A0A9D4X825 · A0A9D4X825_PEA

Function

function

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

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

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 site98ATP (UniProtKB | ChEBI)
Site188Important for substrate specificity; cannot use PPi as phosphoryl donor
Binding site215-217substrate
Active site217Proton acceptor
Binding site260-262substrate
Binding site316substrate
Binding site374-377substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentmembrane
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
      KIW84_058125

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Zhongwan 6
  • 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 > Fabeae > Pisum

Accessions

  • Primary accession
    A0A9D4X825

Proteomes

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane6-27Helical

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain92-398Phosphofructokinase

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    463
  • Mass (Da)
    51,435
  • Last updated
    2023-05-03 v1
  • Checksum
    26E8F5E08557D0C0
MFLTLYLRMFLTCLITSLIFLHILTHYKIILLMQLSMIKLVNSCFHRQYYVNQDDTVAQQIVVHKNSSRGTLFRRAGPAQKVYFDSKEVYACIVTCGGLCPGLNTVIRELVCGLYHMYGVHKVLGIEGGYRGFYSRNTIPLTPKIVNDIHKRGGTILKTSYGGHDTSKIVDSIQDRGINQVYILGGFGTQNEAAMIFEEIRRRGLKVAVVGIPKTIDNDIPVIDKSIGFDTAVEEAQRAINSAHVEAESAENGIGVVKLMGRCSGFIAMYATLASRDVDCCLIPESPFYLEGPGGVLEFIEKRLREQGHMVIVIAEGAGQELILPSDKSNKNRPDAASDDLFHDVGLWLSLKIKDHFARSKKMAINLKYIDPTYMIRAIPSNASDNVFCTLLAQSAVHGAMAGYTGFTVGPVNGRNCYIPFHLINEGQKRVVITDRMWARLLSSTHQPSFVNPLHITEEAKAE

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A9D4X5K1A0A9D4X5K1_PEAPFK460

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAMSHJ010000005
EMBL· GenBank· DDBJ
KAI5413866.1
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