A0A7C9HFA0 · A0A7C9HFA0_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 site14ATP (UniProtKB | ChEBI)
Binding site24-28ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site75-76ATP (UniProtKB | ChEBI)
Binding site105-108ATP (UniProtKB | ChEBI)
Binding site106Mg2+ (UniProtKB | ChEBI); catalytic
Binding site129-131substrate; ligand shared between dimeric partners; in other chain
Active site131Proton acceptor
Binding site158ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site166substrate; ligand shared between dimeric partners
Binding site173-175substrate; ligand shared between dimeric partners; in other chain
Binding site189-191ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site215ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site217-219ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site226substrate; ligand shared between dimeric partners; in other chain
Binding site249substrate; ligand shared between dimeric partners
Binding site255-258substrate; 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
      F0475_10860

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • A2879
  • Taxonomic lineage
    Bacteria > Bacteroidota > Bacteroidia > Bacteroidales > Prevotellaceae > Prevotella

Accessions

  • Primary accession
    A0A7C9HFA0

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-281Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    325
  • Mass (Da)
    35,144
  • Last updated
    2021-02-10 v1
  • Checksum
    924F83283051D803
MARIKTIGILTSGGDAPGMNAAIRAVTRAGIYNGFNIKAVYRGYDGLITNDIRPFTTENVSGIIGQGGTILKTARSKGFATVEGRQTAYDNLVAEGIDALVVIGGNGSLTGAMKFAQEHDFCCIGLPGTIDNDLYGTDSTIGYDTTMNTIMECVDRIRDTAQSHERIFFVEVMGRDAGFLAQNSAIASGAEAAIIPEDSTDVDQLARFMERGIRKSKRSCIVIVSESPKCGAMYYADRVHKEFPDYDVRVSILGHLQRGGRPSARDRILASCTGVGAVEAIMQGQRNIMVGVRNNEVVYVPLSEAIRSDKPFDRKLIKVLDELSI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VVIQ01000014
EMBL· GenBank· DDBJ
MUL28785.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help