H3DAQ8 · H3DAQ8_TETNG

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.

TypeIDPosition(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 site200substrate; ligand shared between dimeric partners
Binding site207-209substrate; ligand shared between dimeric partners; in other chain
Binding site263substrate; ligand shared between dimeric partners; in other chain
Binding site291substrate; ligand shared between dimeric partners
Binding site297-300substrate; 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 Componentcytoplasm
Molecular Function6-phosphofructokinase activity
Molecular FunctionATP binding
Molecular Functionmetal ion binding
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

Accessions

  • Primary accession
    H3DAQ8

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Homo- and heterotetramers.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-390N-terminal catalytic PFK domain 1
Domain18-324Phosphofructokinase
Domain401-685Phosphofructokinase
Region401-779C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    779
  • Mass (Da)
    85,182
  • Last updated
    2012-04-18 v1
  • Checksum
    E47F04EE4C2937FB
MAHTVPINVSKMGEGRAIAVLTSGGDAQGMNAAVRATVRVGLYTGAKVYFVHEGYQGLVDGGDNIRPATWESVSMMLQLGGTVIGSARCQDFRTKEGRTKAAHNLVKLGITNLCVVGGDGSLTGANQFRTEWRDLLADLVKAGKITANEAKNSSHLNIVGMVGSIDNDFCGTDMTIGTDSALHRIIEVDAITTTAQSHQRTFILEVMGRHCGYLALVTALACGADWVFIPEMPPEEGWEEHLCRRLSDQRGRGSRLNIIIVAEGAMDRHGKPITCEQVKQLVSKKLGFDTRTTILGHVQRGGTPSAFDRILPRPSRMGVEAVMALLEATPDTPACVVSLSGNMAVRLPLMECVQVTKDVTTAMAERFEEAIKLRGKSFENNWNTYRMLAHVNLPETKSNINIALLNVGAPCAGMNAVVRSAVRIGILQGHQMLAVHDGFDGLAQGMIEPISWSGVAGWTGKGGSFLGTKRSLPEDVMEEISLNIAKFNIHAMVIIGGFEAFRGGLQMVQAREKYEELCIPLVVVPATVSNNIPGSDFSVGADTALNTITMTCDRIKQSAAGTKRRVFIVETMGGYCGYLATMAGLASGADAAYIHEEPFKIHDLQVNVDHLVEKMKTTVKRGLILRNEKCNANYTTDFIFNLYAEEGKGVFDCRKNVLGHMQQGGTPSPFDRNFGTKMGMKSVLWLTDKLKECYRHGRIFANSPDSACVLGMRKRALVFTSLADLKEQTDFEHRIPKTQWWIKLRPLLKILAKYKINLDITEKTAMEHVIKKRGAFKFS

Keywords

Genome annotation databases

Similar Proteins

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