ID PYRF_SALTI Reviewed; 245 AA. AC P58643; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 1. DT 24-JAN-2024, entry version 127. 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=STY1344, t1620; OS Salmonella typhi. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=90370; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT18; RX PubMed=11677608; DOI=10.1038/35101607; RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T., RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., RA Barrell B.G.; RT "Complete genome sequence of a multiple drug resistant Salmonella enterica RT serovar Typhi CT18."; RL Nature 413:848-852(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700931 / Ty2; RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003; RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., RA Kodoyianni V., Schwartz D.C., Blattner F.R.; RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and RT CT18."; RL J. Bacteriol. 185:2330-2337(2003). 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; AL513382; CAD08424.1; -; Genomic_DNA. DR EMBL; AE014613; AAO69247.1; -; Genomic_DNA. DR RefSeq; NP_455790.1; NC_003198.1. DR RefSeq; WP_001763993.1; NZ_WSUR01000006.1. DR AlphaFoldDB; P58643; -. DR SMR; P58643; -. DR STRING; 220341.gene:17585304; -. DR KEGG; stt:t1620; -. DR KEGG; sty:STY1344; -. DR PATRIC; fig|220341.7.peg.1353; -. DR eggNOG; COG0284; Bacteria. DR HOGENOM; CLU_067069_0_0_6; -. DR OMA; FWKVGLE; -. DR OrthoDB; 9806203at2; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000000541; Chromosome. DR Proteomes; UP000002670; Chromosome. 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 3: Inferred from homology; KW Decarboxylase; Lyase; Pyrimidine biosynthesis. FT CHAIN 1..245 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_0000134570" FT ACT_SITE 73 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 22 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 44 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 71..80 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 131 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 192 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 201 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 221 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 222 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" SQ SEQUENCE 245 AA; 26256 MW; 81596122D76E7C45 CRC64; MTFTASSSSC AITESPVVVA LDYHERDKAL AFVDKIDPRD CRLKVGKEMF TLFGPQLVRD LQQRGFDVFL DLKFHDIPNT TARAVAAAAD LGVWMVNVHA SGGARMMAAA RDALAPFSKD APLLIAVTVL TSMGTSDLHD LGVTLSPAEH AERLARLTQQ CGLDGVVCSA QEAVRFKQAF GAAFKLVTPG IRPAGSEAGD QRRIMTPEQA LSAGVDYMVI GRPVTQSVDP AQTLKDINAS LKREA //