A0A6A4PKU8 · A0A6A4PKU8_LUPAL

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.
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

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.

TypeIDPosition(s)Description
Binding site108diphosphate (UniProtKB | ChEBI)
Binding site202Mg2+ (UniProtKB | ChEBI); catalytic
Site203Important 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
Site229Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi
Binding site230-232substrate
Active site232Proton acceptor
Binding site269-270substrate; ligand shared between dimeric partners
Binding site277-279substrate
Binding site338substrate
Binding site443-446substrate

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 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
      Lalb_Chr12g0196021

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Amiga
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > genistoids sensu lato > core genistoids > Genisteae > Lupinus

Accessions

  • Primary accession
    A0A6A4PKU8

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

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

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-21Disordered
Domain100-465Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    570
  • Mass (Da)
    62,964
  • Last updated
    2020-06-17 v1
  • Checksum
    93C5E20639968082
MPQRQQKKLKMAPSFPTNGGFTGVRMDPPSALYSEVQKSRIDHCIPLPSVLKNPFKMVDVHQISSAANSDEIAKLFPHLFGQPSVTLMPIETDTVQPSLKIGVVLSGGQAPGGHNVIAGIFDYMQDLAKGSILYGFRGGPAGIMNCKYLELTSHYIYPYRNQGGFDIIRSGRDKIETPDQFKQAEETVQKLDLDGLVVIGGDDSNTNACLLAEYFRSKNIKTHVIGCPKTIDGDLKCKEVPTSFGFDTACKIYAEMIGNVMIDARSTGKYYHFVRLMGRAASHITLECALQTHPNITIIGEEVAAKKLTLKNVTDYIVDIICKRAEVNYRYGVILIPEGLIDFIPEAQHLIVELNEIMASCSVDEGGLWKKKLTDQSLKLFEFLPQAIKEQLMLERDPHGNVQVAKIETEKMLIQMVETELEKRKHEGTYQAVFRGQSHFFGYEGRCGLPTNFDSTYCYALGYGAGALVQSGKTGLISSVGNLCAPVEEWTVGGTDLTSLMDLERRHGKFKPVIKKAMVELEGAPFKEFASLRDEWALKNHYISPGPIQFTGPGSDAISYTLGLELGTQA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WOCE01000012
EMBL· GenBank· DDBJ
KAE9602102.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp