ID   PYRF_DIURU              Reviewed;         265 AA.
AC   Q9HFN9;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 67.
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   Diutina rugosa (Yeast) (Candida rugosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Diutina.
OX   NCBI_TaxID=5481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Biasio W.;
RL   Thesis (2000), University of Vienna, Austria.
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; AJ279021; CAC08811.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HFN9; -.
DR   SMR; Q9HFN9; -.
DR   VEuPathDB; FungiDB:DIURU_003156; -.
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..265
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134653"
FT   ACT_SITE        93
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT   BINDING         37
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         91..100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   265 AA;  28633 MW;  0A2F0D013F8DD499 CRC64;
     MPAPSYSTRA AAHPSPVARK LLALMDEKKS NLCASVDVTT TAELLALVEK LAPYICMVKT
     HIDIVSDFSY EGTVVPLVAL AKKHRFLLFE DRKFADIGNT VKHQYAGGVY QIARWADITN
     AHGVTGAGIV AGLKQAAEET TSEPRGLLML AELSSKGAIA HGKYTEETVE IAKTDKEFVF
     GFIAQGDMGG REEGFDWVVM TPGVGLDDTG DALGQQYRTV DTVVQTGTDV IIVGRGLFGK
     GRHPAVEGER YRKAGWDAYT KRVSP