Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A875RQG0 · A0A875RQG0_EENNA

Function

function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.

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 site226ATP (UniProtKB | ChEBI)
Binding site289-290ATP (UniProtKB | ChEBI)
Binding site319-322ATP (UniProtKB | ChEBI)
Binding site320Mg2+ (UniProtKB | ChEBI); catalytic
Binding site365-367substrate; ligand shared between dimeric partners; in other chain
Active site367Proton acceptor
Binding site402substrate; ligand shared between dimeric partners
Binding site409-411substrate; ligand shared between dimeric partners; in other chain
Binding site466substrate; ligand shared between dimeric partners; in other chain
Binding site493substrate; ligand shared between dimeric partners
Binding site499-502substrate; ligand shared between dimeric partners; in other chain
Binding site676beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site733-737beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site771beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site778-780beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site838beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site864beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site870-873beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site975beta-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
      FOA43_004234

Organism names

Accessions

  • Primary accession
    A0A875RQG0

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Heterooctamer of 4 alpha and 4 beta chains.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-591N-terminal catalytic PFK domain 1
Domain8-109Phosphofructokinase N-terminal
Domain218-524Phosphofructokinase
Region592-605Interdomain linker
Domain606-896Phosphofructokinase
Region606-1008C-terminal regulatory PFK domain 2

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,008
  • Mass (Da)
    110,628
  • Last updated
    2022-01-19 v1
  • MD5 Checksum
    C58931384B3EC8196E99300FC2B348A6
MVKSLVSNISFTSFSASKTKDYEDLISFYRSFGFRVVRIFNKDASSTGIELNGISSDSRNECWLAAYPVTRLDTRGNVIPFQETAEYTHPELESDLARFNKGVMLKIRLVSHDVHKNIEMPGRMVILTQDPASVRSVAEKNGYKTSESTDAWVDFYVSDPVGNLVGFTANALPGNDQVSHQLKQEADFFASDASIKAVYTQEAHNAIAEVTRKSSKKRLAVMTSGGDSPGMCAAVRAVVRAGLFFDCEVFGCYEGYSGLVQGGDLLKPMAWEDVRGWLSLGGTLIGTARCLEFKERAGRLLAARNMILRGIDALIVCGGDGSLTGADLFRAEWPSLLEELIKTGKLTEEQANPYKTLTIVGMVGSIDNDMAMTDNTIGAYSSLERICEMVDYIDTTAASHSRAFVVEVMGRHCGWLAIMAGVCCGADYVFVPEQPPSASGWKDELKKVCLRHRKRGRRKTTVIVAEGAIDDSLQPITSEQVKDTLVELGLDTRVTTLGHVQRGGSAVAFDRLLATMQGVEAVKAVLESTPNTPSPMIGIQENQIVRIPLVEAVSQTKAVAKCIEKKDFAGAFNLRDAAFQETWLDFASLSAGDDASYLLPEDQRLNIAIVHVGAPTAALNAATRAAVLYLLSRGHTPYGVENGFSGLIRHGAMRKLSWMDVVEWHNVGGSFLGTNRSLPSSDIGTVAFYLQKFQIQGLLIIGGFEAYRSLYELKHSRDKYPIFNMPLVCLPSTVSNNVPGTEYSLGCDTCLNVLVSYCDAVKQSASASRRRVFVVEVQGGNCGYVASYIGLATGALAVYRPEDSITLKSVREDLILLEKSFVNDQGEDRSGKMVIRNENASDIYSTELIADILREEADGKFESRTAIPGHVQQGKIPSSMDRCYAARFAIKACKFLEENNEEIKKSVKLLESEGFGSNETDLGRSDSELKFVYKHGRKVVVPELNNAKLVGIHGTKVTFEDIDFLWKKNTNVEARTALEVHWDQMNVVNDILSGRLMIRKQGDNNDNN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP064815
EMBL· GenBank· DDBJ
QPG76840.1
EMBL· GenBank· DDBJ
Genomic DNA

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