Function and Biology Details
Reaction catalysed:
(R)-methylmalonyl-CoA = succinyl-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Methylmalonyl-CoA mutase, alpha/beta chain, catalytic
- Cobalamin (vitamin B12)-binding domain
- Cobalamin-binding domain superfamily
- Cobalamin (vitamin B12)-dependent enzyme, catalytic
- Methylmalonyl-CoA mutase, small subunit
- Methylmalonyl-CoA mutase small subunit, N-terminal
- Methylmalonyl-CoA mutase, C-terminal
- Methylmalonyl-CoA mutase, alpha chain, catalytic
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Methylmalonyl-CoA mutase (preferred)
PDBe Complex ID:
PDB-CPX-145887 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Methylmalonyl-CoA mutase large subunit
Molecule details ›
Chains: A, C
Length: 727 amino acids
Theoretical weight: 80.14 KDa
Source organism: Propionibacterium freudenreichii subsp. shermanii
Expression system: K38 PGP1-2
UniProt:
Sequence domains:
Structure domains:
Length: 727 amino acids
Theoretical weight: 80.14 KDa
Source organism: Propionibacterium freudenreichii subsp. shermanii
Expression system: K38 PGP1-2
UniProt:
- Canonical:
P11653 (Residues: 2-728; Coverage: 100%)
Sequence domains:
Structure domains:
Methylmalonyl-CoA mutase small subunit
Molecule details ›
Chains: B, D
Length: 637 amino acids
Theoretical weight: 69.43 KDa
Source organism: Propionibacterium freudenreichii subsp. shermanii
Expression system: Escherichia coli
UniProt:
Sequence domains: Methylmalonyl-CoA mutase
Structure domains:
Length: 637 amino acids
Theoretical weight: 69.43 KDa
Source organism: Propionibacterium freudenreichii subsp. shermanii
Expression system: Escherichia coli
UniProt:
- Canonical: P11652 (Residues: 2-638; Coverage: 100%)
Sequence domains: Methylmalonyl-CoA mutase
Structure domains:
