A0A484C067 · A0A484C067_PERFV

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 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 site475beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site583-587beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site621beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site628-630beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site684beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site710beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site716-719beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site790beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Component6-phosphofructokinase complex
Cellular Componentmembrane
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
      EPR50_G00222230

Organism names

  • Taxonomic identifier
  • Strain
    • YP-PL-M2
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Perciformes > Percoidei > Percidae > Percinae > Perca

Accessions

  • Primary accession
    A0A484C067

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Homo- and heterotetramers.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-393N-terminal catalytic PFK domain 1
Domain21-326Phosphofructokinase
Region406-839C-terminal regulatory PFK domain 2
Domain557-742Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    839
  • Mass (Da)
    91,492
  • Last updated
    2019-06-05 v1
  • Checksum
    B06D6F025A328BCD
MAQPDGKKIFFENLSGAGKAIAVLTSGGDAQGMNAAVRAVVRMGLYVGAKVYFIHEGYQGMVDGGENIKEATWESVSSMLQVGGTVIGSARCKEFRSHEGRLKAAHNLVQHGITNLCVIGGDGSLTGANLFREEWSGLLGELAEQGLIEADAVQKYSALHIVGMVGSIDNDFCGTDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVLIPEMPPEDGWEEKMCEKLSANRAGMKRLNIIIVAEGAIDRSNTPITTDYIKDLVVKCLGFDTRVTILGHVQRGGTPSAFDRILASRMGVEAVLALLETTANTPACVVSLCGNQSVRLPLMECVQMTQEVQRAMDGKRFEEAVKLRGRSFENNLRTYKLLAHRKPESELPVSNFNVAVLNVGAPAAGMNAAVRSAVRVGISEGHKMFAVSDGFEGFYKGQIKEIKWADVGGWTGQGGSLLGTKRTLPAKHIDKIAEQMRKNNINALLIVGGFEGFLSLLELLTARGKYDEFCVPMVMVPATVSNNVPGSDLSIGADTALNAITTAFESLLQLYEARSAYEELCIPMCMLPATISNNVPGTDLSIGADTALNAIVETCDRIKQSASGTKRRVFIIETMGGYCGYLASVGGLAAGADAAYIYEEPFDIRDLQANVEHLTEKMKTSIQRGLVLRNENCNENYTTDFIYQLYSEEGRGVFDSRKNVLGHMQQGGAPSPFDRNFGTKISAKAMQWVSKKLLETFRQGRVFANTEDSCCLLGMRRRALVFQPVVQLKDETDFVHRIPKEQWWLKLRPLMKILAKYKTTFDVSDSGQLEHVVRNRPKESDASVAM

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SCKG01000022
EMBL· GenBank· DDBJ
TDG97080.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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