PYRE_YEAST
ID PYRE_YEAST Reviewed; 226 AA.
AC P13298; D6W0H8;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Orotate phosphoribosyltransferase 1;
DE Short=OPRT 1;
DE Short=OPRTase 1;
DE EC=2.4.2.10;
GN Name=URA5; Synonyms=PYR5; OrderedLocusNames=YML106W; ORFNames=YM8339.13;
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].
RX PubMed=2651891; DOI=10.1007/bf00427043;
RA de Montigny J., Belarbi A., Hubert J.-C., Lacroute F.;
RT "Structure and expression of the URA5 gene of Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 215:455-462(1989).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-226.
RA Stirling C.J.;
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213 AND SER-225, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(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: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 -!- MISCELLANEOUS: There are two genes coding for OPRT in yeast.
CC -!- MISCELLANEOUS: Present with 39300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. PyrE subfamily. {ECO:0000305}.
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DR EMBL; X14795; CAA32901.1; -; Genomic_DNA.
DR EMBL; Z49210; CAA89112.1; -; Genomic_DNA.
DR EMBL; AY693160; AAT93179.1; -; Genomic_DNA.
DR EMBL; X65783; CAA46665.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09792.1; -; Genomic_DNA.
DR PIR; S53966; XJBY5.
DR RefSeq; NP_013601.1; NM_001182468.1.
DR PDB; 2PRY; X-ray; 2.35 A; A=1-226.
DR PDB; 2PRZ; X-ray; 1.90 A; A/B/C/D=1-226.
DR PDB; 2PS1; X-ray; 1.75 A; A/B=1-226.
DR PDB; 4WML; X-ray; 1.73 A; A=2-226.
DR PDB; 4WN3; X-ray; 1.80 A; A=1-226.
DR PDBsum; 2PRY; -.
DR PDBsum; 2PRZ; -.
DR PDBsum; 2PS1; -.
DR PDBsum; 4WML; -.
DR PDBsum; 4WN3; -.
DR AlphaFoldDB; P13298; -.
DR BMRB; P13298; -.
DR SMR; P13298; -.
DR BioGRID; 35037; 173.
DR DIP; DIP-4859N; -.
DR IntAct; P13298; 4.
DR MINT; P13298; -.
DR STRING; 4932.YML106W; -.
DR iPTMnet; P13298; -.
DR MaxQB; P13298; -.
DR PaxDb; P13298; -.
DR PRIDE; P13298; -.
DR TopDownProteomics; P13298; -.
DR EnsemblFungi; YML106W_mRNA; YML106W; YML106W.
DR GeneID; 854865; -.
DR KEGG; sce:YML106W; -.
DR SGD; S000004574; URA5.
DR VEuPathDB; FungiDB:YML106W; -.
DR eggNOG; KOG1377; Eukaryota.
DR GeneTree; ENSGT00390000001856; -.
DR HOGENOM; CLU_074878_0_1_1; -.
DR InParanoid; P13298; -.
DR OMA; MKAYQRQ; -.
DR BioCyc; MetaCyc:YML106W-MON; -.
DR BioCyc; YEAST:YML106W-MON; -.
DR BRENDA; 2.4.2.10; 984.
DR UniPathway; UPA00070; UER00119.
DR EvolutionaryTrace; P13298; -.
DR PRO; PR:P13298; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P13298; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IDA:SGD.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IMP: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; IDA: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 3D-structure; Glycosyltransferase; Phosphoprotein; Pyrimidine biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..226
FT /note="Orotate phosphoribosyltransferase 1"
FT /id="PRO_0000110804"
FT BINDING 30
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 38..39
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000250"
FT BINDING 76..77
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 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:0000250"
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 /note="in other chain"
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 /evidence="ECO:0000250"
FT BINDING 112
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 132..140
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 136
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000250"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 150
FT /note="N -> S (in Ref. 1; CAA32901)"
FT /evidence="ECO:0000305"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:4WML"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:4WML"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4WN3"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:4WML"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:4WML"
FT HELIX 47..63
FT /evidence="ECO:0007829|PDB:4WML"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:4WML"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:4WML"
FT HELIX 78..92
FT /evidence="ECO:0007829|PDB:4WML"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:4WML"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:4WML"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:4WML"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:4WML"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:4WN3"
FT HELIX 139..150
FT /evidence="ECO:0007829|PDB:4WML"
FT STRAND 154..163
FT /evidence="ECO:0007829|PDB:4WML"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:4WML"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:4WML"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:4WML"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:4WML"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:4WML"
FT HELIX 209..222
FT /evidence="ECO:0007829|PDB:4WML"
SQ SEQUENCE 226 AA; 24664 MW; ECF3A01EB35BC03F CRC64;
MPIMLEDYQK NFLELAIECQ ALRFGSFKLK SGRESPYFFN LGLFNTGKLL SNLATAYAIA
IIQSDLKFDV IFGPAYKGIP LAAIVCVKLA EIGGSKFQNI QYAFNRKEAK DHGEGGIIVG
SALENKRILI IDDVMTAGTA INEAFEIISN AKGQVVGSII ALDRQEVVST DDKEGLSATQ
TVSKKYGIPV LSIVSLIHII TYLEGRITAE EKSKIEQYLQ TYGASA
