L8HYJ7 · L8HYJ7_9CETA
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids850 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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
- ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + 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 | 95 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 158-159 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 188-191 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 189 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 234-236 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 236 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 271 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 278-280 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 334 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 362 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 368-371 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR | ||||||
Binding site | 541 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 598-602 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TVSNN | ||||||
Binding site | 636 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 643-645 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGG | ||||||
Binding site | 699 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 725 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 731-734 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HMQQ | ||||||
Binding site | 805 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | 6-phosphofructokinase complex | |
Cellular Component | apical plasma membrane | |
Cellular Component | nucleus | |
Cellular Component | sperm principal piece | |
Molecular Function | 6-phosphofructokinase activity | |
Molecular Function | ATP binding | |
Molecular Function | fructose binding | |
Molecular Function | identical protein binding | |
Molecular Function | kinase binding | |
Molecular Function | metal ion binding | |
Biological Process | canonical glycolysis | |
Biological Process | fructose 6-phosphate metabolic process | |
Biological Process | glucose homeostasis | |
Biological Process | glycogen catabolic process | |
Biological Process | glycolysis from storage polysaccharide through glucose-1-phosphate | |
Biological Process | muscle cell cellular homeostasis | |
Biological Process | positive regulation of insulin secretion | |
Biological Process | positive regulation of transcription by RNA polymerase II |
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 accessionL8HYJ7
Proteomes
Subcellular Location
PTM/Processing
Keywords
- PTM
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-460 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MRKVELHLKFFMCVTQSRQLVRTPQRTAEEASTSSMLMQKPPSRTDVLKSLDTVDDPDTVEGIPIFANEWIMTHEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIYTGARVFFVHEGYQGLVDGGDNIREATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAHNLVKRGITNLCVIGGDGSLTGADTFRSEWSDLLSDLQKSGKITAEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDSALHRIIEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWEEHLCRRLSETRNRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTRAMDERRFDEALKLRGRSFMNNWEVYKLLAH | ||||||
Domain | 88-393 | Phosphofructokinase | ||||
Sequence: IAVLTSGGDAQGMNAAVRAVVRVGIYTGARVFFVHEGYQGLVDGGDNIREATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAHNLVKRGITNLCVIGGDGSLTGADTFRSEWSDLLSDLQKSGKITAEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDSALHRIIEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWEEHLCRRLSETRNRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMA | ||||||
Region | 472-850 | C-terminal regulatory PFK domain 2 | ||||
Sequence: TVAVMNVGAPAAGMNAAVRSTVRIGLIQGNRMLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQYDELCIPFVVIPATVSNNVPGSDFSVGADTALNTICMTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEDPFTIRDLQVNVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLGHMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANSPDSGCVLGMRKRALVFQPVTELKEQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSEHAHLEHISRKRSGEANV | ||||||
Domain | 473-756 | Phosphofructokinase | ||||
Sequence: VAVMNVGAPAAGMNAAVRSTVRIGLIQGNRMLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQYDELCIPFVVIPATVSNNVPGSDFSVGADTALNTICMTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEDPFTIRDLQVNVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLGHMQQGGSPTPFDRNFATKMGAKAMNW |
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
- Length850
- Mass (Da)93,427
- Last updated2013-04-03 v1
- Checksum337A26DF1D656827
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JH882468 EMBL· GenBank· DDBJ | ELR49260.1 EMBL· GenBank· DDBJ | Genomic DNA |