ID   DUT_SUHVK               Reviewed;         268 AA.
AC   Q90030; Q85226;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000255|HAMAP-Rule:MF_04031};
DE            Short=dUTPase {ECO:0000255|HAMAP-Rule:MF_04031};
DE            EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_04031};
DE   AltName: Full=dUTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_04031};
GN   Name=DUT {ECO:0000255|HAMAP-Rule:MF_04031}; OrderedLocusNames=UL50;
OS   Suid herpesvirus 1 (strain Kaplan) (SuHV-1) (Pseudorabies virus (strain
OS   Kaplan)).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=33703;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8551588; DOI=10.1128/jvi.70.2.1242-1245.1996;
RA   Joens A., Mettenleiter T.C.;
RT   "Identification and characterization of pseudorabies virus dUTPase.";
RL   J. Virol. 70:1242-1245(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 196-268.
RX   PubMed=7637001; DOI=10.1128/jvi.69.9.5560-5567.1995;
RA   Baumeister J., Klupp B.G., Mettenleiter T.C.;
RT   "Pseudorabies virus and equine herpesvirus 1 share a nonessential gene
RT   which is absent in other herpesviruses and located adjacent to a highly
RT   conserved gene cluster.";
RL   J. Virol. 69:5560-5567(1995).
CC   -!- FUNCTION: Involved in nucleotide metabolism: produces dUMP, the
CC       immediate precursor of thymidine nucleotides and decreases the
CC       intracellular concentration of dUTP to avoid uracil incorporation into
CC       viral DNA. {ECO:0000255|HAMAP-Rule:MF_04031}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_04031};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_04031};
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_04031}.
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DR   EMBL; U38547; AAB02855.1; -; Genomic_DNA.
DR   EMBL; X87246; CAA60688.1; -; Genomic_DNA.
DR   RefSeq; YP_068324.1; NC_006151.1.
DR   SMR; Q90030; -.
DR   GeneID; 2952537; -.
DR   KEGG; vg:2952537; -.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046080; P:dUTP metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   Gene3D; 2.70.40.10; -; 2.
DR   HAMAP; MF_04031; HSV_DUT; 1.
DR   InterPro; IPR029054; dUTPase-like.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR033704; dUTPase_trimeric.
DR   InterPro; IPR034745; HSV_DUT.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; SSF51283; 2.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism.
FT   CHAIN           1..268
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182964"
FT   BINDING         172..174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04031"
FT   BINDING         263..264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04031"
SQ   SEQUENCE   268 AA;  28618 MW;  79D7CFA999204776 CRC64;
     MEESAGATSA QSAATSVSES PAEETILVCA SEPVTVDGGR LLVCRSPGPE GFYKVPLGLK
     VALPTGYAML VAQRGGGRTT NGIVDAGFRG EVQAIVAPGR PRAQFYCTPL RLAPGIATDV
     PFFEVFAPKR DEDAGYDIPC PRELVLPPGG AETVTLPVHR TDGRHWAYVF GRSSLNLRGI
     VVFPTPWESG PCRFRIQNRG AHPVTLESGQ RVAQLVLTRE PLGWITGRSP FPATPRAPMQ
     HRPAWLFARD FVAPSSARGA RGFGSTGL