A0A7C4RD80 · A0A7C4RD80_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 site11diphosphate (UniProtKB | ChEBI)
Binding site103Mg2+ (UniProtKB | ChEBI); catalytic
Site104Important 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
Site124Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi
Binding site125-127substrate; ligand shared between dimeric partners; in other chain
Active site127Proton acceptor
Binding site162substrate; ligand shared between dimeric partners
Binding site169-171substrate; ligand shared between dimeric partners; in other chain
Binding site222substrate; ligand shared between dimeric partners; in other chain
Binding site267substrate; ligand shared between dimeric partners
Binding site273-276substrate; ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function6-phosphofructokinase activity
Molecular FunctionATP binding
Molecular Functiondiphosphate-fructose-6-phosphate 1-phosphotransferase activity
Molecular Functionmetal ion binding
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
      ENT44_00120

Organism names

Accessions

  • Primary accession
    A0A7C4RD80

Subcellular Location

Keywords

Interaction

Subunit

Homodimer or homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-299Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    350
  • Mass (Da)
    38,110
  • Last updated
    2020-12-02 v1
  • Checksum
    9500B64B86FF4958
MSKIAVLTGGGDCPGLNAVIQGVFVRACQYGYEVYGVEDGYKGLLYGKARKLTPKDIEDIYWLGGTILGTSRKNPAKSQEELKTIIENVKKLRLDALITIGGDDTLGAAKKLYDMGIPVVGVPKTIDNDLPLTDYSIGFWTAIETIADALGKLHTTARSHKRVMIAEIMGRYAGWLTLMGGLAGGAHIILIPEKPVDIDEVCRIIKQRRERGEPYTLIAVAEGVMVPTTGEIVTASTEKDEFGHVRLGGVSKVLEEEIKKRTGEEVRSVVLGHIQRGGIPSAYDRVLGIRLGFKAVDLVKEQKFGYVVVVKGVDIIPVKIDEVVGTIRKVPSELHEFTDVFTGLTVNHKS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DSYR01000007
EMBL· GenBank· DDBJ
HGU02230.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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