Function and Biology Details
Reaction catalysed:
D-glyceraldehyde 3-phosphate + phosphate + NADP(+) = 3-phospho-D-glyceroyl phosphate + NADPH
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Glyceraldehyde/Erythrose phosphate dehydrogenase family
- Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain
- Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain
- Glyceraldehyde 3-phosphate dehydrogenase, active site
- Glyceraldehyde-3-phosphate dehydrogenase, type I
- NAD(P)-binding domain superfamily
- CP12 domain
- Calvin cycle protein CP12-like
Structure analysis Details
Assemblies composition:
Assembly name:
PDBe Complex ID:
PDB-CPX-150604 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic
Molecule details ›
Chains: A, B, C, D, E, F
Length: 337 amino acids
Theoretical weight: 36.39 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 337 amino acids
Theoretical weight: 36.39 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P25856 (Residues: 60-396; Coverage: 85%)
Sequence domains:
- Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain
- Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain
Calvin cycle protein CP12-2, chloroplastic
Molecule details ›
Chains: G, H, I
Length: 82 amino acids
Theoretical weight: 8.75 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: CP12 domain
Length: 82 amino acids
Theoretical weight: 8.75 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: Q9LZP9 (Residues: 54-131; Coverage: 60%)
Sequence domains: CP12 domain
