K7FNM8 · K7FNM8_PELSI

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 site117ATP (UniProtKB | ChEBI)
Binding site180-181ATP (UniProtKB | ChEBI)
Binding site210-213ATP (UniProtKB | ChEBI)
Binding site211Mg2+ (UniProtKB | ChEBI); catalytic
Binding site256-258substrate; ligand shared between dimeric partners; in other chain
Active site258Proton acceptor
Binding site293substrate; ligand shared between dimeric partners
Binding site300-302substrate; ligand shared between dimeric partners; in other chain
Binding site356substrate; ligand shared between dimeric partners; in other chain
Binding site384substrate; ligand shared between dimeric partners
Binding site390-393substrate; ligand shared between dimeric partners; in other chain
Binding site562beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site619-623beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site657beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site664-666beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site720beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site746beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site752-755beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site826beta-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 Componentapical plasma membrane
Cellular Componentnucleus
Cellular Componentsperm principal piece
Molecular Function6-phosphofructokinase activity
Molecular FunctionAMP binding
Molecular FunctionATP binding
Molecular Functionfructose binding
Molecular Functionfructose-6-phosphate binding
Molecular Functionidentical protein binding
Molecular Functionkinase binding
Molecular Functionmetal ion binding
Biological Processcanonical glycolysis
Biological Processfructose 1,6-bisphosphate metabolic process
Biological Processfructose 6-phosphate metabolic process
Biological Processglucose homeostasis
Biological Processglycogen catabolic process
Biological Processglycolysis from storage polysaccharide through glucose-1-phosphate
Biological Processmuscle cell cellular homeostasis
Biological Processpositive regulation of insulin secretion
Biological Processpositive regulation of transcription by RNA polymerase II

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
      PFKM

Organism names

Accessions

  • Primary accession
    K7FNM8

Proteomes

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane60-79Helical

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Homo- and heterotetramers.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-482N-terminal catalytic PFK domain 1
Domain110-415Phosphofructokinase
Region493-872C-terminal regulatory PFK domain 2
Domain494-777Phosphofructokinase

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    872
  • Mass (Da)
    95,785
  • Last updated
    2013-01-09 v1
  • Checksum
    8F88CE74552D5AB8
MRFKPFQCKAVPFTSASKRQAWERQLLQQADIMSINTREEGWHFPVMWTSLDLSVIGSKLFISVSLAFAVFFFFSFFPFSQNKKEPPAKKMLQPKEKHEHTHNLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGAKVYFVHEGYQGLVDGGDNIKEATWESVSMMLQLGGTVIGSARCQDFRTREGRLKAARNLVKRGITNLCVIGGDGSLTGADTFRAEWSNLLMELVKTGGITAEETKNSSHLNIVGMVGSIDNDFCGTDMTIGTDSALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALITALACGADWVFIPESPPEDDWEEHLCRRLTETRGRGSRLNIIIVAEGAINKQGKPITSEDIKNLVVKRLGYDTRVTILGHVQRGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTTAMNEGRFEDAVKLRGRSFQNNWNVYKLLAHVRPPSTKSGYNLAVMNVGAPAAGMNAAVRAAVRIGLIHGHKMLAVHDGFEGLAHGQVEEIVWGGVGGWTGLGGSKLGTKRTLPKKYFEEISATISTFNIHGLIVIGGFEAFTGSLELVEGRSKYEELCIPLCVIPATVSNNVPGSDFSIGADTALNTITMTCDRIKQSAAGTKRRVFIIETMGGFCGYLATMAGLASGADAAYIYEDPFTIRDLQVNVEHLTEKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFESRKNVLGHMQQGGTPTPFDRNFGTKMGAKSVVWLTGKIKECSRHGRIFANTLDSACLLGMRRRSLVFQPLAELENQTDFEHRIPKQQWWLKLRPILKILAKYKIDLDTSEKAHLEHVARKGLPVEANI

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
K7FNL7K7FNL7_PELSIPFKM782

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AGCU01201673
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AGCU01201674
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AGCU01201675
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

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