M5DEU6 · M5DEU6_9METZ

  • Protein
    ATP-dependent 6-phosphofructokinase
  • Gene
    PFK
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • 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

Lacks conserved residue(s) required for the propagation of feature annotation.

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 site61ATP (UniProtKB | ChEBI)
Binding site124-125ATP (UniProtKB | ChEBI)
Binding site154-157ATP (UniProtKB | ChEBI)
Binding site155Mg2+ (UniProtKB | ChEBI); catalytic
Binding site200-202substrate; ligand shared between dimeric partners; in other chain
Active site202Proton acceptor
Binding site237substrate; ligand shared between dimeric partners
Binding site244-246substrate; ligand shared between dimeric partners; in other chain
Binding site300substrate; ligand shared between dimeric partners; in other chain
Binding site328substrate; ligand shared between dimeric partners
Binding site334-337substrate; ligand shared between dimeric partners; in other chain
Binding site509beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site567-571beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site605beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site612-614beta-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; in other chain
Binding site694beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site700-703beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site770beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Component6-phosphofructokinase complex
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
      PFK

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Porifera > Calcarea > Calcaronea > Leucosolenida > Sycettidae > Sycon

Accessions

  • Primary accession
    M5DEU6

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-41Disordered
Region1-426N-terminal catalytic PFK domain 1
Domain54-359Phosphofructokinase
Domain440-722Phosphofructokinase
Region440-811C-terminal regulatory PFK domain 2

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    811
  • Mass (Da)
    89,164
  • Last updated
    2013-05-29 v1
  • Checksum
    C24007CEEAF44FD8
MAKRTSSSTSFGSELCPPEKMPRITLPPQSPQPSFAVSRSSSPLTVELERRKCIAVMTSGGDSQGMNAALRGLVRMAMYRHARVFLIYEGYQGLVQGGDLIKETTWYGVSHIMGKGGTVIGTARCKEFRERWGRRAAALNLVKKRITNLIVIGGDGSLTGANLFREEWPELLQELVEEGNISAQEQTECDHLNIVGMVGSIDNDMCGTDMTLGADSALHRIVEAVDAISFTASSHQRCFVLEVMGRHCGYLALVSSLGCNADWCLIPESPPSDNWEKKMCEQLCRSREEGARMNLIIVAEGAVDRQGQPISSQYVKSVIEKELGYDTRITVLGHVQRGGAPSAYDRLMGCRVGAAAANAVLDADKDNEPVLVGLQGNRVVQSPLMKCVRETQGIAGAMKDGNFKEALSMRAGSFVRHWATFRRLSRYDKLPVVPATEKLRFALLHVGAPAAGVNTCTQAFFRLTTYHGHQVYAVHEGFDGLAKGSIQLLDRSQVLKWSVAGGSHLGTNRSLPSKEGLPLIAEQLKKHRINGLLVIGGFEAFHSLCILEDARKDYPAFCIPMLNVAATISNNVPGTDHSMGCDTALNIIIETTDRLKQSAVASRKRVFVIETMGGHCGFLATMGGLAGGADAAYIFEEKFTISDLQNDVRHLVSKFQQGIWRGIILRNEKCSPYYTTDFITNLYSAEGGELFTTRSNVLGHMQQGGLPSPYDRHLGVRFAKCSLDFFLDHCTLEPQPQCSSATACTVGMRARKTVFTPVSELKLRTDFKNRLPLDQWWLELRPLLRILAKHRDYHFKPGDLAADEIEQSTTP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HF583277
EMBL· GenBank· DDBJ
CCQ42783.1
EMBL· GenBank· DDBJ
mRNA

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