A0A7U7EYV4 · A0A7U7EYV4_STAAU
- ProteinATP-dependent 6-phosphofructokinase
- GenepfkA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids322 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Catalytic activity
- beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + H+
Cofactor
Activity regulation
Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.
Pathway
Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 11 | ATP (UniProtKB | ChEBI) | |||
Binding site | 21-25 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 72-73 | ATP (UniProtKB | ChEBI) | |||
Binding site | 102-105 | ATP (UniProtKB | ChEBI) | |||
Binding site | 103 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 127-129 | substrate; ligand shared between dimeric partners; in other chain | |||
Active site | 129 | Proton acceptor | |||
Binding site | 156 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 164 | substrate; ligand shared between dimeric partners | |||
Binding site | 171-173 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 187-189 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 213 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 215-217 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 224 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 245 | substrate; ligand shared between dimeric partners | |||
Binding site | 251-254 | 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 | 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 nameATP-dependent 6-phosphofructokinase
- EC number
- Short namesATP-PFK ; Phosphofructokinase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus
Accessions
- Primary accessionA0A7U7EYV4
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 3-277 | Phosphofructokinase | |||
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length322
- Mass (Da)34,840
- Last updated2021-06-02 v1
- Checksum1FAE41C0BA7CA7F1
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
HE579071 EMBL· GenBank· DDBJ | CCJ22986.1 EMBL· GenBank· DDBJ | Genomic DNA |