S0AWD4 · S0AWD4_ENTHI
- ProteinPyrophosphate--fructose 6-phosphate 1-phosphotransferase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids546 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
Catalytic activity
- beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + phosphate + H+
Cofactor
Activity regulation
Non-allosteric.
Pathway
Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 80 | diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 174 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Site | 175 | Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP | ||||
Sequence: D | ||||||
Site | 201 | Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi | ||||
Sequence: K | ||||||
Binding site | 202-204 | substrate | ||||
Sequence: TID | ||||||
Active site | 204 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 241-242 | substrate; ligand shared between dimeric partners | ||||
Sequence: KY | ||||||
Binding site | 249-251 | substrate | ||||
Sequence: MGR | ||||||
Binding site | 310 | substrate | ||||
Sequence: E | ||||||
Binding site | 420-423 | substrate | ||||
Sequence: YEGR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 6-phosphofructokinase activity | |
Molecular Function | ATP binding | |
Molecular Function | diphosphate-fructose-6-phosphate 1-phosphotransferase activity | |
Molecular Function | metal ion binding | |
Biological Process | fructose 6-phosphate metabolic process | |
Biological Process | response to glucose |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyrophosphate--fructose 6-phosphate 1-phosphotransferase
- EC number
- Alternative names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Amoebozoa > Evosea > Archamoebae > Mastigamoebida > Entamoebidae > Entamoeba
Accessions
- Primary accessionS0AWD4
Organism-specific databases
Subcellular Location
Interaction
Subunit
Homodimer or monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 72-328 | Phosphofructokinase | ||||
Sequence: RCGFILSGGPAAGGHNVVAGLFDGLMKGNKENKLYGFRCGAGGILSNDYIEITAELVDKHRNTGGFDLVGSGRTKIETEEQFATAFEHITALKLNAMVVVGGDDSNTNAALLAEYFAAHGSDCVFVGVPKTIDGDLKNQYIETSFGFDTACKTYSELIGNIQRDAISSRKYWHFIKVMGRSASHIALEAALETQPTYCIISEEVEDKKMTVSQIASEIADIVIERHKKGLNFGVVLIPEGLVEFIPEVKALIKELNN |
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length546
- Mass (Da)60,162
- Last updated2013-09-18 v1
- Checksum562DB85D8F7A8360