PYRF_COCPS
ID PYRF_COCPS Reviewed; 274 AA.
AC Q4VWW3; E9DDC0; Q9C0T0;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE EC=4.1.1.23;
DE AltName: Full=OMP decarboxylase;
DE Short=OMPDCase;
DE Short=OMPdecase;
DE AltName: Full=Uridine 5'-monophosphate synthase;
DE Short=UMP synthase;
GN Name=URA3; ORFNames=CPSG_08082;
OS Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=443226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chen X., Hung C.-Y., Cole G.T.;
RT "Isolation and confirmation of function of the Coccidioides posadasii URA3
RT (orotidine-5'-monophosphate decarboxylase) gene.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 757 / Silveira;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J.,
RA Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M.,
RA Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Coccidioides posadasii strain Silveira.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-201.
RC STRAIN=RMSCC 2233 / TX2, RMSCC 2343 / MX1, and RMSCC 757 / Silveira;
RX PubMed=9144263; DOI=10.1073/pnas.94.10.5478;
RA Koufopanou V., Burt A., Taylor J.W.;
RT "Concordance of gene genealogies reveals reproductive isolation in the
RT pathogenic fungus Coccidioides immitis.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:5478-5482(1997).
RN [4]
RP ERRATUM OF PUBMED:9144263.
RA Koufopanou V., Burt A., Taylor J.W.;
RL Proc. Natl. Acad. Sci. U.S.A. 95:8414-8414(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP;
CC Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10110};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. {ECO:0000305}.
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DR EMBL; AY282521; AAQ16206.1; -; Genomic_DNA.
DR EMBL; GL636500; EFW15645.1; -; Genomic_DNA.
DR EMBL; AJ292100; CAC35044.1; -; Genomic_DNA.
DR EMBL; AJ292101; CAC35045.1; -; Genomic_DNA.
DR EMBL; AJ292102; CAC35046.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4VWW3; -.
DR SMR; Q4VWW3; -.
DR STRING; 443226.Q4VWW3; -.
DR EnsemblFungi; EFW15645; EFW15645; CPSG_08082.
DR VEuPathDB; FungiDB:CPSG_08082; -.
DR eggNOG; KOG1377; Eukaryota.
DR HOGENOM; CLU_030821_0_0_1; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000002497; Unassembled WGS sequence.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR014732; OMPdecase.
DR InterPro; IPR018089; OMPdecase_AS.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR32119:SF2; PTHR32119:SF2; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR01740; pyrF; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..274
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134657"
FT ACT_SITE 95
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 62..64
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 93..102
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 274 AA; 29683 MW; 642F23A5FAC8CC20 CRC64;
MASKSQFPYE DRARDHPNPL ARRLFQIATE KQSNVVVSAD VTTTKELLDL ADRLGPYMVV
LKTHIDILAD FSAETITGLQ SLSQKHNFLI FEDRKFVDIG NTVQKQYHGG ALHISEWAHI
VNATVLPGPG IIDALAQVAS APDFPHASDR GLLILATMTS KGSLATGQYT ELSVELARKY
KGFVLGFVAS RSLEGVETAG KADDEDFVLF TTGVNLASKG DALGQQYQTP ESAIGGGADF
IISGRGIYAA PDPVDAARRY QKAGWDAYLK RVGR
