A0A1B9ITA2 · A0A1B9ITA2_9TREE
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids967 (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, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
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 | 90 | ATP (UniProtKB | ChEBI) | |||
Binding site | 275-276 | ATP (UniProtKB | ChEBI) | |||
Binding site | 305-308 | ATP (UniProtKB | ChEBI) | |||
Binding site | 306 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 351-353 | substrate; ligand shared between dimeric partners; in other chain | |||
Active site | 353 | Proton acceptor | |||
Binding site | 388 | substrate; ligand shared between dimeric partners | |||
Binding site | 395-397 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 452 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 480 | substrate; ligand shared between dimeric partners | |||
Binding site | 486-489 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 661 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 718-722 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 756 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 763-765 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 823 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 849 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 941 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | 6-phosphofructokinase complex | |
Cellular Component | mitochondrion | |
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 lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Tremellomycetes > Tremellales > Cryptococcaceae > Kwoniella
Accessions
- Primary accessionA0A1B9ITA2
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-37 | Polar residues | |||
Region | 1-49 | Disordered | |||
Region | 1-578 | N-terminal catalytic PFK domain 1 | |||
Domain | 82-129 | Phosphofructokinase | |||
Region | 125-166 | Disordered | |||
Compositional bias | 128-166 | Polar residues | |||
Domain | 252-512 | Phosphofructokinase | |||
Domain | 592-881 | Phosphofructokinase | |||
Region | 592-967 | C-terminal regulatory PFK domain 2 | |||
Region | 889-908 | Disordered | |||
Sequence similarities
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.
Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length967
- Mass (Da)105,052
- Last updated2016-11-02 v1
- MD5 ChecksumFD75E4D024EEE7E4D7A06393C2F83CDB
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-37 | Polar residues | |||
Compositional bias | 128-166 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KI669461 EMBL· GenBank· DDBJ | OCF58772.1 EMBL· GenBank· DDBJ | Genomic DNA |