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
Structure domains:
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146343 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glyceraldehyde-3-phosphate dehydrogenase B, chloroplastic
Molecule details ›
Chains: O, Q, T
Length: 368 amino acids
Theoretical weight: 39.4 KDa
Source organism: Spinacia oleracea
UniProt:
Sequence domains:
Length: 368 amino acids
Theoretical weight: 39.4 KDa
Source organism: Spinacia oleracea
UniProt:
- Canonical:
P12860 (Residues: 84-451; Coverage: 82%)
Sequence domains:
- Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain
- Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain
Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic
Molecule details ›
Chains: P, R, S
Length: 337 amino acids
Theoretical weight: 36.26 KDa
Source organism: Spinacia oleracea
UniProt:
Sequence domains:
Length: 337 amino acids
Theoretical weight: 36.26 KDa
Source organism: Spinacia oleracea
UniProt:
- Canonical: P19866 (Residues: 66-401; Coverage: 84%)
Sequence domains:
- Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain
- Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain
