A0A5I3TR16 · A0A5I3TR16_SALET

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.

TypeIDPosition(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
      APM01_18680
      , BFV08_20450
      , DM677_17315
      , DN927_11365
      , DOG83_09560
      , DPE57_12445
      , DQK10_20425
      , DU046_20210
      , DYS13_13750
      , DYT81_04860
      , E5908_17565
      , EJO80_22485
      , EWI81_06660
      , G4R07_004037

Organism names

  • Taxonomic identifier
  • Strains
    • 146074
    • 275776
    • 298956
    • M210
    • FSIS11811772
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella

Accessions

  • Primary accession
    A0A5I3TR16

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-276Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    320
  • Mass (Da)
    34,915
  • Last updated
    2019-12-11 v1
  • Checksum
    68B0DDFCF689F420
MIKKIGVLTSGGDAPGMNAAIRGVVRAALTEGLEVMGIYDGYLGLYEDRMVQLDRYSVSDMINRGGTFLGSARFPEFRDENIRAVAIENLKKRGIDALVVIGGDGSYMGAKRLTEMGFPCIGLPGTIDNDIKGTDYTIGYFTALGTVVEAIDRLRDTSSSHQRISIVEVMGRYCGDLTLAAAIAGGCEFIVVPEVEFNREDLVAEIKAGIAKGKKHAIVAITEHMCDVDELAHFIEKETGRETRATVLGHIQRGGSPVPYDRILASRMGAYAIDLLLEGHGGRCVGIQNEQLVHHDIIDAIENMKRPFKSDWMECAKKLY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAGVGK010000011
EMBL· GenBank· DDBJ
EBS3932693.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHDUY010000014
EMBL· GenBank· DDBJ
EBU9894877.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHXHM010000009
EMBL· GenBank· DDBJ
ECB3376635.1
EMBL· GenBank· DDBJ
Genomic DNA
AAHYZU010000016
EMBL· GenBank· DDBJ
ECB8846429.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKIXE010000015
EMBL· GenBank· DDBJ
ECS2230324.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKLKV010000012
EMBL· GenBank· DDBJ
ECT0132628.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKLWJ010000080
EMBL· GenBank· DDBJ
ECT1544736.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKMFT010000010
EMBL· GenBank· DDBJ
ECT2690384.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKNWZ010000009
EMBL· GenBank· DDBJ
ECT7929716.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKSPP010000023
EMBL· GenBank· DDBJ
ECV1597875.1
EMBL· GenBank· DDBJ
Genomic DNA
AAKSBI010000011
EMBL· GenBank· DDBJ
ECV3388902.1
EMBL· GenBank· DDBJ
Genomic DNA
DAATIJ010000012
EMBL· GenBank· DDBJ
HAE8738827.1
EMBL· GenBank· DDBJ
Genomic DNA
RVCL01000015
EMBL· GenBank· DDBJ
MLO07005.1
EMBL· GenBank· DDBJ
Genomic DNA
CP068783
EMBL· GenBank· DDBJ
QRA26669.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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