A0A0F2PNK2 · A0A0F2PNK2_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.

TypeIDPosition(s)Description
Binding site11ATP (UniProtKB | ChEBI)
Binding site21-25ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site72-73ATP (UniProtKB | ChEBI)
Binding site102-105ATP (UniProtKB | ChEBI)
Binding site103Mg2+ (UniProtKB | ChEBI); catalytic
Binding site126-128substrate; ligand shared between dimeric partners; in other chain
Active site128Proton acceptor
Binding site155ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site163substrate; ligand shared between dimeric partners
Binding site170-172substrate; ligand shared between dimeric partners; in other chain
Binding site186-188ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site212ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site214-216ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site223substrate; ligand shared between dimeric partners; in other chain
Binding site244substrate; ligand shared between dimeric partners
Binding site250-253substrate; 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
      VR67_00785

Organism names

Accessions

  • Primary accession
    A0A0F2PNK2

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-276Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    320
  • Mass (Da)
    34,136
  • Last updated
    2015-06-24 v1
  • Checksum
    E62DF523C81E8A11
MLRIAVLTSGGDSPGMNAAIRAVVRKAIYHGLEVIGIQRGFSGFIEADMGPMNLGSVADIIHRGGTILRTARSEEFMTSQGRARAYANVERFGIQGLVVIGGDGSFKGAEIFHNEFNVPVTGVPGTIDNDIAGTDYSIGFDTAVNTVVEAINKIRDTATSHERTFIVEVMGRESGCIAMTSGLAGGAESILIPELEYNLDEVCDKLYRGYKRGKLHSIIIVAEGAASGIDVSRAIKEKTGLDTKVTILGHLQRGGTPTAFDRILASRMGARAVDLLMSGYRQHMVGMVAGEIIACPLETVFTVKKPIDMDVYNLAGILSI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LADP01000003
EMBL· GenBank· DDBJ
KJS14062.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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