ID   PYRF_PICST              Reviewed;         267 AA.
AC   P49434; A3M000;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=PICST_50417;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=7811063; DOI=10.1128/aem.60.12.4245-4254.1994;
RA   Yang V.W., Marks J.A., Davis B.P., Jeffries T.W.;
RT   "High-efficiency transformation of Pichia stipitis based on its URA3 gene
RT   and a homologous autonomous replication sequence, ARS2.";
RL   Appl. Environ. Microbiol. 60:4245-4254(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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; U08629; AAA65978.1; -; Genomic_DNA.
DR   EMBL; CP000502; ABN68626.1; -; Genomic_DNA.
DR   RefSeq; XP_001386655.1; XM_001386618.1.
DR   AlphaFoldDB; P49434; -.
DR   SMR; P49434; -.
DR   STRING; 4924.XP_001386655.1; -.
DR   EnsemblFungi; ABN68626; ABN68626; PICST_50417.
DR   GeneID; 4840866; -.
DR   KEGG; pic:PICST_50417; -.
DR   eggNOG; KOG1377; Eukaryota.
DR   HOGENOM; CLU_030821_0_0_1; -.
DR   InParanoid; P49434; -.
DR   OMA; KNFVMGF; -.
DR   OrthoDB; 1303452at2759; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000002258; Chromosome 8.
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; Reference proteome.
FT   CHAIN           1..267
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134675"
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   267 AA;  29529 MW;  D98361C398F49E06 CRC64;
     MVNVQTYTQR AESHQSPVAQ RLFKLMDSKK TNLCASVDVK TTSEFLSLID KLGPYICLVK
     THIDIIDDFS YEGTIVPLLE LSKKHNFMIF EDRKFADIGN TVKSQYSGGV YKIAQWSDIT
     NAHGVTGSGI VQGLKEAARE TTDEPRGLLM LAELSSKGSI AHGKYTEETV EIAKTDKEFV
     IGFIAQRDMG GQDEGFDWIV MTPGVGLDDK GDSLGQQYRT VDEVVSTGTD IIIVGRGLFG
     KGRDPDVEGQ RYREAGWNAY LKKTSQV