A0A0D2H344 · A0A0D2H344_9EURO

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.

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 site26ATP (UniProtKB | ChEBI)
Binding site89-90ATP (UniProtKB | ChEBI)
Binding site119-122ATP (UniProtKB | ChEBI)
Binding site120Mg2+ (UniProtKB | ChEBI); catalytic
Binding site165-167substrate; ligand shared between dimeric partners; in other chain
Active site167Proton acceptor
Binding site202substrate; ligand shared between dimeric partners
Binding site209-211substrate; ligand shared between dimeric partners; in other chain
Binding site265substrate; ligand shared between dimeric partners; in other chain
Binding site293substrate; ligand shared between dimeric partners
Binding site299-302substrate; ligand shared between dimeric partners; in other chain
Binding site484beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site541-545beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site579beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site586-588beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site646beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site672beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site678-681beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site754beta-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
      Z517_00675

Organism names

  • Taxonomic identifier
  • Strain
    • CBS 271.37
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Chaetothyriomycetidae > Chaetothyriales > Herpotrichiellaceae > Fonsecaea

Accessions

  • Primary accession
    A0A0D2H344

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-391N-terminal catalytic PFK domain 1
Domain18-325Phosphofructokinase
Domain408-704Phosphofructokinase
Region408-811C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    811
  • Mass (Da)
    88,866
  • Last updated
    2015-04-29 v1
  • Checksum
    AEE632776F917D80
MAFGRNTTPSASSVGPRRVGIMTSGGDSQGMNGVVRAVVRMSIHMGCEAYAILEGYEGLVRGGDAIRRMHWEDVRGYLSLGGTLIGTRRCREFFERAGRVKAAKNLILKGISGLVVCGGDGSLTGADRFRAEWPSLLDELVQTRQLTPSQVEPYRHLNVCGLVGSIDNDFSGTDATIGCYSSLQRICEMVDAVFDTAASHARGFVIEVMGRHCGWLALMASIATGADYVFIPEKPPGADWADEMCEIVTSHRNLGKRRTIIIIAEGATDIELNKITADQVVETLSEKLDLDTRKTVLGHIQRGGLASYYDRWLATLQGVEAVKALLEATPDTPSPVITVRENKILRSDLQECVRLTKSAAAAVKEKDWTRAMKLRDVEFKDYFDSYKLTTSTTEERPRLRLPEEKHMRIAIIHVGAPAAGMNPATRAAVAYCLSRGHTPLAIYNGFPGLQRHHDDKPVGSVRELKWIDVDDWVNQGGSELGTNRSLPSEDLAQTAYCFDLYEFDALFLIGGFEAFTSASQIRNNRDKYPSFRIPLLVLPATISNNVPGTEYSLGSDTCLNTLVGFCDVIRQSASASRRRVFVVDTQGGKSGYLATMTGLAVGASAVYTPEAGINMRMLLRDIDFIREDFQNDRGAARAGKIILRNERASQTYTAQMIADVINVEAQGRFDARAAVPAHYQQGMKPSPIDRIRSFKLAIKCMQFLEENFAGKDPDEINANPLNAAIIGIQGSEAVFSPMGSDLGLEATETDWSSRRQLNEYWRPVEAVIDILSGRPTDLDGTADYATLPETPGEAFVSVAPSRAITPRPQIL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KN846969
EMBL· GenBank· DDBJ
KIW85285.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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