CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.460 | Beta Polymerase; domain 2 |
|
3.30.460.10 | Beta Polymerase, domain 2 |
Domain Context
CATH Clusters
| Superfamily | Beta Polymerase, domain 2 |
| Functional Family | Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme |
Enzyme Information
| 2.7.7.89 |
[Glutamine synthetase]-adenylyl-L-tyrosine phosphorylase.
based on mapping to UniProt P30870
[Glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP.
-!- This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2. -!- The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42). -!- The two activities are present on separate domains. -!- Formerly EC 3.1.4.15.
|
| 2.7.7.42 |
[Glutamine synthetase] adenylyltransferase.
based on mapping to UniProt P30870
ATP + [glutamine synthetase]-L-tyrosine = diphosphate + [glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine.
-!- This bacterial enzyme adenylates a tyrosine residue of EC 6.3.1.2. -!- The enzyme is bifunctional, and also catalyzes a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC 2.7.7.89). -!- The two activities are present on separate domains.
|
UniProtKB Entries (1)
| P30870 |
GLNE_ECOLI
Escherichia coli K-12
Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
|
PDB Structure
| PDB | 3K7D |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure of the Adenylylation Domain of E. coli Glutamine Synthetase Adenylyl Transferase: Evidence for Gene Duplication and Evolution of a New Active Site.
J.Mol.Biol.
|
