ID   PYRF_STRCO              Reviewed;         278 AA.
AC   Q9KXR8;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=SCO1481; ORFNames=SC9C5.05c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(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; AL939109; CAB93361.1; -; Genomic_DNA.
DR   RefSeq; NP_625761.1; NC_003888.3.
DR   RefSeq; WP_011027809.1; NC_003888.3.
DR   AlphaFoldDB; Q9KXR8; -.
DR   SMR; Q9KXR8; -.
DR   STRING; 100226.SCO1481; -.
DR   GeneID; 1096907; -.
DR   KEGG; sco:SCO1481; -.
DR   PATRIC; fig|100226.15.peg.1490; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_060704_0_0_11; -.
DR   OMA; QSAFFER; -.
DR   PhylomeDB; Q9KXR8; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000001973; 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..278
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134634"
FT   ACT_SITE        96
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   278 AA;  28791 MW;  9B3574E71E21FDC6 CRC64;
     MEPFGARLRR AMDERGPLCV GIDPHASLLA EWGLNDDVAG LERFSRTVVE AMADRVAVLK
     PQSAFFERFG SRGVAVLETT VQEARAAGAL VVMDAKRGDI GSTMAAYAES FLHKDAPLFS
     DALTVSPYLG YGSLKPAVDL ARESGAGLFV LALTSNPEGG EVQHAVRGDG RSVGATMLAH
     LAAENAGEEP LGSFGAVVGA TLGDLSSYDL GINGPLLAPG IGAQGATPAD LPRVFGAALR
     NVVPNVSRGV LRHGPDVTAL RTAADRFAVE IRTAVTAS