ID C6XTP1_PEDHD Unreviewed; 221 AA. AC C6XTP1; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 28-JAN-2026, entry version 96. 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=Phep_1463 {ECO:0000313|EMBL:ACU03677.1}; OS Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 OS / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3). OC Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia; OC Sphingobacteriales; Sphingobacteriaceae; Pedobacter. OX NCBI_TaxID=485917 {ECO:0000313|EMBL:ACU03677.1, ECO:0000313|Proteomes:UP000000852}; RN [1] {ECO:0000313|EMBL:ACU03677.1, ECO:0000313|Proteomes:UP000000852} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / RC NCIMB 9290 / NRRL B-14731 / HIM 762-3 RC {ECO:0000313|Proteomes:UP000000852}; RX PubMed=21304637; DOI=10.4056/sigs.22138; RA Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A., RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y.J., Jeffries C.C., Saunders E., Chertkov O., RA Brettin T., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.; RT "Complete genome sequence of Pedobacter heparinus type strain (HIM 762- RT 3)."; RL Stand. Genomic Sci. 1:54-62(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; CP001681; ACU03677.1; -; Genomic_DNA. DR RefSeq; WP_012781621.1; NC_013061.1. DR AlphaFoldDB; C6XTP1; -. DR STRING; 485917.Phep_1463; -. DR KEGG; phe:Phep_1463; -. DR eggNOG; COG0461; Bacteria. DR HOGENOM; CLU_074878_1_1_10; -. DR OrthoDB; 9802134at2; -. DR UniPathway; UPA00070; UER00119. DR Proteomes; UP000000852; 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:UP000000852}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01208}. FT DOMAIN 52..167 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 221 AA; 24364 MW; 7CC3DDE6C9085AF2 CRC64; MYNKSDIELK VAEFLLQIKA IKLQPANPFT WASGWKSPIY CDNRVTLSHP SVRTYIRQKL SQLIQEEFGS VDLIAGVATA GIPQGALVAQ ELGLPFAYVR AKAKEHGTGS LIEGEIVEGQ RVVVIEDLIS TGKSSLQAVE ALRKAGLSVA GLVAIFTYGF DQADENFAAA KCRYATLSNY NTLIEYAAEH SFIAQKDVDL LTKWRRNPAE WGKELEELNN S //