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PYRF_SCHPO
ID   PYRF_SCHPO              Reviewed;         264 AA.
AC   P14965;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 148.
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=ura4; ORFNames=SPCC330.05c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3241624; DOI=10.1007/bf00331307;
RA   Grimm C., Kohli J., Murray J., Maundrell K.;
RT   "Genetic engineering of Schizosaccharomyces pombe: a system for gene
RT   disruption and replacement using the ura4 gene as a selectable marker.";
RL   Mol. Gen. Genet. 215:81-86(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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; X13976; CAA32157.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAA20910.1; -; Genomic_DNA.
DR   PIR; S08503; S08503.
DR   RefSeq; NP_587705.1; NM_001022700.2.
DR   AlphaFoldDB; P14965; -.
DR   SMR; P14965; -.
DR   BioGRID; 275351; 14.
DR   STRING; 4896.SPCC330.05c.1; -.
DR   iPTMnet; P14965; -.
DR   PaxDb; P14965; -.
DR   PRIDE; P14965; -.
DR   EnsemblFungi; SPCC330.05c.1; SPCC330.05c.1:pep; SPCC330.05c.
DR   GeneID; 2538768; -.
DR   KEGG; spo:SPCC330.05c; -.
DR   PomBase; SPCC330.05c; ura4.
DR   VEuPathDB; FungiDB:SPCC330.05c; -.
DR   eggNOG; KOG1377; Eukaryota.
DR   HOGENOM; CLU_030821_0_0_1; -.
DR   InParanoid; P14965; -.
DR   OMA; KNFVMGF; -.
DR   PhylomeDB; P14965; -.
DR   UniPathway; UPA00070; UER00120.
DR   PRO; PR:P14965; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0140453; C:protein aggregate center; IDA:PomBase.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IMP:PomBase.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IGI:PomBase.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IMP:PomBase.
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..264
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134683"
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         62..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         93..102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   264 AA;  29362 MW;  C9B78224E1EE1299 CRC64;
     MDARVFQSYS ARAEGMKNPI AKELLALMEE KQSNLSVAVD LTKKSEILEL VDKIGPYVCV
     IKTHIDVVED FDQDMVEKLV ALGKKHRFLI FEDRKFADIG NTVKLQYASG VYKIASWAHI
     TNCHTVPGEG IIQGLKEVGL PLGRGLLLLA EMSSKGSLAT GSYTEKTLEW FEKHTDFCFG
     FIAGRRFPNL QSDYITMSPG IGLDVKGDGL GQQYRTPEEV IVNCGSDIII VGRGVYGAGR
     NPVVEAKRYR EAGWKAYQQR LSQH
 
 
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