Function and Biology Details
Reaction catalysed:
D-fructose 6-phosphate + phosphate = acetyl phosphate + D-erythrose 4-phosphate + H(2)O
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase
- Thiamin diphosphate-binding fold
- Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II
- Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, C-terminal
- Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, thiamine diphosphate binding site
- Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, conserved site
- Xylulose 5-phosphate/Fructose 6-phosphate phosphoketolase, N-terminal
Structure analysis Details
Assembly composition:
homo octamer (preferred)
Assembly name:
Phosphoketolase (preferred)
PDBe Complex ID:
PDB-CPX-112768 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoketolase
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 831 amino acids
Theoretical weight: 93.45 KDa
Source organism: Bifidobacterium longum subsp. longum F8
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 831 amino acids
Theoretical weight: 93.45 KDa
Source organism: Bifidobacterium longum subsp. longum F8
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
D6D942 (Residues: 1-825; Coverage: 100%)
Sequence domains:
