DATPH_BPPMB
ID DATPH_BPPMB Reviewed; 194 AA.
AC A0A2L0V156;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=dATP triphosphohydrolase {ECO:0000303|PubMed:33926954};
DE Short=dATPase {ECO:0000303|PubMed:33926954};
GN Name=datZ;
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).
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; MG641885; AUZ95524.1; -; Genomic_DNA.
DR SMR; A0A2L0V156; -.
DR Proteomes; UP000241443; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW ATP-binding; Cobalt; Hydrolase; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..194
FT /note="dATP triphosphohydrolase"
FT /id="PRO_0000453682"
FT BINDING 17
FT /ligand="dATP"
FT /ligand_id="ChEBI:CHEBI:61404"
FT /evidence="ECO:0000250|UniProtKB:A0A7U3TCA2"
FT BINDING 32
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 71
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 72
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 75
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 80
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 123
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 194 AA; 21903 MW; 399BBC944240B5FC CRC64;
MMTMTPRDLM RAQYVTRWQI VPTTRSQSVA QHSWAVAMLA MNLWCRRTGG QPGEAATDVE
LGKIAVMALW HDAPEVFTGD INTPTKIFLN ASNALDELEN TAGDGYLESM DGGPIRTCVK
IADFLEAMYW LMEHGDGHYA NNQLHGLNER FHQYLNEHAP LWRDSAVALW KELSDVNAET
TTFQRVNYLK ANDA
