A0A553IH07 · A0A553IH07_ACHLA

  • 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 site10ATP (UniProtKB | ChEBI)
Binding site20-24ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site71-72ATP (UniProtKB | ChEBI)
Binding site101-104ATP (UniProtKB | ChEBI)
Binding site102Mg2+ (UniProtKB | ChEBI); catalytic
Binding site124-126substrate; ligand shared between dimeric partners; in other chain
Active site126Proton acceptor
Binding site153ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site161substrate; ligand shared between dimeric partners
Binding site168-170substrate; ligand shared between dimeric partners; in other chain
Binding site184-186ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site221substrate; ligand shared between dimeric partners; in other chain
Binding site242substrate; ligand shared between dimeric partners
Binding site248-251substrate; 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
      FNV44_00145

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • PG8REry
  • Taxonomic lineage
    Bacteria > Mycoplasmatota > Mollicutes > Acholeplasmatales > Acholeplasmataceae > Acholeplasma

Accessions

  • Primary accession
    A0A553IH07

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-274Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    316
  • Mass (Da)
    34,104
  • Last updated
    2019-11-13 v1
  • Checksum
    021ACA04E55B3103
MKIAVLTSGGDAPGMNAAIRAIVRTGIAEGHEMFGIMDGYRGLLEDRFIPLAAKDVSGMLSIGGTKLGTARVSEFKEVPVQMVAIDNLRNRGIDALIVIGGDGSYRGAQALHELEFQTIAIPGTIDNDVYGTDYTIGFHTALNTIVEAIDKLRDTSSSHRRCSIIEVMGRTSGDLALYAGICGGAEFIITPENPINKDKLISTLKKHNEEGRRHAIIVVTEQQFDVHKLAAEISIKSGFSSRATVLGYIQRGGTPIAEDRILASRMGAFAVEMLAKGVSGQCVGIKDDKLVTSPLSDIINHPKERVELYDLIKKLR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VKID01000001
EMBL· GenBank· DDBJ
TRX99484.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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