K7KRS4 · K7KRS4_SOYBN

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 site101ATP (UniProtKB | ChEBI)
Binding site164-165ATP (UniProtKB | ChEBI)
Binding site189-192ATP (UniProtKB | ChEBI)
Binding site190Mg2+ (UniProtKB | ChEBI); catalytic
Site191Important for substrate specificity; cannot use PPi as phosphoryl donor
Binding site218-220substrate
Active site220Proton acceptor
Binding site263-265substrate
Binding site319substrate
Binding site376-379substrate

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
      100795344
    • Synonyms
      PFK
    • ORF names
      GLYMA_05G224900

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Williams 82
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > indigoferoid/millettioid clade > Phaseoleae > Glycine > Glycine subgen. Soja

Accessions

  • Primary accession
    K7KRS4

Proteomes

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Proteomic databases

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain94-400Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    471
  • Mass (Da)
    51,838
  • Last updated
    2013-01-09 v1
  • Checksum
    DD37F2282016225E
MGSSPNSKPKIIRGTAGYVLEDVPHMADYIPDLPTYSNPLQNNPAYSVVKQYFVHIDDSVPQKIIANKDSPRGVHFRRAGPRQRVYFESDDVQAAIVTCGGLCPGLNTVIRELVCALYHMYGVKKILGINGGYKGFYAHNTITLTPKSVNDIHKRGGTILGSSRGGHDTTKIVDSIQDRGINQVYIIGGDGTQRGADRIFEEIRRRRLKVAVVGIPKTIDNDIPVIDKSFGFDTAVEEAQRAINAAHVEAESGENGIGVVKLMGRYSGFIAMYATLASRDVDCCLIPESPFHLEGPGGLFEFTEKRLKENGHMVIVIAEGAGQELVSESIQSLHKQDASGNKLLQDVGLWISQKIKDHFTKQKTMTINLKYIDPTYMIRAVPSNASDNVYCTLLAQSAVHGAMAGYTGFTSGLVNGRQTYIPFYRITEGQNKVIITDRMWARLLSSTNQPSFTIAKTVSEEKREEEANGHE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM000838
EMBL· GenBank· DDBJ
KRH60180.1
EMBL· GenBank· DDBJ
Genomic DNA
CM000838
EMBL· GenBank· DDBJ
KRH60181.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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