ID   PYRF_PARD8              Reviewed;         280 AA.
AC   A6LDS0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=BDI_2103;
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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; CP000140; ABR43834.1; -; Genomic_DNA.
DR   RefSeq; WP_005854382.1; NC_009615.1.
DR   AlphaFoldDB; A6LDS0; -.
DR   SMR; A6LDS0; -.
DR   STRING; 435591.BDI_2103; -.
DR   EnsemblBacteria; ABR43834; ABR43834; BDI_2103.
DR   KEGG; pdi:BDI_2103; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_060704_1_0_10; -.
DR   OMA; QSAFFER; -.
DR   OrthoDB; 1181405at2; -.
DR   BioCyc; PDIS435591:G1G5A-2158-MON; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000000566; 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..280
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_1000138957"
FT   ACT_SITE        96
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01215"
SQ   SEQUENCE   280 AA;  31263 MW;  D234180F1706413F CRC64;
     MNKQQLFENI KKKQSFLCVG LDTDIKKIPQ HLLSEEDPIF AFNKAIIDAT ADYCVAYKPN
     LAFYESLGTK GMMAFEKTVA YLRENYPDQF IIADAKRGDI GNTSEMYARS FFDHIKVDAV
     TVAPYMGEDS VKPFLIYPEA WVILLALTSN KGSHDFQMTE DANGERLFEK VLKKSQEWAN
     DEQMMYVVGA TQGKMFLDIR KQAPNHFLLV PGVGAQGGSL AEVAQYGMND QCGLLVNSSR
     AIIYADKTEA FANVAREAAH AVQKEMAGYL HDKGIIPCKA