ID   PYRF_CLOTE              Reviewed;         288 AA.
AC   Q891J1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
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}; OrderedLocusNames=CTC_02381;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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}.
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DR   EMBL; AE015927; AAO36854.1; -; Genomic_DNA.
DR   RefSeq; WP_011100515.1; NC_004557.1.
DR   AlphaFoldDB; Q891J1; -.
DR   SMR; Q891J1; -.
DR   STRING; 212717.CTC_02381; -.
DR   EnsemblBacteria; AAO36854; AAO36854; CTC_02381.
DR   GeneID; 64179544; -.
DR   KEGG; ctc:CTC_02381; -.
DR   HOGENOM; CLU_060704_1_1_9; -.
DR   OMA; QSAFFER; -.
DR   OrthoDB; 1181405at2; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000001412; 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   Gene3D; 3.20.20.70; -; 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   PANTHER; PTHR43375; PTHR43375; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR02127; pyrF_sub2; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..288
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_1000066467"
FT   ACT_SITE        97
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01215"
SQ   SEQUENCE   288 AA;  32456 MW;  E3C843E0AB5E1F64 CRC64;
     MMIDKLYKRV EKNGHVCAGL DTSLDYIPEY FKTKYFNEED IIFNFNKEII DATYDKVACF
     KIQIAYYEAL GLKGLRAYKR TLDYIKESDG IVISDIKRGD ISSTAKMYAR AHFEGDFETD
     FITLSPYMGL DSIEPYFEYM KQKGKGVFVL VRTSNEGAKD IEFIESKDGN KVYEIIGKKL
     KNMGQDFLGN CGYSSIGGVV GCTHIDEAVK LRKDLGGMFF LIPGYGAQGG KAEDVALYLK
     NGNGGVVNSS RGILLAYKKQ NDEKNFAKCS RNEVIRMRDD ILQAINSK