A0A4W4H5S7 · A0A4W4H5S7_ELEEL
- ProteinATP-dependent 6-phosphofructokinase
- GenePFKL
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids780 (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. Negatively regulates the phagocyte oxidative burst in response to bacterial infection by controlling cellular NADPH biosynthesis and NADPH oxidase-derived reactive oxygen species. Upon macrophage activation, drives the metabolic switch toward glycolysis, thus preventing glucose turnover that produces NADPH via pentose phosphate pathway.
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 | 25 | ATP (UniProtKB | ChEBI) | |||
Binding site | 88-89 | ATP (UniProtKB | ChEBI) | |||
Binding site | 118-121 | ATP (UniProtKB | ChEBI) | |||
Binding site | 119 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 164-166 | substrate; ligand shared between dimeric partners; in other chain | |||
Active site | 166 | Proton acceptor | |||
Binding site | 201 | substrate; ligand shared between dimeric partners | |||
Binding site | 208-210 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 264 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 292 | substrate; ligand shared between dimeric partners | |||
Binding site | 298-301 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 470 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 527-531 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 565 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 572-574 | 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; in other chain | |||
Binding site | 654 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 660-663 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 734 | 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 accessionA0A4W4H5S7
Proteomes
Subcellular Location
PTM/Processing
Keywords
- PTM
Interaction
Subunit
Homo- and heterotetramers.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-390 | N-terminal catalytic PFK domain 1 | |||
Domain | 18-323 | Phosphofructokinase | |||
Region | 401-780 | C-terminal regulatory PFK domain 2 | |||
Domain | 402-686 | 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
- Length780
- Mass (Da)84,620
- Last updated2019-09-18 v1
- MD5 Checksum6083A9BFBB3C80C4CA50CCE4A74519C0
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A4W4GY74 | A0A4W4GY74_ELEEL | PFKL | 784 | ||
A0A4W4H4Q2 | A0A4W4H4Q2_ELEEL | PFKL | 775 | ||
A0A4W4H5H8 | A0A4W4H5H8_ELEEL | PFKL | 755 | ||
A0A4W4H5A6 | A0A4W4H5A6_ELEEL | PFKL | 777 | ||
A0A4W4H5X1 | A0A4W4H5X1_ELEEL | PFKL | 763 | ||
A0A4W4H5X9 | A0A4W4H5X9_ELEEL | PFKL | 762 | ||
A0A4W4H5M5 | A0A4W4H5M5_ELEEL | PFKL | 765 | ||
A0A4W4H611 | A0A4W4H611_ELEEL | PFKL | 779 | ||
A0A4W4GY99 | A0A4W4GY99_ELEEL | PFKL | 766 |
Keywords
- Technical term