A0A834REN8 · A0A834REN8_SARSC
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids841 (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 | 76 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 139-140 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 169-172 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 170 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 215-217 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 217 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 252 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 259-261 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 315 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 343 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 349-352 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR | ||||||
Binding site | 523 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 581-585 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TISNN | ||||||
Binding site | 619 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 626-628 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGG | ||||||
Binding site | 682 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 708 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 714-717 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HMQQ | ||||||
Binding site | 799 | 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 | |
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 > Ecdysozoa > Arthropoda > Chelicerata > Arachnida > Acari > Acariformes > Sarcoptiformes > Astigmata > Psoroptidia > Sarcoptoidea > Sarcoptidae > Sarcoptinae > Sarcoptes
Accessions
- Primary accessionA0A834REN8
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-28 | Disordered | ||||
Sequence: MDSGGGGGGSNRSGSAAEIPPLPNKTPK | ||||||
Region | 1-441 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MDSGGGGGGSNRSGSAAEIPPLPNKTPKMSAPVLQHLYRVRTMSTVDDHDAPVSTEGNIPEGVQKGKIIGVFTSGGDSQGMNAAVRAVVRMGLYLGCRVYFIKEGYQGMVDGGDHIIEASWVSVSGIIHKGGTVIGSARCKEFRTHEGRLKAAYNLIQYGITNLVVIGGDGSLTGANLFRQEWSSLVKELVDSGQITTKKAEAVEHLHIVGMVGSIDNDFCGTDMTIGTDSALHRIIEAIDAIVTTASSHQRTFILEVMGRHCGYLALVAALASEADYVFIPEWPPEANWPEKLCNKIEEERRHGKRLNIIIVAEGATDLEGNDIEAEHVKDVIVKNTGQDTRITVLGHVQRGGSPSAFDRILGSRMGAEAVLALLEATPESQACVVSLDGNLAVRVPLMQCVEKTKSVACAMGDKKWDNAVQLRGVSFKRNLETYRMLTK | ||||||
Domain | 69-374 | Phosphofructokinase | ||||
Sequence: IGVFTSGGDSQGMNAAVRAVVRMGLYLGCRVYFIKEGYQGMVDGGDHIIEASWVSVSGIIHKGGTVIGSARCKEFRTHEGRLKAAYNLIQYGITNLVVIGGDGSLTGANLFRQEWSSLVKELVDSGQITTKKAEAVEHLHIVGMVGSIDNDFCGTDMTIGTDSALHRIIEAIDAIVTTASSHQRTFILEVMGRHCGYLALVAALASEADYVFIPEWPPEANWPEKLCNKIEEERRHGKRLNIIIVAEGATDLEGNDIEAEHVKDVIVKNTGQDTRITVLGHVQRGGSPSAFDRILGSRMGAEAVLA | ||||||
Domain | 454-740 | Phosphofructokinase | ||||
Sequence: RLAVMHCGAPCCGMNSAVRSFVRNIIFRGDTALAIHDGFDGFIEGDIRPITWTEVSGWVGQGGANLGTRRTLPDDKNIEQIVKQLKQFRIQGLLVIGGFEAFHSVLNLAERRNQFAELCIPMCVIPATISNNVPGTDFSLGTDTALNEITEICDRIRQSAQGTKRRVFVVETMGGYCGYLATLAGLAGGADAAYIFEEPFTINDLISDIRLMHAKMDEGVTRGLILRNEKANSNYTTDFLYKLYCEEGKDNFSTRMNVLGHMQQGAQPSPFDRNFGTKLAAKAADWL | ||||||
Region | 454-841 | C-terminal regulatory PFK domain 2 | ||||
Sequence: RLAVMHCGAPCCGMNSAVRSFVRNIIFRGDTALAIHDGFDGFIEGDIRPITWTEVSGWVGQGGANLGTRRTLPDDKNIEQIVKQLKQFRIQGLLVIGGFEAFHSVLNLAERRNQFAELCIPMCVIPATISNNVPGTDFSLGTDTALNEITEICDRIRQSAQGTKRRVFVVETMGGYCGYLATLAGLAGGADAAYIFEEPFTINDLISDIRLMHAKMDEGVTRGLILRNEKANSNYTTDFLYKLYCEEGKDNFSTRMNVLGHMQQGAQPSPFDRNFGTKLAAKAADWLQQQLLDHVKPPASSANEEEYELVYNATSPDTAVLLGLIGRQYRFSPVQTLKSRADFKNRLGEHQWWLRLRPLLRALASPSNLPLSDVNKTVHHFVELLDKE |
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.
Family and domain databases
Sequence
- Sequence statusComplete
- Length841
- Mass (Da)91,997
- Last updated2021-09-29 v1
- Checksum6A1B3B61650553D8
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
WVUK01000054 EMBL· GenBank· DDBJ | KAF7494122.1 EMBL· GenBank· DDBJ | Genomic DNA |