A0A922HPI9 · A0A922HPI9_DERFA

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 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 site62ATP (UniProtKB | ChEBI)
Binding site125-126ATP (UniProtKB | ChEBI)
Binding site155-158ATP (UniProtKB | ChEBI)
Binding site156Mg2+ (UniProtKB | ChEBI); catalytic
Binding site201-203substrate; ligand shared between dimeric partners; in other chain
Active site203Proton acceptor
Binding site238substrate; ligand shared between dimeric partners
Binding site245-247substrate; ligand shared between dimeric partners; in other chain
Binding site301substrate; ligand shared between dimeric partners; in other chain
Binding site329substrate; ligand shared between dimeric partners
Binding site335-338substrate; ligand shared between dimeric partners; in other chain
Binding site509beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site567-571beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site605beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site612-614beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site668beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site694beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site700-703beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site781beta-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
      DERF_013443

Organism names

  • Taxonomic identifier
  • Strain
    • Derf
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Chelicerata > Arachnida > Acari > Acariformes > Sarcoptiformes > Astigmata > Psoroptidia > Analgoidea > Pyroglyphidae > Dermatophagoidinae > Dermatophagoides

Accessions

  • Primary accession
    A0A922HPI9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-427N-terminal catalytic PFK domain 1
Domain55-360Phosphofructokinase
Domain440-726Phosphofructokinase
Region440-876C-terminal regulatory PFK domain 2

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    876
  • Mass (Da)
    97,846
  • Last updated
    2023-02-22 v1
  • Checksum
    B84D72A07899B43D
MEVEDVLPPLRSPSMQAPQLQHLYRLRTMSTIDERDFPISTEGNIPESVQKGKIIGVFTSGGDSQGMNAAVRAVVRMGLYLGCRVYFIKEGYQGMVDGGDHIIEASWVSVSGIIHKGGTVIGSARCAEFRERQGRLKAAYNLIQYEITNLVVIGGDGSLTGANLFRQEWQSLVEELVNTGKITPQKASTVEHLHIVGMVGSIDNDFCGTDMTIGTDSALHRIIESIDAIVTTASSHQRTFILEVMGRHCGYLALVAALASEADFVFIPEWPPEADWSQRLCRKIEQERRLGKRLSIVIVAEGAIDMNGNPIQAETVKDVIVKNTGQDTRITVLGHVQRGGSPSAFDRVLGSRMGAEAVLALLEATPESQACVVSLDGNQAVRVPLMQCVERTKSVATAMKNKQWEEAVKLRGISFKRNLETYRMLTKHDPPKTIDHKGFRLAVMNCGAPCCGMNSAVRSFVRNVIFRGDTVLSIHDGFDGLIDGDIRPITWSEVRGWVGQGGANLGTRRTLPDDQNIEKIIANLRLYRVQALLVIGGFEAFQSVLYLAERRHQYVELRMPMCCVPATISNNVPGTDFSLGADTALNEITEICDRIRQSAQGTKRRVFIIETMGGFCGYLATLAGLAGGADAAYIFEEPFSINDLIGDIRLMHVKMEEGVTRGLVLRNEKANSNYTTDFMFKLYSEEGKDNFSTRMNILGHMQQGASPSPFDRNFGTKLAAKAAEWLTRQLEHHSRPLTEDYNELVYNSTSPDTAVLLGLIGRQYRFTPVQTLKTQTDFKNRLGKVQWWIRLRPLLRALASPEQLELKDVDNHISCSSIYNKYILKQLYRHRIPYSHWYKKLRPLLRILAHHEDIYQPEVIQVQEMDDIFNDDVFDA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ASGP02000007
EMBL· GenBank· DDBJ
KAH9497450.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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