A0A641ARF4 · A0A641ARF4_9ACTN

  • 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.

TypeIDPosition(s)Description
Binding site10diphosphate (UniProtKB | ChEBI)
Binding site103Mg2+ (UniProtKB | ChEBI); catalytic
Site104Important 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
Site124Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi
Binding site125-127substrate; ligand shared between dimeric partners; in other chain
Active site127Proton acceptor
Binding site162substrate; ligand shared between dimeric partners
Binding site169-171substrate; ligand shared between dimeric partners; in other chain
Binding site221substrate; ligand shared between dimeric partners; in other chain
Binding site266substrate; ligand shared between dimeric partners
Binding site272-275substrate; ligand shared between dimeric partners; in other chain

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
      pfp
    • ORF names
      ESP62_010005

Organism names

  • Taxonomic identifier
  • Strain
    • NRBC 14897
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Propionibacteriales > Nocardioidaceae > Aeromicrobium

Accessions

  • Primary accession
    A0A641ARF4

Subcellular Location

Keywords

Interaction

Subunit

Homodimer or homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-297Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    342
  • Mass (Da)
    36,468
  • Last updated
    2020-04-22 v1
  • Checksum
    B1DCACDBA0250605
MRVGMLTGGGDCPGLNAVIRAAVRKGVQQYRHEFIGFRDGWRGPLEDDTMTLGVDEVRGILPRGGTILGSSRTNPFAIDDGVQRIKDNLDRNGCDALIAIGGEDTLGVATKLADLGVAVVGVPKTIDNDLSGTDFTFGFDTAVNIATEAIDRLHTTAESHHRVLVVEVMGRHAGWIALHSGLAGGANIILIPERPFDIEQVCAQVESRFATHYAPIIVVSEGAVPAEGGDMSLVSGQKDAFGHVRLGGIGDRLASEIEHRTGKEARAVVLGHVQRGGSPTAFDRWLATRFGLHAITAVHEGDFGTMMSLRGTEIARVPLADGTEKLKTVRADLYEEAEVFFG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SDPP02000002
EMBL· GenBank· DDBJ
KAA1378662.1
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