A0A0A0KH95 · A0A0A0KH95_CUCSA

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

Function

function

Catalytic subunit of pyrophosphate--fructose 6-phosphate 1-phosphotransferase. 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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

Allosterically activated by fructose 2,6-bisphosphate.

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 site105diphosphate (UniProtKB | ChEBI)
Binding site199Mg2+ (UniProtKB | ChEBI); catalytic
Site200Important 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
Site226Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi
Binding site227-229substrate
Active site229Proton acceptor
Binding site266-267substrate; ligand shared between dimeric partners
Binding site274-276substrate
Binding site335substrate
Binding site440-443substrate

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
Biological Processphotosynthesis
Biological Processresponse to glucose

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta
  • EC number
  • Short names
    PFP
  • Alternative names
    • 6-phosphofructokinase, pyrophosphate dependent
    • PPi-PFK
    • Pyrophosphate-dependent 6-phosphofructose-1-kinase

Gene names

    • Name
      PFP-BETA
    • ORF names
      Csa_6G512900

Organism names

  • Taxonomic identifier
  • Strain
    • cv. 9930
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Cucurbitales > Cucurbitaceae > Benincaseae > Cucumis

Accessions

  • Primary accession
    A0A0A0KH95

Proteomes

Genome annotation databases

Subcellular Location

Keywords

Interaction

Subunit

Tetramer of two alpha (regulatory) and two beta (catalytic) chains.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain97-460Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    567
  • Mass (Da)
    61,952
  • Last updated
    2015-01-07 v1
  • MD5 Checksum
    A07688A05E48143977B717FCA256906A
MSISFISNGEAAVKSSSPPLSGRVSSVYSEVQSSRINHNLPLPSVLRSPFTIVDGPPSSAAGNPDEIAKLFPNLFGQPSAKLVPSDSNKGQPDKKLKIGVVLSGGQAPGGHNVISGIFDYLQDHAKGSVLYGFRGGPAGIMKCKYLELTSDYIYPYRNQGGFDMICSGRDKIETPEQFKQAEETAKKLDLDGLVVIGGDDSNTNACLLAENFRGKNLKTRVIGCPKTIDGDLKCKEVPTSFGFDTACRIYAEMIGNVMIDARSTGKYYHFVRLMGRAASHITLECALQTHPNITIIGEEVYAQKQTLKSVTDYIVDVVCKRAELGYNYGVILIPEGLIDFIPEVQQLIAELNEILAHDVVDDEGLWKKKLTSQSLELFEFLPQAIQEQLMLERDPHGNVQVARIETEKMLIQMVETELEKRKSEGAYKGQFKGQSHFFGYEGRCGLPTNFDSTYCYALGYGAGALLQSGKTGLISSVGNLAAPVEEWTVGGTALTSLMDVERRHGKFKPVIKKAMVELDGAPFKKFASLRDDWAFNNRYISPGPIQFVGPASNAVNHTLLLELGVEA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM002927
EMBL· GenBank· DDBJ
KGN49075.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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