A0A8J7Z5C4 · A0A8J7Z5C4_9ARCH

  • Protein
    Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
  • Gene
    pfp
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.

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

Non-allosteric.

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.

Features

Showing features for binding site, site, active site.

TypeIDPosition(s)Description
Binding site12diphosphate (UniProtKB | ChEBI)
Binding site104Mg2+ (UniProtKB | ChEBI); catalytic
Site105Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP
Site125Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi
Binding site126-128substrate; ligand shared between dimeric partners; in other chain
Active site128Proton acceptor
Binding site163substrate; ligand shared between dimeric partners
Binding site170-172substrate; ligand shared between dimeric partners; in other chain
Binding site223substrate; ligand shared between dimeric partners; in other chain
Binding site269substrate; ligand shared between dimeric partners
Binding site275-278substrate; 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 Functiondiphosphate-fructose-6-phosphate 1-phosphotransferase activity
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
    Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
  • EC number
  • Alternative names
    • 6-phosphofructokinase, pyrophosphate dependent
    • PPi-dependent phosphofructokinase
      (PPi-PFK
      )
    • Pyrophosphate-dependent 6-phosphofructose-1-kinase

Gene names

    • Name
      pfp
    • ORF names
      FK733_00360

Organism names

Accessions

  • Primary accession
    A0A8J7Z5C4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer or homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-301Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    345
  • Mass (Da)
    37,606
  • Last updated
    2022-05-25 v1
  • Checksum
    853A48A9CA411144
MAKKVGILTSGGDAPGLNPVIAGFTRKAIENGYEVVGFLDGWKGLIEGNIEKLTLERVKEIVQEGGTILGSSRTNPRKVENGYEKIFKTLKELDIYALATCGGDDTQGVAKELNEKGAKVVGVPKTIDNDLEATDQTFGFDTSINIAMDAIDRLRTTAKSHHRVFVLELMGRHSGWIALEAGMAGNANIIVIPEFDYPLNELCEVLKKRHDGNRTYSIIVVAEGVVFPEMKEKIEKAGKDSFGNIILADLKVGEFLADAIKEKTKLPVRAVTLGHIQRGGPPSAYDRFLGLRYGAKAAELIHDGKFGRMTSLQGTNIVDVPIEKAVAKRKVVPKDLWLLAKSFFG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VIKN01000015
EMBL· GenBank· DDBJ
NHJ46213.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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