A0A232EP66 · A0A232EP66_9HYME

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 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 site300substrate; ligand shared between dimeric partners; in other chain
Binding site328substrate; ligand shared between dimeric partners
Binding site334-337substrate; ligand shared between dimeric partners; in other chain
Binding site519beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site577-581beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site615beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site622-624beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site678beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site704beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site710-713beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site785beta-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
      TSAR_005227

Organism names

  • Taxonomic identifier
  • Strain
    • Alberta
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Hymenoptera > Apocrita > Proctotrupomorpha > Chalcidoidea > Pteromalidae > Pteromalinae > Trichomalopsis

Accessions

  • Primary accession
    A0A232EP66

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-426N-terminal catalytic PFK domain 1
Domain21-241Phosphofructokinase
Domain250-359Phosphofructokinase
Region450-830C-terminal regulatory PFK domain 2
Domain451-735Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    830
  • Mass (Da)
    91,722
  • Last updated
    2017-10-25 v1
  • Checksum
    2BE5EC4519C26EDA
MDEEQVAHRFIKPGSHRGKGLAVFTSGGDSQGMNAAVRAVVRMGIYLGCKVFFIREGYQGMVDGGDNIVEANWSSVSCIIHRGGTVIGSARCMEFREREGRKRAAKNLVTRGISNLCVIGGDGSLTGANLFKEEWADLLKELVKDGEITQEQSEKYKHLHIVGLVGSIDNDFCGTDMTIGTDTALHRIIESIDAIASTAYSHQRTFIMEVMGRHCGYLAIVGALASEADYVFFPESPPPADWPEKLCKNYLALVAAMCSEADYVFIPEWPPEQDWPNKLCKKLIQERLTGQRLNIIIVAEGAVDRNGDPITAEKVRQVVVEKLQQDTRITVLGHVQRGGNPSAFDRVLGCRMGAEAVMALVEATPETEACVVTLDGNQAVRLPLMECVRRTKAVAQAMADKNWDLAVQLRGKGFVRNLETYKMLTRLKAPVEIDPNKEGGHPVLTKDHYTLAVMHVGSPSCGMNAAVRSFVRNCIYRGDKVYGIMDGVLGLATGKLKLMDWPSVTGWVAQGGAYLGTKRAPPKDDQLPLIAQKLKEFGIQALLIIGGFEGFQTGLSFYNARTQHPEFRIPIAMIPATISNNVPGTEFSLGCDTALNEITEICDRIRQSAQGTKRRVFIIETMGGYCGYLATLAGLAGGADAAYIFEEKFNIKDLNQDIIAMAAKMSEGVQRGLILRNESANSNYNTEFMQRLFTEEGKGLFSCRMNIIGHMQQGGSPTPFDRNLGTKMGAKAVEWFTERLKKDTTADGQTVSNSDESAVMLGIVRRQYRYTPFSKLIDTTDFEHRIPTYQWWMKLRPLLKVLAKHESTYEEEGLYITVEDMDKNNDAPLV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NNAY01002997
EMBL· GenBank· DDBJ
OXU20150.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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