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W5MUA1 · W5MUA1_LEPOC

Function

function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. Negatively regulates the phagocyte oxidative burst in response to bacterial infection by controlling cellular NADPH biosynthesis and NADPH oxidase-derived reactive oxygen species. Upon macrophage activation, drives the metabolic switch toward glycolysis, thus preventing glucose turnover that produces NADPH via pentose phosphate pathway.

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 site25ATP (UniProtKB | ChEBI)
Binding site88-89ATP (UniProtKB | ChEBI)
Binding site118-121ATP (UniProtKB | ChEBI)
Binding site119Mg2+ (UniProtKB | ChEBI); catalytic
Binding site164-166substrate; ligand shared between dimeric partners; in other chain
Active site166Proton acceptor
Binding site201substrate; ligand shared between dimeric partners
Binding site208-210substrate; ligand shared between dimeric partners; in other chain
Binding site264substrate; ligand shared between dimeric partners; in other chain
Binding site292substrate; ligand shared between dimeric partners
Binding site298-301substrate; ligand shared between dimeric partners; in other chain
Binding site470beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site527-531beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site565beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site572-574beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site628beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site654beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site660-663beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site734beta-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 Componentmembrane
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

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Holostei > Semionotiformes > Lepisosteidae > Lepisosteus

Accessions

  • Primary accession
    W5MUA1

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Expression

Gene expression databases

Interaction

Subunit

Homo- and heterotetramers.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-390N-terminal catalytic PFK domain 1
Domain18-323Phosphofructokinase
Region401-780C-terminal regulatory PFK domain 2
Domain402-685Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    780
  • Mass (Da)
    85,120
  • Last updated
    2014-04-16 v1
  • MD5 Checksum
    FA67086E7DF29B84B160E0897BB97512
FIIMDLEKLRMTGAGKAIAVLTSGGDAQGMNAAVRAVTRMGIFVGAKVYLIYEGYQGLVDGGDNIKLANWQSVSNIIQLGGTVIGSARCKAFTTREGRLAAAFNLVQRGITNLCVCGGDGSLTGANIFRTEWSGLLADLVKSGRITEAMAQQYKHLNIVGLVGSIDNDFCGTDMTIGADSALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEEGWEDHMCARLGESRSKGSRLNVVIIAEGAITKTGEPISSNYVKDLVVQRLGYDTRVTVLGHVQRGGTPSAFDRVLSSKMGVEAVVALLEATPETPACVIGLSGNMAMRLPLMECVQMTKEVQKAMNEQRFEETIQLRGKSFENNWNTYKLLAHQKPAQSKSNFTMAILNVGAPAAGMNAAVRSAVRVGLAQGHRIYTVNDGFEGLANGAVTEVNWHDVAGWTGQGGSLLGTKRTLPSSCMEKIVESISKYNIQALLVVGGFEAYEGVLQLAEARGRYDELCIVMCVIPATISNNVPGTDFSLGADTAVNAAMESCDKIKQSASGTKRRVFIVETMGGYCGYLATTTGIAVGADASYIFEEPFNIHDLEINVEHLTEKMKNDIQRGLVLRNEKCHKFYTTEFIHNLYSAEGKGIFDCRMNVLGHLQQGGSPTPFDRNYGTKLGVKAVLWITDKLKETYRQGRVFANAPDTACVIGMMRKVLSFRPVTELKAHTDFEHRMPKEQWWLNLRLMLKMLAKYQTSFDEYVTGEIEHVTRRTLSIETGF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AHAT01016456
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AHAT01016457
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AHAT01016458
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

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.
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