G2GY46 · G2GY46_9ENTR

Function

function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.

Caution

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 site12ATP (UniProtKB | ChEBI)
Binding site22-26ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site55-60ADP (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 site127-129substrate; ligand shared between dimeric partners; in other chain
Active site129Proton acceptor
Binding site156ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site164substrate; ligand shared between dimeric partners
Binding site171-173substrate; ligand shared between dimeric partners; in other chain
Binding site187-189ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site213ADP (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 Functiondiphosphate-fructose-6-phosphate 1-phosphotransferase activity
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
      Rin_00006970

Organism names

  • Taxonomic identifier
  • Strain
    • R5.15
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > aphid secondary symbionts > Candidatus Regiella

Accessions

  • Primary accession
    G2GY46

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
    326
  • Mass (Da)
    35,507
  • Last updated
    2011-11-16 v1
  • Checksum
    6B73F0CFFC2F0BF1
MVKKIGVLTSGGDAPGMNAAIRGVVRTALAAGKEVYGIYDGYKGLYEKRGKELDRYSVSDMINRGGTFLGSARFPEFKDKNIRKQAIDNMKSLGIDGLVVIGGDGSYAGADLLTEEGKIPCIGLPGTIDNDVAGTDYTIGFFTALETVVEAIDRLRDTSSSHQRISLVEVMGRHCGDLTLAAAIAGGCEFIIVPEVKFKREELLSEITAGIKKGKRHTIVAITEHVCDINELAKYIEEKTKRETRPTVLGHIQRGGAPVAYDRILASRMGAHAVELLINNSACAEARCVGIQNDKMVNELISICINAENRKRKFKQDWLDTARKLF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AGCA01000155
EMBL· GenBank· DDBJ
EGY29323.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
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