A0A4W4H5S7 · A0A4W4H5S7_ELEEL

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

Gene names

    • Name
      PFKL

Organism names

Accessions

  • Primary accession
    A0A4W4H5S7

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Homo- and heterotetramers.

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
Domain402-686Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    780
  • Mass (Da)
    84,620
  • Last updated
    2019-09-18 v1
  • MD5 Checksum
    6083A9BFBB3C80C4CA50CCE4A74519C0
MFSQGLETLRMTGAGKAIAVLTSGGDAQGMNAAVRAVTRMGIYVGAKVYLIYEGYQGLVDGGDNITLAHWHSVTNIIQLGGTVIGSARCKAFTTREGRVAAAFNLVKRGITNLCVCGGDGSLTGANIFRNEWSGLLAELLAKGRITAETAKQYGHLNIVGLVGSIDNDFCGTDMTIGADSALHRIMEIVDAITTTAISHQRTFVLEVMGRHCGYLALVTALASGADWLFIPEAPPEEGWEELMCTRLGESRSKGSRLNVIIVAEGAINKKGEQISSGYIKDLVVKRLGYDTRVTVLGHVQRGGTPSAFDRVLSSKLGVEAVVALMEATPDTPACVIGLSGNQSVRLPLMEGVEMTKEVQRAMNEKRFEEAIQLRGRSFENNWGIYKLLAYQKPAQVESNFSLAILNVGAPAAGMNAAVRSAVRVGLAAGHKVYTVSDGFEGLANGAVKEVSWNTVAGWTGQGGSLLGTKRTLPSSCMEKLVENINKYNIQALLVVGGFEAYEGILELFEARGSYNELCIPMCIIPATISNNVPGTDFSLGSDTAVNAAMESCDKIKQSATGTKRRVFVVETMGGYCGYLATTTGIAVGADAAYIFEEPFNIHDLKMNVEHLTEKMKKDIQRGLVLRNEKCHMHYTTDFIYNLYSAEGKGIFDCRVNVLGHLQQGGTPSPFDRNFGTKLGVRAVQWLTERMTSTLRHGRVFANSPDTACVVGLNKKVISFSPVTELKAQTDFEHRMPKEQWWLSLRLMLKMLAKYQTSFNQYITGEIEHVTRQSLSIDTGF

Computationally mapped potential isoform sequences

There are 9 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A4W4GY74A0A4W4GY74_ELEELPFKL784
A0A4W4H4Q2A0A4W4H4Q2_ELEELPFKL775
A0A4W4H5H8A0A4W4H5H8_ELEELPFKL755
A0A4W4H5A6A0A4W4H5A6_ELEELPFKL777
A0A4W4H5X1A0A4W4H5X1_ELEELPFKL763
A0A4W4H5X9A0A4W4H5X9_ELEELPFKL762
A0A4W4H5M5A0A4W4H5M5_ELEELPFKL765
A0A4W4H611A0A4W4H611_ELEELPFKL779
A0A4W4GY99A0A4W4GY99_ELEELPFKL766

Keywords

Genome annotation databases

Similar Proteins

Disclaimer

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