Function and Biology Details
Reaction catalysed:
D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH
Biochemical function:
Biological process:
Cellular component:
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-141862 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glyceraldehyde-3-phosphate dehydrogenase A
Molecule details ›
Chains: A, B, C
Length: 331 amino acids
Theoretical weight: 35.64 KDa
Source organism: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 331 amino acids
Theoretical weight: 35.64 KDa
Source organism: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P0A9B2 (Residues: 1-331; Coverage: 100%)
Sequence domains:
- Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain
- Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain
Glyceraldehyde-3-phosphate dehydrogenase, testis-specific
Molecule details ›
Chain: D
Length: 334 amino acids
Theoretical weight: 36.38 KDa
Source organism: Rattus norvegicus
UniProt:
Sequence domains:
Length: 334 amino acids
Theoretical weight: 36.38 KDa
Source organism: Rattus norvegicus
UniProt:
- Canonical: Q9ESV6 (Residues: 100-432; Coverage: 77%)
Sequence domains:
- Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain
- Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain
