A0A1W0X131 · A0A1W0X131_HYPEX

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.

Type
IDPosition(s)Description
Binding site65ATP (UniProtKB | ChEBI)
Binding site128-129ATP (UniProtKB | ChEBI)
Binding site158-161ATP (UniProtKB | ChEBI)
Binding site159Mg2+ (UniProtKB | ChEBI); catalytic
Binding site204-206substrate; ligand shared between dimeric partners; in other chain
Active site206Proton acceptor
Binding site241substrate; ligand shared between dimeric partners
Binding site248-250substrate; ligand shared between dimeric partners; in other chain
Binding site304substrate; ligand shared between dimeric partners; in other chain
Binding site332substrate; ligand shared between dimeric partners
Binding site338-341substrate; ligand shared between dimeric partners; in other chain
Binding site512beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site569-573beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site607beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site614-616beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site670beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site696beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site702-705beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site771beta-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
      BV898_04921

Organism names

Accessions

  • Primary accession
    A0A1W0X131

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-430N-terminal catalytic PFK domain 1
Domain58-363Phosphofructokinase
Region443-812C-terminal regulatory PFK domain 2
Domain444-727Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    812
  • Mass (Da)
    88,813
  • Last updated
    2017-06-07 v1
  • Checksum
    E6DDBA1D7582D9CB
MGEHVGGNEAQRMKSLERFERRDSISTDPAPRIKNVKGGIETDALRMMKPNSWNGKAIGVFCSGGDSQGMNAAVRGVVRMGLYCGCKVYFIHEGYVGMVEGGKLIQEASWEAVSGIIQKGGTIIGSARCAEFRQRPGRVAAAYNLVIRGISNIVCIGGDGSLTGANLFRAEWASLLQELVDSLKITPEQQEQFKHLNIVGLVGSIDNDFCGTDMTIGTDSALHRIVECIDAITTTAQSHQRTFVLEVMGRHCGYLALVASLACEADWVFIPEWPPEENWPEQMCKKLAQEREMGHRLNIVIVSEGAIDRTGKPITSEQVKNVIVDRLKQDCRITVLGHVQRGGNASAFDRILGTRMGAEAVFALMDATPETEACVMSIDGNQAVRTQLTQCVDRTQMVAKAMADKNWELAVKLRGRSFVRNLTTYKMLTKLKAPVKPDNKNFNLAVMCIGAPCGGINAAVRSFVRNGQYKGYKTFAIYDGIEGLAAGNVKEITWTDVNGWNGEGGALLGIKRTLAGDYLSALAENIKKFQLAGLVIIGGFEAYHSVLQLAEARKTFPEFHIPIIVVPATISNNVPGTDFCLGADTALNEICEICDRLKQSAIGTRRRVFVIETMGGYCGYLATLAGMAAGADAAYIFEEPVDIDGLRNDVLHLTAKMSTNVQRGLIIRNENAHSNYSLDFIRRLYAEEGKDVFSCREAILGHVQQGGRPTPFDRNLGTKLAARAIEFMDDMLSKGGLGNEPTSCGLLGITKRQVNLTPVQALAVQTDFLHRVPRTQWWLNLRPLLRIMAKHDSVYRSDAENIDAAAQKAEIL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MTYJ01000025
EMBL· GenBank· DDBJ
OQV21160.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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