PYRX_YEAST
ID PYRX_YEAST Reviewed; 227 AA.
AC P30402; D6W097;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Orotate phosphoribosyltransferase 2;
DE Short=OPRT 2;
DE Short=OPRTase 2;
DE EC=2.4.2.10 {ECO:0000305|PubMed:2182197};
GN Name=URA10; OrderedLocusNames=YMR271C; ORFNames=YM8156.13C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2182197; DOI=10.1007/bf00312853;
RA de Montigny J., Kern L., Hubert J.-C., Lacroute F.;
RT "Cloning and sequencing of URA10, a second gene encoding orotate
RT phosphoribosyl transferase in Saccharomyces cerevisiae.";
RL Curr. Genet. 17:105-111(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7882422; DOI=10.1007/bf00310492;
RA Hohmann S., Van Dijck P., Luyten K., Thevelein J.M.;
RT "The byp1-3 allele of the Saccharomyces cerevisiae GGS1/TPS1 gene and its
RT multi-copy suppressor tRNA(GLN) (CAG): Ggs1/Tps1 protein levels restraining
RT growth on fermentable sugars and trehalose accumulation.";
RL Curr. Genet. 26:295-301(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(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:0000305|PubMed:2182197}.
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:0000305|PubMed:2182197};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10382;
CC Evidence={ECO:0000305|PubMed:2182197};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 1/2. {ECO:0000305|PubMed:2182197}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: There are two genes coding for OPRT in yeast.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 815 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrE subfamily. {ECO:0000305}.
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DR EMBL; X52194; CAA36440.1; -; Genomic_DNA.
DR EMBL; X66375; CAA47016.1; -; Genomic_DNA.
DR EMBL; Z49260; CAA89254.1; -; Genomic_DNA.
DR EMBL; AY557976; AAS56302.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10171.1; -; Genomic_DNA.
DR PIR; S48223; XJBY10.
DR RefSeq; NP_013998.1; NM_001182778.1.
DR AlphaFoldDB; P30402; -.
DR SMR; P30402; -.
DR BioGRID; 35449; 42.
DR DIP; DIP-2790N; -.
DR IntAct; P30402; 2.
DR MINT; P30402; -.
DR STRING; 4932.YMR271C; -.
DR MaxQB; P30402; -.
DR PaxDb; P30402; -.
DR PRIDE; P30402; -.
DR EnsemblFungi; YMR271C_mRNA; YMR271C; YMR271C.
DR GeneID; 855313; -.
DR KEGG; sce:YMR271C; -.
DR SGD; S000004884; URA10.
DR VEuPathDB; FungiDB:YMR271C; -.
DR eggNOG; KOG1377; Eukaryota.
DR GeneTree; ENSGT00390000001856; -.
DR HOGENOM; CLU_074878_0_1_1; -.
DR InParanoid; P30402; -.
DR OMA; ANVFYLY; -.
DR BioCyc; MetaCyc:YMR271C-MON; -.
DR BioCyc; YEAST:YMR271C-MON; -.
DR UniPathway; UPA00070; UER00119.
DR PRO; PR:P30402; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P30402; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IMP:SGD.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IGI:SGD.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0046132; P:pyrimidine ribonucleoside biosynthetic process; IMP:SGD.
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 2"
FT /id="PRO_0000110805"
FT BINDING 41..42
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"
FT CONFLICT 143
FT /note="A -> R (in Ref. 1; CAA36440)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="V -> L (in Ref. 1; CAA36440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 24811 MW; ADA6C21380935EDD CRC64;
MSASTTSLEE YQKTFLELGL ECKALRFGSF KLNSGRQSPY FFNLSLFNSG KLLANLATAY
ATAIIQSELK FDVIFGPAYK GIPLAAIVCV KLAEIGGTKF QGIQYAFNRK KVKDHGEGGI
IVGASLEDKR VLIIDDVMTA GTAINEAFEI ISIAQGRVVG CIVALDRQEV IHESDPERTS
ATQSVSKRYN VPVLSIVSLT QVVQFMGNRL SPEQKSAIEN YRKAYGI
