A0A1Y3QN23 · A0A1Y3QN23_9FIRM

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 site11ATP (UniProtKB | ChEBI)
Binding site21-25ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site72-73ATP (UniProtKB | ChEBI)
Binding site102-105ATP (UniProtKB | ChEBI)
Binding site103Mg2+ (UniProtKB | ChEBI); catalytic
Binding site125-127substrate; ligand shared between dimeric partners; in other chain
Active site127Proton acceptor
Binding site154ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site162substrate; ligand shared between dimeric partners
Binding site169-171substrate; ligand shared between dimeric partners; in other chain
Binding site185-187ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site211ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site213-215ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site222substrate; ligand shared between dimeric partners; in other chain
Binding site247substrate; ligand shared between dimeric partners
Binding site253-256substrate; 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
      BAA04_12425

Organism names

Accessions

  • Primary accession
    A0A1Y3QN23

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-279Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    323
  • Mass (Da)
    34,464
  • Last updated
    2017-08-30 v1
  • Checksum
    47DD3D4B98E83F56
MKRIAVLTSGGDAPGMNAAIRAVVRTGIAAGLEVYGVRNGYAGLINGEIERLTNRDVGGIMQQAGTMLRSARSKEFREEAGRRQAIRKLSERRIDGLVVIGGNGTQTGSYELSKMGFPVVGVASTIDNDLYGTDISIGADTAVNTVLEAIDRIKATASSHSRAFLVEVMGRDTGYIALMAGITGGAEAVIIPEVPIEPDDVLQELKDAYARGKSHAILVVAEGAKPNASQLIEYFREHKADTGFELRLTVLGHVQRGGTPTAFDRMLGTRLGAAAVQALLGGHHGVLVGWVNHRPHVTPLSEVAGRTRYADRELYELARVLAR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LZRQ01000101
EMBL· GenBank· DDBJ
OUM98828.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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