Function and Biology Details
Reaction catalysed:
(1a) L-glutamate + NH(3) = L-glutamine + H(2)O
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Glutamate synthase, alpha subunit, C-terminal
- Glutamate synthase, alpha subunit, C-terminal domain superfamily
- Glutamate synthase domain
- Aldolase-type TIM barrel
- Nucleophile aminohydrolases, N-terminal
- Glutamine amidotransferase type 2 domain
- FAD/NAD(P)-binding domain superfamily
- FAD/NAD(P)-binding domain
4 more domains
Structure analysis Details
Assembly composition:
hetero dodecamer (preferred)
Assembly name:
Glutamate synthase [NADPH] (preferred)
PDBe Complex ID:
PDB-CPX-170243 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutamate synthase [NADPH] large chain
Molecule details ›
Chains: A, B, C, D, E, F
Length: 1515 amino acids
Theoretical weight: 166.22 KDa
Source organism: Azospirillum brasilense
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 1515 amino acids
Theoretical weight: 166.22 KDa
Source organism: Azospirillum brasilense
Expression system: Escherichia coli
UniProt:
- Canonical:
Q05755 (Residues: 1-1515; Coverage: 100%)
Sequence domains:
Glutamate synthase [NADPH] small chain
Molecule details ›
Chains: G, H, I, J, K, L
Length: 482 amino acids
Theoretical weight: 52.43 KDa
Source organism: Azospirillum brasilense
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 482 amino acids
Theoretical weight: 52.43 KDa
Source organism: Azospirillum brasilense
Expression system: Escherichia coli
UniProt:
- Canonical: Q05756 (Residues: 1-482; Coverage: 100%)
Sequence domains:
