F0XGG3 · F0XGG3_GROCL

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.

Type
IDPosition(s)Description
Binding site34ATP (UniProtKB | ChEBI)
Binding site97-98ATP (UniProtKB | ChEBI)
Binding site127-130ATP (UniProtKB | ChEBI)
Binding site128Mg2+ (UniProtKB | ChEBI); catalytic
Binding site173-175substrate; ligand shared between dimeric partners; in other chain
Active site175Proton acceptor
Binding site210substrate; ligand shared between dimeric partners
Binding site217-219substrate; ligand shared between dimeric partners; in other chain
Binding site273substrate; ligand shared between dimeric partners; in other chain
Binding site303substrate; ligand shared between dimeric partners
Binding site309-312substrate; ligand shared between dimeric partners; in other chain
Binding site493beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site551-555beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site589beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site596-598beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site656beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site682beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site688-691beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site760beta-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
      CMQ_2660

Organism names

Accessions

  • Primary accession
    F0XGG3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-401N-terminal catalytic PFK domain 1
Domain26-334Phosphofructokinase
Domain417-713Phosphofructokinase
Region417-804C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    804
  • Mass (Da)
    87,030
  • Last updated
    2011-05-03 v1
  • Checksum
    8651D72BAF1324A3
MASASAPGAAAPASTAPVAAAASKKKIAIMTSGGDSPGMNGVVRACVRMAIHLDCDAFCVYEGYDGLVRGGDYIRKMEWDDVRGWLSEGGTLIGTARCMAFYERPGRLVAAKNMIINGIDALIICGGDGSLTGADKFRAEWPSLLSELVQTGELTAAQTAPYQHLNIVGLVGSIDNDLSGTDATIGCYSALTRICEMVDYIEATASSHSRAFVIEVMGRHCGWLALMAGVATGADFIFIPEKPREDNWREEMCAIVHKNRQLGKRKTIVIIAEGALDREGNKISSEMIRALLADKDGLALDTRITTLGHVQRGGTAVAYDRMLATLQGVEAVRAVLEATPESETCFIAITENKIVRKPLMAAVQNTKSVVAAIEAHDFDRAMALRDTEFSDQYKSYIMTTAVQLDQHMRLPEKERMRIGFINVGAPAGGMNAAIRAGVAYCISRGHEPLAIHNGFAGFARHHADSPLRSVRPFDWLEVDGWASKGGSEIGTNRELPSDSGMETIANLIEEYQFDGLFLIGGFEAFHALSQLRTAREQYPSLCIPMVLLPATISNNVPGTEASLGSDTCLNELVSYCDKIKQSASATRRRVFVIETQGGRCGYVATLAGLSIGASAVYTPEEGLSLDMLATDVRHLKEVFANDKGQSRAGRLILINERTSSVYTAKLVADIIREEAHNRFEARDSIPGHVQQGGVPSAMDRCRAVRLAIKCIEHLEAFGRNAHNRVKKDPTSAAVIGIKAASVVFTSVEELEKTDTDWPNRRPLDAFWLNMKDVVDVLSGRPPYHPPKEILTGLQAKDAKRGIIS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GL629769
EMBL· GenBank· DDBJ
EFX02731.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help