ID   DGTPH_BPSHA             Reviewed;         385 AA.
AC   A0A2H5BHG5;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-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:0000269|PubMed:33926954};
DE   AltName: Full=dATP/dGTP pyrophosphohydrolase {ECO:0000303|PubMed:33926954};
GN   ORFNames=SHab15497_00040 {ECO:0000312|EMBL:AUG85482.1};
OS   Acinetobacter phage SH-Ab 15497.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae.
OX   NCBI_TaxID=2060946;
OH   NCBI_TaxID=470; Acinetobacter baumannii.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=31555825; DOI=10.1093/abbs/gmz094;
RA   Hua Y., Xu M., Wang R., Zhang Y., Zhu Z., Guo M., He P.;
RT   "Characterization and whole genome analysis of a novel bacteriophage SH-Ab
RT   15497 against multidrug resistant Acinetobacater baummanii.";
RL   Acta Biochim. Biophys. Sin. 51:1079-1081(2019).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RX   PubMed=33926954; DOI=10.1126/science.abe4882;
RA   Zhou Y., Xu X., Wei Y., Cheng Y., Guo Y., Khudyakov I., Liu F., He P.,
RA   Song Z., Li Z., Gao Y., Ang E.L., Zhao H., Zhang Y., Zhao S.;
RT   "A widespread pathway for substitution of adenine by diaminopurine in phage
RT   genomes.";
RL   Science 372:512-516(2021).
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:0000269|PubMed:33926954}.
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:0000269|PubMed:33926954};
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:0000269|PubMed:33926954};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:33926954};
CC   -!- PATHWAY: Purine metabolism. {ECO:0000269|PubMed:33926954}.
CC   -!- SIMILARITY: Belongs to the Caudovirales dATP/dGTP diphosphohydrolase
CC       family. {ECO:0000305}.
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DR   EMBL; MG674163; AUG85482.1; -; Genomic_DNA.
DR   SMR; A0A2H5BHG5; -.
DR   Proteomes; UP000241732; Genome.
DR   GO; GO:0008828; F:dATP pyrophosphohydrolase activity; IDA:UniProtKB.
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   Pfam; PF04447; DUF550; 1.
DR   Pfam; PF18909; DUF5664; 1.
PE   1: Evidence at protein level;
KW   Cobalt; Hydrolase; Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..385
FT                   /note="dATP/dGTP diphosphohydrolase"
FT                   /id="PRO_0000453684"
SQ   SEQUENCE   385 AA;  43586 MW;  8CBB3C25491CE852 CRC64;
     MSGNKFDQEK VDLHVLDPFF IEGTARVAQF GEQKYGRSNW MQGLTQTRII NAIKRHIAQI
     EKGEDIDEES GFHHAYHAAW GCQVLAYQHR NGQTHLDDRR WSESVRDADT KIGTCEGISG
     HTVPCMYEGP FGRLHPVDGE KDGLVMSFVQ SEADEGTAQG DPIQQLQQMI SEWADQVYPD
     RTVENALTKM MLHEIPELLH GKAMDPAEFA DVAILLFDVA HLQGIDIAQA MREKMEINQA
     RDWKIDPATG LMSHVKPKGM METIRDAVQG IGDAARIMAA PSRLLNGNNM ELAEYTAETL
     PKPPEKPWEI TIPNWALKTE EGTHIKLRAG SGVFGRVKYQ SQCILMHKNM RKRSHLETYY
     CATIKDTVTE DEYNVPWSEI EPWTN