ID   DUT_ADEG1               Reviewed;         178 AA.
AC   Q89662; Q86612;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE            Short=dUTPase;
DE            EC=3.6.1.23;
DE   AltName: Full=dUTP pyrophosphatase;
GN   ORFNames=1;
OS   Fowl adenovirus A serotype 1 (strain CELO / Phelps) (FAdV-1) (Avian
OS   adenovirus gal1 (strain Phelps)).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Aviadenovirus; Fowl aviadenovirus A.
OX   NCBI_TaxID=10553;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1338734;
RA   Akopian T.A., Kaverina E.N., Naroditskii B.S., Tikhonenko T.I.;
RT   "Analysis of the nucleotide sequence of a fragment (92-100%) of the CELO
RT   avian adenovirus genome.";
RL   Mol. Genet. Mikrobiol. Virusol. 11:19-23(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8627769; DOI=10.1128/jvi.70.5.2939-2949.1996;
RA   Chiocca S., Kurzbauer R., Schaffner G., Baker A., Mautner V., Cotten M.;
RT   "The complete DNA sequence and genomic organization of the avian adenovirus
RT   CELO.";
RL   J. Virol. 70:2939-2949(1996).
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   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
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DR   EMBL; Z17216; CAA78921.1; -; Genomic_DNA.
DR   EMBL; S61107; AAB26434.1; -; Genomic_DNA.
DR   EMBL; U46933; AAC54895.1; -; Genomic_DNA.
DR   PIR; S26429; S26429.
DR   RefSeq; NP_043869.1; NC_001720.1.
DR   SMR; Q89662; -.
DR   GeneID; 1733464; -.
DR   KEGG; vg:1733464; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000001594; Genome.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046081; P:dUTP catabolic process; IEA:InterPro.
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   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..178
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182967"
FT   CONFLICT        156
FT                   /note="S -> F (in Ref. 1; AAB26434)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   178 AA;  19219 MW;  477C885A944D16F1 CRC64;
     MDPFGSSSVP PCSTSDLPEP KLYFVRLSPH AVPPVRATHG AAGYDLFSAY DIKVPARGRA
     LVPTDLVFQF PPGCYGRIAP RSGLAAKFFI DVGAGVIDPD YRGNVSVVLF NFSESSFNIR
     RGDRVAQLIL ERIMVPELSE LTQLGETDRG ASGFGSTGMG AVDRNQRSVL EWLTPGSR