A0A4W4GNB7 · A0A4W4GNB7_ELEEL
- ProteinATP-dependent 6-phosphofructokinase
- Genepfkpa
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids787 (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 | 27 | ATP (UniProtKB | ChEBI) | |||
Binding site | 90-91 | ATP (UniProtKB | ChEBI) | |||
Binding site | 120-123 | ATP (UniProtKB | ChEBI) | |||
Binding site | 121 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 166-168 | substrate; ligand shared between dimeric partners; in other chain | |||
Active site | 168 | Proton acceptor | |||
Binding site | 203 | substrate; ligand shared between dimeric partners | |||
Binding site | 210-212 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 266 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 294 | substrate; ligand shared between dimeric partners | |||
Binding site | 300-303 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 474 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 531-535 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 569 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 576-578 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 632 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 658 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 664-667 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 738 | 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 | |
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
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Gymnotiformes > Gymnotoidei > Gymnotidae > Electrophorus
Accessions
- Primary accessionA0A4W4GNB7
Proteomes
Subcellular Location
Interaction
Subunit
Homo- and heterotetramers.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-392 | N-terminal catalytic PFK domain 1 | |||
Domain | 20-325 | Phosphofructokinase | |||
Domain | 405-690 | Phosphofructokinase | |||
Region | 405-787 | 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
- Length787
- Mass (Da)86,065
- Last updated2019-09-18 v1
- MD5 Checksum2BF6566BA7BD3EE546400D65CD45E75E
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A4W4GK39 | A0A4W4GK39_ELEEL | pfkpa | 795 | ||
A0A4W4GIF0 | A0A4W4GIF0_ELEEL | pfkpa | 565 | ||
A0A4W4GN31 | A0A4W4GN31_ELEEL | pfkpa | 768 | ||
A0A4W4GK46 | A0A4W4GK46_ELEEL | pfkpa | 761 | ||
A0A4W4GNS9 | A0A4W4GNS9_ELEEL | pfkpa | 788 |
Keywords
- Technical term