ID   PYRF_CANTR              Reviewed;         268 AA.
AC   O42771;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 83.
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=URA3;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M4;
RX   PubMed=9734982; DOI=10.1007/pl00022802;
RA   Su J.-H., Hsia J.-H., Chang M.-C.;
RT   "Cloning and sequence analysis of the Candida tropicalis URA3 gene encoding
RT   orotidine-5'-phosphate decarboxylase.";
RL   Curr. Microbiol. 37:210-213(1998).
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; AF040702; AAB96773.1; -; Genomic_DNA.
DR   AlphaFoldDB; O42771; -.
DR   SMR; O42771; -.
DR   VEuPathDB; FungiDB:CTMYA2_051200; -.
DR   VEuPathDB; FungiDB:CTRG_02175; -.
DR   UniPathway; UPA00070; UER00120.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
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:EnsemblFungi.
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   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   NCBIfam; TIGR01740; pyrF; 1.
DR   PANTHER; PTHR19278; OROTATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19278:SF9; URIDINE 5'-MONOPHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS00156; OMPDECASE; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT   CHAIN           1..268
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134654"
FT   ACT_SITE        94
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         60..62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         92..101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   268 AA;  29672 MW;  A43CC1ED1CB24237 CRC64;
     MVNTETYTER ASKHPSKVAQ RLFQLMESKK TNLCASIDVP TTKEFLSLID KLGPFICLVK
     THIDIISDFS YEGTILPLIE LSKKHNFMIF EDRKFADIGN TVKLQYTSGV YKISSWSDIT
     NAHGVTGKGG VEGLKKGADE TTNEPRGLLM LAELSSKGSL AYGEYTNKTI EIAKSDKEFV
     IGFIAQRDMG GHDQGFDWII MTPGVGLDDK GDALGQQYRT VDEVISTGTD VIIVGRGLFG
     KGRDPEVEGK RYREAGWNAY LKKNGQLE
//