ID   PYRF_PHYB8              Reviewed;         267 AA.
AC   P21593;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE            EC=4.1.1.23;
DE   AltName: Full=OMP decarboxylase;
DE            Short=OMPDCase;
DE            Short=OMPdecase;
DE   AltName: Full=Uridine 5'-monophosphate synthase;
DE            Short=UMP synthase;
GN   Name=pyrG;
OS   Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS   33097 / NRRL 1555).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX   NCBI_TaxID=763407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC 33097 / NRRL 1555;
RX   PubMed=2277645; DOI=10.1007/bf00271561;
RA   Diaz-Minguez J.M., Iturriaga E.A., Benito E.P., Corrochano L., Eslava A.P.;
RT   "Isolation and molecular analysis of the orotidine-5'-phosphate
RT   decarboxylase gene (pyrG) of Phycomyces blakesleeanus.";
RL   Mol. Gen. Genet. 224:269-278(1990).
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|PROSITE-ProRule:PRU10110};
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. {ECO:0000305}.
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DR   EMBL; X53601; CAA37670.1; -; Genomic_DNA.
DR   PIR; S13736; DCUMOP.
DR   RefSeq; XP_018289133.1; XM_018439727.1.
DR   AlphaFoldDB; P21593; -.
DR   SMR; P21593; -.
DR   GeneID; 29000633; -.
DR   UniPathway; UPA00070; UER00120.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-EC.
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   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR014732; OMPdecase.
DR   InterPro; IPR018089; OMPdecase_AS.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR32119:SF2; PTHR32119:SF2; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR01740; pyrF; 1.
DR   PROSITE; PS00156; OMPDECASE; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT   CHAIN           1..267
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134671"
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         62..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         93..102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   267 AA;  29899 MW;  CE5B132327F3FDDC CRC64;
     MMLNTYKSYT ERAEQHPNAC ARSLFELMER KKTNLSVAVD VTTKKELLSI ADSVGPYVCV
     LKTHIDIVED FDKDLVAQLE ALAKKHDFLI FEDRKFADIG NTVKHQYEKG VYKIASWSHI
     TNAHTVPGEG IIKGLGEVGL PLGRGLLLLA EMSSKGALTK GSYTTESVEM ARRNKDFVFG
     FIAQHKMNEY PDEDFVVMTP GVGLDIKGDG LGQQYRTPHE VIVESGCDVI IVGRGIYGKP
     DEVEAQSKRY REAGWNAYLE RVRMHKA