DATPH_BPVC8
ID DATPH_BPVC8 Reviewed; 170 AA.
AC G3FFN4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=dATP triphosphohydrolase {ECO:0000250|UniProtKB:A0A2H5BHG9};
DE Short=dATPase {ECO:0000250|UniProtKB:A0A2H5BHG9};
GN Name=datZ; ORFNames=phiVC8_p25;
OS Vibrio phage phiVC8.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Podoviridae; Enhodamvirus.
OX NCBI_TaxID=1076759;
OH NCBI_TaxID=666; Vibrio cholerae.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27000701; DOI=10.1186/s12985-016-0490-x;
RA Solis-Sanchez A., Hernandez-Chinas U., Navarro-Ocana A., De la Mora J.,
RA Xicohtencatl-Cortes J., Eslava-Campos C.;
RT "Genetic characterization of OVC8 lytic phage for Vibrio cholerae O1.";
RL Virol. J. 13:47-47(2016).
CC -!- FUNCTION: Catalyzes the hydrolysis of dATP, dADP and dAMP into dA. This
CC step is essential for Z-genome synthesis (containing aminoadenine
CC instead of adenine). Specifically removes dATP and its precursor dADP
CC from the nucleotide pool of the host, preventing the incorporation of A
CC into the phage genome and favoring the integration of the Z-base into
CC the viral genome. {ECO:0000250|UniProtKB:A0A2H5BHG9}.
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:0000250|UniProtKB:A0A2H5BHG9};
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:0000250|UniProtKB:A0A2H5BHG9};
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:0000250|UniProtKB:A0A2H5BHG9};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:A0A2H5BHG9};
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; JF712866; AEM62922.1; -; Genomic_DNA.
DR RefSeq; YP_009140154.1; NC_027118.1.
DR SMR; G3FFN4; -.
DR GeneID; 24366409; -.
DR KEGG; vg:24366409; -.
DR Proteomes; UP000008906; 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; IPR003607; HD/PDEase_dom.
DR SMART; SM00471; HDc; 1.
PE 3: Inferred from homology;
KW Cobalt; Hydrolase; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..170
FT /note="dATP triphosphohydrolase"
FT /id="PRO_0000453678"
FT BINDING 15
FT /ligand="dATP"
FT /ligand_id="ChEBI:CHEBI:61404"
FT /evidence="ECO:0000250|UniProtKB:A0A7U3TCA2"
FT BINDING 30
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 62
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 63
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 66
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 71
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 111
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 170 AA; 19221 MW; F986E8B7EF0387FA CRC64;
MMQIQNILRA GHVPRWQLCD TTRTQSIAEH MFNVALIARH MCAHIGINGD EMNEIVVQAL
THDMDEVILG DMPTVTKQRL REAGIEPNGL IDCVETIITD PFAKQLVKIA DLIEAAWWID
EHGIGRHAER VAEITRHRLF SMLNNAKVDK ALTSAGMDAW ERIKHGELLI
