ID   DATPH_BPSHA             Reviewed;         203 AA.
AC   A0A2H5BHG9;
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 triphosphohydrolase {ECO:0000303|PubMed:33926954};
DE            Short=dATPase {ECO:0000303|PubMed:33926954};
GN   Name=datZ; ORFNames=SHab15497_00041;
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, AND COFACTOR.
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 dATP, dADP and dAMP into dA
CC       (PubMed:33926954). This step is essential for Z-genome synthesis
CC       (containing aminoadenine instead of adenine). Specifically removes dATP
CC       and its precursor dADP from the nucleotide pool of the host, preventing
CC       the incorporation of A into the phage genome and favoring the
CC       integration of the Z-base into the viral genome (PubMed:33926954).
CC       {ECO:0000269|PubMed:33926954}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dATP + H2O = 2'-deoxyadenosine + H(+) + triphosphate;
CC         Xref=Rhea:RHEA:67648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17256, ChEBI:CHEBI:18036, ChEBI:CHEBI:61404;
CC         Evidence={ECO:0000269|PubMed:33926954};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dADP + H2O = 2'-deoxyadenosine + diphosphate;
CC         Xref=Rhea:RHEA:67652, ChEBI:CHEBI:15377, ChEBI:CHEBI:17256,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57667;
CC         Evidence={ECO:0000269|PubMed:33926954};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dAMP + H2O = 2'-deoxyadenosine + phosphate;
CC         Xref=Rhea:RHEA:29371, ChEBI:CHEBI:15377, ChEBI:CHEBI:17256,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58245;
CC         Evidence={ECO:0000269|PubMed:33926954};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:33926954};
CC       Note=Uses a typical 2 metal-ion mechanism to dephosphorylate dATP.
CC       {ECO:0000250|UniProtKB:A0A7U3TCA2};
CC   -!- SIMILARITY: Belongs to the Caudovirales dATP triphosphohydrolase
CC       family. {ECO:0000305}.
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DR   EMBL; MG674163; AUG85483.1; -; Genomic_DNA.
DR   SMR; A0A2H5BHG9; -.
DR   Proteomes; UP000241732; Genome.
DR   GO; GO:0016787; F:hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cobalt; Hydrolase; Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..203
FT                   /note="dATP triphosphohydrolase"
FT                   /id="PRO_0000453681"
FT   BINDING         17
FT                   /ligand="dATP"
FT                   /ligand_id="ChEBI:CHEBI:61404"
FT                   /evidence="ECO:0000250|UniProtKB:A0A7U3TCA2"
FT   BINDING         31
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:A0A7U3TCA2"
FT   BINDING         73
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:A0A7U3TCA2"
FT   BINDING         74
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:A0A7U3TCA2"
FT   BINDING         77
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:A0A7U3TCA2"
FT   BINDING         82
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:A0A7U3TCA2"
FT   BINDING         130
FT                   /ligand="Co(2+)"
FT                   /ligand_id="ChEBI:CHEBI:48828"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:A0A7U3TCA2"
SQ   SEQUENCE   203 AA;  23094 MW;  0F19685B549EDC5D CRC64;
     MDKLNIRDIL RAQDVTRWQI VRTKKQSVAE HTFAVQAVLM RLVPLLISTY TAPMKVGFEE
     RLLCECIMGA FWHDIPEVIT GDIASPVKRL IRDGGDITPL DDLEKKVDPA FIKCYTAAKP
     LTLAIIKCAD LMEMVYHLNE YGDQRANSHS WRVQHGINNA FHEHIHNCSE NFPAFKWDVA
     HGLLIEMLDP SQETDIDSIV NGI