A0A232EP66 · A0A232EP66_9HYME
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids830 (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 | 28 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 91-92 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 121-124 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 122 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 167-169 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 169 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 204 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 211-213 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 300 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 328 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 334-337 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR | ||||||
Binding site | 519 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 577-581 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TISNN | ||||||
Binding site | 615 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 622-624 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGG | ||||||
Binding site | 678 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 704 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 710-713 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HMQQ | ||||||
Binding site | 785 | 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
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Hymenoptera > Apocrita > Proctotrupomorpha > Chalcidoidea > Pteromalidae > Pteromalinae > Trichomalopsis
Accessions
- Primary accessionA0A232EP66
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-426 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MDEEQVAHRFIKPGSHRGKGLAVFTSGGDSQGMNAAVRAVVRMGIYLGCKVFFIREGYQGMVDGGDNIVEANWSSVSCIIHRGGTVIGSARCMEFREREGRKRAAKNLVTRGISNLCVIGGDGSLTGANLFKEEWADLLKELVKDGEITQEQSEKYKHLHIVGLVGSIDNDFCGTDMTIGTDTALHRIIESIDAIASTAYSHQRTFIMEVMGRHCGYLAIVGALASEADYVFFPESPPPADWPEKLCKNYLALVAAMCSEADYVFIPEWPPEQDWPNKLCKKLIQERLTGQRLNIIIVAEGAVDRNGDPITAEKVRQVVVEKLQQDTRITVLGHVQRGGNPSAFDRVLGCRMGAEAVMALVEATPETEACVVTLDGNQAVRLPLMECVRRTKAVAQAMADKNWDLAVQLRGKGFVRNLETYKMLTR | ||||||
Domain | 21-241 | Phosphofructokinase | ||||
Sequence: LAVFTSGGDSQGMNAAVRAVVRMGIYLGCKVFFIREGYQGMVDGGDNIVEANWSSVSCIIHRGGTVIGSARCMEFREREGRKRAAKNLVTRGISNLCVIGGDGSLTGANLFKEEWADLLKELVKDGEITQEQSEKYKHLHIVGLVGSIDNDFCGTDMTIGTDTALHRIIESIDAIASTAYSHQRTFIMEVMGRHCGYLAIVGALASEADYVFFPESPPPAD | ||||||
Domain | 250-359 | Phosphofructokinase | ||||
Sequence: YLALVAAMCSEADYVFIPEWPPEQDWPNKLCKKLIQERLTGQRLNIIIVAEGAVDRNGDPITAEKVRQVVVEKLQQDTRITVLGHVQRGGNPSAFDRVLGCRMGAEAVMA | ||||||
Region | 450-830 | C-terminal regulatory PFK domain 2 | ||||
Sequence: TLAVMHVGSPSCGMNAAVRSFVRNCIYRGDKVYGIMDGVLGLATGKLKLMDWPSVTGWVAQGGAYLGTKRAPPKDDQLPLIAQKLKEFGIQALLIIGGFEGFQTGLSFYNARTQHPEFRIPIAMIPATISNNVPGTEFSLGCDTALNEITEICDRIRQSAQGTKRRVFIIETMGGYCGYLATLAGLAGGADAAYIFEEKFNIKDLNQDIIAMAAKMSEGVQRGLILRNESANSNYNTEFMQRLFTEEGKGLFSCRMNIIGHMQQGGSPTPFDRNLGTKMGAKAVEWFTERLKKDTTADGQTVSNSDESAVMLGIVRRQYRYTPFSKLIDTTDFEHRIPTYQWWMKLRPLLKVLAKHESTYEEEGLYITVEDMDKNNDAPLV | ||||||
Domain | 451-735 | Phosphofructokinase | ||||
Sequence: LAVMHVGSPSCGMNAAVRSFVRNCIYRGDKVYGIMDGVLGLATGKLKLMDWPSVTGWVAQGGAYLGTKRAPPKDDQLPLIAQKLKEFGIQALLIIGGFEGFQTGLSFYNARTQHPEFRIPIAMIPATISNNVPGTEFSLGCDTALNEITEICDRIRQSAQGTKRRVFIIETMGGYCGYLATLAGLAGGADAAYIFEEKFNIKDLNQDIIAMAAKMSEGVQRGLILRNESANSNYNTEFMQRLFTEEGKGLFSCRMNIIGHMQQGGSPTPFDRNLGTKMGAKAVEW |
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
- Length830
- Mass (Da)91,722
- Last updated2017-10-25 v1
- Checksum2BE5EC4519C26EDA
Keywords
- Technical term