ID   PYRE_COLGR              Reviewed;         233 AA.
AC   P35788;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Orotate phosphoribosyltransferase;
DE            Short=OPRT;
DE            Short=OPRTase;
DE            EC=2.4.2.10;
GN   Name=PYR1;
OS   Colletotrichum graminicola (Maize anthracnose fungus) (Glomerella
OS   graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=31870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1435732; DOI=10.1007/bf00286183;
RA   Rasmussen J.B., Panaccione D.G., Fang G.C., Hanau R.M.;
RT   "The PYR1 gene of the plant pathogenic fungus Colletotrichum graminicola:
RT   selection by intraspecific complementation and sequence analysis.";
RL   Mol. Gen. Genet. 235:74-80(1992).
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   -!- 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   -!- 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; S47907; AAB24061.1; -; Genomic_DNA.
DR   PIR; S30118; S30118.
DR   AlphaFoldDB; P35788; -.
DR   SMR; P35788; -.
DR   PRIDE; P35788; -.
DR   VEuPathDB; FungiDB:GLRG_02772; -.
DR   UniPathway; UPA00070; UER00119.
DR   GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
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.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Pyrimidine biosynthesis; Transferase.
FT   CHAIN           1..233
FT                   /note="Orotate phosphoribosyltransferase"
FT                   /id="PRO_0000110795"
FT   BINDING         29
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         37..38
FT                   /ligand="orotate"
FT                   /ligand_id="ChEBI:CHEBI:30839"
FT                   /evidence="ECO:0000250"
FT   BINDING         79..80
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         109
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         110
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         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         115
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         135..143
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         139
FT                   /ligand="orotate"
FT                   /ligand_id="ChEBI:CHEBI:30839"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="orotate"
FT                   /ligand_id="ChEBI:CHEBI:30839"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   233 AA;  25232 MW;  1E6CDB822CA29664 CRC64;
     MASQLPPYKQ DFLKAAIAGV LKFGSFELKS KRISPYFFNA GDFYRADLLR AISLAYAHTV
     IEAREATGLD FDVVFGPAYK GIPLATSTTD KLAELDPARY GTTCYSFDRK EAKDHGEGGN
     IVGAPLKGQK VLIVDDVITA GTAKREAIAK IRKEGGEVVG IVVALDRMEK LPAADGDDSK
     PGPSALGEIK KEYGIPIFSI LTLDDIIEGA KSFASAEDIK RTEEYRAKYK ATD