A0A3B3IMJ2 · A0A3B3IMJ2_ORYLA
- ProteinATP-dependent 6-phosphofructokinase
- GenePFKP
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids874 (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 | 33 | ATP (UniProtKB | ChEBI) | |||
Binding site | 96-97 | ATP (UniProtKB | ChEBI) | |||
Binding site | 126-129 | ATP (UniProtKB | ChEBI) | |||
Binding site | 127 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 172-174 | substrate; ligand shared between dimeric partners; in other chain | |||
Active site | 174 | Proton acceptor | |||
Binding site | 209 | substrate; ligand shared between dimeric partners | |||
Binding site | 216-218 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 272 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 332 | substrate; ligand shared between dimeric partners | |||
Binding site | 338-341 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 512 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 620-624 | 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 | 665-667 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 721 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 747 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 753-756 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 827 | 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
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Ovalentaria > Atherinomorphae > Beloniformes > Adrianichthyidae > Oryziinae > Oryzias
Accessions
- Primary accessionA0A3B3IMJ2
Proteomes
Subcellular Location
Expression
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-430 | N-terminal catalytic PFK domain 1 | |||
Domain | 26-286 | Phosphofructokinase | |||
Domain | 287-363 | Phosphofructokinase | |||
Region | 443-874 | C-terminal regulatory PFK domain 2 | |||
Domain | 596-779 | 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
- Length874
- Mass (Da)95,502
- Last updated2018-12-05 v1
- Checksum2636B346A5AB08F1
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A3B3HD46 | A0A3B3HD46_ORYLA | PFKP | 842 | ||
A0A3B3IGG9 | A0A3B3IGG9_ORYLA | PFKP | 842 | ||
A0A3B3HFI8 | A0A3B3HFI8_ORYLA | PFKP | 736 | ||
A0A3B3IIB5 | A0A3B3IIB5_ORYLA | PFKP | 823 | ||
A0A3B3IIQ0 | A0A3B3IIQ0_ORYLA | PFKP | 823 | ||
H2LMF2 | H2LMF2_ORYLA | PFKP | 756 | ||
A0A3B3HTR3 | A0A3B3HTR3_ORYLA | PFKP | 759 | ||
A0A3B3H5T7 | A0A3B3H5T7_ORYLA | PFKP | 740 |
Keywords
- Technical term