F2CS69 · F2CS69_HORVV
- ProteinPyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta
- GenePFP-BETA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids560 (go to sequence)
- Protein existenceEvidence at transcript level
- 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 | 98 | diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 192 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Site | 193 | 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 | 219 | Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi | ||||
Sequence: K | ||||||
Binding site | 220-222 | substrate | ||||
Sequence: TID | ||||||
Active site | 222 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 259-260 | substrate; ligand shared between dimeric partners | ||||
Sequence: KY | ||||||
Binding site | 267-269 | substrate | ||||
Sequence: MGR | ||||||
Binding site | 328 | substrate | ||||
Sequence: E | ||||||
Binding site | 433-436 | 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
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Pooideae > Triticodae > Triticeae > Hordeinae > Hordeum
Accessions
- Primary accessionF2CS69
Proteomes
Genome annotation databases
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 | 90-343 | Phosphofructokinase | ||||
Sequence: KIGVVLSGGQAPGGHNVICGIFDYLQERAKGSTMYGFKGGPAGVMKGKYVELTADFVYPYRNQGGFDMICSGRDKIETPEQFKQAEDTVNRLDLDGLVVIGGDDSNTNACLLGEYFRGRNLKTRVIGCPKTIDGDLKCKEVPTSFGFDTACKIYSEMIGNVMTDARSTGKYYHFVRLMGRAASHITLECALQTHPNVALIGEEVAEKKETLKNVTDYITDVVCKRAELGYNYGVVLIPEGLIDFIPEIQKLIAE |
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length560
- Mass (Da)60,621
- Last updated2011-05-31 v1
- ChecksumD46A75FEF8A4B0AB
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK354471 EMBL· GenBank· DDBJ | BAJ85690.1 EMBL· GenBank· DDBJ | mRNA | ||
AK354615 EMBL· GenBank· DDBJ | BAJ85834.1 EMBL· GenBank· DDBJ | mRNA |