ID PYRF_MAGMU Reviewed; 284 AA. AC Q12604; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 75. 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 Magnusiomyces magnusii (Yeast) (Dipodascus magnusii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Dipodascaceae; Magnusiomyces. OX NCBI_TaxID=43963; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=270; RA Adamikova L., Nosek J., Tomaska L.; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. 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; X95886; CAA65135.1; -; Genomic_DNA. DR AlphaFoldDB; Q12604; -. DR SMR; Q12604; -. 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..284 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_0000134660" FT ACT_SITE 98 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10110" FT BINDING 42 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 64..66 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 96..105 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 237 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 255 FT /ligand="substrate" FT /evidence="ECO:0000250" SQ SEQUENCE 284 AA; 31448 MW; 0E8F8A38FDB8792E CRC64; MSTSTQITKP YSTRALTHQS QTARRLLKLM SDKRTNLCAS LDVTTSAELL SLADKLGPYI CMVKTHVDII SDFTYDETVV KLVALAKKHG FMIFEDRKFA DIGNTVKNQY SKGVYRIVEW ADITNAHSVP GEGIINGLRE AANEYVESEK AKGGECENLD RGLIMLAELS SKGSLATGSY TTKTVELAHN NSDFVFGFIA QNRMEEVQDS EGNYEDWLIL TPGVGLDDKG DGLGQQYRTV DTVIKNGSDV IIVGRGLFGK GRDPVVEGKR YRDAGWKAYE ERIN //