Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A496Y1E8 · A0A496Y1E8_UNCDE

  • 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.
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

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 site99diphosphate (UniProtKB | ChEBI)
Binding site193Mg2+ (UniProtKB | ChEBI); catalytic
Site194Important 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
Site218Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi
Binding site219-221substrate; ligand shared between dimeric partners; in other chain
Active site221Proton acceptor
Binding site259-260substrate; ligand shared between dimeric partners
Binding site267-269substrate; ligand shared between dimeric partners; in other chain
Binding site328substrate; ligand shared between dimeric partners; in other chain
Binding site449-452substrate; ligand shared between dimeric partners; in other chain

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 Processresponse to glucose

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
      DRG58_07320

Organism names

Accessions

  • Primary accession
    A0A496Y1E8

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain91-332Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    575
  • Mass (Da)
    63,848
  • Last updated
    2019-06-05 v1
  • MD5 Checksum
    D83A5DAE0A53B542F0FB61B82C4CA07A
MTAEPKPQTYYSQAAIAQLLSSESPIKVERRSYQPCLCERLQSGPGGTRPLTGFELEVLRSAQEQLPLVSQNKLLEIVPGQPQSRLQQPCRLGIVLSGGPAPGGHNVIAGVFEAAKQAHPDNRLIGFLAGPKGIITNKHAEIAGEMVAHYKNSGGFHMLGTGRDKIDTPEKMEQCRQTCAELQLSGLIIVGGDDSNTNAAFLAENLHDLGTRVIGIPKTIDGDLQVPGLCQIPFGYHSACMAFATEVGNLNSDCKSDLKYWHFNRLMGRSASHIALEVAFQTHPNVILIGEEIEEKELTIHEVVRLIADIIVERAKIGKNYGTILIPEGILEFIHEINCLIIKISYIIAAYNREAAEEESFHKLPFEDQVQLIDNSDIWRDYDSRIFLGLPPRLQTGLLLPRDAHGNFQYALVNTERILLDMVATYLRKQRARGIYKGNFRTQNHYYGYDGRGTFPTKFDCDYAYNLGHTAFSLLANGATGYMAALKDLHKPITEWQPIGIPLAPLMHLEERKGRLELVIQKQKVDLESPAFQILAQERQKWALEDDYRFPGPIQFSGAGAEAKPITMMLNALGG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QMLD01000049
EMBL· GenBank· DDBJ
RLA88669.1
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.
Help