ID PYRF_PHOV8 Reviewed; 272 AA. AC A6KWL1; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 24-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 85. 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=BVU_0095; OS Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / OS NBRC 14291 / NCTC 11154) (Bacteroides vulgatus). OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Phocaeicola. OX NCBI_TaxID=435590; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / RC NCTC 11154; RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156; RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C., RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H., RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K., RA Knight R.D., Gordon J.I.; RT "Evolution of symbiotic bacteria in the distal human intestine."; RL PLoS Biol. 5:1574-1586(2007). 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; CP000139; ABR37825.1; -; Genomic_DNA. DR RefSeq; WP_005843024.1; NZ_JANSWM010000057.1. DR AlphaFoldDB; A6KWL1; -. DR SMR; A6KWL1; -. DR STRING; 435590.BVU_0095; -. DR PaxDb; 435590-BVU_0095; -. DR GeneID; 69838452; -. DR KEGG; bvu:BVU_0095; -. DR eggNOG; COG0284; Bacteria. DR HOGENOM; CLU_060704_1_0_10; -. DR BioCyc; BVUL435590:G1G59-101-MONOMER; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000002861; 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..272 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_1000138946" FT ACT_SITE 96 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01215" SQ SEQUENCE 272 AA; 30600 MW; C376240C83A23AE8 CRC64; MNKQQLFENI QKKKSFLCVG LDTDIKKIPE HLLKEEDPIF AFNKAIIDAT APYCIAYKPN LAFYESMGVK GWIAFEKTVS YIKENYPDQF IIADAKRGDI GNTSAMYART FFEELDIDSV TVAPYMGEDS VTPFLSYEGK WVILLALTSN KGSHDFQLTE DTNGERLFEK VLRKSQEWAN DENMMYVVGA TQGRAFEDIR KIVPNHFLLV PGIGAQGGSL EEVCKYGMNS TCGLIVNSSR AIIYADKTEN FATVAGQEAQ KVQAQMEKIM CQ //