A0A958ESU4 · A0A958ESU4_UNCCD
- ProteinPyrophosphate--fructose 6-phosphate 1-phosphotransferase
- Genepfp
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids439 (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 + H+ + phosphate
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 | 13 | diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 108 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Site | 109 | 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 | 132 | Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi | ||||
Sequence: K | ||||||
Binding site | 133-135 | substrate | ||||
Sequence: TID | ||||||
Active site | 135 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 179-181 | substrate | ||||
Sequence: MGR | ||||||
Binding site | 240 | substrate | ||||
Sequence: E | ||||||
Binding site | 300-303 | substrate | ||||
Sequence: YELR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
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 | |
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
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Calditrichota
Accessions
- Primary accessionA0A958ESU4
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-325 | Phosphofructokinase | ||||
Sequence: RLAILVAGGPAPGINSVIGAATIRAILSGAEVIGIKDGFKWLMEGNISNIIPLSIDSVSRIHFRGGSYLGIARENPTKNKKHLENTISSLLRLNVDKLITIGGDDTCYSAYKVEQVANGRIQVAHVPKTIDNDLDLPHGIPTFGYQTARHIGVEIVKNIMTDARTTSRWYFVVTMGRKAGHLALGTGKSAGATLTLIPEEFPEEKVSLGHMVDTLVGAIIKRISYGRQDGVAIIAEGLIDKLDPHAFDTLVNIEKDAHDNLRFAEINFGEILKYHVQQRLKQFGIKTTIVAKNIGYELRCADPIPFDMEYTRDLGYMAAKF | ||||||
Region | 419-439 | Disordered | ||||
Sequence: SHKQAKKKEDEKKENKTVDAK | ||||||
Compositional bias | 420-439 | Basic and acidic residues | ||||
Sequence: HKQAKKKEDEKKENKTVDAK |
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'Short' sub-subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length439
- Mass (Da)48,930
- Last updated2023-02-22 v1
- Checksum6E2CEC7FBC9B2C7D
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 420-439 | Basic and acidic residues | ||||
Sequence: HKQAKKKEDEKKENKTVDAK |