A0A8G1QVE0 · A0A8G1QVE0_9EURO

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 site23ATP (UniProtKB | ChEBI)
Binding site86-87ATP (UniProtKB | ChEBI)
Binding site116-119ATP (UniProtKB | ChEBI)
Binding site117Mg2+ (UniProtKB | ChEBI); catalytic
Binding site162-164substrate; ligand shared between dimeric partners; in other chain
Active site164Proton acceptor
Binding site199substrate; ligand shared between dimeric partners
Binding site206-208substrate; ligand shared between dimeric partners; in other chain
Binding site263substrate; ligand shared between dimeric partners; in other chain
Binding site291substrate; ligand shared between dimeric partners
Binding site297-300substrate; ligand shared between dimeric partners; in other chain
Binding site480beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site537-541beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site575beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site582-584beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site642beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site668beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site674-677beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site749beta-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
      BO85DRAFT_453074

Organism names

  • Taxonomic identifier
  • Strain
    • CBS 112811
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati

Accessions

  • Primary accession
    A0A8G1QVE0

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-20Disordered
Region1-389N-terminal catalytic PFK domain 1
Domain15-322Phosphofructokinase
Region390-403Interdomain linker
Domain404-698Phosphofructokinase
Region404-783C-terminal regulatory PFK domain 2

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    783
  • Mass (Da)
    85,721
  • Last updated
    2022-01-19 v1
  • Checksum
    89EEDADB139CD0E7
MAPTQAPVQPPKRRRIGVLTSGGDAPGMNGVVRAVVRMAIHSDCEAFAVYEGYEGLVNGGDMIRQLHWEDVRGWLSRGGTLIGSARCMTFRERPGRLRAAKNMVLRGIDALVVCGGDGSLTGADLFRSEWPGLLKELVETGELTEEQVKPYQILNIVGLVGSIDNDMSGTDATIGCYSSLTRICDAVDDVFDTAFSHQRGFVIEVMGRHCGWLALMSAISTGADWLFVPEMPPKDGWEDDMCAIITKNRKERGKRRTIVIVAEGAQDRHLNKISSSKIKDILTERLNLDTRVTVLGHTQRGGAACAYDRWLSTLQGVEAVRAVLDMQPGAPSPVITIRENKILRMPLMDAVQHTKTVTKHIQNKEFAEAMALRDSEFKEYHYSYINTSTPDHPKLLLPENKRMRIGIIHVGAPAGGMNQATRAAVAYCLTRGHTPLAIHNGFPGLCRHYDDTPICSVREVAWQESDSWVNEGGSDIGTNRGLPGDDLATTAKSFKKFGFDALFVVGGFEAFTAVSQLRQAREKYPEFKIPMTVLPATISNNVPGTEYSLGSDTCLNTLIDFCDAIRQSASSSRRRVFVIETQGGKSGYIATTAGLSVGAVAVYIPEEGIDIKMLARDIDFLRDNFARDKGANRAGKIILRNECASSTYTTQVVADMIKEEAKGRFESRAAVPGHFQQGGKPSPMDRIRALRMATKCMLHLESYAGKSADEIAADELSASVIGIKGSQVLFSPMGGANGLEATETDWARRRPKTEFWLELQDTVNILSGRASVNNATWSCYENV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KZ825076
EMBL· GenBank· DDBJ
RAH53562.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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