PYRE_CAEEL
ID PYRE_CAEEL Reviewed; 227 AA.
AC O61790;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Orotate phosphoribosyltransferase {ECO:0000303|PubMed:19645718};
DE Short=OPRT {ECO:0000303|PubMed:19645718};
DE Short=OPRTase {ECO:0000303|PubMed:19645718};
DE EC=2.4.2.10 {ECO:0000269|PubMed:19645718};
DE AltName: Full=Uracil phosphoribosyltransferase {ECO:0000305|PubMed:19645718};
DE EC=2.4.2.9 {ECO:0000269|PubMed:19645718};
GN ORFNames=R12E2.11 {ECO:0000312|WormBase:R12E2.11};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND TISSUE SPECIFICITY.
RX PubMed=19645718; DOI=10.1111/j.1742-4658.2009.07168.x;
RA Kim S., Park D.H., Kim T.H., Hwang M., Shim J.;
RT "Functional analysis of pyrimidine biosynthesis enzymes using the
RT anticancer drug 5-fluorouracil in Caenorhabditis elegans.";
RL FEBS J. 276:4715-4726(2009).
CC -!- FUNCTION: Phosphoribosyltransferase which catalyzes the formation of
CC UMP from uracil in vitro and thus may be involved in UMP biosynthesis
CC via the salvage pathway. May also participate in the first step of UMP
CC synthesis by catalyzing the formation of orotidine 5'-phosphate, a UMP
CC precursor, from orotate. {ECO:0000269|PubMed:19645718}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-
CC ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380,
CC ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538,
CC ChEBI:CHEBI:58017; EC=2.4.2.10;
CC Evidence={ECO:0000269|PubMed:19645718};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9;
CC Evidence={ECO:0000269|PubMed:19645718};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 1/2. {ECO:0000269|PubMed:19645718}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uracil: step 1/1. {ECO:0000269|PubMed:19645718}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P08870}.
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscles, spermatheca and
CC vulva muscles. {ECO:0000269|PubMed:19645718}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrE subfamily. {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; BX284601; CCD65178.1; -; Genomic_DNA.
DR PIR; T33094; T33094.
DR RefSeq; NP_491317.1; NM_058916.4.
DR AlphaFoldDB; O61790; -.
DR SMR; O61790; -.
DR IntAct; O61790; 1.
DR STRING; 6239.R12E2.11; -.
DR EPD; O61790; -.
DR PaxDb; O61790; -.
DR PeptideAtlas; O61790; -.
DR EnsemblMetazoa; R12E2.11.1; R12E2.11.1; WBGene00020036.
DR GeneID; 172008; -.
DR KEGG; cel:CELE_R12E2.11; -.
DR UCSC; R12E2.11; c. elegans.
DR CTD; 172008; -.
DR WormBase; R12E2.11; CE18143; WBGene00020036; -.
DR eggNOG; KOG1377; Eukaryota.
DR HOGENOM; CLU_074878_2_0_1; -.
DR InParanoid; O61790; -.
DR OMA; ENPFTWA; -.
DR OrthoDB; 1303452at2759; -.
DR PhylomeDB; O61790; -.
DR UniPathway; UPA00070; UER00119.
DR UniPathway; UPA00574; UER00636.
DR PRO; PR:O61790; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00020036; Expressed in larva and 4 other tissues.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IDA:WormBase.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0006222; P:UMP biosynthetic process; IDA:WormBase.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
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; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR00336; pyrE; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Pyrimidine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..227
FT /note="Orotate phosphoribosyltransferase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000439230"
FT BINDING 51
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:0000250|UniProtKB:P08870"
FT BINDING 119
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:0000250|UniProtKB:P08870"
FT BINDING 120
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:0000250|UniProtKB:P08870"
FT BINDING 123
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:0000250|UniProtKB:P08870"
FT BINDING 149
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000250|UniProtKB:P08870"
FT BINDING 177
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000250|UniProtKB:P08870"
SQ SEQUENCE 227 AA; 25192 MW; 164C1B151B207482 CRC64;
MTAATATANG NHSIEDPVVM KVQAASPIQE TDFFENLYQM ECFRTGEFYL KSGQMTPIYI
DLRRIMSSPR VLRMAAQAMC EKIVASNLKF DYVVGVPYAA LPLATLVSDI LNVPMLMKRK
EAKAYGTKQL IEGVYQPGGT VLLVEDVVTS GESIRETAEA IRNENLLVTD AIAVLDRQQG
ATANLAEDNL NFLSFLTMEK ILDGLITKNE MTEERKHEII AHLAKPF