C5YAA9 · C5YAA9_SORBI

Function

function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

Allosterically activated by AMP.

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 site125ATP (UniProtKB | ChEBI)
Binding site190-191ATP (UniProtKB | ChEBI)
Binding site215-218ATP (UniProtKB | ChEBI)
Binding site216Mg2+ (UniProtKB | ChEBI); catalytic
Site217Important for substrate specificity; cannot use PPi as phosphoryl donor
Binding site244-246substrate
Active site246Proton acceptor
Binding site289-291substrate
Binding site345substrate
Binding site403-406substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function6-phosphofructokinase activity
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Biological Processfructose 6-phosphate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent 6-phosphofructokinase
  • EC number
  • Short names
    ATP-PFK
    ; Phosphofructokinase
  • Alternative names
    • Phosphohexokinase

Gene names

    • Name
      PFK
    • ORF names
      SORBI_3006G114700

Organism names

  • Taxonomic identifier
  • Strain
    • cv. BTx623
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Panicoideae > Andropogonodae > Andropogoneae > Sorghinae > Sorghum

Accessions

  • Primary accession
    C5YAA9

Proteomes

Genome annotation databases

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-33Disordered
Compositional bias14-32Polar residues
Domain118-427Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    484
  • Mass (Da)
    51,972
  • Last updated
    2009-09-01 v1
  • Checksum
    078F61B4B948AC1F
MDPTAARSSGGTPAAAENDATAPTNTTVTLPPLTLRDVPRLPSALASAASPSPTPAVQNPISRHPYFHPPATFYISPGDVTLRHAFFDLASAAPSPLVAYRRAGPRGEIAVDPAAARAALVTCGGLCPGLNTVLRELVVGLHELYGVRHVFGVAAGYRGFYGTDEDHVRLDPAAVDDWHKKGGTVLKTTRGGFDLGKIVDGIVARGYTQIYAIGGDGTMRGAVAIFQEFKRRGLNISITGIPKTVDNDIGIIDRSFGFQTAVEIAQQAIDAAHVEAVSAVNGVGLVKLMGRSTGHIALHATLSSRDVDCCLIPEVDFHLEGKGGLFEFLYERIKKKGHAVIVVAEGAGQELIPRTDDQKREQDESGNIVFLDVGPWLKSELGRWWKREHPDELFTVKYIDPTYMIRAVPANATDNLYCTLLAHSAIHGVMAGFTGFVPGPVNGTYSYIPLEDVAVAKNPVDVNDHKWAWVRSVTNQPDFLKSQA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias14-32Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM000765
EMBL· GenBank· DDBJ
EES12338.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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