A0A8T4ZQR9 · A0A8T4ZQR9_9ARCH

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 site10diphosphate (UniProtKB | ChEBI)
Binding site102Mg2+ (UniProtKB | ChEBI); catalytic
Site103Important 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
Site123Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi
Binding site124-126substrate; ligand shared between dimeric partners; in other chain
Active site126Proton acceptor
Binding site161substrate; ligand shared between dimeric partners
Binding site168-170substrate; ligand shared between dimeric partners; in other chain
Binding site221substrate; ligand shared between dimeric partners; in other chain
Binding site266substrate; ligand shared between dimeric partners
Binding site272-275substrate; 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
      KEJ34_04935

Organism names

Accessions

  • Primary accession
    A0A8T4ZQR9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer or homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-298Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    342
  • Mass (Da)
    36,453
  • Last updated
    2022-10-12 v1
  • Checksum
    616ABBD5842CD738
MRVGVLTGGGDAPGLNAAIRAVVKKCEKYGFEVLGVRRGWAGMLEGDAIPLKYENIKDIISRGGTVIKTSRTNPLKQPDGINKISENFKNLGLDALIAIGGDDTLSVAKALSDAGLNVVGIPKTIDYDVPGTEFTIGFDTAINEAMHQIENIKATADAHERVFVVEVMGRHAGWIALYSGLAAGADLILIPEEPFSIEDVANFVKRKIESGQKAIVIVIAEGALIKGYKGLVTKDMKVDQFGHVYLGGIGDFLAKEIEKAIGVETRSVTPAHTIRGGSPTALDRLISTRYGLAAVDLVKEGKFGMMVALKAGNIVAVPLSEATGKTKQVDSQLYDEAKIFFE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAGTQL010000031
EMBL· GenBank· DDBJ
MBS7634824.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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