PURZ_BPPMB
ID PURZ_BPPMB Reviewed; 367 AA.
AC A0A2L0V130;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=N6-succino-2-amino-2'-deoxyadenylate synthase {ECO:0000250|UniProtKB:G3FFN6, ECO:0000255|HAMAP-Rule:MF_04166};
DE AltName: Full=PurZ {ECO:0000255|HAMAP-Rule:MF_04166};
GN Name=purZ {ECO:0000255|HAMAP-Rule:MF_04166};
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 BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND ACTIVE SITE.
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: Involved in the synthesis of the atypical nucleotide dZTP (2-
CC amino-2'-deoxyadenosine-5'-triphosphate). Involved in the synthesis of
CC N6-succino-2-amino-2'-deoxyadenylate, which undergoes defumarylation
CC and phosphorylation respectively by host PurB and guanylate/nucleoside
CC diphosphate kinases to give dZTP (2-amino-2'-deoxyadenosine-5'-
CC triphosphate). dZTP is integrated into the viral genome instead of
CC adenine by the viral 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. {ECO:0000255|HAMAP-Rule:MF_04166}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_04166,
CC ECO:0000269|PubMed:33926954};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04166};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 uM for dGMP {ECO:0000269|PubMed:33926954};
CC KM=12.6 uM for ATP {ECO:0000269|PubMed:33926954};
CC KM=40.4 uM for Asp {ECO:0000269|PubMed:33926954};
CC -!- PATHWAY: Purine metabolism. {ECO:0000255|HAMAP-Rule:MF_04166}.
CC -!- SIMILARITY: Belongs to the Caudovirales PurZ family.
CC {ECO:0000255|HAMAP-Rule:MF_04166}.
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DR EMBL; MG641885; AUZ95522.1; -; Genomic_DNA.
DR SMR; A0A2L0V130; -.
DR Proteomes; UP000241443; Genome.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.440.10; -; 2.
DR HAMAP; MF_04166; Phage_PURZ; 1.
DR InterPro; IPR042109; Adenylosuccinate_synth_dom1.
DR InterPro; IPR001114; Adenylosuccinate_synthetase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR046383; Phage_PurZ.
DR PANTHER; PTHR11846; PTHR11846; 2.
DR Pfam; PF00709; Adenylsucc_synt; 2.
DR SMART; SM00788; Adenylsucc_synt; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1..367
FT /note="N6-succino-2-amino-2'-deoxyadenylate synthase"
FT /id="PRO_0000453691"
FT ACT_SITE 17
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166,
FT ECO:0000305|PubMed:33926954"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 315..318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:33926954"
SQ SEQUENCE 367 AA; 40309 MW; 43B466DE5E336CA2 CRC64;
MNSNKKATIV VDAQFGSTGK GLIAGYLAER DQPDVVMTAW SANAGHTYIN AEGRKFVHCM
LANGIVSPKL TTVLIGPGSQ MNAELLRDEI LSCADLLQGK TILLHASAAL ILQKHVEEEA
GPMTKIGSTK KGCGAAMIAK IRRNPDDNNT VGANGDYMEE HIYGPVREAG VFIRTATNAE
YMAVVYDAER IQVEGAQGFS LGINNGFYPY VTSRECTPAQ VAVDVNLPLA FIDKVVACMR
TLPIRVANRY NDKGEQIGWS GPCYPDQKEL DWEKDLGMEA ELTTVTKLPR RIFTFSYEQT
KAALEVIRPD EVFLNFCNYL EPDEVAAVIG TIERAAHELK VPGPMPLARY YGYGPTVNDI
DLDMRHQ
