PURZ_BPSHA
ID PURZ_BPSHA Reviewed; 387 AA.
AC A0A2H5BHJ6;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 1.
DT 03-AUG-2022, entry version 19.
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};
GN ORFNames=SHab15497_00039 {ECO:0000312|EMBL:AUG85481.1};
OS Acinetobacter phage SH-Ab 15497.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae.
OX NCBI_TaxID=2060946;
OH NCBI_TaxID=470; Acinetobacter baumannii.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=31555825; DOI=10.1093/abbs/gmz094;
RA Hua Y., Xu M., Wang R., Zhang Y., Zhu Z., Guo M., He P.;
RT "Characterization and whole genome analysis of a novel bacteriophage SH-Ab
RT 15497 against multidrug resistant Acinetobacater baummanii.";
RL Acta Biochim. Biophys. Sin. 51:1079-1081(2019).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, ACTIVE SITE,
RP AND PATHWAY.
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) (PubMed:33926954). Catalyzes
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
CC (PubMed:33926954). 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
CC (PubMed:33926954). The resulting non-standard viral DNA is called Z-
CC genome (PubMed:33926954). The chemically modified DNA is probably
CC harder for the host bacteria to digest with nucleases or restriction
CC enzymes (Probable). {ECO:0000255|HAMAP-Rule:MF_04166,
CC ECO:0000269|PubMed:33926954}.
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=5.1 uM for dGMP {ECO:0000269|PubMed:33926954};
CC KM=21.1 uM for ATP {ECO:0000269|PubMed:33926954};
CC KM=90.9 uM for Asp {ECO:0000269|PubMed:33926954};
CC -!- PATHWAY: Purine metabolism. {ECO:0000255|HAMAP-Rule:MF_04166,
CC ECO:0000269|PubMed:33926954}.
CC -!- SIMILARITY: Belongs to the Caudovirales PurZ family.
CC {ECO:0000255|HAMAP-Rule:MF_04166}.
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DR EMBL; MG674163; AUG85481.1; -; Genomic_DNA.
DR SMR; A0A2H5BHJ6; -.
DR BRENDA; 6.3.4.25; 17968.
DR Proteomes; UP000241732; 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; 1.10.300.10; -; 1.
DR Gene3D; 3.40.440.10; -; 1.
DR HAMAP; MF_00011; Adenylosucc_synth; 1.
DR HAMAP; MF_04166; Phage_PURZ; 1.
DR InterPro; IPR042109; Adenylosuccinate_synth_dom1.
DR InterPro; IPR042110; Adenylosuccinate_synth_dom2.
DR InterPro; IPR001114; Adenylosuccinate_synthetase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR046383; Phage_PurZ.
DR PANTHER; PTHR11846; PTHR11846; 1.
DR Pfam; PF00709; Adenylsucc_synt; 1.
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..387
FT /note="N6-succino-2-amino-2'-deoxyadenylate synthase"
FT /id="PRO_0000453689"
FT ACT_SITE 14
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166,
FT ECO:0000305|PubMed:33926954"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166,
FT ECO:0000305|PubMed:33926954"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04166"
FT BINDING 324..327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:G3FFN6"
SQ SEQUENCE 387 AA; 42646 MW; 38B6C3732215CEBB CRC64;
MKKATVICDM QFGSTGKGLI AGFLAERDQP DVVVTAWSAN AGHTYINREG RKWVHCMLAN
GIVSPKLKAV LIGGGSQMSI PTLISEIMGS LDILQGKSIL IHENACIIQQ RHVEEEAGPM
TKIGSTKKGC GAAMMEKIRR NPESKIVAKD FIDDGLEIPD FKLDGTVGFK DISRHFEELG
VCIKVVSNEV YLAVLHKAER VQVEGAQGFS LGLHNGFYPY VTSRECTPAQ ICSDCNVPIS
MVDKVVGTMR TYPIRVANRF DDEGKMVGWS GPCYSDQTEL TWEQMGVTPE KTTVTKLTRR
IFSFSRMQTR QAMLVCMPDE IFLNFANYCA SEDELASIIE VISNEGGDVS YIGWGDSAAH
IETTLEGDWS DDTNPLFNQY NKSSNIA
