Function and Biology Details
Reaction catalysed:
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 class-I, adenylation site
- Glutamine synthetase, glycine-rich site
- Glutamine synthetase/guanido kinase, catalytic domain
- Glutamine synthetase, N-terminal conserved site
- Glutamine synthetase type I
Structure domains:
Structure analysis Details
Assembly composition:
homo dodecamer (preferred)
Assembly name:
Glutamine synthetase (preferred)
PDBe Complex ID:
PDB-CPX-161830 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamine synthetase
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Length: 477 amino acids
Theoretical weight: 53.5 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 477 amino acids
Theoretical weight: 53.5 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
- Canonical:
P9WN39 (Residues: 2-478; Coverage: 100%)
Sequence domains:
Structure domains:
