F8PXU8 · F8PXU8_SERL3

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 site16ATP (UniProtKB | ChEBI)
Binding site130-131ATP (UniProtKB | ChEBI)
Binding site160-163ATP (UniProtKB | ChEBI)
Binding site161Mg2+ (UniProtKB | ChEBI); catalytic
Binding site207-209substrate; ligand shared between dimeric partners; in other chain
Active site209Proton acceptor
Binding site244substrate; ligand shared between dimeric partners
Binding site251-253substrate; ligand shared between dimeric partners; in other chain
Binding site308substrate; ligand shared between dimeric partners; in other chain
Binding site336substrate; ligand shared between dimeric partners
Binding site342-345substrate; ligand shared between dimeric partners; in other chain
Binding site517beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site574-578beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site612beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site619-621beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site679beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site705beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site786beta-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
      SERLA73DRAFT_89685

Organism names

Accessions

  • Primary accession
    F8PXU8

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-434N-terminal catalytic PFK domain 1
Domain8-368Phosphofructokinase
Domain448-736Phosphofructokinase
Region448-810C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    810
  • Mass (Da)
    88,066
  • Last updated
    2011-09-21 v1
  • Checksum
    EC3E398DE3A39055
MSGQQKMKLAVLTSGGDSAGMNAVVRSVVRAGILKGCETWIVREGYEGLVRGNVDAQNVNKDPPTIPLPLNGADADLINNLRFGDGELLLDGTGDHPGGRTLIGRYIVRVGWDDVRGWFAQGGTLIGTARSTAFRTVEGRLAAAYNLIKEGIDALVVCGGDGSLTGADVFRSEWPKLIAELRSQGKDMFLPPIARHGHLKIVGLVGSIDNDMSMTDLTIGAPTALHRICEAIDNINSTAASHSRAFVLEVMGRHCGWLALLAGVSAGADFIFIPERPPETNPWEDEMCDAIKRHRKVGKRKTIVIVAEGAHDSLLQPIRAEYVKDVLTDRLGLDTRVTTLGHTQRGGRPCAFDRILPTLQGVEAVNALLEATPEKPSYMIGIRENKITRVPLMEAVAMTRAVADAIAAKDFTKAMSLRDPEFCESLDGFFSTAALYKEKQLPESKRMRVAIMHMGAPAGGMNAATRAAVRYCIRQGHTPIAIHNGFRGLLNDNIHELSWLGVDNWTARGGSELGTNRTLPDVDLGAVAARFQEHNFHALLMIGGFEAFSALMILENGRQYYPAFHIPMVHLPATLSNNVPLTEFSLGSDTSLNALVDACDSIKQSASASRNRVFVVETQGGKCGYLATMGALATGASLVYTPEHGMNLDTLRADVRFLKRRYGLDAKGRSEGRLVIRNETASSVYTTDVVTKMFKEEGGDLFDSRSASLGHTLQGGIPSPMDRARAVRLSLKCMAFLERYHDELQKQPSKVKQAEPESAAVITIQGSTIKWVPVKDMVQHADMKNRRGKTAWWGDIKDLVEALVGRPQLT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GL945480
EMBL· GenBank· DDBJ
EGN98711.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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