Q95V79 · Q95V79_9EUKA
- ProteinPyrophosphate--fructose 6-phosphate 1-phosphotransferase
- Genepp-pfk
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids545 (go to sequence)
- Protein existenceInferred from homology
- 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 + H+ + phosphate
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 | 78 | diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 172 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Site | 173 | 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 | 199 | Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi | ||||
Sequence: K | ||||||
Binding site | 200-202 | substrate | ||||
Sequence: TID | ||||||
Active site | 202 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 240-241 | substrate; ligand shared between dimeric partners | ||||
Sequence: KY | ||||||
Binding site | 248-250 | substrate | ||||
Sequence: MGR | ||||||
Binding site | 309 | substrate | ||||
Sequence: E | ||||||
Binding site | 412-415 | substrate | ||||
Sequence: YEGR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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 |
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
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metamonada > Diplomonadida > Hexamitidae > Hexamitinae > Hexamita
Accessions
- Primary accessionQ95V79
Subcellular Location
Interaction
Subunit
Homodimer or monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 71-434 | Phosphofructokinase | ||||
Sequence: IGVIFSGGQAPGGHNVLCGLYDKLQQLAPNSKLLGFLGGPKGLMDNKHMILTKEYLATFRNMGGFHAIGSGRDKIASTKDFDAAANTAAVEKLDGLVIIGGDDSNTNACLLAEDFIKRGLKTRVIGVPKTIDRDLISKRGIETSFGFDTSCKVYSELIGNLCYDALSAKKYWHFIRLMGRSASHITLECGLQTHPNICLIGEEILAKNMTSKQVFEYMADIIAQRAANGKNYGICLIPEGLIEFIPENNKLFDYLNNKLLPGWQGEITAELVAQKLPADLKVTFESIPPTIRTQLLLDRDPHGNIAISQIETEKFLVSGVQQVIKERELKIKFSALYHFFGYEGRCAAPSAFDSSYCYGLGSVA |
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
- Length545
- Mass (Da)59,904
- Last updated2001-12-01 v1
- ChecksumFBFA250B14E4A2C3