A0A5F9D5Z9 · A0A5F9D5Z9_RABIT
- ProteinATP-dependent 6-phosphofructokinase
- GenePFKM
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids801 (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 | 96 | ATP (UniProtKB | ChEBI) | |||
Binding site | 159-160 | ATP (UniProtKB | ChEBI) | |||
Binding site | 189-192 | ATP (UniProtKB | ChEBI) | |||
Binding site | 190 | Mg2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 235-237 | substrate; ligand shared between dimeric partners; in other chain | |||
Active site | 237 | Proton acceptor | |||
Binding site | 272 | substrate; ligand shared between dimeric partners | |||
Binding site | 279-281 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 335 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 363 | substrate; ligand shared between dimeric partners | |||
Binding site | 369-372 | substrate; ligand shared between dimeric partners; in other chain | |||
Binding site | 492 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 549-553 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 587 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 594-596 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 650 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 676 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | |||
Binding site | 682-685 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | |||
Binding site | 756 | 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
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus
Accessions
- Primary accessionA0A5F9D5Z9
Proteomes
Subcellular Location
PTM/Processing
Keywords
- PTM
Expression
Gene expression databases
Interaction
Subunit
Homo- and heterotetramers.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-461 | N-terminal catalytic PFK domain 1 | |||
Region | 22-62 | Disordered | |||
Domain | 89-394 | Phosphofructokinase | |||
Domain | 468-707 | Phosphofructokinase | |||
Region | 468-801 | 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
- Length801
- Mass (Da)88,290
- Last updated2019-12-11 v1
- ChecksumF60A5395AC04317F
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A5F9DGX0 | A0A5F9DGX0_RABIT | PFKM | 851 | ||
A0A5F9CE16 | A0A5F9CE16_RABIT | PFKM | 694 | ||
A0A5F9DKQ9 | A0A5F9DKQ9_RABIT | PFKM | 94 | ||
G1TDQ5 | G1TDQ5_RABIT | PFKM | 749 | ||
A0A5F9DCR3 | A0A5F9DCR3_RABIT | PFKM | 816 | ||
A0A5F9D2K9 | A0A5F9D2K9_RABIT | PFKM | 753 | ||
A0A5F9CT34 | A0A5F9CT34_RABIT | PFKM | 758 |
Keywords
- Technical term