ID PYRF_DEHM1 Reviewed; 270 AA. AC Q3ZAI1; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 94. 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=DET0013; OS Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195) OS (Dehalococcoides ethenogenes (strain 195)). OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalococcoidales; OC Dehalococcoidaceae; Dehalococcoides. OX NCBI_TaxID=243164; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195; RX PubMed=15637277; DOI=10.1126/science.1102226; RA Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A., RA Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J., RA Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E., RA Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M., RA Zinder S.H., Heidelberg J.F.; RT "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides RT ethenogenes."; RL Science 307:105-108(2005). 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; CP000027; AAW39163.1; -; Genomic_DNA. DR RefSeq; WP_010935823.1; NC_002936.3. DR AlphaFoldDB; Q3ZAI1; -. DR SMR; Q3ZAI1; -. DR STRING; 243164.DET0013; -. DR KEGG; det:DET0013; -. DR PATRIC; fig|243164.10.peg.12; -. DR eggNOG; COG0284; Bacteria. DR HOGENOM; CLU_060704_1_0_0; -. DR InParanoid; Q3ZAI1; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000008289; 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. FT CHAIN 1..270 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_1000066470" FT ACT_SITE 89 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01215" SQ SEQUENCE 270 AA; 29786 MW; 33EFBCC7B816224F CRC64; MKFLEKLKQA GNSHNSLLCV GLDPDPKLMP VGMTALEFNR EIIAATAPFV CGYKINLAFY EALGKQGWEI LSETCKLIPP ELLSIADAKR GDIGNTSKAY ARAVFDELGC DGVTASPYLG YDSLEPFIEY QDKGIFILCR TSNQGSADFQ MLKTEYLGQK RFLYEVVADK SLQWNRYENI GLVVGATQQE ELKKLRLSYP KMPFLIPGIG AQGGDLKATV ENGTNQSGQL ALICASRGIL YARSGSEFAQ GAAEAAKQMR DAINHYRKRF //