Q9ZST3 · Q9ZST3_CITPA

  • Protein
    Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta
  • Gene
    PPi-PFKb
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • 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 site104diphosphate (UniProtKB | ChEBI)
Binding site198Mg2+ (UniProtKB | ChEBI); catalytic
Site199Important 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
Site225Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi
Binding site226-228substrate
Active site228Proton acceptor
Binding site265-266substrate; ligand shared between dimeric partners
Binding site273-275substrate
Binding site334substrate
Binding site439-442substrate

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
      PPi-PFKb
    • Synonyms
      PFP-BETA

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Sapindales > Rutaceae > Aurantioideae > Citrus

Accessions

  • Primary accession
    Q9ZST3

Subcellular Location

Keywords

Interaction

Subunit

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

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain96-459Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    566
  • Mass (Da)
    61,696
  • Last updated
    1999-05-01 v1
  • Checksum
    AA21391701BCD2ED
MSPSLVANADLSPVTSGTVKGRVASVYSELQTSRIDHALPLPSVLKNPFKIVDGPASSAAGNPDEIAKLFPNLFGQPSALLVPNGADAVRSDEKLKIGVVLSGGQAPGGHNVISGIYDYLQDRAKGSVLYGFRGGPAGIMKCKYVELTSNYIYPYRNQGGFDMICSGRDKIETPEQFKQATETAVKLDLDGLVVIGGDDSNTNACLLAEHFRSKNLKTLVMGCPKTIDGDLKCKEVPASFGFDTACKIYAEMIGNVMIDARSTGKYYHFVRLMGRAASHITLECALQTHPNITIIGEEVAAKKQTLKNVTDYIVDIICKRAELGYNYGVILIPEGLIDFIPEVQQLIAELNEILAHEVVDEGGQWKKKLTKQSLQLFEFLPQAIQEQLMLERDPHGNVQVAKIETEKMLIQMVETELENRKQEGVNKGQFKGQSHFFGYEGRCGLPTNFDATYCYALGYGAGALLHSGKTGLISSVGNLAAPVEEWTVSGTALTALMDVERRHGKFKPVIKKAMVELDGTPFKKFVSMRDEWALNNRYISPGPIQFTGPTSGDVNHTLLLELGAQV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF095520
EMBL· GenBank· DDBJ
AAC67586.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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