A0A6N7SKK5 · A0A6N7SKK5_9CLOT

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.
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 and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.

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 site17ATP (UniProtKB | ChEBI)
Binding site27-31ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site78-79ATP (UniProtKB | ChEBI)
Binding site108-111ATP (UniProtKB | ChEBI)
Binding site109Mg2+ (UniProtKB | ChEBI); catalytic
Binding site131-133substrate; ligand shared between dimeric partners; in other chain
Active site133Proton acceptor
Binding site160ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site168substrate; ligand shared between dimeric partners
Binding site175-177substrate; ligand shared between dimeric partners; in other chain
Binding site191-193ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site218ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site220-222ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site229substrate; ligand shared between dimeric partners; in other chain
Binding site250substrate; ligand shared between dimeric partners
Binding site256-259substrate; 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
      pfkA
    • ORF names
      GKG44_04090

Organism names

  • Taxonomic identifier
  • Strain
    • BIOML-A7
  • Taxonomic lineage
    Bacteria > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Lactonifactor

Accessions

  • Primary accession
    A0A6N7SKK5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain10-282Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    333
  • Mass (Da)
    35,986
  • Last updated
    2020-10-07 v1
  • Checksum
    D41B68E256005C10
MTAKKEIKTIGVLTSGGDAPGMNAAIRAVVRRGLSKGCKMKGILKGYNGLLNEEIIDMTAVDVSDTIERGGTILYTARCAEFRTEEGQKRGAEICRKHGIDALVVIGGDGSFAGAQKLANLGINTVGVPGTIDLDIACTEYTIGFDTAVNTAMEAIDKVRDTSTSHERCSIIEVMGRNAGYLALWCGIANGAEDILLPEKYDYDEQKVINNIIENRKRGKKHHIIINAEGIGHSEAMAKRIEAATGIETRATILGHMQRGGSPTCKDRVYASIMGAKAVDVLLEGKTQRVIGYKNGEYVDFDINEALAMTKSIPEYTYEIGHALSHNYSKNVK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WKYT01000004
EMBL· GenBank· DDBJ
MSB68047.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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