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 analysis Details
Assembly composition:
hetero 28-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146162 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutamine synthetase
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Length: 447 amino acids
Theoretical weight: 50.62 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 447 amino acids
Theoretical weight: 50.62 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
UniProt:
- Canonical:
P12425 (Residues: 1-444; Coverage: 100%)
Sequence domains:
Structure domains:
HTH-type transcriptional regulator TnrA
Molecule details ›
Chains: 1, 2, O, P, Q, R, S, T, U, V, W, X, Y, Z
Length: 15 amino acids
Theoretical weight: 1.9 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Not provided
UniProt:
Length: 15 amino acids
Theoretical weight: 1.9 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Not provided
UniProt:
- Canonical: Q45666 (Residues: 95-110; Coverage: 14%)
