G7LJ94 · G7LJ94_MEDTR

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.

Type
IDPosition(s)Description
Binding site181ATP (UniProtKB | ChEBI)
Binding site245-246ATP (UniProtKB | ChEBI)
Binding site270-273ATP (UniProtKB | ChEBI)
Binding site271Mg2+ (UniProtKB | ChEBI); catalytic
Site272Important for substrate specificity; cannot use PPi as phosphoryl donor
Binding site299-301substrate
Active site301Proton acceptor
Binding site344-346substrate
Binding site400substrate
Binding site452-455substrate

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
      11423706
    • Synonyms
      PFK
    • ORF names
      MtrunA17_Chr8g0367681
    • Ordered locus names
      MTR_8g069040

Organism names

  • Taxonomic identifier
  • Strains
    • A17
    • cv. Jemalong A17
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > Hologalegina > IRL clade > Trifolieae > Medicago

Accessions

  • Primary accession
    G7LJ94

Proteomes

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Proteomic databases

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain174-476Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    529
  • Mass (Da)
    58,138
  • Last updated
    2012-01-25 v1
  • Checksum
    A3419391CD3C4DF8
MASISHAITTTTNPYFNLPHQTQTPSSILTLSHSNSRRVFKNVGVFAEHRNSSSTSIDFNDPDWKFKFQQDFESRFRLPHITDIFPDSPPIPSTFCLRMRTPIGKDIPGHYTLDEEWNGYINNNDRVLLKTINYSSPKSAGAECIDPDCTWVEQWVHRAGPREKIYYKPEDVKAAIVTCGGLCPGLNDVIRQIVITLEIYGVKKIVGIPFGYRGFSDKELTEVPLSRKVVQNIHLSGGSLLGVSRGGPGVSDIVDSLEDRGINMLFVLGGNGTHAGANAIHNECCKRRLKVSVIGVPKTIDNDILLMDKTFGFDTAVEEAQRAINSAYIEAHSAYHGIGVVKLMGRSSGFIAMQASLSSGQVDICLIPEVPFNLHGPHGVLRHLQYLLEMKGSAVVCVAEGAGQNLLQNTNAKDASGNIVFGDIGVYIQQETKKYFKEIGVHADVKYIDPTYMIRACRANASDGILCTVLGQNAVHGAFAGYSGISVGICNTHYAYFPIPEVISHPRLVDPNSRMWHRCLTSTGQPDFI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM001224
EMBL· GenBank· DDBJ
AET03390.1
EMBL· GenBank· DDBJ
Genomic DNA
PSQE01000008
EMBL· GenBank· DDBJ
RHN41591.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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