H3DAQ8 · H3DAQ8_TETNG
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids779 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 | 25 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 88-89 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 118-121 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 119 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 164-166 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 166 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 200 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 207-209 | 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: HVQR | ||||||
Binding site | 470 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 527-531 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TVSNN | ||||||
Binding site | 565 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 572-574 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGG | ||||||
Binding site | 628 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 654 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 660-663 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HMQQ | ||||||
Binding site | 734 | 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 | cytoplasm | |
Molecular Function | 6-phosphofructokinase activity | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
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
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Tetraodontiformes > Tetradontoidea > Tetraodontidae > Tetraodon
Accessions
- Primary accessionH3DAQ8
Proteomes
Subcellular Location
PTM/Processing
Keywords
- PTM
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-390 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MAHTVPINVSKMGEGRAIAVLTSGGDAQGMNAAVRATVRVGLYTGAKVYFVHEGYQGLVDGGDNIRPATWESVSMMLQLGGTVIGSARCQDFRTKEGRTKAAHNLVKLGITNLCVVGGDGSLTGANQFRTEWRDLLADLVKAGKITANEAKNSSHLNIVGMVGSIDNDFCGTDMTIGTDSALHRIIEVDAITTTAQSHQRTFILEVMGRHCGYLALVTALACGADWVFIPEMPPEEGWEEHLCRRLSDQRGRGSRLNIIIVAEGAMDRHGKPITCEQVKQLVSKKLGFDTRTTILGHVQRGGTPSAFDRILPRPSRMGVEAVMALLEATPDTPACVVSLSGNMAVRLPLMECVQVTKDVTTAMAERFEEAIKLRGKSFENNWNTYRMLAH | ||||||
Domain | 18-324 | Phosphofructokinase | ||||
Sequence: IAVLTSGGDAQGMNAAVRATVRVGLYTGAKVYFVHEGYQGLVDGGDNIRPATWESVSMMLQLGGTVIGSARCQDFRTKEGRTKAAHNLVKLGITNLCVVGGDGSLTGANQFRTEWRDLLADLVKAGKITANEAKNSSHLNIVGMVGSIDNDFCGTDMTIGTDSALHRIIEVDAITTTAQSHQRTFILEVMGRHCGYLALVTALACGADWVFIPEMPPEEGWEEHLCRRLSDQRGRGSRLNIIIVAEGAMDRHGKPITCEQVKQLVSKKLGFDTRTTILGHVQRGGTPSAFDRILPRPSRMGVEAVMA | ||||||
Domain | 401-685 | Phosphofructokinase | ||||
Sequence: NIALLNVGAPCAGMNAVVRSAVRIGILQGHQMLAVHDGFDGLAQGMIEPISWSGVAGWTGKGGSFLGTKRSLPEDVMEEISLNIAKFNIHAMVIIGGFEAFRGGLQMVQAREKYEELCIPLVVVPATVSNNIPGSDFSVGADTALNTITMTCDRIKQSAAGTKRRVFIVETMGGYCGYLATMAGLASGADAAYIHEEPFKIHDLQVNVDHLVEKMKTTVKRGLILRNEKCNANYTTDFIFNLYAEEGKGVFDCRKNVLGHMQQGGTPSPFDRNFGTKMGMKSVLW | ||||||
Region | 401-779 | C-terminal regulatory PFK domain 2 | ||||
Sequence: NIALLNVGAPCAGMNAVVRSAVRIGILQGHQMLAVHDGFDGLAQGMIEPISWSGVAGWTGKGGSFLGTKRSLPEDVMEEISLNIAKFNIHAMVIIGGFEAFRGGLQMVQAREKYEELCIPLVVVPATVSNNIPGSDFSVGADTALNTITMTCDRIKQSAAGTKRRVFIVETMGGYCGYLATMAGLASGADAAYIHEEPFKIHDLQVNVDHLVEKMKTTVKRGLILRNEKCNANYTTDFIFNLYAEEGKGVFDCRKNVLGHMQQGGTPSPFDRNFGTKMGMKSVLWLTDKLKECYRHGRIFANSPDSACVLGMRKRALVFTSLADLKEQTDFEHRIPKTQWWIKLRPLLKILAKYKINLDITEKTAMEHVIKKRGAFKFS |
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
- Length779
- Mass (Da)85,182
- Last updated2012-04-18 v1
- ChecksumE47F04EE4C2937FB
Keywords
- Technical term