ID PYRF_XANCP Reviewed; 243 AA. AC Q8P3D7; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 109. DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200}; DE EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01200}; DE AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200}; DE Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01200}; DE Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01200}; GN Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01200}; GN OrderedLocusNames=XCC4134; OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB OS 528 / LMG 568 / P 25). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=190485; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25; RX PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing host RT specificities."; RL Nature 417:459-463(2002). CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate CC (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000255|HAMAP- CC Rule:MF_01200}. 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|HAMAP-Rule:MF_01200}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC UMP from orotate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01200}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01200}. CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01200}. 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; AE008922; AAM43355.1; -; Genomic_DNA. DR RefSeq; NP_639473.1; NC_003902.1. DR RefSeq; WP_011039203.1; NC_003902.1. DR AlphaFoldDB; Q8P3D7; -. DR SMR; Q8P3D7; -. DR STRING; 190485.XCC4134; -. DR EnsemblBacteria; AAM43355; AAM43355; XCC4134. DR KEGG; xcc:XCC4134; -. DR PATRIC; fig|190485.4.peg.4429; -. DR eggNOG; COG0284; Bacteria. DR HOGENOM; CLU_067069_1_0_6; -. DR OrthoDB; 9806203at2; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000001010; Chromosome. 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 HAMAP; MF_01200_B; OMPdecase_type1_B; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR014732; OMPdecase. DR InterPro; IPR018089; OMPdecase_AS. DR InterPro; IPR047596; OMPdecase_bac. DR InterPro; IPR001754; OMPdeCOase_dom. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR NCBIfam; TIGR01740; pyrF; 1. DR PANTHER; PTHR32119; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1. DR PANTHER; PTHR32119:SF2; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 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..243 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_0000134603" FT ACT_SITE 71 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 19 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 41 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 69..78 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 124 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 185 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 194 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 214 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 215 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" SQ SEQUENCE 243 AA; 25688 MW; AC24F2E0D839BB64 CRC64; MNRPPLPLAA HDRLIFALDV PGHDEAIAWV DRLGESVAFY KIGMELLASG EYFHVLDALA KRNKRVFVDL KFFDIPATVA GTIRRLSQWP VSYCTVHGWH AGMLEAAAAA NQGDMRLLAV TVLTSMGRPD LAAMGIDREP VDVVVERALA AQAAGIDGVI ASGQEAGMIR RATGPAFSIV CPGIRPGGPV GDDQQRTVGV AQAFADGADA IVVGRPIRLA NDPAAAAAAI QAEIRAAVVQ HRD //