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A0A6A6EHD9 · A0A6A6EHD9_9PEZI

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.

Type
IDPosition(s)Description
Binding site23ATP (UniProtKB | ChEBI)
Binding site91-92ATP (UniProtKB | ChEBI)
Binding site121-124ATP (UniProtKB | ChEBI)
Binding site122Mg2+ (UniProtKB | ChEBI); catalytic
Binding site167-169substrate; ligand shared between dimeric partners; in other chain
Active site169Proton acceptor
Binding site204substrate; ligand shared between dimeric partners
Binding site211-213substrate; ligand shared between dimeric partners; in other chain
Binding site267substrate; ligand shared between dimeric partners; in other chain
Binding site295substrate; ligand shared between dimeric partners
Binding site301-304substrate; ligand shared between dimeric partners; in other chain
Binding site484beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site541-545beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site579beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site586-588beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site646beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site672beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site678-681beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site750beta-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
      K469DRAFT_655738

Organism names

  • Taxonomic identifier
  • Strain
    • CBS 207.26
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Dothideomycetes incertae sedis > Zopfiaceae > Zopfia

Accessions

  • Primary accession
    A0A6A6EHD9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-393N-terminal catalytic PFK domain 1
Domain15-326Phosphofructokinase
Region394-407Interdomain linker
Domain408-703Phosphofructokinase
Region408-777C-terminal regulatory PFK domain 2

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    777
  • Mass (Da)
    85,083
  • Last updated
    2020-06-17 v1
  • MD5 Checksum
    87D31DDE73FBE7BEED64DC3A747EDF00
MSGPQTTTHSPPRRRIAVMTSGGDAPGMNGAVRAVVRTAIANDCEAYAIYEGYDGLVKGVDKKGNEMIKKMEFDDVRGFLGVGGTKIGTARCKEFRERAGRLRAAKNMIQKGIDALIICGGDGSLTGADLFREEWPGLLEELVKTGELSGNDIQPHKHLNIVGLVGSIDNDLSMTDATIGCYSSLERICRNVDDVYDTAASHQRAFVVEVMGRHCGWLALMAGLATGADYVFLPENPPPEDWQDKMGKIVETHRARGKRTTIVIVAEGAHDRNLQKIPAQEVTKFLAESLGLDARTTVLGHTQRGGVPCFYDRFLGTLQGAEAVKAVLDTTPETPSPVICMIENKIVRRPLLEAVKQTKEVAKAIESKDFGRAMSLRDAEFEEYMKVFNIIAGTGTENIKLPEEKRLRIGIIHVGAPAGGFNAATRAAVAYCLARGHTPVALHNGFPGLIRHHSDKPIGSVRDIDWLDAESWVNLGGSEIGTNRGLPSEDLETVAMVFKEYNIQALFLIGGFEAFTALSELRTSRQYYSAFKIPMTILPGTVSNNVPGTEYSIGSDTSLNALIQYCDTCRQSASSSRRRVFIIETQGGESGYLATLAGLSIGALAVYTPEEGIGIDMIKRDIDHLREVFAADKGKARAGKIILVNEKASKTYDVKTIKGIIDEEAKGRFESRWNVPGHWQQGTTPSPMDRVRAARFGVRSIEHLESFGGKSKDDIDEDPMSATVIGIKGAKVLLSPMEVVEKRETNWKLRRPKNEYWLGLKDMVDELSGRPYKRAEH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ML994617
EMBL· GenBank· DDBJ
KAF2191114.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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