A0A9P7EGQ4 · A0A9P7EGQ4_9AGAM

  • Protein
    ATP-dependent 6-phosphofructokinase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 site17ATP (UniProtKB | ChEBI)
Binding site135-136ATP (UniProtKB | ChEBI)
Binding site165-168ATP (UniProtKB | ChEBI)
Binding site166Mg2+ (UniProtKB | ChEBI); catalytic
Binding site211-213substrate; ligand shared between dimeric partners; in other chain
Active site213Proton acceptor
Binding site248substrate; ligand shared between dimeric partners
Binding site255-257substrate; ligand shared between dimeric partners; in other chain
Binding site315substrate; ligand shared between dimeric partners; in other chain
Binding site343substrate; ligand shared between dimeric partners
Binding site349-352substrate; ligand shared between dimeric partners; in other chain
Binding site527beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site584-588beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site622beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site629-631beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site689beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site715beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site796beta-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 Componentmitochondrion
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
      BJ212DRAFT_1337781

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MN1
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Boletales > Suillineae > Suillaceae > Suillus

Accessions

  • Primary accession
    A0A9P7EGQ4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-434N-terminal catalytic PFK domain 1
Domain9-375Phosphofructokinase
Region458-820C-terminal regulatory PFK domain 2
Domain463-746Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    820
  • Mass (Da)
    89,004
  • Last updated
    2023-09-13 v1
  • Checksum
    A2FEE4DC9F9D0C77
MSQSTGKMKLAVLTSGGDSAGMNAVVRAIVKIGILRGCETWIVREGYEGLVRGNTQAHAIHADLPADASALKCAHRGVPTNLTRNLRFGDGDLLRDGTGDHHHGRTLKGRYIVRVGWDDVRGWFAEGGTLIGTARSAAFRTSEGRLSAAHNLIKEGIDALAVCGGDGSLTGADLFRSEWPSLVSQLLTQGMITEEQAEKHGHLKIVGLVGSIDNDMSMTDLTIGAPTALHRICEAIDNINSTAASHSRAFVLEVMGRHCGWLALLAGVSSGADFIFIPERPPQTIPGGTWEDDMCEAIRGHREAGKRKTIVIVAEGAHDADLQPIRAEYVKEVLTERLGLDTRVTTLGHTQRGGRPCAFDRILPTLQGEEAVKALLEATPDTPSYMIGVRENKITRVPLMEAADAIGAKDFTKAMSMRDPEFYQSLEGFFATSTLFKEKQLPHHRVIRPCTLHLTKYCLILRSMGAPAGGMNAATRAAVRYCIKQGHHPLAVHNGFRGLLDDNIHELSWLGVDAWTSRGGSELGTNRTLPDVDLGAVAARFQEHNFHALLMIGGFEAFNALLILETGRKHYPAFHIPMTHLPATISNNVPMTEFSLGSDTSLNALVDACDSIKQSASASRNRVFVVETQGGKCGYLATMGALATGASIVYTPEQGMNLDTLRQDVKFLKIRYGLDAKGKSEGRMVIRNECASTVYTTDVVTKMFKEEGGNLFDSRSASLGHTLQGGVPSPMDRARAARLSLRCMTFLEEHHDALQKQVGKVKQAPPESAAVITIQGSTIKWVPVQEMVQHADMKNRRGKTAWWGEIKNLVEALAGRPEIL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABBWG010000007
EMBL· GenBank· DDBJ
KAG1821130.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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