A0A914ZDQ6 · A0A914ZDQ6_PARUN

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 site68ATP (UniProtKB | ChEBI)
Binding site131-132ATP (UniProtKB | ChEBI)
Binding site161-164ATP (UniProtKB | ChEBI)
Binding site162Mg2+ (UniProtKB | ChEBI); catalytic
Binding site207-209substrate; ligand shared between dimeric partners; in other chain
Active site209Proton acceptor
Binding site244substrate; ligand shared between dimeric partners
Binding site251-253substrate; ligand shared between dimeric partners; in other chain
Binding site307substrate; ligand shared between dimeric partners; in other chain
Binding site335substrate; ligand shared between dimeric partners
Binding site341-344substrate; ligand shared between dimeric partners; in other chain
Binding site519beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site576-580beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site614beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site621-623beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site677beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site703beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site709-712beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site785beta-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
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Spirurina > Ascaridomorpha > Ascaridoidea > Ascarididae > Parascaris

Accessions

  • Primary accession
    A0A914ZDQ6

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-44Disordered
Region1-433N-terminal catalytic PFK domain 1
Domain61-366Phosphofructokinase
Domain450-734Phosphofructokinase
Region450-824C-terminal regulatory PFK domain 2

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    824
  • Mass (Da)
    90,158
  • Last updated
    2023-02-22 v1
  • Checksum
    AB2D6A33D7689D71
MEKQQPTAQLADMSAEDSVGPLPDVNTPRNRFSKGRSDSIVPTAGKEGSVIVPHLYKGQSIAVFTSGGDAPGMNSAVRSVVRMGMYLGCRVYFIYEGYQGMVDGGDNIKEADWNSVSDIIQKGGTIIGSARCKEFREREGRLRAAENLIAHNITNLVCIGGDGSLTGANLFRQEWPGLVKDLLAAGRITPEKAQQCANIQIVGLVGSIDNDFCGTDMTIGTDTALQRIIEAIDSVMSTAQSHQRCFVIEVMGRHCGYLAVVAALASEADFCFIPEWPAPTDWPDVLCKKLQTMRAEGQRLNIIIVAEGAIDREGKAITAEIVRGVVKSTLHYDTRVTVLGHVQRGGSPSAFDRLLGCRMGAEAVLALMEMTPESEPCVVSIDGNLMVRVPLMQCVLRTQAVQKAMDARDWETAVKLRGRSFQRNLETYRLLTKLHIPKDKDNLTAGHKFNVAVINVGAPAGGMNAAVRSFVRMAIYHHCRVYGVQNSFEGLARGDLKEMEWSDVNNWVMHGGSFLGTQKQLPDKSMPEVAAVLAKFNIHAILLVGGFEAYHSCLLLSRARSIYPSLRIPMCIIPCTISNNIPGTSLSLGSDTAVNEICHMIDKIKQSATGTKRRVFIVETMGGYCGYLATLSALASGADNAYIFEEKFGVLDILEDVKVITKKMEMGVQRYLIVRCELANRNYTTEFVKQLFAEEGKGAFSTRTNVLGHAQQGGSPTPFDRNLGTKLAARALEYLVTQAKEAVNLKTGVASATNADTATLLGLRGRRVVFTPVEELALETDFEHRLPKEQWWLKVRPLLRILAKHDSIYEAESMAVPECEGEIN

Keywords

Genome annotation databases

Similar Proteins

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