ID PYRF_PSEAE Reviewed; 232 AA. AC Q59654; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 08-DEC-2000, sequence version 2. DT 27-MAR-2024, entry version 136. 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}; OrderedLocusNames=PA2876; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=7765522; DOI=10.1007/bf01570229; RA Strych U., Wohlfarth S., Winkler U.K.; RT "Orotidine-5'-monophosphate decarboxylase from Pseudomonas aeruginosa PAO1: RT cloning, overexpression, and enzyme characterization."; RL Curr. Microbiol. 29:353-359(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate CC (OMP) to uridine 5'-monophosphate (UMP). 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. 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; X65613; CAA46564.1; -; Genomic_DNA. DR EMBL; AE004091; AAG06264.1; -; Genomic_DNA. DR PIR; B83285; B83285. DR PIR; S43188; S43188. DR RefSeq; NP_251566.1; NC_002516.2. DR RefSeq; WP_003090975.1; NZ_QZGE01000011.1. DR AlphaFoldDB; Q59654; -. DR SMR; Q59654; -. DR STRING; 208964.PA2876; -. DR PaxDb; 208964-PA2876; -. DR DNASU; 882585; -. DR GeneID; 882585; -. DR KEGG; pae:PA2876; -. DR PATRIC; fig|208964.12.peg.3017; -. DR PseudoCAP; PA2876; -. DR HOGENOM; CLU_067069_0_0_6; -. DR InParanoid; Q59654; -. DR OrthoDB; 9806203at2; -. DR PhylomeDB; Q59654; -. DR BioCyc; PAER208964:G1FZ6-2926-MONOMER; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000002438; 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 1: Evidence at protein level; KW Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1..232 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_0000134565" FT ACT_SITE 64 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 13 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 35 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 62..71 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 122 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 182 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 191 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 211 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT BINDING 212 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200" FT CONFLICT 111 FT /note="P -> A (in Ref. 1; CAA46564)" FT /evidence="ECO:0000305" SQ SEQUENCE 232 AA; 24394 MW; EE7218004DA944B5 CRC64; MSACQSPIIV ALDFPTREAA LALADQLDPK LCRVKVGKEL FTSCAAGIVE TLRGKGFEVF LDLKFHDIPN TTAMAVKAAA EMGVWMVNVH CSGGLRMMAA CRETLEAFSG PRPLLIGVTV LTSMEREDLA GIGLDIEPQE QVLRLAALAQ KAGMDGLVCS AQEAPALKAA HPGLQLVTPG IRPAGSAQDD QRRILTPRQA LDAGSDYLVI GRPISQAADP AKALAAIVAE LG //