A0A2V0MYL4 · A0A2V0MYL4_9MYCO
- ProteinATP-dependent 6-phosphofructokinase
- GenepfkA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids343 (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 | 10 | ATP (UniProtKB | ChEBI) | |||
Binding site | 73-74 | ATP (UniProtKB | ChEBI) | |||
Binding site | 103-106 | ATP (UniProtKB | ChEBI) | |||
Binding site | 104 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Site | 105 | Important for substrate specificity; cannot use PPi as phosphoryl donor | |||
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 | 267 | substrate; ligand shared between dimeric partners | |||
Binding site | 273-276 | 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 > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium
Accessions
- Primary accessionA0A2V0MYL4
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer or homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 2-298 | Phosphofructokinase | |||
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length343
- Mass (Da)37,072
- Last updated2018-09-12 v1
- Checksum95CB6F1189D0CECB
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BFAB01000007 EMBL· GenBank· DDBJ | GBE66350.1 EMBL· GenBank· DDBJ | Genomic DNA |