ID PYRF_MYCVP Reviewed; 277 AA. AC A1T8H2; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 86. 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=Mvan_2665; OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycolicibacterium. OX NCBI_TaxID=350058; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 / RC PYR-1; RG US DOE Joint Genome Institute; 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 Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Anderson I.J., Miller C., Richardson P.; RT "Complete sequence of Mycobacterium vanbaalenii PYR-1."; 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; CP000511; ABM13472.1; -; Genomic_DNA. DR RefSeq; WP_011779881.1; NZ_JACKSD010000003.1. DR AlphaFoldDB; A1T8H2; -. DR SMR; A1T8H2; -. DR STRING; 350058.Mvan_2665; -. DR KEGG; mva:Mvan_2665; -. DR eggNOG; COG0284; Bacteria. DR HOGENOM; CLU_060704_0_0_11; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000009159; 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..277 FT /note="Orotidine 5'-phosphate decarboxylase" FT /id="PRO_1000066481" FT ACT_SITE 95 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01215" SQ SEQUENCE 277 AA; 27521 MW; 80DE861F2B3A58E2 CRC64; MSGFGDRLAG ATARRGPLCL GIDPHPELLR AWGLGTDAAG LAGFSDICVA AFAGFAVVKP QVAFFEAYGS AGYAVLERTI AALRESGVLV LADAKRGDIG STMAAYASAW AGDSPLAADA VTASPYLGFG SLQPLLDTAR EHDRGVFVLA ATSNPEGASV QCAVAPGAIP GRTVAQAIVD AAAEVNAGAA RGSVGVVVGA TLSAPPDVSA LNGPVLVPGV GAQGGRPEAL AGLGGARRGQ LLPAVSREVL RAGPDVAALR AAAERMRDAV AYLGENP //