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A0A7X7E5N2 · A0A7X7E5N2_9BACT

  • 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.

Type
IDPosition(s)Description
Binding site18ATP (UniProtKB | ChEBI)
Binding site28-32ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site79-80ATP (UniProtKB | ChEBI)
Binding site109-112ATP (UniProtKB | ChEBI)
Binding site110Mg2+ (UniProtKB | ChEBI); catalytic
Binding site132-134substrate; ligand shared between dimeric partners; in other chain
Active site134Proton acceptor
Binding site161ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site169substrate; ligand shared between dimeric partners
Binding site176-178substrate; ligand shared between dimeric partners; in other chain
Binding site192-194ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site218ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site220-222ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site229substrate; ligand shared between dimeric partners; in other chain
Binding site254substrate; ligand shared between dimeric partners
Binding site260-263substrate; 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
      GX640_24370

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • AS06rmzACSIP_543
  • Taxonomic lineage
    Bacteria > Fibrobacterota > Fibrobacteria > Fibrobacterales > Fibrobacteraceae > Fibrobacter

Accessions

  • Primary accession
    A0A7X7E5N2

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain10-285Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    330
  • Mass (Da)
    35,091
  • Last updated
    2021-06-02 v1
  • MD5 Checksum
    02E8CC6A282C1118114CED904B2E4FBC
MGSVKLTYKKLAILTSGGDAPGMNAAIRSATRTAIHAGWEVIGVTHGFQGLIEGRFIKLGKRDVSGIIQKGGTLLKSSRSIAFKSDEGQEAALSMLKNHDISALVIIGGNGSQKGAYALFQKGFPVVGIASTIDNDLYGSDITLGVDTAMNIALEAIDRIKVTASSHHRAFLVEVMGRNCGYIALMSGIAGGAEAIIIPEVQSSPESLALELRDAYARGKAHAIVVVAEGAYWNAERLIHHFRQFKEQLGFELRETKLGHVQRGGTPGVADRLLGTYFGAFAIEQIESNNFGVLVGKQKGVLTATPLSVVVSSKKELDLSEFKLATILAE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAAZBH010001131
EMBL· GenBank· DDBJ
NLE03018.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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