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A0A0J7I9N4 · A0A0J7I9N4_9FLAO

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 site16ATP (UniProtKB | ChEBI)
Binding site26-30ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site77-78ATP (UniProtKB | ChEBI)
Binding site107-110ATP (UniProtKB | ChEBI)
Binding site108Mg2+ (UniProtKB | ChEBI); catalytic
Binding site131-133substrate; ligand shared between dimeric partners; in other chain
Active site133Proton acceptor
Binding site160ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site168substrate; ligand shared between dimeric partners
Binding site175-177substrate; ligand shared between dimeric partners; in other chain
Binding site219-221ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site228substrate; ligand shared between dimeric partners; in other chain
Binding site252substrate; ligand shared between dimeric partners
Binding site258-261substrate; 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
      ACM40_09760

Organism names

  • Taxonomic identifier
  • Strain
    • BLS98
  • Taxonomic lineage
    Bacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Weeksellaceae > Chryseobacterium group > Chryseobacterium

Accessions

  • Primary accession
    A0A0J7I9N4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain8-281Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    328
  • Mass (Da)
    35,427
  • Last updated
    2015-10-14 v1
  • MD5 Checksum
    8662B19E2CEEA2707603F2ADE2C4AE9B
MKESAVKKIAVLTSGGDSPGMNAALRAVVRTANYYNIECYGVREGYNGLINDDFLKMGPRSVKNIINQGGTILKSARSVEFRTPEGRKKAYDNCVKHGVDALVCIGGDGTFTGAKIFNEEFGIRVIGVPGTIDNDIFGTDNTIGYDTALNTAMEAIDKVRDTATSHNRVFFVEVMGRDAGFIALNSGLATGALDILIPEKKDSMQDLFANFRKAEKTGKASSIVVVAEGEKLGSIYDLANQTKEEFPDYDIRVTILGHIQRGGSPSCADRVLASRLGYGAVVGLMEGKTNVMAGMRSNDLVYTPIEEAIKKHNEINKDLLLISEILAI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LFNF01000002
EMBL· GenBank· DDBJ
KMQ62556.1
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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