CATH Classification

Domain Context

CATH Clusters

Superfamily Glutamine synthase adenylyltransferase GlnE
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 1V4A
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structure of the n-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase
Xu, Y., Zhang, R., Joachimiak, A., Carr, P.D., Huber, T., Vasudevan, S.G., Ollis, D.L.
Structure