PYRF_CANMA
ID PYRF_CANMA Reviewed; 266 AA.
AC P32430;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 81.
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; Synonyms=PYRG;
OS Candida maltosa (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5479;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 28140 / CBS 5611 / IAM 12247 / JCM 1504 / NBRC 1977;
RX PubMed=8435849; DOI=10.1007/bf00351497;
RA Ohkuma M., Muraoka S., Hwang C.W., Ohta A., Takagi M.;
RT "Cloning of the C-URA3 gene and construction of a triple auxotroph (his5,
RT ade1, ura3) as a useful host for the genetic engineering of Candida
RT maltosa.";
RL Curr. Genet. 23:205-210(1993).
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; D12720; BAA02215.1; -; Genomic_DNA.
DR PIR; S29791; JS0721.
DR AlphaFoldDB; P32430; -.
DR SMR; P32430; -.
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..266
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134651"
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 266 AA; 29306 MW; 060E7A163BA9978C CRC64;
MVSTKTYTTR ASTHPSPVAQ RLFHLMDTKK ANLCASVDVQ TTSEFLSLID KLGPYICLVK
THIDIIDDFS YEGTIVPLLE LARKHNFMIF EDRKFADIGN TVKHQYTSGV YKISSWSDIT
NAHGVTGAGV VDGLKQGALE TTKEPRGLLM LAELSSKGSL AYGEYTEKTV EIAKLDKEFV
IGFIAQRDMG GHDEGFDWIV MTPGVGLDDK GDGLGQQYRT VDEVVSTGTD VIIVGRGLFG
KGRDPEVEGK RYRDAGWNAY LKRTGQ