A0A4S8JKM0 · A0A4S8JKM0_MUSBA
- ProteinPyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta
- GenePFP-BETA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids616 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalytic subunit of pyrophosphate--fructose 6-phosphate 1-phosphotransferase. 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.
Catalytic activity
- beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H+ + phosphate
Cofactor
Activity regulation
Allosterically activated by fructose 2,6-bisphosphate.
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 | 102 | diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 196 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Site | 197 | 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 | 223 | Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi | ||||
Sequence: K | ||||||
Binding site | 224-226 | substrate | ||||
Sequence: TID | ||||||
Active site | 226 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 263-264 | substrate; ligand shared between dimeric partners | ||||
Sequence: KY | ||||||
Binding site | 271-273 | substrate | ||||
Sequence: MGR | ||||||
Binding site | 384 | substrate | ||||
Sequence: E | ||||||
Binding site | 489-492 | 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 subunit beta
- EC number
- Short namesPFP
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Zingiberales > Musaceae > Musa
Accessions
- Primary accessionA0A4S8JKM0
Proteomes
Subcellular Location
Interaction
Subunit
Tetramer of two alpha (regulatory) and two beta (catalytic) chains.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MAFANSVLPKGGGKSPSPGRL | ||||||
Domain | 94-306 | Phosphofructokinase | ||||
Sequence: KIGVVLSGGQAPGGHNVISGIFDYLQERAKRSTLYGFKGGPAGIMKCKYVDLTPEFIYPYRNQGGFDMICSGRDKIETPEQFKQAEETAMKLDLDGLLVIGGDDSNTNACLLAENFRQKNMKTRVIGCPKTIDGDLKCKEVPASFGFDTACKIYSEMIGNVMTDARSTGKYYHFVRLMGRAASHITLECALQTHPNIAIIGEEPIGKWAKVNQ |
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
- Length616
- Mass (Da)67,177
- Last updated2019-07-31 v1
- Checksum030479BBD8DAFB2E
Keywords
- Technical term