A0A1D1VWQ7 · A0A1D1VWQ7_RAMVA

Function

function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.

Caution

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 site67ATP (UniProtKB | ChEBI)
Binding site130-131ATP (UniProtKB | ChEBI)
Binding site160-163ATP (UniProtKB | ChEBI)
Binding site161Mg2+ (UniProtKB | ChEBI); catalytic
Binding site206-208substrate; ligand shared between dimeric partners; in other chain
Active site208Proton acceptor
Binding site243substrate; ligand shared between dimeric partners
Binding site250-252substrate; ligand shared between dimeric partners; in other chain
Binding site306substrate; ligand shared between dimeric partners; in other chain
Binding site334substrate; ligand shared between dimeric partners
Binding site340-343substrate; ligand shared between dimeric partners; in other chain
Binding site516beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site573-577beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site611beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site618-620beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site674beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site700beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site706-709beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site775beta-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
      RvY_15952-1
    • Synonyms
      RvY_15952.1
    • ORF names
      RvY_15952

Organism names

Accessions

  • Primary accession
    A0A1D1VWQ7

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-432N-terminal catalytic PFK domain 1
Domain60-365Phosphofructokinase
Region433-446Interdomain linker
Region447-819C-terminal regulatory PFK domain 2
Domain448-731Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    819
  • Mass (Da)
    89,872
  • Last updated
    2016-11-30 v1
  • Checksum
    6FEB5866DA21FE35
MATGEDMEAQEMRKMKSLERFERRESVTTDPAPKIVALRGGIESDALRLMKPSTWLGKAVGVYCSGGDSQGMNAAVRGVVRMALYVGAKVFFIHEGYVGMVEGGKLIQEATWESVSGIIQKGGTIIGSARCAEFRQRAGRLNAAYNLVSRGICNIVCIGGDGSLTGANLFRQEWQSLLQELVDNARITPEQQEKYNFLNIVGLVGSIDNDFCGTDMTIGTDSALHRIVECIDAITTTAQSHQRTFVLEVMGRHCGYLALVGALACEADWVFIPEWPPEENWPESMCKKLAQEREMGHRLNIVIVSEGAIDRTGKPITSEQVKNVIVDRLKQDCRITVLGHVQRGGNASAFDRVLGTRMGAEAVFALMDATPETEACVISIDGNQAVRTNLMQCVERTQMVAKAMADKNWDLAVKLRGRSFVRNLTTYKMLTKLKAPEKPGAKDKQRNLAVMCIGAPCGGINAATRSFVRNSQYHGYRTFAVYDGIEGLAAGSIKELTWMDVSGWNGEGGALLGIKRTLAGDYLPACAESLKKFEIEGLVIIGGFEAYHSALQFAEGRKNYPDLRIPIIVVPATISNNVPGTDFCLGADTAINEICEICDRLKQSAIGTRRRVFVIETMGGYCGYLATMAGIAAGADAAYIFEEQVSIDDLRNDVRHLTAKMATNVQRGLIIRNEFAHANYSLDFVRRMYAEEGKDIFSCREAVLGHVQQGGRPTPFDRNLGTKLAARAIEYMDEMITKGNLGNEPTSCALLGMIKRQVNLTPVQALATQTDFLHRIPRTQWWMILRPLLRIMAKHASVYVSEIEDATDDPDAGTRSVLG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BDGG01000012
EMBL· GenBank· DDBJ
GAV05892.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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