A0AAE0JPJ4 · A0AAE0JPJ4_9PEZI
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids844 (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 | 73 | ATP (UniProtKB | ChEBI) | |||
Binding site | 136-137 | ATP (UniProtKB | ChEBI) | |||
Binding site | 166-169 | ATP (UniProtKB | ChEBI) | |||
Binding site | 167 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 212-214 | substrate; ligand shared between dimeric partners; in other chain | |||
Active site | 214 | Proton acceptor | |||
Binding site | 249 | substrate; ligand shared between dimeric partners | |||
Binding site | 256-258 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 312 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 342 | substrate; ligand shared between dimeric partners | |||
Binding site | 348-351 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 531 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 589-593 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 627 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 634-636 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 694 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 720 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 726-729 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 798 | 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 | membrane | |
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 > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Sordariales > Sordariaceae > Neurospora
Accessions
- Primary accessionA0AAE0JPJ4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 20-40 | Helical | |||
Keywords
- Cellular component
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-440 | N-terminal catalytic PFK domain 1 | |||
Domain | 65-373 | Phosphofructokinase | |||
Domain | 456-751 | Phosphofructokinase | |||
Region | 456-844 | 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.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length844
- Mass (Da)91,956
- Last updated2024-05-29 v1
- ChecksumDB0FAC8E7266C25C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAUEPP010000001 EMBL· GenBank· DDBJ | KAK3355331.1 EMBL· GenBank· DDBJ | Genomic DNA |