A0A834REN8 · A0A834REN8_SARSC

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 site76ATP (UniProtKB | ChEBI)
Binding site139-140ATP (UniProtKB | ChEBI)
Binding site169-172ATP (UniProtKB | ChEBI)
Binding site170Mg2+ (UniProtKB | ChEBI); catalytic
Binding site215-217substrate; ligand shared between dimeric partners; in other chain
Active site217Proton acceptor
Binding site252substrate; ligand shared between dimeric partners
Binding site259-261substrate; ligand shared between dimeric partners; in other chain
Binding site315substrate; ligand shared between dimeric partners; in other chain
Binding site343substrate; ligand shared between dimeric partners
Binding site349-352substrate; ligand shared between dimeric partners; in other chain
Binding site523beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site581-585beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site619beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site626-628beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site682beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site708beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site714-717beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site799beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Component6-phosphofructokinase complex
Molecular Function6-phosphofructokinase activity
Molecular FunctionAMP binding
Molecular FunctionATP binding
Molecular Functionfructose-6-phosphate binding
Molecular Functionidentical protein binding
Molecular Functionmetal ion binding
Molecular Functionmonosaccharide binding
Biological Processcanonical glycolysis
Biological Processfructose 1,6-bisphosphate metabolic process
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

    • ORF names
      SSS_2198

Organism names

  • Taxonomic identifier
  • Strain
    • SSS_KF_BRIS2020
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Chelicerata > Arachnida > Acari > Acariformes > Sarcoptiformes > Astigmata > Psoroptidia > Sarcoptoidea > Sarcoptidae > Sarcoptinae > Sarcoptes

Accessions

  • Primary accession
    A0A834REN8

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-28Disordered
Region1-441N-terminal catalytic PFK domain 1
Domain69-374Phosphofructokinase
Domain454-740Phosphofructokinase
Region454-841C-terminal regulatory PFK domain 2

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    841
  • Mass (Da)
    91,997
  • Last updated
    2021-09-29 v1
  • Checksum
    6A1B3B61650553D8
MDSGGGGGGSNRSGSAAEIPPLPNKTPKMSAPVLQHLYRVRTMSTVDDHDAPVSTEGNIPEGVQKGKIIGVFTSGGDSQGMNAAVRAVVRMGLYLGCRVYFIKEGYQGMVDGGDHIIEASWVSVSGIIHKGGTVIGSARCKEFRTHEGRLKAAYNLIQYGITNLVVIGGDGSLTGANLFRQEWSSLVKELVDSGQITTKKAEAVEHLHIVGMVGSIDNDFCGTDMTIGTDSALHRIIEAIDAIVTTASSHQRTFILEVMGRHCGYLALVAALASEADYVFIPEWPPEANWPEKLCNKIEEERRHGKRLNIIIVAEGATDLEGNDIEAEHVKDVIVKNTGQDTRITVLGHVQRGGSPSAFDRILGSRMGAEAVLALLEATPESQACVVSLDGNLAVRVPLMQCVEKTKSVACAMGDKKWDNAVQLRGVSFKRNLETYRMLTKINPPKTIEHKGYRLAVMHCGAPCCGMNSAVRSFVRNIIFRGDTALAIHDGFDGFIEGDIRPITWTEVSGWVGQGGANLGTRRTLPDDKNIEQIVKQLKQFRIQGLLVIGGFEAFHSVLNLAERRNQFAELCIPMCVIPATISNNVPGTDFSLGTDTALNEITEICDRIRQSAQGTKRRVFVVETMGGYCGYLATLAGLAGGADAAYIFEEPFTINDLISDIRLMHAKMDEGVTRGLILRNEKANSNYTTDFLYKLYCEEGKDNFSTRMNVLGHMQQGAQPSPFDRNFGTKLAAKAADWLQQQLLDHVKPPASSANEEEYELVYNATSPDTAVLLGLIGRQYRFSPVQTLKSRADFKNRLGEHQWWLRLRPLLRALASPSNLPLSDVNKTVHHFVELLDKE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WVUK01000054
EMBL· GenBank· DDBJ
KAF7494122.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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