ID PYRF_ECO57 Reviewed; 245 AA. AC P58640; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 1. DT 27-MAR-2024, entry version 129. 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=Z2525, ECs1854; OS Escherichia coli O157:H7. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX PubMed=11206551; DOI=10.1038/35054089; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., RA Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; RX PubMed=11258796; DOI=10.1093/dnares/8.1.11; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., RA Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and RT genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(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 -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01200}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB35277.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AE005174; AAG56532.1; -; Genomic_DNA. DR EMBL; BA000007; BAB35277.2; ALT_INIT; Genomic_DNA. DR PIR; F90860; F90860. DR PIR; H85758; H85758. DR RefSeq; NP_309881.1; NC_002695.1. DR RefSeq; WP_000176265.1; NZ_VOAI01000015.1. DR AlphaFoldDB; P58640; -. DR SMR; P58640; -. DR STRING; 155864.Z2525; -. DR GeneID; 912806; -. DR KEGG; ece:Z2525; -. DR KEGG; ecs:ECs_1854; -. DR PATRIC; fig|386585.9.peg.1954; -. DR eggNOG; COG0284; Bacteria. DR HOGENOM; CLU_067069_0_0_6; -. DR OMA; FWKVGLE; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000000558; Chromosome. DR Proteomes; UP000002519; 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_0000134541" 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; 26230 MW; FCFB47516EB5382D CRC64; MTLTASSSSR AVTNSPVVVA LDYHNRDAAL AFVDKIDPRD CRLKVGKEMF TLFGPQFVRE LQQRGFDIFL DLKFHDIPNT AAHAVAAAAD LGVWMVNVHA SGGARMMTAA REALVPFGKD APLLIAVTVL TSMEASDLAD LGVTLSPADY AERLAALTQK CGLDGVVCSA QEAVRFKQVF GQEFKLVTPG IRPQGSEAGD QRRIMTPEQA LAAGVDYMVI GRPVTQSVDP AQTLKAINAS LQRSA //