DATPH_BPS2L
ID DATPH_BPS2L Reviewed; 175 AA.
AC A0A7U3TCA2;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 1.
DT 03-AUG-2022, entry version 4.
DE RecName: Full=dATP triphosphohydrolase {ECO:0000303|PubMed:33893297, ECO:0000303|PubMed:33926954};
DE Short=dATPase {ECO:0000303|PubMed:33926954};
DE AltName: Full=DatZ {ECO:0000303|PubMed:33893297};
GN Name=datZ; ORFNames=S2L_22 {ECO:0000312|EMBL:QQG31317.1};
OS Cyanophage S-2L (Cyanobacteria phage S-2L).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae.
OX NCBI_TaxID=260586;
OH NCBI_TaxID=1129; Synechococcus.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kaminski P.A.;
RL Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (0.86 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=33893297; DOI=10.1038/s41467-021-22626-x;
RA Czernecki D., Legrand P., Tekpinar M., Rosario S., Kaminski P.A.,
RA Delarue M.;
RT "How cyanophage S-2L rejects adenine and incorporates 2-aminoadenine to
RT saturate hydrogen bonding in its DNA.";
RL Nat. Commun. 12:2420-2420(2021).
CC -!- FUNCTION: Catalyzes the hydrolysis of dATP, dADP and dAMP into dA
CC (PubMed:33926954, PubMed:33893297). This step is essential for Z-genome
CC synthesis (containing aminoadenine instead of adenine). Specifically
CC removes dATP and its precursor dADP from the nucleotide pool of the
CC host, preventing the incorporation of A into the phage genome and
CC favoring the integration of the Z-base into the viral genome
CC (PubMed:33926954, PubMed:33893297). {ECO:0000269|PubMed:33893297,
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:33893297, 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:33893297, 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:33893297, ECO:0000269|PubMed:33926954};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:33893297, ECO:0000269|PubMed:33926954};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:33893297};
CC Note=Uses a typical 2 metal-ion mechanism to dephosphorylate dATP
CC (PubMed:33893297). Zn(2+) in the first binding site is replaced by
CC Co(2+) in excess of the latter (PubMed:33893297).
CC {ECO:0000269|PubMed:33893297};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:33893297}.
CC -!- SIMILARITY: Belongs to the Caudovirales dATP triphosphohydrolase
CC family. {ECO:0000305}.
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DR EMBL; MW334946; QQG31317.1; -; Genomic_DNA.
DR SMR; A0A7U3TCA2; -.
DR KEGG; ag:QQG31317; -.
DR Proteomes; UP000595790; 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..175
FT /note="dATP triphosphohydrolase"
FT /id="PRO_0000453683"
FT BINDING 19
FT /ligand="dATP"
FT /ligand_id="ChEBI:CHEBI:61404"
FT /evidence="ECO:0000269|PubMed:33893297"
FT BINDING 34
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:33893297"
FT BINDING 66
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:33893297"
FT BINDING 67
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:33893297"
FT BINDING 70
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:33893297"
FT BINDING 75
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:33893297"
FT BINDING 119
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:33893297"
SQ SEQUENCE 175 AA; 20113 MW; 24FB59B89005FC08 CRC64;
MTLQITETYE RLRASHISRW GIVQTTYPQN IAEHMWRVWL LCRDWGAAAG MPQHTVRQAC
EFALVHDLAE IRTGDAPTPH KTPELKELLA GIEAQIVPEV AELEATMAPE ARELWKFCDT
AEAVLFLKVN GLGAHAYDVQ HLLMEQMKRR LMDSVLDVEV QDELMFQFER TIKKT
