E6LJJ3 · E6LJJ3_9FIRM

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.

Type
IDPosition(s)Description
Binding site13ATP (UniProtKB | ChEBI)
Binding site23-27ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site74-75ATP (UniProtKB | ChEBI)
Binding site104-107ATP (UniProtKB | ChEBI)
Binding site105Mg2+ (UniProtKB | ChEBI); catalytic
Binding site127-129substrate; ligand shared between dimeric partners; in other chain
Active site129Proton acceptor
Binding site156ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site164substrate; ligand shared between dimeric partners
Binding site171-173substrate; ligand shared between dimeric partners; in other chain
Binding site187-189ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site214ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site216-218ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site225substrate; ligand shared between dimeric partners; in other chain
Binding site246substrate; ligand shared between dimeric partners
Binding site252-255substrate; 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
      HMPREF0381_0128

Organism names

Accessions

  • Primary accession
    E6LJJ3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain6-278Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    322
  • Mass (Da)
    34,547
  • Last updated
    2011-03-08 v1
  • Checksum
    CB838F65F092FD70
MAIKTIGVLTSGGDAPGMNAAIRAVVRTAIHNGINVKGIMRGYAGLLQEEIVDMESTSVSEIIHRGGTILYTARCQEFTTAEGQKKGAEICNKYGIDGVVVIGGDGSFQGAGKLSALGINTIGIPGTIDLDIACTDYTIGFDTAVNTAMDAIDKVRDTSTSHERCSIIEVMGRNAGYIALWCGFANGAEDVLLPERYDGNEQALIDRIIENRKRGKKHHIIINAEGIGHSVSMAKRIEAATGIETRATILGYMQRGGAPTCKDRVYASIMGAKAVELLLAGKSNRLVAYKNGEFVDFDIQEALAMKKDISEDQFRICKLLVR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AEPW01000002
EMBL· GenBank· DDBJ
EFU77988.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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