A0A0J2D5M9 · A0A0J2D5M9_ECOLX

  • 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.

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 site126-128substrate; ligand shared between dimeric partners; in other chain
Active site128Proton acceptor
Binding site155ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site163substrate; ligand shared between dimeric partners
Binding site170-172substrate; ligand shared between dimeric partners; in other chain
Binding site186-188ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site212ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site214-216ADP (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site223substrate; ligand shared between dimeric partners; in other chain
Binding site244substrate; ligand shared between dimeric partners
Binding site250-253substrate; 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
      A2J79_002118
      , A5U30_002140
      , AWP47_23085
      , C2M16_15885
      , D3G36_13270
      , F7F11_14740
      , F9413_09565
      , FPI65_24080
      , FZU14_08635
      , GTP92_14795
      , HI055_002792
      , NCTC8603_03995
      , NCTC8621_04957
      , R8G00_17065

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • 93335
    • 700324
    • BCW_4213
    • B8S18Com
    • NCTC8603
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    A0A0J2D5M9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-276Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    320
  • Mass (Da)
    34,856
  • Last updated
    2015-10-14 v1
  • MD5 Checksum
    1849437F91007D95834BAE7EEE5E902B
MIKKIGVLTSGGDAPGMNAAIRGVVRSALTEGLEVMGIYDGYLGLYEDRMVQLDRYSVSDMINRGGTFLGSARFPEFRDENIRAVAIENLKKRGIDALVVIGGDGSYMGAMRLTEMGFPCIGLPGTIDNDIKGTDYTIGFFTALSTVVEAIDRLRDTSSSHQRISVVEVMGRYCGDLTLAAAIAGGCEFVVVPEVEFSREDLVNEIKAGIAKGKKHAIVAITEHMCDVDELAHFIEKETGRETRATVLGHIQRGGSPVPYDRILASRMGAYAIELLLAGYGGRCVGIQNEQLVHHDIIDAIENMKRPFKGDWLDCAKKLY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AASATZ010000016
EMBL· GenBank· DDBJ
EFA4418829.1
EMBL· GenBank· DDBJ
Genomic DNA
AASKVF010000009
EMBL· GenBank· DDBJ
EFD6884283.1
EMBL· GenBank· DDBJ
Genomic DNA
AASWBF010000011
EMBL· GenBank· DDBJ
EFH4960772.1
EMBL· GenBank· DDBJ
Genomic DNA
AATCLQ010000011
EMBL· GenBank· DDBJ
EFJ6481763.1
EMBL· GenBank· DDBJ
Genomic DNA
AATLZG010000012
EMBL· GenBank· DDBJ
EFM8154528.1
EMBL· GenBank· DDBJ
Genomic DNA
AAXDPX010000013
EMBL· GenBank· DDBJ
EGO6679584.1
EMBL· GenBank· DDBJ
Genomic DNA
DABDSA010000015
EMBL· GenBank· DDBJ
HAI2142445.1
EMBL· GenBank· DDBJ
Genomic DNA
VZEL01000014
EMBL· GenBank· DDBJ
KAB0123776.1
EMBL· GenBank· DDBJ
Genomic DNA
JAWPMK010000001
EMBL· GenBank· DDBJ
MDW9351271.1
EMBL· GenBank· DDBJ
Genomic DNA
VLTB01000389
EMBL· GenBank· DDBJ
NDR94286.1
EMBL· GenBank· DDBJ
Genomic DNA
LRKC01000161
EMBL· GenBank· DDBJ
OKV06213.1
EMBL· GenBank· DDBJ
Genomic DNA
PPHQ01000012
EMBL· GenBank· DDBJ
PNY66853.1
EMBL· GenBank· DDBJ
Genomic DNA
UGBW01000003
EMBL· GenBank· DDBJ
STH84840.1
EMBL· GenBank· DDBJ
Genomic DNA
UGEE01000003
EMBL· GenBank· DDBJ
STK92730.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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