ID PYRF_USTMA Reviewed; 283 AA. AC P15188; A0A0D1DTT3; Q4P6P9; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. DT 27-MAR-2024, entry version 129. 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=PYR6; ORFNames=UMAG_04214; OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina; OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago. OX NCBI_TaxID=237631; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2673937; DOI=10.1016/0378-1119(89)90095-4; RA Kronstad J.W., Wang J., Covert S.F., Holden D.W., McKnight G.L., RA Leong S.A.; RT "Isolation of metabolic genes and demonstration of gene disruption in the RT phytopathogenic fungus Ustilago maydis."; RL Gene 79:97-106(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=521 / FGSC 9021; RX PubMed=17080091; DOI=10.1038/nature05248; RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W., RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., RA Birren B.W.; RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago RT maydis."; RL Nature 444:97-101(2006). RN [3] RP GENOME REANNOTATION. RC STRAIN=521 / FGSC 9021; RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.; RL Submitted (SEP-2014) 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; M27247; -; NOT_ANNOTATED_CDS; Unassigned_DNA. DR EMBL; CM003151; KIS67714.1; -; Genomic_DNA. DR PIR; JQ0013; DCUSOP. DR RefSeq; XP_011390696.1; XM_011392394.1. DR AlphaFoldDB; P15188; -. DR SMR; P15188; -. DR STRING; 237631.P15188; -. DR EnsemblFungi; KIS67714; KIS67714; UMAG_04214. DR GeneID; 23564467; -. DR KEGG; uma:UMAG_04214; -. DR VEuPathDB; FungiDB:UMAG_04214; -. DR eggNOG; KOG1377; Eukaryota. DR HOGENOM; CLU_030821_0_0_1; -. DR InParanoid; P15188; -. DR OMA; CLIKTHI; -. DR OrthoDB; 922at2759; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000000561; Chromosome 12. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase 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 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 2: Evidence at transcript level; KW Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1..283 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_0000134689" 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 220 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 239 FT /ligand="substrate" FT /evidence="ECO:0000250" FT CONFLICT 244 FT /note="A -> T (in Ref. 1)" FT /evidence="ECO:0000305" SQ SEQUENCE 283 AA; 30864 MW; 7C2F0DBB3C7DDF47 CRC64; MSSITLQSYA SRAAKQPNPA AKALLECMER KQTNLCVSID VTNKQDLLDV CEAVGRNVCL VKTHIDIVED FDMDLVHQLT QLSEKHDFLI FEDRKFADIG NTVSLQYSAG VHKIASWSHI TNAHLVPGPS VISGLAKVGQ PLGRGLLLLA EMSSEGALTK GDYTQACVDE AHKDTTGFVC GFIAMSRVDE RERANTHRDL LILTPGVGLD VKGDGLGQQY RTPDQVIRES GCDVIIVGRG IYGALTTEEG KADKKAAFAK VSEQGERYKT AGWDAYLKRI GQK //