ID A5FGN8_FLAJ1 Unreviewed; 214 AA. AC A5FGN8; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 28-JAN-2026, entry version 121. DE RecName: Full=Orotate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011971, ECO:0000256|HAMAP-Rule:MF_01208}; DE Short=OPRT {ECO:0000256|HAMAP-Rule:MF_01208}; DE Short=OPRTase {ECO:0000256|HAMAP-Rule:MF_01208}; DE EC=2.4.2.10 {ECO:0000256|ARBA:ARBA00011971, ECO:0000256|HAMAP-Rule:MF_01208}; GN Name=pyrE {ECO:0000256|HAMAP-Rule:MF_01208}; GN OrderedLocusNames=Fjoh_2604 {ECO:0000313|EMBL:ABQ05631.1}; OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / BCRC OS 14874 / CCUG 350202 / NBRC 14942 / NCIMB 11054 / UW101) (Cytophaga OS johnsonae). OC Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ05631.1, ECO:0000313|Proteomes:UP000006694}; RN [1] {ECO:0000313|EMBL:ABQ05631.1, ECO:0000313|Proteomes:UP000006694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / BCRC 14874 / CCUG 350202 / RC NBRC 14942 / NCIMB 11054 / UW101 {ECO:0000313|Proteomes:UP000006694}; RX PubMed=19717629; DOI=10.1128/AEM.01495-09; RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G., RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R., RA Cheng Y.Q., Stein J.L.; RT "Novel features of the polysaccharide-digesting gliding bacterium RT Flavobacterium johnsoniae as revealed by genome sequence analysis."; RL Appl. Environ. Microbiol. 75:6864-6875(2009). CC -!- FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5- CC phosphoribose 1-diphosphate to orotate, leading to the formation of CC orotidine monophosphate (OMP). {ECO:0000256|HAMAP-Rule:MF_01208}. CC -!- CATALYTIC ACTIVITY: CC Reaction=orotidine 5'-phosphate + diphosphate = orotate + 5-phospho- CC alpha-D-ribose 1-diphosphate; Xref=Rhea:RHEA:10380, CC ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, CC ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01208}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01208}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC UMP from orotate: step 1/2. {ECO:0000256|ARBA:ARBA00004889, CC ECO:0000256|HAMAP-Rule:MF_01208}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01208}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase CC family. PyrE subfamily. {ECO:0000256|HAMAP-Rule:MF_01208}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01208}. 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; CP000685; ABQ05631.1; -; Genomic_DNA. DR RefSeq; WP_012024670.1; NC_009441.1. DR AlphaFoldDB; A5FGN8; -. DR STRING; 376686.Fjoh_2604; -. DR GeneID; 31765513; -. DR KEGG; fjo:Fjoh_2604; -. DR eggNOG; COG0461; Bacteria. DR HOGENOM; CLU_074878_1_1_10; -. DR OrthoDB; 9802134at2; -. DR UniPathway; UPA00070; UER00119. DR Proteomes; UP000006694; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IEA:TreeGrafter. DR CDD; cd06223; PRTases_typeI; 1. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_01208; PyrE; 1. DR InterPro; IPR023031; OPRT. DR InterPro; IPR004467; Or_phspho_trans_dom. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR000836; PRTase_dom. DR NCBIfam; TIGR00336; pyrE; 1. DR PANTHER; PTHR19278; OROTATE PHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR19278:SF9; URIDINE 5'-MONOPHOSPHATE SYNTHASE; 1. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; PRTase-like; 1. PE 3: Inferred from homology; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP- KW Rule:MF_01208}; Magnesium {ECO:0000256|HAMAP-Rule:MF_01208}; KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP- KW Rule:MF_01208}; Reference proteome {ECO:0000313|Proteomes:UP000006694}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01208}. FT DOMAIN 59..174 FT /note="Phosphoribosyltransferase" FT /evidence="ECO:0000259|Pfam:PF00156" FT BINDING 100 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01208" FT BINDING 104 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01208" FT BINDING 106 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01208" FT BINDING 126..134 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01208" FT BINDING 130 FT /ligand="orotate" FT /ligand_id="ChEBI:CHEBI:30839" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01208" SQ SEQUENCE 214 AA; 23746 MW; C91047E6CE61EA85 CRC64; MIFNKDTAEK TAELLLQINA IKLNPENPFT WASGWKSPIY CDNRLILSFP SIRNYVRDEF AKNIEKQFGK PDVIAGVATG AIGVGILVAE SLGLPFVYVR PEPKKHGRQN QVEGFLQKGQ NVVVVEDLIS TGKSSLLAVE ALRNEGANIK GMAAVFTYGF GVAEENFKEA NVDLFTLSNY ENLLDLAVQK QYITEDQQST LQEWSVSPST WGQE //