A0A7U3VU82 · A0A7U3VU82_9GAMM
- ProteinPyrophosphate--fructose 6-phosphate 1-phosphotransferase
- GenepfkA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids414 (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 + phosphate + H+
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 | 11 | diphosphate (UniProtKB | ChEBI) | |||
Site | 113 | 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 | 139 | Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi | |||
Binding site | 140-142 | substrate | |||
Active site | 142 | Proton acceptor | |||
Binding site | 188-190 | substrate | |||
Binding site | 242 | substrate | |||
Binding site | 292-295 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 6-phosphofructokinase activity | |
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria
Accessions
- Primary accessionA0A7U3VU82
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 7-288 | Phosphofructokinase | |||
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'B2' sub-subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length414
- Mass (Da)44,844
- Last updated2021-09-29 v1
- Checksum10DFC59217860EF9
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP012977 EMBL· GenBank· DDBJ | BBB23236.1 EMBL· GenBank· DDBJ | Genomic DNA |