A0A922HPI9 · A0A922HPI9_DERFA
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids876 (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 | 62 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 125-126 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 155-158 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 156 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 201-203 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 203 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 238 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 245-247 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 301 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 329 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 335-338 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR | ||||||
Binding site | 509 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 567-571 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TISNN | ||||||
Binding site | 605 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 612-614 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGG | ||||||
Binding site | 668 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 694 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 700-703 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HMQQ | ||||||
Binding site | 781 | 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 > Analgoidea > Pyroglyphidae > Dermatophagoidinae > Dermatophagoides
Accessions
- Primary accessionA0A922HPI9
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-427 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MEVEDVLPPLRSPSMQAPQLQHLYRLRTMSTIDERDFPISTEGNIPESVQKGKIIGVFTSGGDSQGMNAAVRAVVRMGLYLGCRVYFIKEGYQGMVDGGDHIIEASWVSVSGIIHKGGTVIGSARCAEFRERQGRLKAAYNLIQYEITNLVVIGGDGSLTGANLFRQEWQSLVEELVNTGKITPQKASTVEHLHIVGMVGSIDNDFCGTDMTIGTDSALHRIIESIDAIVTTASSHQRTFILEVMGRHCGYLALVAALASEADFVFIPEWPPEADWSQRLCRKIEQERRLGKRLSIVIVAEGAIDMNGNPIQAETVKDVIVKNTGQDTRITVLGHVQRGGSPSAFDRVLGSRMGAEAVLALLEATPESQACVVSLDGNQAVRVPLMQCVERTKSVATAMKNKQWEEAVKLRGISFKRNLETYRMLTK | ||||||
Domain | 55-360 | Phosphofructokinase | ||||
Sequence: IGVFTSGGDSQGMNAAVRAVVRMGLYLGCRVYFIKEGYQGMVDGGDHIIEASWVSVSGIIHKGGTVIGSARCAEFRERQGRLKAAYNLIQYEITNLVVIGGDGSLTGANLFRQEWQSLVEELVNTGKITPQKASTVEHLHIVGMVGSIDNDFCGTDMTIGTDSALHRIIESIDAIVTTASSHQRTFILEVMGRHCGYLALVAALASEADFVFIPEWPPEADWSQRLCRKIEQERRLGKRLSIVIVAEGAIDMNGNPIQAETVKDVIVKNTGQDTRITVLGHVQRGGSPSAFDRVLGSRMGAEAVLA | ||||||
Domain | 440-726 | Phosphofructokinase | ||||
Sequence: RLAVMNCGAPCCGMNSAVRSFVRNVIFRGDTVLSIHDGFDGLIDGDIRPITWSEVRGWVGQGGANLGTRRTLPDDQNIEKIIANLRLYRVQALLVIGGFEAFQSVLYLAERRHQYVELRMPMCCVPATISNNVPGTDFSLGADTALNEITEICDRIRQSAQGTKRRVFIIETMGGFCGYLATLAGLAGGADAAYIFEEPFSINDLIGDIRLMHVKMEEGVTRGLVLRNEKANSNYTTDFMFKLYSEEGKDNFSTRMNILGHMQQGASPSPFDRNFGTKLAAKAAEWL | ||||||
Region | 440-876 | C-terminal regulatory PFK domain 2 | ||||
Sequence: RLAVMNCGAPCCGMNSAVRSFVRNVIFRGDTVLSIHDGFDGLIDGDIRPITWSEVRGWVGQGGANLGTRRTLPDDQNIEKIIANLRLYRVQALLVIGGFEAFQSVLYLAERRHQYVELRMPMCCVPATISNNVPGTDFSLGADTALNEITEICDRIRQSAQGTKRRVFIIETMGGFCGYLATLAGLAGGADAAYIFEEPFSINDLIGDIRLMHVKMEEGVTRGLVLRNEKANSNYTTDFMFKLYSEEGKDNFSTRMNILGHMQQGASPSPFDRNFGTKLAAKAAEWLTRQLEHHSRPLTEDYNELVYNSTSPDTAVLLGLIGRQYRFTPVQTLKTQTDFKNRLGKVQWWIRLRPLLRALASPEQLELKDVDNHISCSSIYNKYILKQLYRHRIPYSHWYKKLRPLLRILAHHEDIYQPEVIQVQEMDDIFNDDVFDA |
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
- Length876
- Mass (Da)97,846
- Last updated2023-02-22 v1
- ChecksumB84D72A07899B43D
Keywords
- Technical term