ID PYRF_SALAI Reviewed; 278 AA. AC A8LY20; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 1. DT 27-MAR-2024, entry version 76. 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=Sare_1852; OS Salinispora arenicola (strain CNS-205). OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales; OC Micromonosporaceae; Salinispora. OX NCBI_TaxID=391037; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNS-205; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C., RA Udwary D., Xiang L., Gontang E., Richardson P.; RT "Complete sequence of Salinispora arenicola CNS-205."; RL Submitted (OCT-2007) 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; CP000850; ABV97737.1; -; Genomic_DNA. DR AlphaFoldDB; A8LY20; -. DR SMR; A8LY20; -. DR STRING; 391037.Sare_1852; -. DR KEGG; saq:Sare_1852; -. DR PATRIC; fig|391037.6.peg.1880; -. DR eggNOG; COG0284; Bacteria. DR HOGENOM; CLU_060704_0_0_11; -. DR OrthoDB; 9808470at2; -. DR UniPathway; UPA00070; UER00120. 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; IPR018089; OMPdecase_AS. 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. DR PROSITE; PS00156; OMPDECASE; 1. PE 3: Inferred from homology; KW Decarboxylase; Lyase; Pyrimidine biosynthesis. FT CHAIN 1..278 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_1000085577" FT ACT_SITE 96 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01215" SQ SEQUENCE 278 AA; 28171 MW; F8DC107CF37CC3E4 CRC64; MESFGARLHR AVAERGPLCV GIDPHPGLLA RWGLDDDVHG LERFADTVVE ALGDRVAVVK PQSAFFERFG SRGVAVLEST IRQLRLAGSL VLLDVKRGDI GSTVAAYASA YLEPSSPLHV DAVTVSPYLG VGALAPMFDM AAAKGGGVFV LALTSNPEGA AVQRARTAGG RTVAQVVIDE ISQLNAGAQP LGSVGLVVGA TIGETGHDLA AVNGPLLAPG LGAQGASAAD LRVVFGSALP AVLPAYSREV LAAGPDVAAL RAAADRVLAD CRAALTGS //