ID PYRF_SHIFL Reviewed; 245 AA. AC Q83RM1; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 125. 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=SF1285, S1368; OS Shigella flexneri. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=623; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 / Serotype 2a; RX PubMed=12384590; DOI=10.1093/nar/gkf566; RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.; RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity RT through comparison with genomes of Escherichia coli K12 and O157."; RL Nucleic Acids Res. 30:4432-4441(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003; RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.; RT "Complete genome sequence and comparative genomics of Shigella flexneri RT serotype 2a strain 2457T."; RL Infect. Immun. 71:2775-2786(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; AE005674; AAN42897.1; -; Genomic_DNA. DR EMBL; AE014073; AAP16781.1; -; Genomic_DNA. DR RefSeq; NP_707190.1; NC_004337.2. DR RefSeq; WP_000176258.1; NZ_WPGW01000009.1. DR AlphaFoldDB; Q83RM1; -. DR SMR; Q83RM1; -. DR STRING; 198214.SF1285; -. DR PaxDb; 198214-SF1285; -. DR GeneID; 1024264; -. DR KEGG; sfl:SF1285; -. DR KEGG; sfx:S1368; -. DR PATRIC; fig|198214.7.peg.1507; -. DR HOGENOM; CLU_067069_0_0_6; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000001006; Chromosome. DR Proteomes; UP000002673; 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; Reference proteome. FT CHAIN 1..245 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_0000134573" 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; 26295 MW; EBCA7BDE333375EA CRC64; MTLTASSSSR AVTNSPVVVA LDYHNCDDAL SFVDKIDPRD CRLKVGKEMF TLFGPQFVRE LQQRGFDIFL DLKFHDIPNT AAHAVAAAAD LGVWMVNVHA SGGARMMTAA REALVPFGKD APLLIAVTVL TSMEASDLAD LGVTLSPADY AERLAALTQK CDLDGVVCSA QEAVRFKQVF GQEFKLVTPG IRPQGSEAGD QRRIMTPEQA LAAGVDYMVI GRPVTQSVDP AQTLKAINAS LQRSA //