L8HYJ7 · L8HYJ7_9CETA

  • Protein
    ATP-dependent 6-phosphofructokinase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

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.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site95ATP (UniProtKB | ChEBI)
Binding site158-159ATP (UniProtKB | ChEBI)
Binding site188-191ATP (UniProtKB | ChEBI)
Binding site189Mg2+ (UniProtKB | ChEBI); catalytic
Binding site234-236substrate; ligand shared between dimeric partners; in other chain
Active site236Proton acceptor
Binding site271substrate; ligand shared between dimeric partners
Binding site278-280substrate; ligand shared between dimeric partners; in other chain
Binding site334substrate; ligand shared between dimeric partners; in other chain
Binding site362substrate; ligand shared between dimeric partners
Binding site368-371substrate; ligand shared between dimeric partners; in other chain
Binding site541beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site598-602beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site636beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site643-645beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site699beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site725beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site731-734beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site805beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Component6-phosphofructokinase complex
Cellular Componentapical plasma membrane
Cellular Componentnucleus
Cellular Componentsperm principal piece
Molecular Function6-phosphofructokinase activity
Molecular FunctionATP binding
Molecular Functionfructose binding
Molecular Functionidentical protein binding
Molecular Functionkinase binding
Molecular Functionmetal ion binding
Biological Processcanonical glycolysis
Biological Processfructose 6-phosphate metabolic process
Biological Processglucose homeostasis
Biological Processglycogen catabolic process
Biological Processglycolysis from storage polysaccharide through glucose-1-phosphate
Biological Processmuscle cell cellular homeostasis
Biological Processpositive regulation of insulin secretion
Biological Processpositive regulation of transcription by RNA polymerase II

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

    • ORF names
      M91_21474

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • yakQH1
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    L8HYJ7

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Homo- and heterotetramers.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-460N-terminal catalytic PFK domain 1
Domain88-393Phosphofructokinase
Region472-850C-terminal regulatory PFK domain 2
Domain473-756Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    850
  • Mass (Da)
    93,427
  • Last updated
    2013-04-03 v1
  • Checksum
    337A26DF1D656827
MRKVELHLKFFMCVTQSRQLVRTPQRTAEEASTSSMLMQKPPSRTDVLKSLDTVDDPDTVEGIPIFANEWIMTHEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIYTGARVFFVHEGYQGLVDGGDNIREATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAHNLVKRGITNLCVIGGDGSLTGADTFRSEWSDLLSDLQKSGKITAEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDSALHRIIEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWEEHLCRRLSETRNRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTRAMDERRFDEALKLRGRSFMNNWEVYKLLAHVRPPKSKSGSHTVAVMNVGAPAAGMNAAVRSTVRIGLIQGNRMLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQYDELCIPFVVIPATVSNNVPGSDFSVGADTALNTICMTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEDPFTIRDLQVNVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLGHMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANSPDSGCVLGMRKRALVFQPVTELKEQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSEHAHLEHISRKRSGEANV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JH882468
EMBL· GenBank· DDBJ
ELR49260.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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