A0A8P0TRT9 · A0A8P0TRT9_CANLF

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 site25ATP (UniProtKB | ChEBI)
Binding site88-89ATP (UniProtKB | ChEBI)
Binding site118-121ATP (UniProtKB | ChEBI)
Binding site119Mg2+ (UniProtKB | ChEBI); catalytic
Binding site164-166substrate; ligand shared between dimeric partners; in other chain
Active site166Proton acceptor
Binding site201substrate; ligand shared between dimeric partners
Binding site208-210substrate; ligand shared between dimeric partners; in other chain
Binding site264substrate; ligand shared between dimeric partners; in other chain
Binding site292substrate; ligand shared between dimeric partners
Binding site298-301substrate; ligand shared between dimeric partners; in other chain
Binding site473beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site530-534beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site568beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site575-577beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site631beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site657beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site663-666beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site740beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function6-phosphofructokinase activity
Molecular FunctionATP binding
Molecular Functionmetal ion binding
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

Gene names

    • Name
      PFKM

Organism names

Accessions

  • Primary accession
    A0A8P0TRT9

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Homo- and heterotetramers.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-390N-terminal catalytic PFK domain 1
Domain18-323Phosphofructokinase
Region404-785C-terminal regulatory PFK domain 2
Domain405-691Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    785
  • Mass (Da)
    85,845
  • Last updated
    2022-10-12 v1
  • Checksum
    BDB75AD0B26FD231
MTHEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVDGGDHIREATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAHNLVKRGITNLCVIGGDGSLTGADTFRSEWSDLLSDLQKAGKITAEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDSALHRIIEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWEEHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEEIKELVVKRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTKAMNDRKFDEAMKLRGRSFMNNWEVYKLLAHIRPPVSKTSATMHTVAVMNVGAPAAGMNAAVRSTVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQISANITKFNIQGLIIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSVGADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPFTIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLGHMQQVGKGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVFQPVTELKDQTDFDHRIPKEQWWLKLRPILKILAKYEIDLDTTEHAHLEHISRKRSGETSI

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp