A0A1Y3QJW4 · A0A1Y3QJW4_9BACL
- 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 | 14 | ATP (UniProtKB | ChEBI) | |||
Binding site | 24-28 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 75-76 | ATP (UniProtKB | ChEBI) | |||
Binding site | 105-108 | ATP (UniProtKB | ChEBI) | |||
Binding site | 106 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 128-130 | substrate; ligand shared between dimeric partners; in other chain | |||
Active site | 130 | Proton acceptor | |||
Binding site | 157 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 165 | substrate; ligand shared between dimeric partners | |||
Binding site | 172-174 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 188-190 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 214 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 216-218 | ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 225 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 246 | substrate; ligand shared between dimeric partners | |||
Binding site | 252-255 | 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
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Paenibacillaceae
Accessions
- Primary accessionA0A1Y3QJW4
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 6-276 | 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)34,694
- Last updated2017-08-30 v1
- Checksum7884F2390622076D
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LZRV01000054 EMBL· GenBank· DDBJ | OUM99961.1 EMBL· GenBank· DDBJ | Genomic DNA |