ID PYRF_STRPN Reviewed; 233 AA. AC P0CB75; Q9ZHA7; DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 24-NOV-2009, sequence version 1. DT 27-MAR-2024, entry version 74. 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=SP_0701; OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=170187; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-334 / TIGR4; RX PubMed=11463916; DOI=10.1126/science.1061217; RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D., RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L., RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K., RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A., RA Morrison D.A., Hollingshead S.K., Fraser C.M.; RT "Complete genome sequence of a virulent isolate of Streptococcus RT pneumoniae."; RL Science 293:498-506(2001). 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 -!- INTERACTION: CC P0CB75; P63588: aroD; NbExp=2; IntAct=EBI-2207109, EBI-2207290; CC P0CB75; Q97SE6: gatA; NbExp=2; IntAct=EBI-2207109, EBI-2207039; CC P0CB75; Q97SE5: gatC; NbExp=2; IntAct=EBI-2207109, EBI-2207053; CC P0CB75; Q97NV3: groES; NbExp=2; IntAct=EBI-2207109, EBI-2206949; CC P0CB75; P65887: purA; NbExp=2; IntAct=EBI-2207109, EBI-2206955; CC P0CB75; P0CB75: pyrF; NbExp=2; IntAct=EBI-2207109, EBI-2207109; CC P0CB75; Q97NX5: scpA; NbExp=3; IntAct=EBI-2207109, EBI-2207368; CC P0CB75; Q97SR4: uppS; NbExp=2; IntAct=EBI-2207109, EBI-2206983; 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; AE005672; AAK74844.1; -; Genomic_DNA. DR PIR; C95081; C95081. DR RefSeq; WP_001206711.1; NZ_CP089948.1. DR AlphaFoldDB; P0CB75; -. DR SMR; P0CB75; -. DR IntAct; P0CB75; 7. DR PaxDb; 170187-SP_0701; -. DR EnsemblBacteria; AAK74844; AAK74844; SP_0701. DR KEGG; spn:SP_0701; -. DR eggNOG; COG0284; Bacteria. DR PhylomeDB; P0CB75; -. DR BioCyc; SPNE170187:G1FZB-719-MONOMER; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000000585; Chromosome. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-UniRule. 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 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 1: Evidence at protein level; KW Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1..233 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_0000134587" FT ACT_SITE 63 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 11 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 34 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 61..70 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 117 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 179 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 188 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 208 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 209 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" SQ SEQUENCE 233 AA; 25423 MW; 29AB36FBCBF7B4C9 CRC64; MREHRPIIAL DFPSFEAVKE FLALFPAEES LYLKVGMELY YAAGPEIVSY LKGLGHSVFL DLKLHDIPNT VKSAMKILSQ LGVDMTNVHA AGGVEMMKAA REGLGSQAKL IAVTQLTSTS EAQMQEFQNI QTSLQESVIH YAKKTAEAGL DGVVCSAQEV QVIKQATNPD FICLTPGIRP AGVAVGDQKR VMTPADAYQI GSDYIVVGRP ITQAEDPVAA YHAIKDEWTQ DWN //