ID   PYRF_PORG3              Reviewed;         276 AA.
AC   B2RME4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=PGN_2021;
OS   Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS   12257 / NCTC 11834 / 2561).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=431947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX   PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA   Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA   Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA   Nakayama K.;
RT   "Determination of the genome sequence of Porphyromonas gingivalis strain
RT   ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT   rearrangements in P. gingivalis.";
RL   DNA Res. 15:215-225(2008).
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; AP009380; BAG34539.1; -; Genomic_DNA.
DR   RefSeq; WP_012458691.1; NZ_CP025930.1.
DR   AlphaFoldDB; B2RME4; -.
DR   SMR; B2RME4; -.
DR   STRING; 431947.PGN_2021; -.
DR   EnsemblBacteria; BAG34539; BAG34539; PGN_2021.
DR   GeneID; 29257157; -.
DR   KEGG; pgn:PGN_2021; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_060704_1_0_10; -.
DR   OMA; QSAFFER; -.
DR   BioCyc; PGIN431947:G1G2V-2254-MON; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000008842; 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.
FT   CHAIN           1..276
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_1000138958"
FT   ACT_SITE        96
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01215"
SQ   SEQUENCE   276 AA;  30558 MW;  626DD3BDDC3E168D CRC64;
     MTTKELFDRI CRKRSFLCVG LDTDVKKIPP HLLNEDDPIL AFNKAIIDAT AEYCVAFKPN
     MAFYESMGSF GAHSFEKTIE YIRERYPDQF IIADAKRGDI GNTSDMYARS FFEHLKVDAL
     TVSPYMGEDS ISPFLSYAGK FTVLLALTSN KGSQDFQMMR DADGEYLFER VIRISQTWDN
     AGQLMYVVGA TQASMLKDIR EIVPDAFLLV PGVGAQGGSL EDVAEYGMNA HCGLLVNASR
     SIIYADNTEG FAAKAAGEAA AMQRQMEIAL RAKGLI