Q95V79 · Q95V79_9EUKA

  • Protein
    Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
  • Gene
    pp-pfk
  • 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.

TypeIDPosition(s)Description
Binding site78diphosphate (UniProtKB | ChEBI)
Binding site172Mg2+ (UniProtKB | ChEBI); catalytic
Site173Important 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
Site199Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi
Binding site200-202substrate
Active site202Proton acceptor
Binding site240-241substrate; ligand shared between dimeric partners
Binding site248-250substrate
Binding site309substrate
Binding site412-415substrate

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

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
      pp-pfk
    • ORF names
      HINF_LOCUS21208
      , HINF_LOCUS59309

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metamonada > Diplomonadida > Hexamitidae > Hexamitinae > Hexamita

Accessions

  • Primary accession
    Q95V79

Subcellular Location

Keywords

Interaction

Subunit

Homodimer or monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain71-434Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    545
  • Mass (Da)
    59,904
  • Last updated
    2001-12-01 v1
  • Checksum
    FBFA250B14E4A2C3
MSTFELYRRQYNPLLPASLQGTGYTLKKGEPMAPVADGEEIAKQFPMTTNLPAISIEPSTEQSKLLEPLTIGVIFSGGQAPGGHNVLCGLYDKLQQLAPNSKLLGFLGGPKGLMDNKHMILTKEYLATFRNMGGFHAIGSGRDKIASTKDFDAAANTAAVEKLDGLVIIGGDDSNTNACLLAEDFIKRGLKTRVIGVPKTIDRDLISKRGIETSFGFDTSCKVYSELIGNLCYDALSAKKYWHFIRLMGRSASHITLECGLQTHPNICLIGEEILAKNMTSKQVFEYMADIIAQRAANGKNYGICLIPEGLIEFIPENNKLFDYLNNKLLPGWQGEITAELVAQKLPADLKVTFESIPPTIRTQLLLDRDPHGNIAISQIETEKFLVSGVQQVIKERELKIKFSALYHFFGYEGRCAAPSAFDSSYCYGLGSVAAVLLGNGITGYMSCLKNLSEQPDKWIAGAIPLTSLMNIEMRHGARTAVIQKQMVDLAGRPFGFLVVNREKWAEQDCYQQPGPIQLIECQDVEGRNVVYQSSVTLLEEARGL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF422165
EMBL· GenBank· DDBJ
AAL16943.1
EMBL· GenBank· DDBJ
Genomic DNA
CATOUU010000543
EMBL· GenBank· DDBJ
CAI9933563.1
EMBL· GenBank· DDBJ
Genomic DNA
CATOUU010001095
EMBL· GenBank· DDBJ
CAI9971664.1
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