ID PYRF_NATPD Reviewed; 269 AA. AC Q3ISC9; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 97. 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=NP_1734A; OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis). OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales; OC Haloarculaceae; Natronomonas. OX NCBI_TaxID=348780; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / RC NCIMB 2260 / Gabara; RX PubMed=16169924; DOI=10.1101/gr.3952905; RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J., RA Oesterhelt D.; RT "Living with two extremes: conclusions from the genome sequence of RT Natronomonas pharaonis."; RL Genome Res. 15:1336-1343(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; CR936257; CAI48958.1; -; Genomic_DNA. DR RefSeq; WP_011322591.1; NC_007426.1. DR AlphaFoldDB; Q3ISC9; -. DR SMR; Q3ISC9; -. DR STRING; 348780.NP_1734A; -. DR EnsemblBacteria; CAI48958; CAI48958; NP_1734A. DR GeneID; 3703085; -. DR KEGG; nph:NP_1734A; -. DR eggNOG; arCOG00081; Archaea. DR HOGENOM; CLU_060704_1_0_2; -. DR OrthoDB; 94124at2157; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000002698; 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; 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; Reference proteome. FT CHAIN 1..269 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_1000066482" FT ACT_SITE 92 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01215" SQ SEQUENCE 269 AA; 29255 MW; D72248AD21ED11AB CRC64; MSFFETLADR IDDRDSVVSV GLDPDPDRLP EFLDADLPRW AFNRRVIDAT HEHAACYKPN AAFYEDSDGW RALEETIAYA HGKGVPVLLD AKRGDIGNTA RQYATLLDDD GLGADAITAN PYMGRDTLEP YLSRADKGVF ILCRTSNSGG ADFQNLTVGN DKRLYEYVAQ RCQEWNEHEN VGLVVGATAP EELESVRDLV DLPFLVPGVG AQGGDAAAAV DHGLADGVGL VNSSRGIIFA GEGAADEDEY FRAVGAAAKR LKQRLNKHR //