A0A8R2NM69 · A0A8R2NM69_ACYPI

Function

function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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.

TypeIDPosition(s)Description
Binding site26ATP (UniProtKB | ChEBI)
Binding site89-90ATP (UniProtKB | ChEBI)
Binding site119-122ATP (UniProtKB | ChEBI)
Binding site120Mg2+ (UniProtKB | ChEBI); catalytic
Binding site165-167substrate; ligand shared between dimeric partners; in other chain
Active site167Proton acceptor
Binding site202substrate; ligand shared between dimeric partners
Binding site209-211substrate; ligand shared between dimeric partners; in other chain
Binding site265substrate; ligand shared between dimeric partners; in other chain
Binding site293substrate; ligand shared between dimeric partners
Binding site299-302substrate; ligand shared between dimeric partners; in other chain
Binding site483beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site540-544beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site578beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site585-587beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site641beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site667beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site673-676beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site748beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Component6-phosphofructokinase complex
Molecular Function6-phosphofructokinase activity
Molecular FunctionAMP binding
Molecular FunctionATP binding
Molecular Functionfructose-6-phosphate binding
Molecular Functionidentical protein binding
Molecular Functionmetal ion binding
Molecular Functionmonosaccharide binding
Biological Processcanonical glycolysis
Biological Processfructose 1,6-bisphosphate metabolic process
Biological Processfructose 6-phosphate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent 6-phosphofructokinase
  • EC number
  • Short names
    ATP-PFK
    ; Phosphofructokinase
  • Alternative names
    • Phosphohexokinase

Organism names

  • Taxonomic identifier
  • Strain
    • LSR1
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Hemiptera > Sternorrhyncha > Aphidomorpha > Aphidoidea > Aphididae > Macrosiphini > Acyrthosiphon

Accessions

  • Primary accession
    A0A8R2NM69

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-391N-terminal catalytic PFK domain 1
Domain19-324Phosphofructokinase
Region414-792C-terminal regulatory PFK domain 2
Domain415-699Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    792
  • Mass (Da)
    87,583
  • Last updated
    2022-10-12 v1
  • Checksum
    10763FFF3B653A00
MEEDQKRFIERGSHKGKGLAVFTSGGDSQGMNAAVRAVVRMAIYLGCKVFFIKEGYQGMVDGGDNIEEANWSSVSSIIHKGGTVIGSARCMDFKERVGRLKAACNLVKRGITNLVVIGGDGSLTGANLFRQEWSSLLDELLQTSQINKAEREKYKQLNIVGMVGSIDNDFCGTDMTIGTDSALHRIMDAIDAIVSTAYSHQRTFIMEVMGRHCGYLALVTALAAEADFVFIPEWPPHQDWASKMCKKLLQERTAGQRLNIIIVSEGAIDRDGQPITAEMVKQVVVDNLKQDTRITVLGHVQRGGAPSAFDRVLGCRMGAEAVMALMEATPETEACVVSLDGNQAVRLPLMECVEKTKAVAKAMADKEWELAVQLRGRSFARNLETYKMLTRLKPPRSAFDELGRGLSLNREGYTLAVMHIGAPACGMNSAVRSFVRNCIYRGDTVYGIHDGVEGLVAGNIQVMQWSDVTGWVGQGGAMLGTKRTLPEKRMPEIAARLKEFNIQALLIIGGFEAYQAGIQLVQNRNNFPEFCIPMVIIPSTISNNVPGTEFSLGCDTALNEITEICDRIRQSAQGTKRRVFVIETMGGYCGYLATVAGLAGGADAAYIYEEKFTIKDLQNDVYHMASKMAEGVQRGLILRNEKCSENYNTDFIFRLYTEEGKGLFSTRMNVLGHMQQGGSPTPFDRNMGTKQAAKCVEWLVEKLRESTRPDGTIYTDNPDTAAMMGVIRRQYRFTPLTDLLPLTNFEQRIAKTQWWLKLRPLLRILAKHDSAYEEEGMYITVEEGLEADTLLA

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8R2A979A0A8R2A979_ACYPI799
A0A8R2A536A0A8R2A536_ACYPI788
A0A8R2A3C8A0A8R2A3C8_ACYPI788
A0A8R2FDH1A0A8R2FDH1_ACYPI799

Keywords

Genome annotation databases

Similar Proteins

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