Function and Biology Details
Reactions catalysed:
Palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA
ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Glutamine synthetase, catalytic domain
- Glutamine synthetase, N-terminal domain
- Glutamine synthetase, N-terminal domain superfamily
- Glutamine synthetase, glycine-rich site
- Glutamine synthetase/guanido kinase, catalytic domain
- Glutamine synthetase, N-terminal conserved site
- Flavoprotein-like superfamily
Structure analysis Details
Assembly composition:
homo decamer (preferred)
Assembly name:
Glutamine synthetase (preferred)
PDBe Complex ID:
PDB-CPX-147217 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamine synthetase
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 384 amino acids
Theoretical weight: 43.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 384 amino acids
Theoretical weight: 43.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P15104 (Residues: 5-365; Coverage: 97%)
Sequence domains:
Structure domains:
