ID   PYRF_CLONN              Reviewed;         287 AA.
AC   A0Q2N3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
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};
GN   OrderedLocusNames=NT01CX_0393;
OS   Clostridium novyi (strain NT).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=386415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NT;
RX   PubMed=17115055; DOI=10.1038/nbt1256;
RA   Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA   Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA   Zhou S.;
RT   "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT   NT.";
RL   Nat. Biotechnol. 24:1573-1580(2006).
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; CP000382; ABK62436.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0Q2N3; -.
DR   SMR; A0Q2N3; -.
DR   STRING; 386415.NT01CX_0393; -.
DR   KEGG; cno:NT01CX_0393; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_060704_1_1_9; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000008220; 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   CDD; cd04725; OMP_decarboxylase_like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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   NCBIfam; TIGR02127; pyrF_sub2; 1.
DR   PANTHER; PTHR43375; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43375:SF1; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 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_1000066464"
FT   ACT_SITE        99
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01215"
SQ   SEQUENCE   287 AA;  32269 MW;  60464FD53A1E39D0 CRC64;
     MVLIIDRLYE EVNKKGNVCV GLDTDLSYIP QRFLKNYENI EDAIFQFNRK IIDATHDAVA
     CYKVQIAYYE SFGLKGLMAY KRTLEYIKKV GCIAISDVKR GDISKTAEMY AKAHFEGDFE
     TDFITVNPYM GMDSIEPYMP YLQNKEKGLF ALVRTSNPGS KDFEYIQSGS GRRVYEIVGE
     KLERLGEKVM GQCGYSSIGG VVGCTTLEDG KEIRKNFGKT FFLIPGFGAQ GGGAKEANVY
     LKDGNGGVVN SSRGILLAYK KYENGEKNFD ECSRKEVLKM QKELGRE
//