ID PYRF_NOCSJ Reviewed; 273 AA. AC A1SJF3; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 83. DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01215}; DE EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01215}; DE AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01215}; DE Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01215}; DE Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01215}; GN Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01215}; GN OrderedLocusNames=Noca_2433; OS Nocardioides sp. (strain ATCC BAA-499 / JS614). OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales; OC Nocardioidaceae; Nocardioides. OX NCBI_TaxID=196162; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-499 / JS614; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J., RA Richardson P.; RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. 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_01215}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC UMP from orotate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01215}. CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01215}. 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; CP000509; ABL81938.1; -; Genomic_DNA. DR RefSeq; WP_011755879.1; NC_008699.1. DR AlphaFoldDB; A1SJF3; -. DR SMR; A1SJF3; -. DR STRING; 196162.Noca_2433; -. DR KEGG; nca:Noca_2433; -. DR eggNOG; COG0284; Bacteria. DR HOGENOM; CLU_060704_0_0_11; -. DR OrthoDB; 9808470at2; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000000640; 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_01215; OMPdecase_type2; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011995; OMPdecase_type-2. DR InterPro; IPR001754; OMPdeCOase_dom. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR NCBIfam; TIGR02127; pyrF_sub2; 1. DR PANTHER; PTHR43375; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1. DR PANTHER; PTHR43375:SF1; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1. DR Pfam; PF00215; OMPdecase; 1. DR SMART; SM00934; OMPdecase; 1. DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1. PE 3: Inferred from homology; KW Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1..273 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_1000213895" FT ACT_SITE 96 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01215" SQ SEQUENCE 273 AA; 28231 MW; C200671AD2395144 CRC64; MIPFGSRLHA AIADRGPLCV GIDPHAGLLS DWGLGDDVAG LETFALEVVE AIAPYVSVVK PQSAFFERFG SRGIAVLERV IAQSRAAGAL VLLDVKRGDI GSTSQAYADA YLDPTSPLAS DAITVSPFLG FGSLDPIVET ARTHGAGLFV LALTSNKEGP EVQHARVDGV AGGGTVAGLM LDHLRRLNAE ASPLGSFGAV VGATIGSTDE DLAFNGPVLA PGFGAQGGTI ADVRRLFGAA AAVLPSSSRD VLRLQDPDVM RDFVVRTNDE LRS //