A0A4W4GNB7 · A0A4W4GNB7_ELEEL

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 site27ATP (UniProtKB | ChEBI)
Binding site90-91ATP (UniProtKB | ChEBI)
Binding site120-123ATP (UniProtKB | ChEBI)
Binding site121Mg2+ (UniProtKB | ChEBI); catalytic
Binding site166-168substrate; ligand shared between dimeric partners; in other chain
Active site168Proton acceptor
Binding site203substrate; ligand shared between dimeric partners
Binding site210-212substrate; ligand shared between dimeric partners; in other chain
Binding site266substrate; ligand shared between dimeric partners; in other chain
Binding site294substrate; ligand shared between dimeric partners
Binding site300-303substrate; ligand shared between dimeric partners; in other chain
Binding site474beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site531-535beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site569beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site576-578beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site632beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site658beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site664-667beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site738beta-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
      pfkpa

Organism names

Accessions

  • Primary accession
    A0A4W4GNB7

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homo- and heterotetramers.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-392N-terminal catalytic PFK domain 1
Domain20-325Phosphofructokinase
Domain405-690Phosphofructokinase
Region405-787C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    787
  • Mass (Da)
    86,065
  • Last updated
    2019-09-18 v1
  • MD5 Checksum
    2BF6566BA7BD3EE546400D65CD45E75E
MAQPDNKKFFENLSGAGKAIAVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFIHEGYQGMVDGGDNIKEATWESVSSMLQVGGTVIGSARCMEFRTHEGRLKAAHNLVQHGITNLCVIGGDGSLTGANLFREEWSSLLAKLVQQGMINDDAAEKYSALHIVGMVGSIDNDFCGTDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVLIPEMPPEDGWEEKMCEKLSANRAGRKRLNIIIVAEGAIDRNNKPITTEHVKDLVVRSLGFDTRVTILGHVQRGGTPSAFDRILASRMGVEAVLALLETTANTPACVVSLCGNQAVRLPLMECVQMTQEVQKAMDEKRFEDAVKLRGRSFENNLRTYKLLAHRKPESELPHSNFNVAVLNVGAPAAGMNAAVRSAVRVGISEGHKMFAISDGFEGFYKGQIKEIKWGAVGGWTGQGGSLLGTKRTLPAKYIGKIAEQIRKYNINALLVIGGFEAYLGIAELLAARGTCEEFCVPMIMVPATVSNNVPGSDLSIGADTALNAITDTCDRIKQSASGTKRRVFIIETMGGYCGYLASVGGLAAGADAVYIYEEPFDIRELQSNVEHLTEKMKTSIQRGLVLRNENSNVNYTTDFIYQLYSEEGKGVFDCRKNILGHMQQGGAPSPFDRNFGTKIAAKAMQWISKKLQESYRQGRVFANTEDSACLLGMRRRALVFQPVTQLKDQTDFIHRIPKEQWWLKLRPLMKILAKYKTSYDVSDSGQLEHVVCNRTKESDTTTTI

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A4W4GK39A0A4W4GK39_ELEELpfkpa795
A0A4W4GIF0A0A4W4GIF0_ELEELpfkpa565
A0A4W4GN31A0A4W4GN31_ELEELpfkpa768
A0A4W4GK46A0A4W4GK46_ELEELpfkpa761
A0A4W4GNS9A0A4W4GNS9_ELEELpfkpa788

Keywords

Genome annotation databases

Similar Proteins

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