Function and Biology Details
Reaction catalysed:
L-phenylalanine + H(2)O + NAD(+) = phenylpyruvate + 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
- Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, bacterial/archaeal
- NAD(P)-binding domain superfamily
- Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, dimerisation domain
- Aminoacid dehydrogenase-like, N-terminal domain superfamily
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Phenylalanine dehydrogenase (preferred)
PDBe Complex ID:
PDB-CPX-176823 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Phenylalanine dehydrogenase
Molecule details ›
Chain: A
Length: 355 amino acids
Theoretical weight: 36.41 KDa
Source organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 355 amino acids
Theoretical weight: 36.41 KDa
Source organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q59771 (Residues: 2-356; Coverage: 100%)
Sequence domains:
- Glu/Leu/Phe/Val dehydrogenase, dimerisation domain
- Glutamate/Leucine/Phenylalanine/Valine dehydrogenase
Phenylalanine dehydrogenase
Molecule details ›
Chain: B
Length: 355 amino acids
Theoretical weight: 36.44 KDa
Source organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 355 amino acids
Theoretical weight: 36.44 KDa
Source organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: Q59771 (Residues: 2-356; Coverage: 100%)
Sequence domains:
- Glu/Leu/Phe/Val dehydrogenase, dimerisation domain
- Glutamate/Leucine/Phenylalanine/Valine dehydrogenase
