ID   PYRF_COREF              Reviewed;         280 AA.
AC   Q8FT43;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=CE1728;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(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   -!- 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; BA000035; BAC18538.1; -; Genomic_DNA.
DR   RefSeq; WP_006767728.1; NZ_GG700683.1.
DR   AlphaFoldDB; Q8FT43; -.
DR   SMR; Q8FT43; -.
DR   STRING; 196164.23493568; -.
DR   EnsemblBacteria; BAC18538; BAC18538; BAC18538.
DR   KEGG; cef:CE1728; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_060704_0_0_11; -.
DR   OMA; ARMPHTF; -.
DR   OrthoDB; 1181405at2; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000001409; 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..280
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134624"
FT   ACT_SITE        97
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   280 AA;  28927 MW;  815854B480C73D32 CRC64;
     MTQTFGENLL DAASTRGRLC VGIDPHESLL RAWGLPVDAT GLAEFSRICV EAFADTVALV
     KPQVAFYERF GSRGFAVLEE TIGTLRERGC LVVSDAKRGD IGSTMAGYAT AWLDPGSPLS
     SDAVTVSPYL GFGSLQPVFD LAEEHGRGVF VLAATSNPEA RVLQDQTDAS GVSISQQIVN
     EAAALNAPHL AQHRAGNIGV VVGATLTDPP ALSGLNGAIL MPGVGTQGGT AQDVGTIAGD
     MAHLAFPNVS RAVLAQGPDV GNLRVAVSET AAEFPGFPRS