A0A5C6GE54 · A0A5C6GE54_9HYPO
- ProteinATP-dependent 6-phosphofructokinase
- GenePFK1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids785 (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 | 15 | ATP (UniProtKB | ChEBI) | |||
Binding site | 78-79 | ATP (UniProtKB | ChEBI) | |||
Binding site | 108-111 | ATP (UniProtKB | ChEBI) | |||
Binding site | 109 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 154-156 | substrate; ligand shared between dimeric partners; in other chain | |||
Active site | 156 | Proton acceptor | |||
Binding site | 191 | substrate; ligand shared between dimeric partners | |||
Binding site | 198-200 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 254 | 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 | |||
Binding site | 475 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 533-537 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 571 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 578-580 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 638 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 664 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 670-673 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 742 | 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 > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Clavicipitaceae > Metarhizium
Accessions
- Primary accessionA0A5C6GE54
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-384 | N-terminal catalytic PFK domain 1 | |||
Domain | 7-317 | Phosphofructokinase | |||
Region | 385-398 | Interdomain linker | |||
Domain | 399-695 | Phosphofructokinase | |||
Region | 399-785 | 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
- Length785
- Mass (Da)85,672
- Last updated2019-11-13 v1
- ChecksumD12573C6B244B37D
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
SBHS01000008 EMBL· GenBank· DDBJ | TWU75138.1 EMBL· GenBank· DDBJ | Genomic DNA |