A0A414ZG67 · A0A414ZG67_9BACE
- ProteinPyrophosphate--fructose 6-phosphate 1-phosphotransferase
- Genepfp
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids548 (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 | 78 | diphosphate (UniProtKB | ChEBI) | |||
Binding site | 172 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Site | 173 | 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 | 199 | Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi | |||
Binding site | 200-202 | substrate; ligand shared between dimeric partners; in other chain | |||
Active site | 202 | Proton acceptor | |||
Binding site | 239-240 | substrate; ligand shared between dimeric partners | |||
Binding site | 247-249 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 308 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 421-424 | substrate; ligand shared between dimeric partners; in other chain | |||
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 | 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 > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Bacteroides
Accessions
- Primary accessionA0A414ZG67
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 70-331 | 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
- Length548
- Mass (Da)59,933
- Last updated2019-05-08 v1
- MD5 ChecksumF3FF158CD682B0600855D2FD29DDCEF7
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
QRKI01000001 EMBL· GenBank· DDBJ | RHI12824.1 EMBL· GenBank· DDBJ | Genomic DNA |