ID   PYRF_CLOPE              Reviewed;         287 AA.
AC   Q8XL62;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE            EC=4.1.1.23;
DE   AltName: Full=OMP decarboxylase;
DE            Short=OMPDCase;
DE            Short=OMPdecase;
GN   Name=pyrF; OrderedLocusNames=CPE1180;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BA000016; BAB80886.1; -; Genomic_DNA.
DR   RefSeq; WP_003481260.1; NC_003366.1.
DR   AlphaFoldDB; Q8XL62; -.
DR   SMR; Q8XL62; -.
DR   STRING; 195102.gene:10490443; -.
DR   EnsemblBacteria; BAB80886; BAB80886; BAB80886.
DR   KEGG; cpe:CPE1180; -.
DR   HOGENOM; CLU_060704_1_1_9; -.
DR   OMA; QSAFFER; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000000818; 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; IPR018089; OMPdecase_AS.
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.
DR   PROSITE; PS00156; OMPDECASE; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..287
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134623"
FT   ACT_SITE        97
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   287 AA;  31823 MW;  B21A668216B06803 CRC64;
     MIADKLFEKV EKNGVVCVGL DTSLDYIPEE FKSKFSNESD MLFAFNKEII DATLDVSACF
     KVQIAYYEAL GLKGLEAYKN TLSYLREKNA LIIADIKRGD IAATAKMYAK AHFEGDFESD
     FITLNPYMGM DSIDPYLPYI EKNEKGVFVL VRTSNKGAED IEYLEAGHGK KVYDVVGEKL
     NTLGKNYLGK HGYSSIGGVV GCTHQEEAKE MRDKLDTMPF LIPGYGAQGG TAKDVAAYLK
     NGNGGIVNSS RKILLAYKAM EDNKNFAECA RKEAISMRDS IREAILK