A0A421CTU5 · A0A421CTU5_9EURO

  • Protein
    ATP-dependent 6-phosphofructokinase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 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
      CFD26_101312

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • HMR AF 1038
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati

Accessions

  • Primary accession
    A0A421CTU5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-389N-terminal catalytic PFK domain 1
Domain15-322Phosphofructokinase
Region390-403Interdomain linker
Domain404-698Phosphofructokinase
Region404-799C-terminal regulatory PFK domain 2

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    799
  • Mass (Da)
    87,926
  • Last updated
    2019-05-08 v1
  • Checksum
    A86B5DF52E0B4827
MSATQAPVEPPKRRRIGVLTSGGDAPGMNGAVRAVVRMAIYSDCEAYAVFEGYEGLVHGGNMIRQLHWEDVRGWLSKGGTLIGSARSMAFRERAGRLKAAKNMVLRGIDALVVCGGDGSLTGADVFRSEWPGLLEELVKNGELTEEQIKPYKVLNIVGLVGSIDNDMSGTDATIGCYSSLTRICDAVDDVFDTAFSHQRGFVIEVMGRHCGWLALMSAISTGADWLFIPEMPPRDGWEDDMCSIITKNRKERGKRRTIVIVAEGAQDRSLNKISSSTIKDILTQRLGLDTRVTVLGHTQRGGAACAYDRWLSTLQGVEAVRAVLDMKPDSPSPVITIRENKIMRTPLMDAVQETKHVAKLIHDKDFEAAMRMRDAEFKEYHFAYRNTATPDHPKMILPEDKRMRIAIIHVGAPAGGMNQATRAVVGYCLTRGHTPLAIHNGFPGLCRHHDDKPVGSVREVKWLEADSWVNEGGSDIGTNRSLPSEDLETTAKCFERYKFDALFVVGGFEAFTAVSQLRQAREKYPAFKIPMVVLPATISNNVPGTEYSLGSDTCLNTLIDFCDAIRQSASSSRRRVFVIETQGGKSGYIATTAGLAVGATAVYIPEEGIDIKMLSNDIDFLRENFARDKGANRAGKLILRNECASSTYTTQVIADIFKEEAKGRFESRSAVPGHFQQGGKPSPMDRIRALRMSIKCMLHLENYAGKSPDEIAADPMSAAVIGIKGSQVMFSAMGGDDGLEATETDWARRRPKTEFWLELQNYVNVLSGRAAAGKPMWSCYECKPQTPSYLHHNTDFYSH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NIDN02000380
EMBL· GenBank· DDBJ
RLL93160.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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