Function and Biology Details
Reaction catalysed:
ATP + protoporphyrin IX + Mg(2+) + H(2)O = ADP + phosphate + Mg-protoporphyrin IX + 2 H(+)
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dodecamer (preferred)
Assembly name:
Magnesium-chelatase kDa (preferred)
PDBe Complex ID:
PDB-CPX-150663 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Magnesium-chelatase 60 kDa subunit
Molecule details ›
Chains: A, B, C, D, E, F
Length: 189 amino acids
Theoretical weight: 19.67 KDa
Source organism: Rhodobacter capsulatus
Expression system: Escherichia coli
UniProt:
Sequence domains: von Willebrand factor type A domain
Length: 189 amino acids
Theoretical weight: 19.67 KDa
Source organism: Rhodobacter capsulatus
Expression system: Escherichia coli
UniProt:
- Canonical:
P26175 (Residues: 373-561; Coverage: 34%)
Sequence domains: von Willebrand factor type A domain
Magnesium-chelatase 38 kDa subunit
Molecule details ›
Chains: G, H, I, J, K, L
Length: 350 amino acids
Theoretical weight: 37.95 KDa
Source organism: Rhodobacter capsulatus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 350 amino acids
Theoretical weight: 37.95 KDa
Source organism: Rhodobacter capsulatus
Expression system: Escherichia coli
UniProt:
- Canonical: P26239 (Residues: 1-350; Coverage: 100%)
Sequence domains:
