ID   DUT_SOLLC               Reviewed;         169 AA.
AC   P32518;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE            Short=dUTPase;
DE            EC=3.6.1.23;
DE   AltName: Full=P18;
DE   AltName: Full=dUTP pyrophosphatase;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Tiny Tim LA154; TISSUE=Meristem;
RX   PubMed=1321683; DOI=10.2307/3869568;
RA   Pri-Hadash A., Hareven D., Lifschitz E.;
RT   "A meristem-related gene from tomato encodes a dUTPase: analysis of
RT   expression in vegetative and floral meristems.";
RL   Plant Cell 4:149-159(1992).
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. It may have as well a metabolic role in
CC       merismatic cells.
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: Homodimer.
CC   -!- TISSUE SPECIFICITY: Vegetative and floral merismatic cells and
CC       provascular and vascular merismatic derivatives.
CC   -!- SIMILARITY: Belongs to the dUTPase 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; S40549; AAB22611.1; -; mRNA.
DR   PIR; JQ1599; JQ1599.
DR   RefSeq; NP_001233870.1; NM_001246941.2.
DR   AlphaFoldDB; P32518; -.
DR   SMR; P32518; -.
DR   STRING; 4081.Solyc01g100030.2.1; -.
DR   PaxDb; P32518; -.
DR   PRIDE; P32518; -.
DR   GeneID; 544274; -.
DR   KEGG; sly:544274; -.
DR   eggNOG; KOG3370; Eukaryota.
DR   OrthoDB; 1495752at2759; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P32518; baseline.
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: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   PANTHER; PTHR11241; PTHR11241; 1.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; SSF51283; 1.
DR   TIGRFAMs; TIGR00576; dut; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..169
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182938"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         91..93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         105..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         164..165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   169 AA;  17929 MW;  60FB80A052BBC224 CRC64;
     MAENQINSPE ITEPSPKVQK LDHPENGNVP FFRVKKLSEN AVLPSRASSL AAGYDLSSAA
     ETKVPARGKA LVPTDLSIAV PQGTYARIAP RSGLAWKYSI DVGAGVIDAD YRGPVGVVLF
     NHSEVDFEVK VGDRIAQLIV QKIVTPEVEQ VDDLDSTVRG SGGFGSTGV