Function and Biology Details
Reaction catalysed:
ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine
Biochemical function:
Biological process:
Sequence domains:
- Maltose/Cyclodextrin ABC transporter, substrate-binding protein
- Glutamine synthetase, catalytic domain
- Glutamine synthetase, N-terminal domain
- Glutamine synthetase, N-terminal domain superfamily
- Solute-binding family 1, conserved site
- Bacterial-type extracellular solute-binding protein
- Glutamine synthetase class-I, adenylation site
- Glutamine synthetase, glycine-rich site
3 more domains
Structure analysis Details
Assembly composition:
hetero 24-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141034 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Glutamine synthetase
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 466 amino acids
Theoretical weight: 51.59 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhi
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 466 amino acids
Theoretical weight: 51.59 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhi
Expression system: Escherichia coli
UniProt:
- Canonical:
P0A1P7 (Residues: 4-469; Coverage: 99%)
Sequence domains:
Maltose/maltodextrin-binding periplasmic protein
Molecule details ›
Chains: M, N, O, P, Q, R, S, T, U, V, W, X
Length: 370 amino acids
Theoretical weight: 40.75 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli
UniProt:
Sequence domains: Bacterial extracellular solute-binding protein
Length: 370 amino acids
Theoretical weight: 40.75 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli
UniProt:
- Canonical: P0AEY0 (Residues: 27-396; Coverage: 100%)
Sequence domains: Bacterial extracellular solute-binding protein
