Detail Information for IndEnz0005001246
IED ID IndEnz0005001246
Enzyme Type ID lipase001246
Protein Name Cyclic GMP-AMP synthase
c-GAMP synthase
c-GMP-AMP synthase
EC 2.7.7.-
3'3'-cGAMP synthase
CD-NTase001
Gene Name dncV DU321_04130
Organism Escherichia coli
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli
Enzyme Sequence MPWDFNNYYSHNMDGLISKLKLSKTESDKLKALRQIVRERTRDVFQEARQVAIDVRRQALTLESVRLKLEKTNVRYLSPEERADLARLIFEMEDEARDDFIKFQPRFWTQGSFQYDTLNRPFHPGQEMDIDDGTYMPMTVFESEPSIGHTLLLLLVDTSLKSLEAENDGWVFEEKNTCGRIKIYREKTHIDVPMYAIPKEQFQKKQTAADSAHLIKSDSVFESFALNRGGREAYAVESDKVNLALREGVRRWSVSDPKIVEDWFNESCKRIGGHLRSVCRFMKAWRDAQWEVGGPSSISLMTAVVNILDRESHNGSDLTGTMKLIARLLPEEFNRGVESPDDTDEKPLFPAESNHNVHHRAIVETMEGLYGILLAAEQSESREEALRKINEAFGKRVTNALLITSSAAAPAFLNAPSKEPSSKPINKTMVSG
Enzyme Length 432
Uniprot Accession Number Q6XGD8
Absorption
Active Site
Activity Regulation
Binding Site BINDING 180; /note=ATP; /evidence=ECO:0000250|UniProtKB:Q9KVG7; BINDING 255; /note=ATP; /evidence=ECO:0000250|UniProtKB:Q9KVG7; BINDING 283; /note=GTP; /evidence=ECO:0000269|PubMed:25865248; BINDING 297; /note=GTP; /evidence=ECO:0000269|PubMed:25865248; BINDING 344; /note=GTP; /evidence=ECO:0000269|PubMed:25865248
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=ATP + GTP = 3',3'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:35647, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:71501; Evidence={ECO:0000269|PubMed:30837338};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35648; Evidence={ECO:0000269|PubMed:30837338};
DNA Binding
EC Number 2.7.7.-
Enzyme Function FUNCTION: CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-C(GA) CBASS system (PubMed:32839535). {ECO:0000303|PubMed:32839535, ECO:0000305}.; FUNCTION: Catalyzes the synthesis of 3'3'-cyclic GMP-AMP (3'3'-cGAMP) from GTP and ATP, a second messenger in cell signal transduction. Is also able to produce c-di-AMP and c-di-GMP from ATP and GTP, respectively; however, 3'3'-cGAMP is the dominant molecule produced by DncV in vivo, contrary to the 2'3'-cGAMP produced by eukaryotes. By producing cGAMP, down-regulates csgD expression and expression of flagellum regulon genes, which leads to the down-regulation of rdar biofilm formation and flagellum-mediated swimming and swarming motility in a temperature-dependent manner (PubMed:30837338). Controls the activity of cGAMP-activated phospholipase CapV, a patatin-like lipase that is a direct 3',3'-cGAMP receptor encoded in the dncV operon (By similarity). {ECO:0000250|UniProtKB:Q9KVG7, ECO:0000269|PubMed:30837338}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 110..115; /note=GTP; /evidence=ECO:0000269|PubMed:25865248
Features Beta strand (10); Binding site (5); Chain (1); Helix (19); Metal binding (3); Mutagenesis (2); Nucleotide binding (1); Region (1); Turn (3)
Keywords 3D-structure;ATP-binding;Antiviral defense;GTP-binding;Magnesium;Metal-binding;Nucleotide metabolism;Nucleotide-binding;Nucleotidyltransferase;Transferase
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 4XJ6;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 49,276
Kinetics
Metal Binding METAL 129; /note="Magnesium"; /evidence="ECO:0000269|PubMed:25865248, ECO:0007744|PDB:4XJ6"; METAL 131; /note="Magnesium"; /evidence="ECO:0000269|PubMed:25865248, ECO:0007744|PDB:4XJ6"; METAL 191; /note="Magnesium"; /evidence="ECO:0000269|PubMed:25865248, ECO:0007744|PDB:4XJ6"
Rhea ID RHEA:35647; RHEA:35648
Cross Reference Brenda