A0A5C6GE54 · A0A5C6GE54_9HYPO

  • Protein
    ATP-dependent 6-phosphofructokinase
  • Gene
    PFK1
  • 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

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 site15ATP (UniProtKB | ChEBI)
Binding site78-79ATP (UniProtKB | ChEBI)
Binding site108-111ATP (UniProtKB | ChEBI)
Binding site109Mg2+ (UniProtKB | ChEBI); catalytic
Binding site154-156substrate; ligand shared between dimeric partners; in other chain
Active site156Proton acceptor
Binding site191substrate; ligand shared between dimeric partners
Binding site198-200substrate; ligand shared between dimeric partners; in other chain
Binding site254substrate; ligand shared between dimeric partners; in other chain
Binding site286substrate; ligand shared between dimeric partners
Binding site292-295substrate; 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 site533-537beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site571beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site578-580beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site638beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site664beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site670-673beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site742beta-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

    • Name
      PFK1
    • ORF names
      ED733_002998

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Cep018-CH2
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Clavicipitaceae > Metarhizium

Accessions

  • Primary accession
    A0A5C6GE54

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-384N-terminal catalytic PFK domain 1
Domain7-317Phosphofructokinase
Region385-398Interdomain linker
Domain399-695Phosphofructokinase
Region399-785C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    785
  • Mass (Da)
    85,672
  • Last updated
    2019-11-13 v1
  • Checksum
    D12573C6B244B37D
MAAPKKKIAVMTSGGDSPGMNGVVRAVVRTAIHKGCEAYAVYEGYEGLVRGGDFIKKMEWHHVRGWLSEGGTLIGTARCMAFYERSGRLTAAKNMVLHGIDALIICGGDGSLTGADRFRSEWPSLLDELVTNGDLSIDQVAPYKHLNIVGIVGSIDNDLSGTDATVGCYSALSRICEMVDYIEATASSHSRAFVIEVMGRHCGWLALLAGVATGADFVFIPERPQEHDWREDMRVVVNRHRKLGKRKTIVIVAEGARDKDGNKITPEEIKDLLADKAEGGLGLDTRITTLGHVQRGGTAVAHDRILATLQGVEAVHAVLEATPNTETCFIAMNENKIVRKPLMKAVQETKKVAKAVDAKDFDKAMSLRDTEFADQYNSYITTTNVMIEDHKLPPKHRMKVGFINVGAPAGGMNAAVRAAVAYCISRGHEPIGIHNGFAGFARHHDDKPVGSVRPFDWLEVDGWASKGGSEIGTNRELPEESGMELIANLIEQYEFDALFIVGGFEAFHSVAQLRKARDEYPSLCIPICLLPATISNNVPGTEYSLGSDTCLNELVSYCDKIKQSASATRRRVFVIETQGGRCGYVATLSGLSVGASAVYIPEEGISLSMLNADVNHLKHVFKNDRGQSRAGRLILVNEKASKVYDAKLIASIIREEAHDRFESRESIPGHVQQGGVPSPMDRCRAVRLAIKCIQHLEDFGCNAHNRVKKDPNSTSVIGIQGSEVVFTPMKALEEQGTDWPNRRPKAAHWLEVRDVVDMLGGRPDYPRPEKSLTGLIAKDTKRGIA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SBHS01000008
EMBL· GenBank· DDBJ
TWU75138.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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