Function and Biology Details
Reaction catalysed:
2 3-phospho-D-glycerate + 2 H(+) = D-ribulose 1,5-bisphosphate + CO(2) + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Chaperonin-like RbcX superfamily
- Chaperonin-like RbcX
- Ribulose bisphosphate carboxylase, large subunit, C-terminal domain superfamily
- Ribulose bisphosphate carboxylase large subunit, type I
- RuBisCO large subunit, N-terminal domain superfamily
- RuBisCO
- RuBisCO chaperone RbcX
- Rubisco accumulation factor 1, C-terminal
7 more domains
Structure analysis Details
Assembly composition:
hetero 32-mer (preferred)
PDBe Complex ID:
PDB-CPX-131471 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
RuBisCO chaperone RbcX
Molecule details ›
Chains: 1, 2, 3, 4, 5, 6, 7, 8, Q, R, S, T, U, V, W, X
Length: 132 amino acids
Theoretical weight: 15.21 KDa
Source organism: Nostoc sp. PCC 7120 = FACHB-418
Expression system: Escherichia coli
UniProt:
Sequence domains: RbcX protein
Length: 132 amino acids
Theoretical weight: 15.21 KDa
Source organism: Nostoc sp. PCC 7120 = FACHB-418
Expression system: Escherichia coli
UniProt:
- Canonical:
O86418 (Residues: 1-132; Coverage: 100%)
Sequence domains: RbcX protein
RuBisCO accumulation factor 1
Molecule details ›
Chains: I, J, K, L, M, N, O, P
Length: 361 amino acids
Theoretical weight: 41.06 KDa
Source organism: Nostoc sp. PCC 7120 = FACHB-418
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 361 amino acids
Theoretical weight: 41.06 KDa
Source organism: Nostoc sp. PCC 7120 = FACHB-418
Expression system: Escherichia coli
UniProt:
- Canonical: Q8YLP6 (Residues: 1-361; Coverage: 100%)
Sequence domains:
Ribulose bisphosphate carboxylase large chain
Molecule details ›
