CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.10 | Roll |
|
3.10.20 | Ubiquitin-like (UB roll) |
|
3.10.20.70 | Glutamine synthetase, N-terminal domain |
Domain Context
CATH Clusters
| Superfamily | Glutamine synthetase, N-terminal domain |
| Functional Family | Glutamine synthetase |
Enzyme Information
| 2.3.1.225 |
Protein S-acyltransferase.
based on mapping to UniProt P15104
Palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA.
-!- The enzyme catalyzes the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. -!- Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.
|
| 6.3.1.2 |
Glutamine synthetase.
based on mapping to UniProt P15104
ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine.
-!- Glutamine synthetase, which catalyzes the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. -!- Several types have been described, differing in their oligomeric structures and cofactor requirements.
|
UniProtKB Entries (1)
| P15104 |
GLNA_HUMAN
Homo sapiens
Glutamine synthetase
|
PDB Structure
| PDB | 2QC8 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design.
J.Mol.Biol.
|
