Function and Biology Details
Reaction catalysed:
Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
homo decamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable transaldolase
Molecule details ›
Chains: A, B, C, D, E
Length: 223 amino acids
Theoretical weight: 24.49 KDa
Source organism: Thermoplasma acidophilum DSM 1728
Expression system: Escherichia coli
UniProt:
Sequence domains: Transaldolase/Fructose-6-phosphate aldolase
Structure domains: Aldolase class I
Length: 223 amino acids
Theoretical weight: 24.49 KDa
Source organism: Thermoplasma acidophilum DSM 1728
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9HKI3 (Residues: 1-223; Coverage: 100%)
Sequence domains: Transaldolase/Fructose-6-phosphate aldolase
Structure domains: Aldolase class I
