A0A9X4G2C5 · A0A9X4G2C5_ACTEU
- ProteinATP-dependent 6-phosphofructokinase
- GenepfkA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids324 (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 | 15 | ATP (UniProtKB | ChEBI) | |||
Binding site | 25-29 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 76-77 | ATP (UniProtKB | ChEBI) | |||
Binding site | 106-109 | ATP (UniProtKB | ChEBI) | |||
Binding site | 107 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 130-132 | substrate; ligand shared between dimeric partners; in other chain | |||
Active site | 132 | Proton acceptor | |||
Binding site | 159 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 167 | substrate; ligand shared between dimeric partners | |||
Binding site | 174-176 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 190-192 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 216 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 218-220 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 227 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 248 | substrate; ligand shared between dimeric partners | |||
Binding site | 254-257 | 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 > Pseudomonadota > Gammaproteobacteria > Pasteurellales > Pasteurellaceae > Actinobacillus
Accessions
- Primary accessionA0A9X4G2C5
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 7-280 | 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
- Length324
- Mass (Da)35,649
- Last updated2023-11-08 v1
- Checksum3C74CD5E916FCC80
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAPHVQ010000001 EMBL· GenBank· DDBJ | MDE8033798.1 EMBL· GenBank· DDBJ | Genomic DNA |