PYRF_CANDC
ID PYRF_CANDC Reviewed; 270 AA.
AC Q9C150; B9WDA6;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
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; ORFNames=CD36_81280;
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11292806; DOI=10.1128/jb.183.9.2859-2865.2001;
RA Staib P., Moran G.P., Sullivan D.J., Coleman D.C., Morschhauser J.;
RT "Isogenic strain construction and gene targeting in Candida dubliniensis.";
RL J. Bacteriol. 183:2859-2865(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ302032; CAC27824.1; -; Genomic_DNA.
DR EMBL; FM992690; CAX42658.1; -; Genomic_DNA.
DR RefSeq; XP_002419073.1; XM_002419028.1.
DR AlphaFoldDB; Q9C150; -.
DR SMR; Q9C150; -.
DR STRING; 42374.XP_002419073.1; -.
DR EnsemblFungi; CAX42658; CAX42658; CD36_81280.
DR GeneID; 8047017; -.
DR KEGG; cdu:CD36_81280; -.
DR CGD; CAL0000163710; URA3.
DR VEuPathDB; FungiDB:CD36_81280; -.
DR eggNOG; KOG1377; Eukaryota.
DR HOGENOM; CLU_030821_0_0_1; -.
DR OrthoDB; 1303452at2759; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000002605; Chromosome 3.
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..270
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134648"
FT ACT_SITE 95
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 61..63
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 93..102
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 270 AA; 29921 MW; 217D05C4926175D9 CRC64;
MTVNTKTYSA RAETHASPVA QRLFRLMESK KTNLCASIDV DTTKEFLELI DKLGPYVCLI
KTHIDIINDF SYESTIEPLL ELSRKHQFMI FEDRKFADIG NTVKKQYIGG VYKISSWADI
TNAHGVTGNG VVEGLKQGAK ETTTDQEPRG LLMLAELSSV GSLAYGEYSQ KTVEIAKSDK
EFVIGFIAQR DMGGQEEGFD WIIMTPGVGL DDKGDGLGQQ YRTVNEVVST GTDIIIVGRG
LFGKGRDPEV EGKRYRDAGW NAYLKKTGQL
