PYRE_CRYNJ
ID PYRE_CRYNJ Reviewed; 225 AA.
AC P0CS95; P0CQ40; P18132; Q55PW2; Q5KDJ6;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Orotate phosphoribosyltransferase;
DE Short=OPRT;
DE Short=OPRTase;
DE EC=2.4.2.10;
GN Name=URA5; OrderedLocusNames=CNG03730;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2201894; DOI=10.1128/mcb.10.9.4538-4544.1990;
RA Edman J.C., Kwon-Chung K.J.;
RT "Isolation of the URA5 gene from Cryptococcus neoformans var. neoformans
RT and its use as a selective marker for transformation.";
RL Mol. Cell. Biol. 10:4538-4544(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=J15, J17, J19, J21, J24, J25, and J26;
RX PubMed=8576325; DOI=10.1128/jcm.33.11.2818-2822.1995;
RA Chen F., Currie B.P., Chen L.C., Spitzer S.G., Spitzer E.D., Casadevall A.;
RT "Genetic relatedness of Cryptococcus neoformans clinical isolates grouped
RT with the repetitive DNA probe CNRE-1.";
RL J. Clin. Microbiol. 33:2818-2822(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C24, C25, C5, C7, E12, E4, and E9;
RA Franzot S.P., Hamdan J.S., Casadevall A.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=184, 3502, and ATCC 24064 / CBS 7812 / 68;
RA Franzot S.P., Fries B.C., Casadevall A.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WM628;
RA Jackson S.;
RT "The URA5 gene of Cryptococcus neoformans: its use as an auxotrophic
RT selection marker for biolistic transformation and as a target for RFLP
RT targeting.";
RL Thesis (2001), University of Western Sydney / Campbelltown, Australia.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; M34606; AAA33076.1; -; Genomic_DNA.
DR EMBL; L38582; AAA99182.1; -; Genomic_DNA.
DR EMBL; L38583; AAA99183.1; -; Genomic_DNA.
DR EMBL; L38584; AAA99184.1; -; Genomic_DNA.
DR EMBL; L38585; AAA99185.1; -; Genomic_DNA.
DR EMBL; L38586; AAA99186.1; -; Genomic_DNA.
DR EMBL; L38587; AAA99187.1; -; Genomic_DNA.
DR EMBL; L38588; AAA99188.1; -; Genomic_DNA.
DR EMBL; U67723; AAB17140.1; -; Genomic_DNA.
DR EMBL; U67724; AAB17141.1; -; Genomic_DNA.
DR EMBL; U67725; AAB17142.1; -; Genomic_DNA.
DR EMBL; U67726; AAB17143.1; -; Genomic_DNA.
DR EMBL; U67728; AAB17145.1; -; Genomic_DNA.
DR EMBL; U67730; AAB17147.1; -; Genomic_DNA.
DR EMBL; U67731; AAB17148.1; -; Genomic_DNA.
DR EMBL; AF032430; AAB86885.1; -; Genomic_DNA.
DR EMBL; AF032432; AAB86887.1; -; Genomic_DNA.
DR EMBL; AF032434; AAB86889.1; -; Genomic_DNA.
DR EMBL; AJ555829; CAD88485.1; -; Genomic_DNA.
DR EMBL; AE017347; AAW44772.1; -; Genomic_DNA.
DR PIR; A36459; A36459.
DR RefSeq; XP_572079.1; XM_572079.1.
DR AlphaFoldDB; P0CS95; -.
DR SMR; P0CS95; -.
DR STRING; 5207.AAW44772; -.
DR PaxDb; P0CS95; -.
DR EnsemblFungi; AAW44772; AAW44772; CNG03730.
DR GeneID; 3258511; -.
DR KEGG; cne:CNG03730; -.
DR VEuPathDB; FungiDB:CNG03730; -.
DR eggNOG; KOG1377; Eukaryota.
DR HOGENOM; CLU_074878_0_1_1; -.
DR InParanoid; P0CS95; -.
DR OMA; MKAYQRQ; -.
DR OrthoDB; 1372586at2759; -.
DR UniPathway; UPA00070; UER00119.
DR PHI-base; PHI:687; -.
DR Proteomes; UP000002149; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome;
KW Transferase.
FT CHAIN 1..225
FT /note="Orotate phosphoribosyltransferase"
FT /id="PRO_0000110796"
FT BINDING 31
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 39..40
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000250"
FT BINDING 78..79
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 105
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 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 /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 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 130..138
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 134
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="orotate"
FT /ligand_id="ChEBI:CHEBI:30839"
FT /evidence="ECO:0000250"
FT VARIANT 8
FT /note="S -> F (in strain: J21)"
FT VARIANT 11
FT /note="V -> I (in strain: J15, J17, J24, J25, C5, C7, C24,
FT E4, E9, E12, 184 and ATCC 24064)"
FT VARIANT 57
FT /note="A -> G (in strain: J26 and J19)"
FT VARIANT 69
FT /note="D -> N (in strain: J25)"
SQ SEQUENCE 225 AA; 24419 MW; A36EEF8D54CDEB81 CRC64;
MSSQALDSAK VAFIEAAIEH GVLLFGNFTL KSGRQSPYFF NAGLLYSSSL LSTTAQAYAK
VLSSSRIPDF DVLFGPAYKG ISLAAVSAVS LYQQTGKDIG YCYNRKEKKD HGEGGTMVGA
PLKGRIVIID DVLTSGKAIR EAIDILKASP EAKLVGIVQL VDRQEKGQSG SGKSTVQEVE
EEFGVPVEPI IGLDDIVKYL ESSGKWEKEL QEVRKYRAEY GVQRS
