A0A3R8RVU8 · A0A3R8RVU8_9ACTN
- ProteinPyrophosphate--fructose 6-phosphate 1-phosphotransferase
- Genepfp
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids342 (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 | 10 | diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 103 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Site | 104 | 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 | 125 | Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi | ||||
Sequence: K | ||||||
Binding site | 126-128 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: TID | ||||||
Active site | 128 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 163 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 170-172 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 222 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 266 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 272-275 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HIQR |
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
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionA0A3R8RVU8
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer or homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-297 | Phosphofructokinase | ||||
Sequence: RVGVLTGGGDCPGLNAVIRAIVRKGVQEYGYDFTGFRDGWRGPLEDAAVPLDIPAVRGILPRGGTILGSSRTNPLKQEDGIRRIRENLAAREIEALIAIGGEDTLGVAAELSGRHGVPCVGVPKTIDNDLSATDYTFGFDTAVGIATEAIDRLHTTAESHMRVLVCEVMGRHAGWIALHSGLAGGANVILIPEQRFDVDQVCAWITSRFKASYAPIVVVAEGAMPKDGDMVLKDESLDSFGHVRLSGVGEWLAKQIEKRTGKEARTTVLGHIQRGGTPSAFDRWLATRFGLHAIDA |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length342
- Mass (Da)36,707
- Last updated2019-04-10 v1
- Checksum33E375E8E47B787B
Keywords
- Technical term