AC   MF_04166;
DC   Protein; auto
TR   HAMAP; MF_04166; -; 1; level=0
XX
Names: Phage_PURZ
XX
ID   PURZ
DE   RecName: Full=N6-succino-2-amino-2'-deoxyadenylate synthase;
DE            EC=6.3.4.25;
DE   AltName: Full=2-amino-2'-deoxyadenylo-succinate synthase;
DE   AltName: Full=PurZ;
GN   Name=purZ;
XX
CC   -!- FUNCTION: Involved in the synthesis of the atypical nucleotide dZTP (2-
CC       amino-2'-deoxyadenosine-5'-triphosphate). Catalyzes the condensation of
CC       aspartate with deoxyguanylate into dSMP (N6-succino-2-amino-2'-
CC       deoxyadenylate), which undergoes defumarylation and phosphorylation
CC       respectively by host PurB and guanylate/nucleoside diphosphate kinases
CC       to give dZTP. dZTP is integrated into the viral genome instead of
CC       adenine by the viral DNA polymerase. This Z-base probably completely
CC       replaces adenosine and forms a triple bond to the opposite T-base. The
CC       resulting non-standard viral DNA is called Z-genome. The chemically
CC       modified DNA is probably harder for the host bacteria to digest with
CC       nucleases or restriction enzymes.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dGMP + L-aspartate = (2S)-2-amino-2'-deoxyadenylo-
CC         succinate + ADP + 2 H(+) + phosphate; Xref=Rhea:RHEA:67628,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57673, ChEBI:CHEBI:172924,
CC         ChEBI:CHEBI:456216; EC=6.3.4.25;
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67629;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
end case
CC   -!- PATHWAY: Purine metabolism.
CC   -!- SIMILARITY: Belongs to the Caudovirales PurZ family.
XX
DR   Pfam; PF00709; Adenylsucc_synt; 0-2; trigger=no
XX
KW   ATP-binding
KW   Ligase
KW   Magnesium
KW   Metal-binding
KW   Nucleotide-binding
KW   Purine biosynthesis
XX
GO   GO:0005524; F:ATP binding
GO   GO:0000287; F:magnesium ion binding
GO   GO:0006164; P:purine nucleotide biosynthetic process
XX
FT   From: PURZ_BPVC8 (G3FFN6)
FT   ACT_SITE        14
FT                   /note="Proton acceptor"
FT   Condition: S
FT   BINDING         14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: S
FT   BINDING         14
FT                   /ligand="dGMP"
FT                   /ligand_id="ChEBI:CHEBI:57673"
FT   Condition: S
FT   BINDING         14
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: S
FT   BINDING         15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: T
FT   BINDING         16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G
FT   BINDING         17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: K
FT   BINDING         18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G
FT   BINDING         40
FT                   /ligand="dGMP"
FT                   /ligand_id="ChEBI:CHEBI:57673"
FT   Condition: N
FT   BINDING         42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G
FT   BINDING         42
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: G
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: H
FT   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: T
FT   BINDING         127
FT                   /ligand="dGMP"
FT                   /ligand_id="ChEBI:CHEBI:57673"
FT   Condition: S
FT   BINDING         128
FT                   /ligand="dGMP"
FT                   /ligand_id="ChEBI:CHEBI:57673"
FT   Condition: T
FT   BINDING         142
FT                   /ligand="dGMP"
FT                   /ligand_id="ChEBI:CHEBI:57673"
FT   Condition: R
FT   BINDING         187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: Q
FT   BINDING         202
FT                   /ligand="dGMP"
FT                   /ligand_id="ChEBI:CHEBI:57673"
FT   Condition: T
FT   BINDING         263
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT   Condition: T
FT   BINDING         263
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: T
FT   BINDING         264
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT   Condition: V
FT   BINDING         269
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT   Condition: R
FT   BINDING         294
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: N
FT   BINDING         297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: N
FT   BINDING         330
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G
XX
Size: 320-420;
Related: None;
Template: G3FFN6;
Scope:
 Viruses; Caudoviricetes
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.5 2022/09/01
//