A0A2V8QVQ0 · A0A2V8QVQ0_UNCAI
- ProteinATP-dependent 6-phosphofructokinase
- GenepfkA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids338 (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
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 | 5 | ATP (UniProtKB | ChEBI) | |||
Binding site | 66-67 | ATP (UniProtKB | ChEBI) | |||
Binding site | 96-99 | ATP (UniProtKB | ChEBI) | |||
Binding site | 97 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Site | 98 | Important for substrate specificity; cannot use PPi as phosphoryl donor | |||
Binding site | 120-122 | substrate; ligand shared between dimeric partners; in other chain | |||
Active site | 122 | Proton acceptor | |||
Binding site | 157 | substrate; ligand shared between dimeric partners | |||
Binding site | 164-166 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 217 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 262 | substrate; ligand shared between dimeric partners | |||
Binding site | 268-271 | 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 nameATP-dependent 6-phosphofructokinase
- EC number
- Short namesATP-PFK ; Phosphofructokinase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Acidobacteriota
Accessions
- Primary accessionA0A2V8QVQ0
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer or homotetramer.
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length338
- Mass (Da)36,628
- Last updated2018-09-12 v1
- Checksum216EBE2499C3B0DF
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
QHXK01000742 EMBL· GenBank· DDBJ | PYS78448.1 EMBL· GenBank· DDBJ | Genomic DNA |