ID   PYRF_CANGA              Reviewed;         265 AA.
AC   P33283;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 119.
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; OrderedLocusNames=CAGL0I03080g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=85/038;
RX   PubMed=8181748; DOI=10.1016/0378-1119(94)90368-9;
RA   Zhou P., Szczypka M.S., Young R.J., Thiele D.J.;
RT   "A system for gene cloning and manipulation in the yeast Candida
RT   glabrata.";
RL   Gene 142:135-140(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; L13661; AAA34325.1; -; Genomic_DNA.
DR   EMBL; CR380955; CAG60321.1; -; Genomic_DNA.
DR   RefSeq; XP_447384.1; XM_447384.1.
DR   AlphaFoldDB; P33283; -.
DR   SMR; P33283; -.
DR   STRING; 5478.XP_447384.1; -.
DR   EnsemblFungi; CAG60321; CAG60321; CAGL0I03080g.
DR   GeneID; 2889164; -.
DR   KEGG; cgr:CAGL0I03080g; -.
DR   CGD; CAL0130376; URA3.
DR   VEuPathDB; FungiDB:CAGL0I03080g; -.
DR   eggNOG; KOG1377; Eukaryota.
DR   HOGENOM; CLU_030821_0_0_1; -.
DR   InParanoid; P33283; -.
DR   OMA; KNFVMGF; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000002428; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IGI:CGD.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IGI:CGD.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IGI:CGD.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046107; P:uracil biosynthetic process; IMP:CGD.
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; Reference proteome.
FT   CHAIN           1..265
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134649"
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;  29054 MW;  19F42505E26EF136 CRC64;
     MSSASYLQRA EAHPSPVASK LLKLMHEKKT NLCASLDVTT TSELLKLVDT LGPYICLLKT
     HVDILSDFSF ENTVKPLKEM AAKHNFLIFE DRKFADIGNT VKLQYTSGVY KIAEWADITN
     AHGVTGQGIV TGLKQGAEET TNEPRGLLML AELSSKGSLA HGEYTKGTVD IAKSDKDFVI
     GFIAQKDMGG RDEGFDWLIM TPGVGLDDKG DALGQQYRTV DEVFSTGTDI IIVGRGLFAK
     GRDPKTEGER YRKAGWDAYL KRIGN