A0A7R7VSN5 · A0A7R7VSN5_ASPCH

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 site21ATP (UniProtKB | ChEBI)
Binding site84-85ATP (UniProtKB | ChEBI)
Binding site114-117ATP (UniProtKB | ChEBI)
Binding site115Mg2+ (UniProtKB | ChEBI); catalytic
Binding site160-162substrate; ligand shared between dimeric partners; in other chain
Active site162Proton acceptor
Binding site197substrate; ligand shared between dimeric partners
Binding site204-206substrate; 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 site747beta-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

    • Name
      PFK1
    • ORF names
      ACHE_51269A

Organism names

  • Taxonomic identifier
  • Strain
    • M1
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Aspergillus

Accessions

  • Primary accession
    A0A7R7VSN5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-387N-terminal catalytic PFK domain 1
Domain13-320Phosphofructokinase
Region388-401Interdomain linker
Domain402-696Phosphofructokinase
Region402-782C-terminal regulatory PFK domain 2

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    782
  • Mass (Da)
    85,842
  • Last updated
    2021-06-02 v1
  • Checksum
    C90001D1888026F6
MPPTQAEPPKRRRIGVLTSGGDAPGMNGAVRAVVRMALYSDCEAYTILEGYEGLVNGGDMIRQVQWEDVRGWLSCGGTLIGSARSMSFRERPGRLQAAKNMVLRGIDALVVCGGDGSLTGADVFRREWPGLLDELIQKGELTKDQVEPYRVLNIVGLVGSIDNDMSGTDATIGCYSSLTRICDAVDDVFDTAFSHQRGFVIEVMGRHCGWLALMSAISTGADWLFIPEMPPRDGWEDDMCANIVKNRKERGKRRTIVIVAEGAQDRHLNKISSNTIKDILTKRLGLDTRTTVLGHTQRGGAACAYDRWLSTLQGVEAVRAVLDMTADSPSPVITIRENKIMRTPLMEAVKATKDVTSLIHNKDFDGAMALRDAEFKEYHFSYLNTATPDHPKMILPENKRMRIGFIHVGAPAGGMNQATRAAVAYCQTRGHIPLAIHNGFPGLCRHHSDEPVSSVREIDWLESDNWVNQGGSEIGTNRSLPSEDYEGTAKCFEEHKFDALFVVGGFEAFTAVSQLRQAREKYPAFKIPMVVLPATVSNNVPGTEYSLGSDTCLNTLIDFCDAIRQSASSSRRRVFVVETQGGQSGYIATTAGLSVGATAVYIPEEGINIKRLSKDIDFLRDSFSKDYGTNRAGKLILRNECASSTYSTQVIADIIKEEACGRFESRAAVPGHFQQGGKPSPMDRIRALRMAIKCMLHLESYAGKAPDEVAADELSSTVIGIKGSQVLFSPMGGENGLEATETDWKRRRPKTEFWLELQDTVNILSGRTSFVAESEESQSFYS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP024420
EMBL· GenBank· DDBJ
BCR90071.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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