A0A1Y3QJW4 · A0A1Y3QJW4_9BACL

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 site128-130substrate; ligand shared between dimeric partners; in other chain
Active site130Proton acceptor
Binding site157ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site165substrate; ligand shared between dimeric partners
Binding site172-174substrate; ligand shared between dimeric partners; in other chain
Binding site188-190ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site214ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site216-218ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site225substrate; ligand shared between dimeric partners; in other chain
Binding site246substrate; ligand shared between dimeric partners
Binding site252-255substrate; 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
      BAA02_10795

Organism names

Accessions

  • Primary accession
    A0A1Y3QJW4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain6-276Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    322
  • Mass (Da)
    34,694
  • Last updated
    2017-08-30 v1
  • Checksum
    7884F2390622076D
MAAVKRIAVLTSGGDSQGMNAAVRAVVRSGLVHGLEVYGIQRGYQGLLNGEIREMDLRSVGDILQRGGTILQTARCQEFMTPEGQRRGAEMLRKHNIDALVVIGGDGSYRGAQKLNELGIRTMGLPGTIDNDIAFTDFTIGFDTAVSIVVDAINKLRDTMTSHERTSVVEVMGRHCGHIALYAGLASGAEVILVPEVPFDLREIAAKLRESAEKGKRHSIIVVAEGAGKGEEVAKKLTEFCGIEPRTTVLGHIQRGGSPTHNDRILASRLGDFAVRRLIAGDSGKACGVIKGELVATDFDIVVNTKKPFDMELYELAMRLSQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LZRV01000054
EMBL· GenBank· DDBJ
OUM99961.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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