Function and Biology Details
Reactions catalysed:
D-glyceraldehyde 3-phosphate + phosphate + NADP(+) = 3-phospho-D-glyceroyl phosphate + NADPH
ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Glyceraldehyde/Erythrose phosphate dehydrogenase family
- Phosphoribulokinase
- Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain
- P-loop containing nucleoside triphosphate hydrolase
- Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain
- Glyceraldehyde 3-phosphate dehydrogenase, active site
- Glyceraldehyde-3-phosphate dehydrogenase, type I
- NAD(P)-binding domain superfamily
3 more domains
Structure analysis Details
Assembly composition:
hetero octamer (preferred)
PDBe Complex ID:
PDB-CPX-150562 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic
Molecule details ›
Phosphoribulokinase, chloroplastic
Molecule details ›
Chains: I, J, K, L
Length: 352 amino acids
Theoretical weight: 39.51 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
Sequence domains: Phosphoribulokinase / Uridine kinase family
Length: 352 amino acids
Theoretical weight: 39.51 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
- Canonical:
P25697 (Residues: 47-395; Coverage: 88%)
Sequence domains: Phosphoribulokinase / Uridine kinase family
Calvin cycle protein CP12-2, chloroplastic
Molecule details ›
Chains: M, N, O, P
Length: 80 amino acids
Theoretical weight: 8.54 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
Sequence domains: CP12 domain
Length: 80 amino acids
Theoretical weight: 8.54 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
- Canonical: Q9LZP9 (Residues: 55-131; Coverage: 59%)
Sequence domains: CP12 domain
