ID   DGTPH_BPPMB             Reviewed;         290 AA.
AC   A0A2L0V161;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   25-APR-2018, sequence version 1.
DT   03-AUG-2022, entry version 14.
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};
OS   Salmonella phage PMBT28.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae.
OX   NCBI_TaxID=2081904;
OH   NCBI_TaxID=28901; Salmonella enterica (Salmonella choleraesuis).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=29954894; DOI=10.1128/genomea.00568-18;
RA   Koberg S., Brinks E., Albrecht V., Neve H., Franz C.M.A.P.;
RT   "Complete Genome Sequence of the Novel Virulent Phage PMBT28 with Lytic
RT   Activity against Thermotolerant Salmonella enterica subsp. enterica Serovar
RT   Senftenberg ATCC 43845.";
RL   Genome Announc. 6:0-0(2018).
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; MG641885; AUZ95523.1; -; Genomic_DNA.
DR   SMR; A0A2L0V161; -.
DR   Proteomes; UP000241443; 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; IPR044038; dATP/dGTP_diPOhydrolase_N.
DR   InterPro; IPR007538; dATP/dGTP_dipphydrolase_MazZ.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF04447; DUF550; 1.
DR   Pfam; PF18909; DUF5664; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   3: Inferred from homology;
KW   Cobalt; Hydrolase; Metal-binding; Nucleotide-binding; Reference proteome;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..290
FT                   /note="dATP/dGTP diphosphohydrolase"
FT                   /id="PRO_0000453685"
FT   ZN_FING         262..285
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          103..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   290 AA;  31970 MW;  115A93A43D2FB806 CRC64;
     MTGIKFDQGK APLSLIDPRF TEEVARVLAI GEQKYGRANW QGLKIERLLD AVKRHVLELE
     KSNDHDDETG LHHAAHAASG LMFIFWLLNN RPTSDDRRWS AAVPGVREQR GSVQPVPDSE
     EGLDMQPVPA PSPSRSKKRA YSTGTIADVQ KLISGWADRT FPDRTIGEAI LKLKKELAEL
     DTASYLDAGE FADVAILLLD IAQLAGIDIA TAVANKMAIN ERRVWQRLED GTHQHVIDGG
     RTDGVDPIIR VAMLPTDPTG SHLCVVCGQR FGSEDDRASH YTTTHGDRKP