A0A6G0UH46 · A0A6G0UH46_9BILA

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 site57ATP (UniProtKB | ChEBI)
Binding site120-121ATP (UniProtKB | ChEBI)
Binding site150-153ATP (UniProtKB | ChEBI)
Binding site151Mg2+ (UniProtKB | ChEBI); catalytic
Binding site196-198substrate; ligand shared between dimeric partners; in other chain
Active site198Proton acceptor
Binding site233substrate; ligand shared between dimeric partners
Binding site240-242substrate; ligand shared between dimeric partners; in other chain
Binding site296substrate; ligand shared between dimeric partners; in other chain
Binding site324substrate; ligand shared between dimeric partners
Binding site330-333substrate; ligand shared between dimeric partners; in other chain
Binding site508beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site565-569beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site603beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site610-612beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site666beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site692beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site698-701beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site774beta-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
      FO519_008495

Organism names

  • Taxonomic identifier
  • Strain
    • NKZ332
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Tylenchina > Panagrolaimomorpha > Panagrolaimoidea > Panagrolaimidae > Halicephalobus

Accessions

  • Primary accession
    A0A6G0UH46

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-422N-terminal catalytic PFK domain 1
Domain50-355Phosphofructokinase
Domain439-723Phosphofructokinase
Region439-813C-terminal regulatory PFK domain 2

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    813
  • Mass (Da)
    89,770
  • Last updated
    2020-08-12 v1
  • Checksum
    2078D4CB6253C7E3
MADPPKEDELGPLREYPENARKVVRTDSIVPTVGREGSDIKRLIYKGRSMAVFTSGGDSQGMNAAIRSVVRMGLYVGCKVYLINEGYQGMVDGGENIWEADWNVVSDIIQKGGTIIGSARCKAFREREGRLKAAQNLLERSITNIVCIGGDGSLTGANTFRQEWPSLLQELVESGKITKEKAEQCSNIQIVGLVGSIDNDFCGTDMTIGTDTALQRIIDAIDAVVATAQSHQRAFVVEVMGRHCGYLGLVAALASEADFCFIPEWPPPTNWPEILCEKLTHTRSTGLRLNIIVVAEGAIDREGKPITSDMVKDVINKTLNYDTRVTVLGHVQRGGNPSAFDRLLGSRMGAEAVLALMEMTPESEPCVISIDGNQMVRVPLMECVHRTQAVQKAMDGKNWDIAVKLRGRSFQRNLDTYRLLTKLHTPQEKDNLSEGKNFNVAVMNVGAPAGGMNAAVRSFVRMGLYHHCTVYGIHNSFEGLAAGEVKKMEWGDVANWVMHGGSKLGTQKQLPLKQLSKIAEMLKHFKIHALLIIGGFEAYNSVLELSRHRTKYEAFRIPMCVIPCTISNNIPGTSHSLGCDTAVNEICHMIDKIKQSATGTKRRVFIIETMGGYCGYLATISALASGADNAYIFEENFTVDDIKEDVSVILSKMQKGVQRYLIVRCENANRHYTTTFVQQLFQEEGKGGFSTRINVLGHAQQGGNPTPFDRNMGTKLAARALEYLVTQAKEFVDPVNGVLGATETDTATLLGLRGRRVVFTPVEELAEETDFEHRLPLDQWWLKLRPLLRILAKHNSTYYTEAMDVPEVVGEMD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VOSG01000575
EMBL· GenBank· DDBJ
KAE9548297.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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