A0A160N5C7 · A0A160N5C7_9GAMM
- ProteinPyrophosphate--fructose 6-phosphate 1-phosphotransferase
- Genepfp
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids423 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 | 19 | diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 117 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: N | ||||||
Site | 118 | 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 | 144 | Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi | ||||
Sequence: K | ||||||
Binding site | 145-147 | substrate | ||||
Sequence: TVD | ||||||
Active site | 147 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 193-195 | substrate | ||||
Sequence: MGR | ||||||
Binding site | 250 | substrate | ||||
Sequence: E | ||||||
Binding site | 300-303 | substrate | ||||
Sequence: YLQR |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Lysobacterales > Rhodanobacteraceae > Dyella
Accessions
- Primary accessionA0A160N5C7
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 13-295 | Phosphofructokinase | ||||
Sequence: LYAQSGGVTSVINATAAGVIEAARAKGVPVYAARNGILGALREDLIDTTKETRSAIAALRHTPGGAFGSCRYKLKSLEANRAEYERLIEVFRAHDIRWFLYNGGNDSADTALKVSQLGKAMGYDIRCIGVPKTVDNDLAITDCCPGFGSVAKYTAVSTLEASLDVASMAETSTKVFILEVMGRHAGWIAAAAGLAGDGVDGAPHVILFPEVPFDEAAFLAKVKATVERVGWCTVVASEGVRNAQGQFLAEAGTRDAFGHTQLGGAAPVLAQLVKDKLGYKYHW |
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'B2' sub-subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length423
- Mass (Da)45,168
- Last updated2016-07-06 v1
- Checksum225F377A0499A672
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP014841 EMBL· GenBank· DDBJ | AND70868.1 EMBL· GenBank· DDBJ | Genomic DNA |