V5GLY8 · V5GLY8_ANOGL

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 site480beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site537-541beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site575beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site582-584beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site638beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site664beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site670-673beta-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
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
      K6PF

Organism names

Accessions

  • Primary accession
    V5GLY8

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-392N-terminal catalytic PFK domain 1
Domain20-325Phosphofructokinase
Region411-789C-terminal regulatory PFK domain 2
Domain412-696Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    789
  • Mass (Da)
    87,210
  • Last updated
    2014-01-22 v1
  • Checksum
    B90410E52B397EC1
MTEKPGAKFIERGAHKGKGIAVFTSGGDSQGMNAAVRAVVRMGIYLGCKVYFIREGYQGMVDGADYIVEANWSSVSSIIHKGGTIIGSARCQDFRERQGRLKAAKNLVEKGITNLVVIGGDGSLTGADLFRQEWNSLLEELVQNKEITPEQKEKYKTLQIAGLVGSIDNDFCGTDMTIGTDSALHRIIEAIDAIVSTAYSHQRTFIMEVMGRHCGYLALVAALTGEADFVFIPEWPADSNWKDVLCKKLMQERTAGQRLNIIIVAEGAIDRNGQPITAEMIKKVVVDNLHQDTRITVLGHVQRGGRPSAFDRILGSRMGAEAVMALMEADEKAEPCVISLDGNQAVRVPLMQCVKQTKAVAQAMADKQWEKAVQLRGKSFMRNLETYKLLTRLKPPKEAFNEKGKGKEGYTMAVMHIGAPACGMNAAVRSFVRNCIYRGDTVLGIHDGIDGLLAGYVKHMSWSDVTGWVSHGGAYLGTKRTLPGHRMGLVASRLQEFGIQALLIIGGFEGFQAALQMYENREEHAAFRIPILVIPSTISNNVPGTEFSLGCDTALNEITEICDRIRQSAQGTKRRVFVIETMGGYCGYLATLAGLAGGADAAYIYEEKFTIKDLQQDVYHMATKMSEGVQRGLILRNEKASENYNTDFIYRLYSEEGKGLFSARMNILGHMQQGGSPTPFDRNLGTKMAAKAVDWLVCQLKNNTDEEGKVSCGDQNTVCLLGIVKRQYKCTSVHALKEETNFEQRIPKEQWWLKLRPLLRILAKHDSTYEEEGMYMSIEDRVLVDPLYG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GALX01003377
EMBL· GenBank· DDBJ
JAB65089.1
EMBL· GenBank· DDBJ
Transcribed RNA

Genome annotation databases

Similar Proteins

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