Q3SIS0 · Q3SIS0_THIDA

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.

Type
IDPosition(s)Description
Binding site14diphosphate (UniProtKB | ChEBI)
Site116Important 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
Site142Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi
Binding site143-145substrate
Active site145Proton acceptor
Binding site191-193substrate
Binding site246substrate
Binding site296-299substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function6-phosphofructokinase activity
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
    • Ordered locus names
      Tbd_1502

Organism names

Accessions

  • Primary accession
    Q3SIS0

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain10-322Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    418
  • Mass (Da)
    45,607
  • Last updated
    2005-10-11 v1
  • MD5 Checksum
    DB368160F3AC7461F58553DAC0732034
MAKKMNAFYAQSGGVTAVINASACGVIETARKNKDKIGKVYAGRNGIIGALTEDLIDTSKESDAAIAALRSTPSGAFGSCRFKLKSLEANKREYERLIEVFKAHNIGYFFYNGGGDSADTCFKVSQLSEAMGYPIQAIHVPKTVDNDLPITDCCPGFGSVAKYIAVSTLEASYDVRSMAKTSTKVFVIEVMGRHAGWIAAAGGLVEDHGIPVVILFPEIEFDQKKFLALVDKKVKEFGFCTVVVSEGCHYPDGKFLAEQGTRDAFGHAQLGGAAPVVANMIKDALGHKFHWAVADYLQRAARHIASKTDVKQAYELGKKAVELAIRGHNSVMPTVDRLSDKPYKYKIGVADLKDVANVEKFMPRDFITKDGFGITDKCKRYLTPLIQGEDYPKYKDGLPVYVTLKNVAVAKKLAEFKL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000116
EMBL· GenBank· DDBJ
AAZ97455.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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