A0A026WQT5 · A0A026WQT5_OOCBI

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 site28ATP (UniProtKB | ChEBI)
Binding site91-92ATP (UniProtKB | ChEBI)
Binding site121-124ATP (UniProtKB | ChEBI)
Binding site122Mg2+ (UniProtKB | ChEBI); catalytic
Binding site167-169substrate; ligand shared between dimeric partners; in other chain
Active site169Proton acceptor
Binding site204substrate; ligand shared between dimeric partners
Binding site211-213substrate; ligand shared between dimeric partners; in other chain
Binding site267substrate; ligand shared between dimeric partners; in other chain
Binding site295substrate; ligand shared between dimeric partners
Binding site301-304substrate; ligand shared between dimeric partners; in other chain
Binding site478beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site536-540beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site574beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site581-583beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site637beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site663beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site669-672beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site744beta-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
      X777_01364

Organism names

Accessions

  • Primary accession
    A0A026WQT5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-393N-terminal catalytic PFK domain 1
Domain21-326Phosphofructokinase
Region409-789C-terminal regulatory PFK domain 2
Domain410-694Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    789
  • Mass (Da)
    87,181
  • Last updated
    2014-07-09 v1
  • Checksum
    024CA81433B48DBF
MAEETPAQKFIKPGSHKGKGIAVFTSGGDSQGMNAAVRAVVRMGIYLGCRVYFIREGYQGMVDGGKNIEEATWSSVSCIIHRGGTVIGSARCKEFRERAGRRKAAKNLVNLGITNLVVIGGDGSLTGANLFKEEWSELLKELTESGEITAEQSEKYKQLHIVGLVGSIDNDFCGTDMTIGTDSALHRIIESIDAIVSTAYSHQRTFIMEVMGRHCGYLAIVGALAAEADYIFIPECPPPIDWPEKLCRKLEQERLTGQRLNIIIVAEGAVDRNGDPITADKVHKVVVEKLQQDTRVTVLGHVQRGGNPSAFDRVLGCRMGAEAVMALMEATPDTEACVVTLDGNQAVRLPLMECVRRTKAVAEAMAVKNWDLAVQLRGKGFERNLETYKMLTRLKAPDLDHDANKDNYTLAVMHIGSPSCGMNAAVRSFVRNCIYRGDKVYGIGDGVLGLIAGRFKLMDWPSVTGWVAEGGAKLGTKRAPPQEDQLPLIAQKLKEFEIQALLIIGGFEGYQTGLTFFKARDKYEEFRIPIAMIPATISNNVPGTEFSLGCDTALNEISEICDRIRQSAQGTKRRVFIIETMGGFCGYLATVAGLAGGADAAYIYEEKFNIKDLNQDVIAMAAKMSEGVERGLIIRNESANENYNTEFMYRLFSEEGKGLFSCRRNILGHMQQGGSPTPFDRNLGTKMGSKAVEWFSDQLRKCTSPDGKTVTTAADSAVMLGIIRRQYRYTPFTELIEVTDFEHRIPTYQWWMKLRPLLKVLAKHESTYEEEGLYITIEEMDEQKDPPLV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KK107128
EMBL· GenBank· DDBJ
EZA58407.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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