A0A340XX08 · A0A340XX08_LIPVE

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 site35ATP (UniProtKB | ChEBI)
Binding site98-99ATP (UniProtKB | ChEBI)
Binding site128-131ATP (UniProtKB | ChEBI)
Binding site129Mg2+ (UniProtKB | ChEBI); catalytic
Binding site174-176substrate; ligand shared between dimeric partners; in other chain
Active site176Proton acceptor
Binding site211substrate; ligand shared between dimeric partners
Binding site218-220substrate; ligand shared between dimeric partners; in other chain
Binding site274substrate; ligand shared between dimeric partners; in other chain
Binding site302substrate; ligand shared between dimeric partners
Binding site308-311substrate; ligand shared between dimeric partners; in other chain
Binding site482beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site539-543beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site577beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site584-586beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site640beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site666beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site672-675beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site745beta-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
      PFKP

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Whippomorpha > Cetacea > Odontoceti > Lipotidae > Lipotes

Accessions

  • Primary accession
    A0A340XX08

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Homo- and heterotetramers.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-400N-terminal catalytic PFK domain 1
Domain28-333Phosphofructokinase
Domain413-698Phosphofructokinase
Region413-791C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    791
  • Mass (Da)
    86,195
  • Last updated
    2018-10-10 v1
  • Checksum
    5425BEE76C30763C
MGDHDVSPNPKGSFRKFLEQLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFIYEGYQGMVDGGSNIVEADWESVSSILQVGGTIIGSARCKDFRSREGRLKAAHNLLQLGITNLCVIGGDGSLTGANIFRKEWSGLLEELAREGKINTEEVQKHGYLNVVGMVGSIDNDFCGTDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLPESPPEEGWQENMCIKLSENRARKKRLNIIIVAEGAIDTQNKAITSEQIKELVVTQLGYDTRVTILGHVQRGGTPSAFDRILASRMGVEAVVALLQATPETPACVVSLSGNQAVRLPLMECVQMTQEVQKAMDERRFKDAVQLRGRSFENNLNTYKRLAIKLPDSQIPKSNCNVGIVNVGAPAAGMNAAVRAAVRVGIADGHKVFAVYDGFEGFAKGQVKEIGWADVGGWTGQGGSILGTKRTLPGKYLEDIATQMRTHGINALLIIGGFEAYLGLLELSAAREKHKEFCVPMVMVPATVSNNVPGSDFSIGADTALNTITDMCDRIKQSASGTKRRVFIIETMGGYCGYLANMGALAAGADAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKGVFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMQWISTKLKEPAGRGKRFVSDDSVCVLGISKRNLLFQPVAELKEETDFVHRIPKEQWWLKLRPLMKILAKYKASFEVSDAGQLEPMQPRGPEEHATI

Keywords

Sequence databases

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help