A0A517W625 · A0A517W625_9PLAN
- ProteinPyrophosphate--fructose 6-phosphate 1-phosphotransferase
- Genepfp
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids344 (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 | 10 | diphosphate (UniProtKB | ChEBI) | |||
Binding site | 103 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
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 | |||
Site | 125 | Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi | |||
Binding site | 126-128 | substrate; ligand shared between dimeric partners; in other chain | |||
Active site | 128 | Proton acceptor | |||
Binding site | 163 | substrate; ligand shared between dimeric partners | |||
Binding site | 170-172 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 223 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 268 | substrate; ligand shared between dimeric partners | |||
Binding site | 274-277 | substrate; ligand shared between dimeric partners; in other chain | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | 6-phosphofructokinase complex | |
Molecular Function | 6-phosphofructokinase activity | |
Molecular Function | AMP binding | |
Molecular Function | ATP binding | |
Molecular Function | diphosphate-fructose-6-phosphate 1-phosphotransferase activity | |
Molecular Function | fructose-6-phosphate binding | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Molecular Function | monosaccharide binding | |
Biological Process | canonical glycolysis | |
Biological Process | fructose 1,6-bisphosphate metabolic process | |
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
- Strains
- Taxonomic lineageBacteria > Planctomycetota > Planctomycetia > Planctomycetales > Planctomycetaceae > Gimesia
Accessions
- Primary accessionA0A517W625
- Secondary accessions
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 similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length344
- Mass (Da)37,277
- Last updated2019-10-16 v1
- ChecksumC3DC59EB684F288A
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP036266 EMBL· GenBank· DDBJ | QDT18610.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP036347 EMBL· GenBank· DDBJ | QDU00690.1 EMBL· GenBank· DDBJ | Genomic DNA |