Function and Biology Details
Reaction catalysed:
L-glutamate + H(2)O + NAD(+) = 2-oxoglutarate + NH(3) + NADH
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase
- Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, C-terminal
- NAD(P)-binding domain superfamily
- NAD(P) binding domain of glutamate dehydrogenase
- Leu/Phe/Val dehydrogenases active site
- Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, dimerisation domain
- Aminoacid dehydrogenase-like, N-terminal domain superfamily
- Glutamate dehydrogenase
Structure analysis Details
Assembly composition:
homo hexamer (preferred)
Assembly name:
NAD-specific glutamate dehydrogenase (preferred)
PDBe Complex ID:
PDB-CPX-151320 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD-specific glutamate dehydrogenase
Molecule details ›
Chains: A, B
Length: 421 amino acids
Theoretical weight: 46.56 KDa
Source organism: Peptoniphilus asaccharolyticus
Expression system: Escherichia coli BL21(DE3)
UniProt:
Length: 421 amino acids
Theoretical weight: 46.56 KDa
Source organism: Peptoniphilus asaccharolyticus
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P28997 (Residues: 1-421; Coverage: 100%)
- Glu/Leu/Phe/Val dehydrogenase, dimerisation domain
- Glutamate/Leucine/Phenylalanine/Valine dehydrogenase
