G0R6Y9 · G0R6Y9_HYPJQ

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

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 site14ATP (UniProtKB | ChEBI)
Binding site77-78ATP (UniProtKB | ChEBI)
Binding site107-110ATP (UniProtKB | ChEBI)
Binding site108Mg2+ (UniProtKB | ChEBI); catalytic
Binding site153-155substrate; ligand shared between dimeric partners; in other chain
Active site155Proton acceptor
Binding site190substrate; ligand shared between dimeric partners
Binding site197-199substrate; ligand shared between dimeric partners; in other chain
Binding site253substrate; ligand shared between dimeric partners; in other chain
Binding site285substrate; ligand shared between dimeric partners
Binding site291-294substrate; ligand shared between dimeric partners; in other chain
Binding site474beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site532-536beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site570beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site577-579beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site637beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site663beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site669-672beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site741beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Component6-phosphofructokinase complex
Cellular Componentmitochondrion
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

Gene names

    • ORF names
      TRIREDRAFT_2091

Organism names

Accessions

  • Primary accession
    G0R6Y9

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-383N-terminal catalytic PFK domain 1
Domain6-316Phosphofructokinase
Region384-397Interdomain linker
Domain398-694Phosphofructokinase
Region398-788C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    788
  • Mass (Da)
    86,224
  • Last updated
    2011-10-19 v1
  • Checksum
    AC6630BE2AA7B322
MAPKKKIAVMTSGGDSPGMNAVVRAVVRMSIHMGCDAYCIYEGYEGLVQGGDFIRQMAWDDVRSFLSEGGTLIGTARCMAFYERPGRLTAAKNMVLNGIDALIICGGDGSLTGADKFRAEWPSLIEELVDNKELTPEQVAPYRHLNIVGLVGSIDNDLSGTDATIGCYSALSRICEMVDYIEATASSHSRAFVIEVMGRHCGWLALLAGVATGADFVFIPERPRDQDWREDMKLVVQRHRKMGKRKTIVIVAEGARDKDGTKITPEQIKDLLADKSEGGLNLDTRITTLGHVQRGGTAVAYDRILGTLQGVEAVKAVLEATPETETCVIAINENKIVRKPLMQAVKETKEVAVAVEAKDFDKAMSLRDTEFSDQYKSYLTTTNVLVDDHKLPEKSRMKIGFINVGAPAGGMNAAVRAAVAYCLSRGHEPLAIHNGFAGFARHHGDSPLGAVRPFDWLEVDGWASKGGSEIGTNRELPSESGMELIANLIEQYEFDALFIVGGFEAFHAVSQLRKARDEYPSLCIPLCLLPATISNNVPGTEYSLGSDTCLNELVNYCDKIKQSASATRRRVFVIETQGGRSGYVATLAGLSVGASAVYIPEEGISLEMLNADVKHLKEVFHHDKGQSRAGRLILVNEKASKVYDAKLIASIIREEAHDRFESRESIPGHVQQGGVPSPMDRCRAVRLAIKCMQHLEGFGRNAHNRVKKDPYSTSVIGIQGSEVVFSPIEELEEKHTDWANRRPKTAHWLDMQDVVNMLGGRPAYPKPEKSLTGLIAKDTKRGLYWGAD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GL985056
EMBL· GenBank· DDBJ
EGR53059.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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