A0A061H3R4 · A0A061H3R4_9BASI
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids862 (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 | 20 | ATP (UniProtKB | ChEBI) | |||
Binding site | 168-169 | ATP (UniProtKB | ChEBI) | |||
Binding site | 198-201 | ATP (UniProtKB | ChEBI) | |||
Binding site | 199 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 244-246 | substrate; ligand shared between dimeric partners; in other chain | |||
Active site | 246 | Proton acceptor | |||
Binding site | 281 | substrate; ligand shared between dimeric partners | |||
Binding site | 288-290 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 346 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 374 | substrate; ligand shared between dimeric partners | |||
Binding site | 380-383 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 555 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 612-616 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 650 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 657-659 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 717 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 743 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 836 | 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
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Ustilaginomycotina > Ustilaginomycetes > Ustilaginales > Ustilaginaceae > Pseudozyma
Accessions
- Primary accessionA0A061H3R4
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-20 | Disordered | |||
Region | 1-472 | N-terminal catalytic PFK domain 1 | |||
Domain | 12-58 | Phosphofructokinase | |||
Domain | 143-405 | Phosphofructokinase | |||
Domain | 486-775 | Phosphofructokinase | |||
Region | 486-862 | C-terminal regulatory PFK domain 2 | |||
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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length862
- Mass (Da)92,906
- Last updated2014-09-03 v1
- Checksum45EC1434C537ED40
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KE361644 EMBL· GenBank· DDBJ | EPQ26510.1 EMBL· GenBank· DDBJ | Genomic DNA |