H0UW67 · H0UW67_CAVPO

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 site34ATP (UniProtKB | ChEBI)
Binding site97-98ATP (UniProtKB | ChEBI)
Binding site127-130ATP (UniProtKB | ChEBI)
Binding site128Mg2+ (UniProtKB | ChEBI); catalytic
Binding site173-175substrate; ligand shared between dimeric partners; in other chain
Active site175Proton acceptor
Binding site210substrate; ligand shared between dimeric partners
Binding site217-219substrate; ligand shared between dimeric partners; in other chain
Binding site273substrate; ligand shared between dimeric partners; in other chain
Binding site301substrate; ligand shared between dimeric partners
Binding site307-310substrate; ligand shared between dimeric partners; in other chain
Binding site481beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site538-542beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site576beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site583-585beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site639beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site665beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site671-674beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site744beta-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
Molecular Functionprotein-containing complex binding
Biological Processcanonical glycolysis
Biological Processcellular response to leukemia inhibitory factor
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
  • Strain
    • 2N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Hystricomorpha > Caviidae > Cavia

Accessions

  • Primary accession
    H0UW67

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Keywords

Expression

Gene expression databases

Interaction

Subunit

Homo- and heterotetramers.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-399N-terminal catalytic PFK domain 1
Domain27-332Phosphofructokinase
Domain412-697Phosphofructokinase
Region412-792C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    792
  • Mass (Da)
    86,230
  • Last updated
    2012-02-22 v1
  • Checksum
    CC9775FB8E5D18F8
MAAGSSSTSRGSLPKFLENLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYTGAKVYFIYEGYQGMVDGGANIVEADWESVSSILQVGGTIIGSARCKAFRSREGRLKAALNLVQLGITNVCVIGGDGSLTGANIFREEWSGLLEELAQNGKISEEAMKKHGYLNVVGMVGSIDNDFCGTDMTIGTDSALHRIIEVIDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLPESPPEEGWEENMCIKLSENRARKKRLNIIIVSEGAIDTQNKPITSEKIKELVVSQLGYDTRVTILGHVQRGGTPSAFDRILASRMGVEAVIALLEATPEIPACVVSLNGNHAVRLPLMECVQMTQDVQKAMDEGRFKDAVKLRGRSFEGNLRTYKRLAIKLPDDQITKTNCNVAVINVGAPAAGMNAAVRSAVRVGIAEGHKMFAIYDGFDGFAKGHIKEIGWTDVGGWTGQGGSILGTKRTLPGKYLEQIAEQIRVHNINALLIIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVSNNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGADAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKGVFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKESQGKGKKFVTDDSICLLGMRKRNLLFQPVTELKEETDFEHRIPKEQWWLKLRPLMKILAKYKASYDVSDSGQLEPVRQRGTQGEEPADI

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A286XJ31A0A286XJ31_CAVPOPFKP792

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAKN02021827
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

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