A0A3Q1NJ70 · A0A3Q1NJ70_BOVIN
- ProteinATP-dependent 6-phosphofructokinase
- GenePFKP
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids842 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 | 35 | ATP (UniProtKB | ChEBI) | |||
Binding site | 98-99 | ATP (UniProtKB | ChEBI) | |||
Binding site | 128-131 | ATP (UniProtKB | ChEBI) | |||
Binding site | 129 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 174-176 | substrate; ligand shared between dimeric partners; in other chain | |||
Active site | 176 | Proton acceptor | |||
Binding site | 211 | substrate; ligand shared between dimeric partners | |||
Binding site | 218-220 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 274 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 302 | substrate; ligand shared between dimeric partners | |||
Binding site | 308-311 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 482 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 590-594 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 628 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 635-637 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 691 | 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 | |||
Binding site | 723-726 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 796 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 6-phosphofructokinase activity | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
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 > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionA0A3Q1NJ70
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Expression
Gene expression databases
Interaction
Subunit
Homo- and heterotetramers.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-400 | N-terminal catalytic PFK domain 1 | |||
Domain | 28-333 | Phosphofructokinase | |||
Region | 413-842 | C-terminal regulatory PFK domain 2 | |||
Domain | 563-749 | Phosphofructokinase | |||
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
- Length842
- Mass (Da)91,476
- Last updated2024-05-29 v2
- Checksum410E72BFAE22E31D
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E1BCW3 | E1BCW3_BOVIN | PFKP | 909 | ||
A0AAA9SFJ5 | A0AAA9SFJ5_BOVIN | PFKP | 714 | ||
A0AAA9TNU4 | A0AAA9TNU4_BOVIN | PFKP | 740 | ||
A0AAA9TMI3 | A0AAA9TMI3_BOVIN | PFKP | 738 |
Keywords
- Technical term