ID   DUT_SCHPO               Reviewed;         140 AA.
AC   Q9P6Q5;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Probable deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE            Short=dUTPase;
DE            EC=3.6.1.23;
DE   AltName: Full=dUTP pyrophosphatase;
GN   ORFNames=SPAC644.05c;
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 [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   -!- FUNCTION: This enzyme is involved in nucleotide metabolism: it produces
CC       dUMP, the immediate precursor of thymidine nucleotides and it decreases
CC       the intracellular concentration of dUTP so that uracil cannot be
CC       incorporated into DNA. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 2/2.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB90132.1; -; Genomic_DNA.
DR   RefSeq; NP_593873.1; NM_001019303.2.
DR   AlphaFoldDB; Q9P6Q5; -.
DR   SMR; Q9P6Q5; -.
DR   STRING; 284812.Q9P6Q5; -.
DR   iPTMnet; Q9P6Q5; -.
DR   MaxQB; Q9P6Q5; -.
DR   PaxDb; 4896-SPAC644-05c-1; -.
DR   EnsemblFungi; SPAC644.05c.1; SPAC644.05c.1:pep; SPAC644.05c.
DR   GeneID; 2543669; -.
DR   KEGG; spo:SPAC644.05c; -.
DR   PomBase; SPAC644.05c; -.
DR   VEuPathDB; FungiDB:SPAC644.05c; -.
DR   eggNOG; KOG3370; Eukaryota.
DR   HOGENOM; CLU_068508_2_1_1; -.
DR   InParanoid; Q9P6Q5; -.
DR   OMA; ICYPDLE; -.
DR   PhylomeDB; Q9P6Q5; -.
DR   Reactome; R-SPO-499943; Interconversion of nucleotide di- and triphosphates.
DR   UniPathway; UPA00610; UER00666.
DR   PRO; PR:Q9P6Q5; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0035870; F:dITP diphosphatase activity; ISO:PomBase.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0035863; P:dITP catabolic process; ISO:PomBase.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0046081; P:dUTP catabolic process; IBA:GO_Central.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   Gene3D; 2.70.40.10; -; 1.
DR   InterPro; IPR008181; dUTPase.
DR   InterPro; IPR029054; dUTPase-like.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR033704; dUTPase_trimeric.
DR   NCBIfam; TIGR00576; dut; 1.
DR   PANTHER; PTHR11241; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR   PANTHER; PTHR11241:SF0; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; dUTPase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..140
FT                   /note="Probable deoxyuridine 5'-triphosphate
FT                   nucleotidohydrolase"
FT                   /id="PRO_0000182935"
FT   BINDING         62..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         76..79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         135..136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   140 AA;  14862 MW;  3C8F2FCC9AAE2CCE CRC64;
     MSFFVQKLSE KATIPTKGSA NSAGYDLYAA AECIVPRRGK VLVDTDLAIA VPEGTYGRVA
     PRSGLASKHS IDTGAGVIDA DYRGHVRVLL FNYSDVDFPI KVGDRIAQLI LERIVNPPVI
     LVESLEATVR GANGFGSTGV
//