Function and Biology Details
Reaction catalysed:
L-threo-3-methylaspartate = L-glutamate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domains:
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Glutamate mutase (preferred)
PDBe Complex ID:
PDB-CPX-160345 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutamate mutase sigma subunit
Molecule details ›
Chains: A, C
Length: 137 amino acids
Theoretical weight: 14.83 KDa
Source organism: Clostridium cochlearium
Expression system: Escherichia coli
UniProt:
Sequence domains: B12 binding domain
Structure domains: Cobalamin-binding domain
Length: 137 amino acids
Theoretical weight: 14.83 KDa
Source organism: Clostridium cochlearium
Expression system: Escherichia coli
UniProt:
- Canonical:
P80078 (Residues: 1-137; Coverage: 100%)
Sequence domains: B12 binding domain
Structure domains: Cobalamin-binding domain
Glutamate mutase epsilon subunit
Molecule details ›
Chains: B, D
Length: 483 amino acids
Theoretical weight: 53.62 KDa
Source organism: Clostridium cochlearium
Expression system: Escherichia coli
UniProt:
Sequence domains: Methylaspartate mutase E chain (MutE)
Structure domains:
Length: 483 amino acids
Theoretical weight: 53.62 KDa
Source organism: Clostridium cochlearium
Expression system: Escherichia coli
UniProt:
- Canonical: P80077 (Residues: 1-483; Coverage: 100%)
Sequence domains: Methylaspartate mutase E chain (MutE)
Structure domains:
