L7VA39 · L7VA39_MYCL1
- ProteinATP-dependent 6-phosphofructokinase
- GenepfkA_1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids377 (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 | 15 | ATP (UniProtKB | ChEBI) | |||
Binding site | 83-84 | ATP (UniProtKB | ChEBI) | |||
Binding site | 124-127 | ATP (UniProtKB | ChEBI) | |||
Binding site | 125 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Site | 126 | Important for substrate specificity; cannot use PPi as phosphoryl donor | |||
Binding site | 147-149 | substrate; ligand shared between dimeric partners; in other chain | |||
Active site | 149 | Proton acceptor | |||
Binding site | 184 | substrate; ligand shared between dimeric partners | |||
Binding site | 191-193 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 244 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 286 | substrate; ligand shared between dimeric partners | |||
Binding site | 292-295 | 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
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium ulcerans group
Accessions
- Primary accessionL7VA39
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer or homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 7-318 | Phosphofructokinase | |||
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length377
- Mass (Da)39,830
- Last updated2013-04-03 v1
- MD5 Checksum6289F3A626EED79036637494949111EA
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP003899 EMBL· GenBank· DDBJ | AGC63323.1 EMBL· GenBank· DDBJ | Genomic DNA |