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HAMAP rule MF_04166

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General rule information [?]

Accession MF_04166
Dates 3-JUN-2021 (Created)
1-SEP-2022 (Last updated, Version 5)
Name Phage_PURZ
Scope(s) Viruses
Caudoviricetes
Template(s) G3FFN6 (PURZ_BPVC8); [ Recover all ]
Triggered by HAMAP; MF_04166 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier PURZ
Protein name RecName: Full=N6-succino-2-amino-2'-deoxyadenylate synthase;
                 EC=6.3.4.25;
AltName: Full=2-amino-2'-deoxyadenylo-succinate synthase;
AltName: Full=PurZ;
Gene name Name=purZ;

Comments [?]

FUNCTIONInvolved in the synthesis of the atypical nucleotide dZTP (2- amino-2'-deoxyadenosine-5'-triphosphate). Catalyzes the condensation of aspartate with deoxyguanylate into dSMP (N6-succino-2-amino-2'- deoxyadenylate), which undergoes defumarylation and phosphorylation respectively by host PurB and guanylate/nucleoside diphosphate kinases to give dZTP. dZTP is integrated into the viral genome instead of adenine by the viral DNA polymerase. This Z-base probably completely replaces adenosine and forms a triple bond to the opposite T-base. The resulting non-standard viral DNA is called Z-genome. The chemically modified DNA is probably harder for the host bacteria to digest with nucleases or restriction enzymes.
CATALYTIC ACTIVITY Reaction=ATP + dGMP + L-aspartate = (2S)-2-amino-2'-deoxyadenylo- succinate + ADP + 2 H(+) + phosphate; Xref=Rhea:RHEA:67628, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57673, ChEBI:CHEBI:172924, ChEBI:CHEBI:456216; EC=6.3.4.25; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67629;
case <FTGroup:1>
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
end case
PATHWAYPurine metabolism.
SIMILARITYBelongs to the Caudovirales PurZ family.

Keywords [?]

ATP-binding
Ligase
Magnesium
Metal-binding
Nucleotide-binding
Purine biosynthesis

Gene Ontology [?]

GO:0005524; Molecular function:ATP binding
GO:0000287; Molecular function:magnesium ion binding
GO:0006164; Biological process:purine nucleotide biosynthetic process

Cross-references [?]

Pfam PF00709; Adenylsucc_synt; 0-2;

Features [?]

From: PURZ_BPVC8 (G3FFN6)
Key From To Description Tag Condition FTGroup
ACT_SITE 14 14 /note="Proton acceptor" S
BINDING 14 14 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 S
BINDING 14 14 /ligand="dGMP"
/ligand_id="ChEBI:CHEBI:57673"		 S
BINDING 14 14 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 S 1
BINDING 15 15 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 T
BINDING 16 16 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G
BINDING 17 17 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 K
BINDING 18 18 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G
BINDING 40 40 /ligand="dGMP"
/ligand_id="ChEBI:CHEBI:57673"		 N
BINDING 42 42 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G
BINDING 42 42 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 G 1
BINDING 43 43 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 H
BINDING 44 44 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 T
BINDING 127 127 /ligand="dGMP"
/ligand_id="ChEBI:CHEBI:57673"		 S
BINDING 128 128 /ligand="dGMP"
/ligand_id="ChEBI:CHEBI:57673"		 T
BINDING 142 142 /ligand="dGMP"
/ligand_id="ChEBI:CHEBI:57673"		 R
BINDING 187 187 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 Q
BINDING 202 202 /ligand="dGMP"
/ligand_id="ChEBI:CHEBI:57673"		 T
BINDING 263 263 /ligand="L-aspartate"
/ligand_id="ChEBI:CHEBI:29991"		 T
BINDING 263 263 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 T 1
BINDING 264 264 /ligand="L-aspartate"
/ligand_id="ChEBI:CHEBI:29991"		 V
BINDING 269 269 /ligand="L-aspartate"
/ligand_id="ChEBI:CHEBI:29991"		 R
BINDING 294 294 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 N
BINDING 297 297 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 N
BINDING 330 330 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G

Additional information [?]

Size range 320-420 amino acids
Related rules None
Fusion Nter: None Cter: None



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