PURZ_BPS2L
ID PURZ_BPS2L Reviewed; 359 AA.
AC A0A7U3TBV6;
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=N6-succino-2-amino-2'-deoxyadenylate synthase {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}; ORFNames=S2L_24;
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 PATHWAY.
RX PubMed=33926955; DOI=10.1126/science.abe6494;
RA Sleiman D., Garcia P.S., Lagune M., Loc'h J., Haouz A., Taib N.,
RA Roethlisberger P., Gribaldo S., Marliere P., Kaminski P.A.;
RT "A third purine biosynthetic pathway encoded by aminoadenine-based viral
RT DNA genomes.";
RL Science 372:516-520(2021).
CC -!- FUNCTION: Involved in the synthesis of the atypical nucleotide dZTP (2-
CC amino-2'-deoxyadenosine-5'-triphosphate) (PubMed:33926955). Involved in
CC the synthesis of N6-succino-2-amino-2'-deoxyadenylate, which undergoes
CC defumarylation and phosphorylation respectively by host PurB and
CC guanylate/nucleoside diphosphate kinases to give dZTP (2-amino-2'-
CC deoxyadenosine-5'-triphosphate) (PubMed:33926955). dZTP is integrated
CC into the viral genome instead of adenine by the viral polymerase. This
CC Z-base probably completely replaces adenosine and forms a triple bond
CC to the opposite T-base (PubMed:33926955). The resulting non-standard
CC viral DNA is called Z-genome (PubMed:33926955). The chemically modified
CC DNA is probably harder for the host bacteria to digest with nucleases
CC or restriction enzymes (Probable). {ECO:0000255|HAMAP-Rule:MF_04166,
CC ECO:0000269|PubMed:33926955}.
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:33926955};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04166,
CC ECO:0000269|PubMed:33926955};
CC -!- PATHWAY: Purine metabolism. {ECO:0000255|HAMAP-Rule:MF_04166,
CC ECO:0000269|PubMed:33926955}.
CC -!- SIMILARITY: Belongs to the Caudovirales PurZ family.
CC {ECO:0000255|HAMAP-Rule:MF_04166}.
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DR EMBL; MW334946; QQG31319.1; -; Genomic_DNA.
DR PDB; 7ODX; X-ray; 1.70 A; A=1-359.
DR PDBsum; 7ODX; -.
DR SMR; A0A7U3TBV6; -.
DR KEGG; ag:QQG31319; -.
DR Proteomes; UP000595790; 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; IDA:UniProtKB.
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 3D-structure; ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1..359
FT /note="N6-succino-2-amino-2'-deoxyadenylate synthase"
FT /id="PRO_0000453690"
FT ACT_SITE 23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 23
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 305..308
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G3FFN6"
SQ SEQUENCE 359 AA; 39379 MW; B8A92C97BFEE1EE6 CRC64;
MLSIPPYYRV KNCNLIVDCQ YGSTGKGLLA GYLGALEAPQ VLCMAPSPNA GHTLVEEDGT
ARVHKMLPLG ITSPSLERIY LGPGSVIDMD RLLEEYLALP RQVELWVHQN AAVVLQEHRD
EEAAGGLAPG STRSGAGSAF IAKIRRRPGT LLFGEAVRDH PLHGVVRVVD TRTAQDMLFR
TRSIQAEGCQ GYSLSVHHGA YPYCTARDVT TAQLIADCGL PYDVARIARV VGSMRTYPIR
VANRPEAGEW SGPCYPDSVE CQFADLGLEQ EYTTVTKLPR RIFTFSAIQA HEAIAQNGVD
EVFLNFAQYP PSLGALEDIL DAIEARAEVT YVGFGPKVTD VYHTPTRAEL EGLYARYRR
