D5BFW0 · D5BFW0_ZUNPS

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 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 site15ATP (UniProtKB | ChEBI)
Binding site25-29ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site76-77ATP (UniProtKB | ChEBI)
Binding site106-109ATP (UniProtKB | ChEBI)
Binding site107Mg2+ (UniProtKB | ChEBI); catalytic
Binding site130-132substrate; ligand shared between dimeric partners; in other chain
Active site132Proton acceptor
Binding site159ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site167substrate; ligand shared between dimeric partners
Binding site174-176substrate; ligand shared between dimeric partners; in other chain
Binding site190-192ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site218-220ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site227substrate; ligand shared between dimeric partners; in other chain
Binding site252substrate; ligand shared between dimeric partners
Binding site258-261substrate; 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
    • Ordered locus names
      ZPR_2751

Organism names

Accessions

  • Primary accession
    D5BFW0

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-284Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    328
  • Mass (Da)
    35,914
  • Last updated
    2010-06-15 v1
  • Checksum
    B819104890558B75
MSKKIKRIGVITSGGDAPGMNAAIRAVVRACSYYHISCYGFYNGYNGLINGNFEELDARSVRNIINLGGTFLKSARSKEFRTKEGREKAYKVLKKEQVDGLILIGGDGTFTGGQIFSREYDIPVIGVPGTIDNDIYGTSHTIGYDTALNTVVEAIDKIRDTASSHDRLFFIEVMGRDAGFIALNTGIGAGAEEILIPEENLGLDRLLDSLEKSRRSGKNSSIVIVSEGDKIGKNVFQLADYVKENLPYYDAKVTVLGHIQRGGIPSCFDRVLASRMSVKAVELLLDGQKNVMVGLKDDDIITCPLDDVIHEKPKINKDLLRISEILST

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001650
EMBL· GenBank· DDBJ
ADF53073.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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