PYRF_YARLI
ID PYRF_YARLI Reviewed; 286 AA.
AC Q12724; Q6C4H6; Q9C1U4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=YALI0E26741g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
RX PubMed=11489863; DOI=10.1128/jb.183.17.5102-5109.2001;
RA Mauersberger S., Wang H., Gaillardin C., Barth G., Nicaud J.-M.;
RT "Insertional mutagenesis in the n-alkane-assimilating yeast Yarrowia
RT lipolytica: generation of tagged mutations in genes involved in hydrophobic
RT substrate utilization.";
RL J. Bacteriol. 183:5102-5109(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Strick C.A., James L.C., O'Donnell M.M., Elsenboss L.A.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-7 AND 250-284.
RC STRAIN=CLIB 122 / E 150;
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}.
CC -!- CAUTION: Strain CLIB 122 / E 150 has a defective URA3 sequence (ura3-
CC 302) which is disrupted (positions 8 to 249) by S.cerevisiae SUC2.
CC {ECO:0000305}.
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DR EMBL; AJ306421; CAC32856.1; -; Genomic_DNA.
DR EMBL; U40564; AAA85392.1; -; Genomic_DNA.
DR EMBL; CR382131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q12724; -.
DR SMR; Q12724; -.
DR STRING; 284591.Q12724; -.
DR InParanoid; Q12724; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
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; 2.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..286
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134691"
FT ACT_SITE 91
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 57..59
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 89..98
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 104..108
FT /note="KNGVY -> RCH (in Ref. 1; CAC32856)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 286 AA; 31630 MW; 7E71BFE84C61F216 CRC64;
MPSYEARANV HKSAFAARVL KLVAAKKTNL CASLDVTTTK ELIELADKVG PYVCMIKTHI
DIIDDFTYAG TVLPLKELAL KHGFFLFEDR KFADIGNTVK HQYKNGVYRI AEWSDITNAH
GVPGTGIIAG LRAGAEETVS EQKKEDVSDY ENSQYKEFLV PSPNEKLARG LLMLAELSCK
GSLATGEYSK QTIELARSDP EFVVGFIAQN RPKGDSEDWL ILTPGVGLDD KGDALGQQYR
TVEDVMSTGT DIIIVGRGLY GQNRDPIEEA KRYQKAGWEA YQKINC