Function and Biology Details
Reaction catalysed:
D-ornithine = (2R,4S)-2,4-diaminopentanoate
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
- Cobalamin (vitamin B12)-binding domain
- D-Lysine 5,6-aminomutase alpha subunit
- Cobalamin (vitamin B12)-dependent enzyme, catalytic
- Rhodococcus equi virulence-associated superfamily
- Cobalamin-binding domain superfamily
- D-lysine 5,6-aminomutase beta subunit KamE, N-terminal
- D-lysine 5,6-aminomutase beta subunit KamE, N-terminal domain superfamily
- D-Lysine 5,6-aminomutase alpha subunit superfamily
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
D-ornithine 4,5-aminomutase (preferred)
PDBe Complex ID:
PDB-CPX-122899 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
D-ornithine 4,5-aminomutase subunit beta
Molecule details ›
Chains: A, B, C, D
Length: 763 amino acids
Theoretical weight: 85.41 KDa
Source organism: Acetoanaerobium sticklandii
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 763 amino acids
Theoretical weight: 85.41 KDa
Source organism: Acetoanaerobium sticklandii
Expression system: Escherichia coli
UniProt:
- Canonical:
E3PY95 (Residues: 1-740; Coverage: 100%)
Sequence domains:
- D-Lysine 5,6-aminomutase TIM-barrel domain of alpha subunit
- Dimerisation domain of d-ornithine 4,5-aminomutase
- B12 binding domain
D-ornithine 4,5-aminomutase subunit alpha
Molecule details ›
Chains: E, F, G, H
Length: 121 amino acids
Theoretical weight: 13.65 KDa
Source organism: Acetoanaerobium sticklandii
Expression system: Escherichia coli
UniProt:
Sequence domains: D-ornithine 4,5-aminomutase alpha-subunit
Structure domains:
Length: 121 amino acids
Theoretical weight: 13.65 KDa
Source organism: Acetoanaerobium sticklandii
Expression system: Escherichia coli
UniProt:
- Canonical: E3PY96 (Residues: 1-121; Coverage: 100%)
Sequence domains: D-ornithine 4,5-aminomutase alpha-subunit
Structure domains:
