ID PYRE_BUCBP Reviewed; 206 AA. AC P59575; DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 11-APR-2003, sequence version 1. DT 04-NOV-2026, entry version 122. DE RecName: Full=Orotate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01208}; DE Short=OPRT {ECO:0000255|HAMAP-Rule:MF_01208}; DE Short=OPRTase {ECO:0000255|HAMAP-Rule:MF_01208}; DE EC=2.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01208}; GN Name=pyrE {ECO:0000255|HAMAP-Rule:MF_01208}; GN OrderedLocusNames=bbp_506; OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Erwiniaceae; Buchnera. OX NCBI_TaxID=224915; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bp; RX PubMed=12522265; DOI=10.1073/pnas.0235981100; RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.; RT "Reductive genome evolution in Buchnera aphidicola."; RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003). 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:0000255|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:0000255|HAMAP- CC Rule:MF_01208}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01208}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC UMP from orotate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01208}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01208}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase CC family. PyrE subfamily. {ECO:0000255|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; AE016826; AAO27209.1; -; Genomic_DNA. DR RefSeq; WP_011091610.1; NC_004545.1. DR AlphaFoldDB; P59575; -. DR SMR; P59575; -. DR STRING; 224915.bbp_506; -. DR KEGG; bab:bbp_506; -. DR eggNOG; COG0461; Bacteria. DR HOGENOM; CLU_074878_0_1_6; -. DR OMA; ACLDHLI; -. DR OrthoDB; 9779060at2; -. DR UniPathway; UPA00070; UER00119. DR Proteomes; UP000000601; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. 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:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:TreeGrafter. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0046132; P:pyrimidine ribonucleoside 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; PTHR46683; OROTATE PHOSPHORIBOSYLTRANSFERASE 1-RELATED; 1. DR PANTHER; PTHR46683:SF1; OROTATE PHOSPHORIBOSYLTRANSFERASE 1-RELATED; 1. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; PRTase-like; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Glycosyltransferase; Magnesium; Pyrimidine biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1..206 FT /note="Orotate phosphoribosyltransferase" FT /id="PRO_0000110682" FT BINDING 26 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:0000255|HAMAP-Rule:MF_01208" FT BINDING 72..73 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:0000255|HAMAP-Rule:MF_01208" FT BINDING 99 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:0000255|HAMAP-Rule:MF_01208" 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 /note="in other chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208" FT BINDING 103 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:0000255|HAMAP-Rule:MF_01208" FT BINDING 105 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:0000255|HAMAP-Rule:MF_01208" FT BINDING 124..132 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:0000255|HAMAP-Rule:MF_01208" FT BINDING 128 FT /ligand="orotate" FT /ligand_id="ChEBI:CHEBI:30839" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208" FT BINDING 157 FT /ligand="orotate" FT /ligand_id="ChEBI:CHEBI:30839" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01208" SQ SEQUENCE 206 AA; 23941 MW; 2247F905DCA16055 CRC64; MCKWKIQFLD FCLEKKVLKF GKFQLKSGKC SPYYFNSGLF NTGNDLQKLG YFYAKTIIES NLDYKAIFGV AYKGIPIVIS TAIALRKYFN INIPYCFNRK ELKKHGEKGN FIGQKLTGKI ILLDDVMTSG FSINDTINFI HSHANTKISG IIIALDRTRN INNKKNIQKN IEKKYNLKIF SIISILDIIN YFKKKKHLHI YLKYII //