Q9ZST3 · Q9ZST3_CITPA
- ProteinPyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta
- GenePPi-PFKb
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids566 (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 + phosphate + H+
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 | 104 | diphosphate (UniProtKB | ChEBI) | |||
Binding site | 198 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Site | 199 | 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 | |||
Site | 225 | Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi | |||
Binding site | 226-228 | substrate | |||
Active site | 228 | Proton acceptor | |||
Binding site | 265-266 | substrate; ligand shared between dimeric partners | |||
Binding site | 273-275 | substrate | |||
Binding site | 334 | substrate | |||
Binding site | 439-442 | substrate | |||
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 | 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
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Sapindales > Rutaceae > Aurantioideae > Citrus
Accessions
- Primary accessionQ9ZST3
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 | 96-459 | Phosphofructokinase | |||
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
- Length566
- Mass (Da)61,696
- Last updated1999-05-01 v1
- ChecksumAA21391701BCD2ED
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF095520 EMBL· GenBank· DDBJ | AAC67586.1 EMBL· GenBank· DDBJ | mRNA |