A0A319E920 · A0A319E920_9EURO
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids784 (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 | 23 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 86-87 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 116-119 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 117 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 162-164 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 164 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 199 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 206-208 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 263 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 291 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 297-300 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HTQR | ||||||
Binding site | 480 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 537-541 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TISNN | ||||||
Binding site | 575 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 582-584 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: QGG | ||||||
Binding site | 642 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 668 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 674-677 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HFQQ | ||||||
Binding site | 749 | 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 | mitochondrion | |
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 > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionA0A319E920
Proteomes
Organism-specific databases
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-389 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MATPHAPVQPPKRRRIGVLTSGGDAPGMNGVVRAVVRMAIHSDCEAYAIYEGYEGLVNGGDMIRQLHWEDVRGWQSRGGTLIGSARCLTFRQRPGRLQGAKNLVLRGIDALVVCGGDGSLTGADVFRSEWPGLLKELVETGELTEEQVKPYLRLNIVGLVGSIDNDMSGTDATIGCYSSLTRICDAVDDVFDTAFSHQRGFVIEVMGRHCGWLALMSAISTGADWLFVPEMPPKDGWEDDMCSIITKNRKDRGKRRTIVIVAEGAQDRHLNKISSSHIKDILTDRLGLDTRVTVLGHTQRGGAACAYDRWLSTLQGVEAVRAVLDMKPESPSPVITIRENKILRMPLMEAVQATQTVTRHIQAKEFTQAMALRDSEFKEYHFSYINTST | ||||||
Domain | 15-322 | Phosphofructokinase | ||||
Sequence: RIGVLTSGGDAPGMNGVVRAVVRMAIHSDCEAYAIYEGYEGLVNGGDMIRQLHWEDVRGWQSRGGTLIGSARCLTFRQRPGRLQGAKNLVLRGIDALVVCGGDGSLTGADVFRSEWPGLLKELVETGELTEEQVKPYLRLNIVGLVGSIDNDMSGTDATIGCYSSLTRICDAVDDVFDTAFSHQRGFVIEVMGRHCGWLALMSAISTGADWLFVPEMPPKDGWEDDMCSIITKNRKDRGKRRTIVIVAEGAQDRHLNKISSSHIKDILTDRLGLDTRVTVLGHTQRGGAACAYDRWLSTLQGVEAVRA | ||||||
Region | 390-403 | Interdomain linker | ||||
Sequence: PDHPKLLLPENKRM | ||||||
Domain | 404-698 | Phosphofructokinase | ||||
Sequence: RIGIVHVGAPAGGMNQATRAAVAYCLTRGHTPLAIHNGFPGLCRHHADTPICSVREVQWQESDSWVNEGGSDIGTNRGLPGDDLETTALAFKKFQFDALFVVGGFEAFTAVSQLRQAREKFAEFKIPMTVLPATISNNVPGTEYSLGSDTCLNTLIDFCDAIRQSASSSRRRVFVIETQGGKSGYIATTAGLSVGAVAVYIPEEGIDIKMLSRDIDFLRDNFARDKGANRAGKIILRNECASSTYTTQVVADMIKTEAKGRFESRAAVPGHFQQGGKPSPMDRIRALRMATKCML | ||||||
Region | 404-784 | C-terminal regulatory PFK domain 2 | ||||
Sequence: RIGIVHVGAPAGGMNQATRAAVAYCLTRGHTPLAIHNGFPGLCRHHADTPICSVREVQWQESDSWVNEGGSDIGTNRGLPGDDLETTALAFKKFQFDALFVVGGFEAFTAVSQLRQAREKFAEFKIPMTVLPATISNNVPGTEYSLGSDTCLNTLIDFCDAIRQSASSSRRRVFVIETQGGKSGYIATTAGLSVGAVAVYIPEEGIDIKMLSRDIDFLRDNFARDKGANRAGKIILRNECASSTYTTQVVADMIKTEAKGRFESRAAVPGHFQQGGKPSPMDRIRALRMATKCMLHLESYAGQTPDAIAADELSASVIGVKGSQVLFSAMGGAEGLEATETDWARRRPKTEFWLELQGTVNILSGRASATNATAWSGYEST |
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
- Length784
- Mass (Da)85,558
- Last updated2018-10-10 v1
- Checksum9A9EC02D9E95CF09
Keywords
- Technical term