A0A6N7S5N2 · A0A6N7S5N2_9FIRM

  • Protein
    ATP-dependent 6-phosphofructokinase
  • Gene
    pfkA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate.

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 site12ATP (UniProtKB | ChEBI)
Binding site22-26ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site73-74ATP (UniProtKB | ChEBI)
Binding site103-106ATP (UniProtKB | ChEBI)
Binding site104Mg2+ (UniProtKB | ChEBI); catalytic
Binding site126-128substrate; ligand shared between dimeric partners; in other chain
Active site128Proton acceptor
Binding site155ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site163substrate; ligand shared between dimeric partners
Binding site170-172substrate; ligand shared between dimeric partners; in other chain
Binding site186-188ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site215-217ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site224substrate; ligand shared between dimeric partners; in other chain
Binding site245substrate; ligand shared between dimeric partners
Binding site251-254substrate; 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
      pfkA
    • ORF names
      GKE08_07530

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • BIOML-A4
  • Taxonomic lineage
    Bacteria > Bacillota > Erysipelotrichia > Erysipelotrichales > Erysipelotrichaceae > Holdemania

Accessions

  • Primary accession
    A0A6N7S5N2

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-277Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    320
  • Mass (Da)
    34,338
  • Last updated
    2020-10-07 v1
  • Checksum
    5D15DC8CD37DD255
MIRRIGILTSGGDAPGMNAAIRAVTRVALANGFEVMGIKDGYRGLVEGNYIPMDKSTVSDILNRGGTVLGSARLTEFKDLEIQKKAVQTLQNAKIDAIVVIGGDGSYRGAMALTKLGINCIGLPGTIDNDIPGTDFTIGFDTALNTVVEAVDKLRDTSSSHHRCSVVEVMGNRCGDLAVWAAISCGAEIVITPETGYDELDVLERLRYLDKAVKKRHAIVVISEKIADVDELARKISQNTGFAGRATVLGHVQRGGSPSPRDRVLASMMGEKAVDLLMEGVGGHCVGMIDNKVTSMPIEEALSSPRHSRKDLYRLFDRLV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WKPJ01000009
EMBL· GenBank· DDBJ
MSA89174.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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