A0AA88R4R4 · A0AA88R4R4_9ASTE
- ProteinPyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta
- GenePFP-BETA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids520 (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 | 152 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Site | 153 | 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 | 179 | Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi | ||||
Sequence: K | ||||||
Binding site | 180-182 | substrate | ||||
Sequence: TID | ||||||
Active site | 182 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 219-220 | substrate; ligand shared between dimeric partners | ||||
Sequence: KY | ||||||
Binding site | 227-229 | substrate | ||||
Sequence: MGR | ||||||
Binding site | 288 | substrate | ||||
Sequence: E | ||||||
Binding site | 393-396 | 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 | photosynthesis | |
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 subunit beta
- EC number
- Short namesPFP
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > campanulids > Escalloniales > Escalloniaceae > Escallonia
Accessions
- Primary accessionA0AA88R4R4
Proteomes
Subcellular Location
Interaction
Subunit
Tetramer of two alpha (regulatory) and two beta (catalytic) chains.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 78-415 | Phosphofructokinase | ||||
Sequence: TKGSTLYGFKGGPAGIMKCTYVELTTDFVYPYRNQGGFDMICSGRDKIETPEQFKQAEETASKLNLDGLVVIGGDDSNTNACLLAENFRGKNMKTSVIGCPKTIDGDLKCKEVPTSFGFDTACKIYAEMIGNVMTDARSTGKYYHFVRLMGRAASHITLECALQTHPNITIIGEEVAARKQTLKSVTDYITDIICKRAELGYNYGVILIPEGLIDFIPEVQQLIAELNEILAHDVVDEDGQWKKKLRSQSHQLFELLPQAIQEQLLLERDPHGNVQVAKIETEKMLIQMVETEVEKRRQEGTYDQQFKGQSHFFGYEGRCGLPSNFDANYCYALGYAA |
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
- Length520
- Mass (Da)57,108
- Last updated2024-03-27 v1
- Checksum2E80DE9B79FF4431
Keywords
- Technical term