ID   PYRE_RHILT              Reviewed;         223 AA.
AC   P42719;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Orotate phosphoribosyltransferase;
DE            Short=OPRT;
DE            Short=OPRTase;
DE            EC=2.4.2.10;
GN   Name=pyrE;
OS   Rhizobium leguminosarum bv. trifolii.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=9305779; DOI=10.1016/s0378-1119(97)00192-3;
RA   Bayles D.O., Fennington G.J. Jr., Hughes T.A.;
RT   "Sequence and phylogenetic analysis of the Rhizobium leguminosarum biovar
RT   trifolii pyrE gene, overproduction, purification and characterization of
RT   orotate phosphoribosyltransferase.";
RL   Gene 195:329-336(1997).
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:0000250,
CC       ECO:0000269|PubMed:9305779}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=27.6 uM for orotate {ECO:0000269|PubMed:9305779};
CC         Vmax=120 umol/min/mg enzyme {ECO:0000269|PubMed:9305779};
CC       pH dependence:
CC         Optimum pH is 10. {ECO:0000269|PubMed:9305779};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 1/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. PyrE subfamily. {ECO:0000305}.
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DR   EMBL; U08434; AAB52372.1; -; Unassigned_DNA.
DR   AlphaFoldDB; P42719; -.
DR   SMR; P42719; -.
DR   UniPathway; UPA00070; UER00119.
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-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.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Magnesium; Pyrimidine biosynthesis; Transferase.
FT   CHAIN           1..223
FT                   /note="Orotate phosphoribosyltransferase"
FT                   /id="PRO_0000110728"
FT   REGION          192..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         107
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"
FT   BINDING         108
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"
FT   BINDING         111
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"
FT   BINDING         113
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"
FT   BINDING         133..141
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"
FT   BINDING         137
FT                   /ligand="orotate"
FT                   /ligand_id="ChEBI:CHEBI:30839"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   223 AA;  24623 MW;  9C758A9C9E8D27D2 CRC64;
     MIQTTFPDRA VMAELLAKML WEIKAVHFNA AQPYKLASGM ASPVYIDCRK LLSFPRIRST
     VMDFAASTLL RDAGFEQFDC IAGGETAGIP FAALLADRLG LPMIYVRKQP KGHGRNAQIE
     GNMPEGSRVL VIEDLTTAGG SMFKFIDAVR AAGGIVDHGI ALFFYGIFGE QRFADGKVRL
     HHIATWRNVL PSPGSRSSST TRRCRKSSPS SMRRWLGRER MVA