A0A8R2NM69 · A0A8R2NM69_ACYPI
- ProteinATP-dependent 6-phosphofructokinase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids792 (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 | 26 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 89-90 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RC | ||||||
Binding site | 119-122 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDGS | ||||||
Binding site | 120 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 165-167 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: SID | ||||||
Active site | 167 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 202 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 209-211 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGR | ||||||
Binding site | 265 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 293 | substrate; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 299-302 | substrate; ligand shared between dimeric partners; in other chain | ||||
Sequence: HVQR | ||||||
Binding site | 483 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 540-544 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: TISNN | ||||||
Binding site | 578 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 585-587 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: MGG | ||||||
Binding site | 641 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: E | ||||||
Binding site | 667 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 673-676 | beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain | ||||
Sequence: HMQQ | ||||||
Binding site | 748 | 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
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Hemiptera > Sternorrhyncha > Aphidomorpha > Aphidoidea > Aphididae > Macrosiphini > Acyrthosiphon
Accessions
- Primary accessionA0A8R2NM69
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-391 | N-terminal catalytic PFK domain 1 | ||||
Sequence: MEEDQKRFIERGSHKGKGLAVFTSGGDSQGMNAAVRAVVRMAIYLGCKVFFIKEGYQGMVDGGDNIEEANWSSVSSIIHKGGTVIGSARCMDFKERVGRLKAACNLVKRGITNLVVIGGDGSLTGANLFRQEWSSLLDELLQTSQINKAEREKYKQLNIVGMVGSIDNDFCGTDMTIGTDSALHRIMDAIDAIVSTAYSHQRTFIMEVMGRHCGYLALVTALAAEADFVFIPEWPPHQDWASKMCKKLLQERTAGQRLNIIIVSEGAIDRDGQPITAEMVKQVVVDNLKQDTRITVLGHVQRGGAPSAFDRVLGCRMGAEAVMALMEATPETEACVVSLDGNQAVRLPLMECVEKTKAVAKAMADKEWELAVQLRGRSFARNLETYKMLTR | ||||||
Domain | 19-324 | Phosphofructokinase | ||||
Sequence: LAVFTSGGDSQGMNAAVRAVVRMAIYLGCKVFFIKEGYQGMVDGGDNIEEANWSSVSSIIHKGGTVIGSARCMDFKERVGRLKAACNLVKRGITNLVVIGGDGSLTGANLFRQEWSSLLDELLQTSQINKAEREKYKQLNIVGMVGSIDNDFCGTDMTIGTDSALHRIMDAIDAIVSTAYSHQRTFIMEVMGRHCGYLALVTALAAEADFVFIPEWPPHQDWASKMCKKLLQERTAGQRLNIIIVSEGAIDRDGQPITAEMVKQVVVDNLKQDTRITVLGHVQRGGAPSAFDRVLGCRMGAEAVMA | ||||||
Region | 414-792 | C-terminal regulatory PFK domain 2 | ||||
Sequence: TLAVMHIGAPACGMNSAVRSFVRNCIYRGDTVYGIHDGVEGLVAGNIQVMQWSDVTGWVGQGGAMLGTKRTLPEKRMPEIAARLKEFNIQALLIIGGFEAYQAGIQLVQNRNNFPEFCIPMVIIPSTISNNVPGTEFSLGCDTALNEITEICDRIRQSAQGTKRRVFVIETMGGYCGYLATVAGLAGGADAAYIYEEKFTIKDLQNDVYHMASKMAEGVQRGLILRNEKCSENYNTDFIFRLYTEEGKGLFSTRMNVLGHMQQGGSPTPFDRNMGTKQAAKCVEWLVEKLRESTRPDGTIYTDNPDTAAMMGVIRRQYRFTPLTDLLPLTNFEQRIAKTQWWLKLRPLLRILAKHDSAYEEEGMYITVEEGLEADTLLA | ||||||
Domain | 415-699 | Phosphofructokinase | ||||
Sequence: LAVMHIGAPACGMNSAVRSFVRNCIYRGDTVYGIHDGVEGLVAGNIQVMQWSDVTGWVGQGGAMLGTKRTLPEKRMPEIAARLKEFNIQALLIIGGFEAYQAGIQLVQNRNNFPEFCIPMVIIPSTISNNVPGTEFSLGCDTALNEITEICDRIRQSAQGTKRRVFVIETMGGYCGYLATVAGLAGGADAAYIYEEKFTIKDLQNDVYHMASKMAEGVQRGLILRNEKCSENYNTDFIFRLYTEEGKGLFSTRMNVLGHMQQGGSPTPFDRNMGTKQAAKCVEWL |
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
- Length792
- Mass (Da)87,583
- Last updated2022-10-12 v1
- Checksum10763FFF3B653A00
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8R2A979 | A0A8R2A979_ACYPI | 799 | |||
A0A8R2A536 | A0A8R2A536_ACYPI | 788 | |||
A0A8R2A3C8 | A0A8R2A3C8_ACYPI | 788 | |||
A0A8R2FDH1 | A0A8R2FDH1_ACYPI | 799 |
Keywords
- Technical term