ID PYRF_TORDE Reviewed; 264 AA. AC Q8J0E6; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 73. 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; OS Torulaspora delbrueckii (Yeast) (Candida colliculosa). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Torulaspora. OX NCBI_TaxID=4950; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=IGC 5321; RX PubMed=12478590; DOI=10.1002/yea.929; RA Hernandez-Lopez M.J., Prieto J.A., Randez-Gil F.; RT "Isolation and characterization of the gene URA3 encoding the orotidine 5'- RT phosphate decarboxylase from Torulaspora delbrueckii."; RL Yeast 19:1431-1435(2002). 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; AF518402; AAN71840.1; -; Genomic_DNA. DR AlphaFoldDB; Q8J0E6; -. DR SMR; Q8J0E6; -. DR UniPathway; UPA00070; UER00120. 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. FT CHAIN 1..264 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_0000134686" FT ACT_SITE 93 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10110" FT BINDING 37 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 59..61 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 91..100 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 217 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 235 FT /ligand="substrate" FT /evidence="ECO:0000250" SQ SEQUENCE 264 AA; 29099 MW; 65655EB51BAF7E7C CRC64; MSVATYQERA AKHPSPVASK LLNLMHEKKT NLCASLDVNT TEELLKLVDT LGPYICLLKT HIDIISDFSI DGTVKPLKEL AKKHNFMIFE DRKFADIGNT VKLQYSSGVY RIAEWADITN AHGVTGAGIV TGLKQAAQET TNEPRGLLML AELSSKGSLA HGEYTQGTVE IAKTDKDFVI GFIAQRDMGG REEGYDWLIM TPGVGLDDKG DALGQQYRTV DEVVSTGSDI IIVGRGLFAK GRDPRVEGER YRKAGWEAYE KRCQ //