A0A0J9RAE5 · A0A0J9RAE5_DROSI

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.

Type
IDPosition(s)Description
Binding site189ATP (UniProtKB | ChEBI)
Binding site252-253ATP (UniProtKB | ChEBI)
Binding site282-285ATP (UniProtKB | ChEBI)
Binding site283Mg2+ (UniProtKB | ChEBI); catalytic
Binding site328-330substrate; ligand shared between dimeric partners; in other chain
Active site330Proton acceptor
Binding site365substrate; ligand shared between dimeric partners
Binding site372-374substrate; ligand shared between dimeric partners; in other chain
Binding site428substrate; ligand shared between dimeric partners; in other chain
Binding site456substrate; ligand shared between dimeric partners
Binding site462-465substrate; ligand shared between dimeric partners; in other chain
Binding site642beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site699-703beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site737beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site744-746beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site800beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site826beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site832-835beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site907beta-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

    • Name
      Dsim\GD10715
    • ORF names
      Dsimw501_GD10715

Organism names

  • Taxonomic identifier
  • Strain
    • W501
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    A0A0J9RAE5

Proteomes

Subcellular Location

Keywords

Expression

Gene expression databases

    • FBgn0182479Expressed in adult organism and 3 other cell types or tissues

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-554N-terminal catalytic PFK domain 1
Compositional bias92-114Basic and acidic residues
Region92-120Disordered
Domain182-486Phosphofructokinase
Domain573-858Phosphofructokinase
Region573-950C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    950
  • Mass (Da)
    105,268
  • Last updated
    2015-10-14 v1
  • Checksum
    119E60DBDAD952A5
MHSIKFRVFTKLKPLFLEINGRIPKCRHFHGPSTFRLEISNKTPPIRQKLTFPNIGIQCTRSLHLCCPRDISGSTLLSVKFNCKRHVIKLRSDSGDKKNDSPGDKNKKNDKSAQRCGKPINNLHSGFLNAENYSEKNVMKKKKRAPKKKCGKTVDELRKCLRTMQDVIDFVHPVKPFKDKGLAVFTSGGDSQGMNAAVRACVRMAIYLGCKVYFIREGYQGMVDGGDCIQEANWASVSSIIHRGGTIIGSARCQDFRERQGRLKAANNLIQRGITNLVVIGGDGSLTGANLFRQEWSSLLDELVKNKTITTEQQEKFNVLHIVGLVGSIDNDFCGTDMTIGTDTALHRIIEAIDAISSTAYSHQRTFIMEVMGRHCGYLALVGGLACEADFIFIPEMPPKVDWPDRLCSQLAQERSAGQRLNIVIVAEGAMDREGHPITAEDVKKVIDERLKHDARITVLGHVQRGGNPSAFDRILACRMGAEATLALMEATKDSVPVVISLDGNQAVRVPLMECVERTQAVAKAMAEKRWADAVKLRGRSFERNLETYKMLTRLKPPKENFDADGKGIEGYRLAVMHIGAPACGMNAAVRSFVRNAIYRGDVVYGINDGVEGLIAGNVRELGWSDVSGWVGQGGAYLGTKRTLPEGKFKEIAARLKEFKIQGLLIIGGFESYHAAGQIADQRDNYPQFCIPIVVIPSTISNNVPGTEFSLGCDTGLNEITEICDRIRQSAQGTKRRVFVIETMGGYCGYLATLAGLAGGADAAYIYEEKFSIKDLQQDVYHMASKMAEGVSRGLILRNEKASENYSTDFIYRLYSEEGKGLFTCRMNILGHMQQGGSPTPFDRNMGTKMAAKCVDWLATQIKANIDANGVVNCKSPDTATLLGIVSRQYRFSPLVDLIAETNFDQRIPKKQWWLRLRPLLRILAKHDSAYEEEGMYITVEEECDTDAVA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias92-114Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM002911
EMBL· GenBank· DDBJ
KMY92684.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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