A0A1I4YQ97 · A0A1I4YQ97_9FLAO

  • 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.

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 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 site191-193ADP (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
      SAMN04487989_101201

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 23925
  • Taxonomic lineage
    Bacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Flavobacteriaceae > Bizionia

Accessions

  • Primary accession
    A0A1I4YQ97

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-280Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    324
  • Mass (Da)
    35,049
  • Last updated
    2017-11-22 v1
  • Checksum
    5FD31AC609816F5B
MSTNKTKHIGVFTSGGDSPGMNAALYAIAKSAEVKNIKVSGFRKGYEGLIDGDLMPLKSHELKKITQKGGTILKTARSKRFLELEGRKKALQTLKTNNIDALIAIGGDGTFKGLLAFSEICDIPFIGIPGTIDNDISGTDYTLGFDSAVNTAIENIDKIKDTAESHNRVFIVEVMGRDSGYIAIHSGLMVGADAILIPESGKDFIYLLDKVKNYNSEDAFLVVVSEGDELGAELISSKIKEINSNVDLRITKLGHVQRGGNPSALDRMLGIRLGVASINALSQGKKNAMVGVLNNQLHLTPFKEVVKQHQVNTELYELLELFGK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FOVN01000001
EMBL· GenBank· DDBJ
SFN40181.1
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