A0A0D2GVV6 · A0A0D2GVV6_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 site22ATP (UniProtKB | ChEBI)
Binding site85-86ATP (UniProtKB | ChEBI)
Binding site115-118ATP (UniProtKB | ChEBI)
Binding site116Mg2+ (UniProtKB | ChEBI); catalytic
Binding site161-163substrate; ligand shared between dimeric partners; in other chain
Active site163Proton acceptor
Binding site198substrate; ligand shared between dimeric partners
Binding site205-207substrate; ligand shared between dimeric partners; in other chain
Binding site261substrate; ligand shared between dimeric partners; in other chain
Binding site289substrate; ligand shared between dimeric partners
Binding site295-298substrate; ligand shared between dimeric partners; in other chain
Binding site478beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site535-539beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site573beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site580-582beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site640beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site666beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site672-675beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site748beta-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
      Z517_01993

Organism names

  • Taxonomic identifier
  • Strain
    • CBS 271.37
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Chaetothyriomycetidae > Chaetothyriales > Herpotrichiellaceae > Fonsecaea

Accessions

  • Primary accession
    A0A0D2GVV6

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
Region1-20Disordered
Region1-387N-terminal catalytic PFK domain 1
Domain14-320Phosphofructokinase
Region388-401Interdomain linker
Domain402-698Phosphofructokinase
Region402-795C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    795
  • Mass (Da)
    87,161
  • Last updated
    2015-04-29 v1
  • Checksum
    DC272928625A8CAE
MAANGVPAPPKKRRIGVMTSGGDSPGMNGAVRAVVRMSIHMGCESYAIYEGYEGLVQGGDLIKEMHWEDVRGYLSRGGTLIGTARCMAFMERWGRLKAAKNMVERGIDALVICGGDGSLTGADKFRAEWPSLLKELVETGELTQAEVDPFQHLNIVGLVGSIDNDMSGTDATIGCYSSLERICGAVDDVFDTAASHQRGFVIEVMGRHCGWLALMASIATGADFVFIPEKPPRVGWEDQMCDIIATHRRRGKRRSIVIIAEGAHDRELNRITANQVKDLLTQKLKLDTRVTVLGHTQRGGHACFYDRWLSTLQGVEAVKAVLEATPSTPSPVITIRENKIERSNLMETVALTKSVSAAIAAKDFDKAMQLRDVEFKEYYNSYVITTSTDHPALLLPKEKRLRIAIIHVGAPAGGMNPATRAAVAYCLTRGHTPIAIHNGFPGLQRHHDDKPLGSVRECRWIDVDPWVNEGGSEIGTNRGLPSADMKKTAECFGIYKFDALFLIGGFEAFTAASELRKAREQYEVFKIPLVVLPATVSNNVPGTEYSIGSDTCLNTLIQFCDAIRQSASSSRRRVFVIETQGGRSGYLATMAGLSVGALAVYIPEEGINIHMIARDIEFLRENFKNDQGASRAGKIILRNERASTTYTTQVIADMIKEEARGRFESRAAVPGHYQQGGKPSPMDRIRALRMAIKCMQHIEDRFTGKSKDWIADDPLSVAVIGIQGSEVVFTPMGGATGLEATGTDWEDRRPKSEFWLSMKETVDILSGRPQLADCCEECGKPLSGETLRRTLSKQV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KN846970
EMBL· GenBank· DDBJ
KIW82750.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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