DUT_EBVB9
ID DUT_EBVB9 Reviewed; 278 AA.
AC P03195; Q777F3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 99.
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}; ORFNames=BLLF3;
OS Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10377;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6087149; DOI=10.1038/310207a0;
RA Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA Tuffnell P.S., Barrell B.G.;
RT "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL Nature 310:207-211(1984).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 4-116 AND 121-256, AND SUBUNIT.
RX PubMed=16154087; DOI=10.1016/j.str.2005.06.009;
RA Tarbouriech N., Buisson M., Seigneurin J.M., Cusack S., Burmeister W.P.;
RT "The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases.";
RL Structure 13:1299-1310(2005).
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 -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16154087}.
CC -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_04031}.
CC -!- CAUTION: BLLF3 is known as BLLF2 in PubMed:6087149. {ECO:0000305}.
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DR EMBL; V01555; CAA24850.1; -; Genomic_DNA.
DR EMBL; AJ507799; CAD53414.1; -; Genomic_DNA.
DR PIR; A03758; QQBE17.
DR RefSeq; YP_401664.1; NC_007605.1.
DR PDB; 2BSY; X-ray; 1.50 A; A=1-278.
DR PDB; 2BT1; X-ray; 2.70 A; A=1-278.
DR PDB; 2WE0; X-ray; 2.01 A; A=1-278.
DR PDB; 2WE1; X-ray; 1.80 A; A=1-278.
DR PDB; 2WE2; X-ray; 1.50 A; A=1-278.
DR PDB; 2WE3; X-ray; 2.00 A; A=1-256.
DR PDBsum; 2BSY; -.
DR PDBsum; 2BT1; -.
DR PDBsum; 2WE0; -.
DR PDBsum; 2WE1; -.
DR PDBsum; 2WE2; -.
DR PDBsum; 2WE3; -.
DR SMR; P03195; -.
DR IntAct; P03195; 5.
DR MINT; P03195; -.
DR PRIDE; P03195; -.
DR DNASU; 3783715; -.
DR GeneID; 3783715; -.
DR KEGG; vg:3783715; -.
DR BRENDA; 3.6.1.23; 2112.
DR EvolutionaryTrace; P03195; -.
DR Proteomes; UP000153037; Genome.
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; 2.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide metabolism; Reference proteome.
FT CHAIN 1..278
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000182962"
FT BINDING 76
FT /ligand="substrate"
FT BINDING 84
FT /ligand="substrate"
FT BINDING 171..173
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04031"
FT BINDING 273..274
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04031"
FT DISULFID 4..246
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 40..51
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:2WE2"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:2BSY"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:2BSY"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:2BSY"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:2BSY"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:2BSY"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:2BSY"
SQ SEQUENCE 278 AA; 30953 MW; 73C90EFF4B863525 CRC64;
MEACPHIRYA FQNDKLLLQQ ASVGRLTLVN KTTILLRPMK TTTVDLGLYA RPPEGHGLML
WGSTSRPVTS HVGIIDPGYT GELRLILQNQ RRYNSTLRPS ELKIHLAAFR YATPQMEEDK
GPINHPQYPG DVGLDVSLPK DLALFPHQTV SVTLTVPPPS IPHHRPTIFG RSGLAMQGIL
VKPCRWRRGG VDVSLTNFSD QTVFLNKYRR FCQLVYLHKH HLTSFYSPHS DAGVLGPRSL
FRWASCTFEE VPSLAMGDSG LSEALEGRQG RGFGSSGQ
