| IED ID | IndEnz0005000420 |
| Enzyme Type ID | lipase000420 |
| Protein Name |
Cyclic UMP-AMP synthase cUMP-AMP synthase EC 2.7.7.- 3',3'-cUAMP synthase cGAS/DncV-like nucleotidyltransferase in E.coli CD-NTase056 |
| Gene Name | cdnE |
| Organism | Escherichia coli |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli |
| Enzyme Sequence | MGIPESQLDTWSHQGSIAQSASTYSIIKNALESANTKYHGKNFKVFLQGSYGNDTNIYAESDVDVVICLDDVYYSDLTQLSPEDKDAYDRAFVPATYSYTQFKQDVLEALTERFGSDVKVGDKAIVVAANGSRRKADVIASMQFRRYWKFKGHYDSQYDEGICFFNGAGERIANYPKQHSENLTLKHQASNKWLKPMVRVLKNLRSKLIADGKLKSGLAPSYYLEGLLYNVPNEKFGTSYADCFVNAMNWIQTEADKDKLVCANEQYYLLWEGTHTSWEKADAEAFIDAAIKMWNEW |
| Enzyme Length | 297 |
| Uniprot Accession Number | Q6XGD5 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 48; /note=UTP; /evidence=ECO:0000250|UniProtKB:G2SLH8; BINDING 64; /note=UTP; /evidence=ECO:0000250|UniProtKB:G2SLH8; BINDING 174; /note=UTP; /evidence=ECO:0000250|UniProtKB:G2SLH8; BINDING 202; /note=ATP; /evidence=ECO:0000250|UniProtKB:G2SLH8; BINDING 221; /note=ATP; /evidence=ECO:0000250|UniProtKB:G2SLH8 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + UTP = 3',3'-cUAMP + 2 diphosphate; Xref=Rhea:RHEA:60456, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:143809; Evidence={ECO:0000269|PubMed:30787435};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60457; Evidence={ECO:0000305|PubMed:30787435}; |
| 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-A(UA) CBASS system (PubMed:32839535). {ECO:0000303|PubMed:32839535, ECO:0000305}.; FUNCTION: Cyclic dinucleotide synthase that catalyzes the synthesis of 3',3'-cyclic UMP-AMP (cUMP-AMP) from UTP and ATP, a second messenger for cell signal transduction. Controls the activity of cUAMP-activated phospholipase CapE, a patatin-like lipase that is a direct cUMP-AMP receptor encoded in the cdnE operon. {ECO:0000269|PubMed:30787435}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.4. {ECO:0000269|PubMed:30787435}; |
| Pathway | |
| nucleotide Binding | NP_BIND 48..50; /note=ATP; /evidence=ECO:0000250|UniProtKB:G2SLH8 |
| Features | Binding site (5); Chain (1); Metal binding (3); Mutagenesis (1); Nucleotide binding (1) |
| Keywords | ATP-binding;Antiviral defense;Magnesium;Metal-binding;Nucleotide metabolism;Nucleotide-binding;Nucleotidyltransferase;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 33,796 |
| Kinetics | |
| Metal Binding | METAL 62; /note=Magnesium; /evidence=ECO:0000250|UniProtKB:G2SLH8; METAL 64; /note=Magnesium; /evidence=ECO:0000250|UniProtKB:G2SLH8; METAL 137; /note=Magnesium; /evidence=ECO:0000250|UniProtKB:G2SLH8 |
| Rhea ID | RHEA:60456; RHEA:60457 |
| Cross Reference Brenda |