A0A517W625 · A0A517W625_9PLAN

  • 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.

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.

Type
IDPosition(s)Description
Binding site10diphosphate (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
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 site268substrate; ligand shared between dimeric partners
Binding site274-277substrate; 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
      HG66A1_03710
      , V6x_03650

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • HG66A1
    • V6
  • Taxonomic lineage
    Bacteria > Planctomycetota > Planctomycetia > Planctomycetales > Planctomycetaceae > Gimesia

Accessions

  • Primary accession
    A0A517W625
  • Secondary accessions
    • A0A517PGV4
    • A0A5A8BD04

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer or homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-297Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    344
  • Mass (Da)
    37,277
  • Last updated
    2019-10-16 v1
  • Checksum
    C3DC59EB684F288A
MRVGILTGGGDCPGLNPVIRGAVRVICNAGGEVYGLLEGWRGAIEGNYIELNSENTDDIIFKGGTILGSSRTNPYKNEAEDVPKVRETFERLGLDCLIAIGGDDTLGVANKLWNDYKLPVIGCPKTIDNDLSSTDVTFGFDTSINIVMEAVDRLRTTAESHRRIMVVETMGRHAGWIALFSGLATAADYTLVPEVPIEMDRMVDVLKKRRANGKMYGIIIVSEGAQFNEEEGVVTQDGEVDDFGHVKLGGIGETVAKMIEDRTGFETRHVTLGHLQRGGSPSAADRVLGTRCGVHAGWLALKHHFGYMVALRGTSIVPVALADAVGEMRALEKNFLEEAEVFLQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP036266
EMBL· GenBank· DDBJ
QDT18610.1
EMBL· GenBank· DDBJ
Genomic DNA
CP036347
EMBL· GenBank· DDBJ
QDU00690.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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