /note="UDP-glucose 6-dehydrogenase" FT /id="PRO_0000074052" 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; 48226 MW; 15991BA7112D5036 CRC64; MNITFIGSGY VGLVSGIIMG YLGHNVTCLD NDDVKISKLN KKILPIYEAK LDEYLKHALE SDRLKFTNIY SNEFRNFDAI FITVGTPSKE LGEADLKYVY DAVDKVSKHI NKDCLIVIKS TVPPGSCNNI IAYLKAKGFS FNVASNPEFL REGSAVEDFL YPDRIVVGVN NKESEALLRK IYAPLIEQGA KFLVTNLVTS ELIKYVSNSF LATKIAFINE MADLCEKIGA NIKDLSQGVG LDQRIGRNFL NAGPGFGGSC FPKDILALNN LVENHKIDCK ILKSVIKSNK LRPSNMVAKI ATLLDGDLKG RNIAILGLTY KAGTDDVRAS PAIEIITILL NKDVYVKAFD PIGLENAKKN LEHKNLLYFA SAVEACKSVD IIVIATEWSE FKELNWQEIY NLVKSPMIID LRNILDNEVM KKIGFRYYAV GSQI //