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 27-MAR-2024, entry version 77. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 VEuPathDB; FungiDB:CPSG_08082; -. DR VEuPathDB; FungiDB:D8B26_002262; -. DR eggNOG; KOG1377; Eukaryota. DR HOGENOM; CLU_030821_0_0_1; -. DR OMA; CLIKTHI; -. 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 CDD; cd04725; OMP_decarboxylase_like; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 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 NCBIfam; TIGR01740; pyrF; 1. DR PANTHER; PTHR19278; OROTATE PHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR19278:SF9; URIDINE 5'-MONOPHOSPHATE SYNTHASE; 1. DR Pfam; PF00215; OMPdecase; 1. DR SMART; SM00934; OMPdecase; 1. DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 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 //