ID   DGTPH_BPS2L             Reviewed;         105 AA.
AC   A0A7U3TBV3;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   02-JUN-2021, sequence version 1.
DT   03-AUG-2022, entry version 5.
DE   RecName: Full=dATP/dGTP diphosphohydrolase {ECO:0000305};
DE            EC=3.6.1.9 {ECO:0000250|UniProtKB:A0A2H5BHG5};
DE   AltName: Full=dATP/dGTP pyrophosphohydrolase {ECO:0000250|UniProtKB:A0A2H5BHG5};
GN   ORFNames=S2L_23 {ECO:0000312|EMBL:QQG31318.1};
OS   Cyanophage S-2L (Cyanobacteria phage S-2L).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae.
OX   NCBI_TaxID=260586;
OH   NCBI_TaxID=1129; Synechococcus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kaminski P.A.;
RL   Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of dGTP into dGMP, which is needed
CC       among other for the first step of biosynthesis of dZTP (2-amino-2'-
CC       deoxyadenosine-5'-triphosphate). {ECO:0000250|UniProtKB:A0A2H5BHG5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dGTP + H2O = dGMP + diphosphate + H(+); Xref=Rhea:RHEA:28362,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57673, ChEBI:CHEBI:61429; EC=3.6.1.9;
CC         Evidence={ECO:0000250|UniProtKB:A0A2H5BHG5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dATP + H2O = dAMP + diphosphate + H(+); Xref=Rhea:RHEA:28334,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58245, ChEBI:CHEBI:61404; EC=3.6.1.9;
CC         Evidence={ECO:0000250|UniProtKB:A0A2H5BHG5};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000250|UniProtKB:A0A2H5BHG5};
CC   -!- PATHWAY: Purine metabolism. {ECO:0000250|UniProtKB:A0A2H5BHG5}.
CC   -!- SIMILARITY: Belongs to the Caudovirales dATP/dGTP diphosphohydrolase
CC       family. {ECO:0000305}.
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DR   EMBL; MW334946; QQG31318.1; -; Genomic_DNA.
DR   PDB; 7ODY; X-ray; 1.43 A; A/B/C/D=1-105.
DR   PDBsum; 7ODY; -.
DR   SMR; A0A7U3TBV3; -.
DR   KEGG; ag:QQG31318; -.
DR   Proteomes; UP000595790; Genome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   InterPro; IPR007538; dATP/dGTP_dipphydrolase_MazZ.
DR   Pfam; PF04447; DUF550; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cobalt; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..105
FT                   /note="dATP/dGTP diphosphohydrolase"
FT                   /id="PRO_0000453686"
SQ   SEQUENCE   105 AA;  11250 MW;  A6DFCB5D6DE540B8 CRC64;
     MPATVAELQA EIAAWIHPLN PDRRPGGTIA KLLEEIGELI ASDRAHDPLE VADVLILALD
     LATLLGVDVT EAIRAKLAIN RARSWARADN GAMRHIPGSD TPSFP