A0A133XTR5 · A0A133XTR5_9BACT

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 site103diphosphate (UniProtKB | ChEBI)
Binding site197Mg2+ (UniProtKB | ChEBI); catalytic
Site198Important 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
Site224Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi
Binding site225-227substrate; ligand shared between dimeric partners; in other chain
Active site227Proton acceptor
Binding site264-265substrate; ligand shared between dimeric partners
Binding site272-274substrate; ligand shared between dimeric partners; in other chain
Binding site333substrate; ligand shared between dimeric partners; in other chain
Binding site463-466substrate; ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Componentcytosol
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
Biological Processresponse to glucose

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
      HMPREF1869_01240

Organism names

Accessions

  • Primary accession
    A0A133XTR5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain96-356Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    599
  • Mass (Da)
    66,930
  • Last updated
    2016-06-08 v1
  • Checksum
    259DAA2774B1F9A4
MTYIRLDKLRQQYKPQMPATFKVGYELMETPFDYPEDDYEMVKARFPHTFGLPLLTFKMLEESHLSDPTIYFDPSLRSGAKGTRQTLFQSERPLHVGVLFSGGQAPGGHNVVAGIYDALKRHSAQSRLYGFLMGPGGLLRGEYKELTGELIQQYRNSGGFDMIGSDRTKLEKQEDLQKVLQVAHDLALNALVIIGGDDSNTNANLLAEYALSIGDPLQVIGCPKTIDGDLKNEYVETSFGFDTCVKVYAELVGNIQRDCFSAKKYYHFIKLMGRSASHLTLECALMCQPTMAIISEEVKARKITLSLLIGQIADVIQERSAKGLTFGTILIPEGLIEFLPGVKELIQELNRIPLETTAPIREEIAKASHQQEHEAKTACDDDRHRVQEIASRLSRENSELFLMLPMDIALSLATERDPHGNVQVSRIPTEQLLADMVKAELEKRRSEGLYEGSFSVLTHFFGYEGRSSMPSNFDASYCYSLGLCATELIVQGKTAYLATLRNLIAHPTDWVPTGLPLTAMMDFEERGGEIKPVIGKAVVDLKGAPMRYFRHHRKEWASGVAFRYPGPLQFFGPSAICDNTTITLRLEQGLSAYENSEPF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LSCS01000080
EMBL· GenBank· DDBJ
KXB34323.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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