S0JAM9 · S0JAM9_9ENTE

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 site11ATP (UniProtKB | ChEBI)
Binding site72-73ATP (UniProtKB | ChEBI)
Binding site125-127substrate; ligand shared between dimeric partners; in other chain
Active site127Proton acceptor
Binding site154ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site162substrate; ligand shared between dimeric partners
Binding site185-187ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site211ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site213-215ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site222substrate; ligand shared between dimeric partners; in other chain
Binding site243substrate; ligand shared between dimeric partners
Binding site249-252substrate; 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
      OMQ_00616

Organism names

Accessions

  • Primary accession
    S0JAM9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-274Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    320
  • Mass (Da)
    34,292
  • Last updated
    2013-09-18 v1
  • MD5 Checksum
    CBC094F309C5F4B25015CF8ADBC3BA0C
MKRLAILTSGGDAPGMNATIRAVLNKAAHHDIEVVGVNYGFLGLVCKNFTSLDTEKVNSSISMGGTILYSSRYPEFAEKEIQLKAIENLKEANIDGLIVIGGRGSHHGALALSNLGFPTIGIPATIDNDIPGTEFTVGFDTAVNTVVSALDKIRDTANSHVRTFVIEVKGLRSGDLALWSGVAGGAESILIPEQELDLAHVASKIKQSVERKKKHCLIVLAEGVMSASELTTKLKEEGVLHIREVELGHVPRGGSPTPYDRVLASKAGAAAVNLFLEEKFGNCLCIQYNKLVPVSLKDALDIEKNFIDLSLYPLNSSISY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AHYT01000002
EMBL· GenBank· DDBJ
EOT29924.1
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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