B2AT75 · B2AT75_PODAN

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, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.

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 site78ATP (UniProtKB | ChEBI)
Binding site141-142ATP (UniProtKB | ChEBI)
Binding site171-174ATP (UniProtKB | ChEBI)
Binding site172Mg2+ (UniProtKB | ChEBI); catalytic
Binding site217-219substrate; ligand shared between dimeric partners; in other chain
Active site219Proton acceptor
Binding site254substrate; ligand shared between dimeric partners
Binding site261-263substrate; ligand shared between dimeric partners; in other chain
Binding site317substrate; ligand shared between dimeric partners; in other chain
Binding site347substrate; ligand shared between dimeric partners
Binding site353-356substrate; ligand shared between dimeric partners; in other chain
Binding site536beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site594-598beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site632beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site639-641beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site699beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site725beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site731-734beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site803beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Component6-phosphofructokinase complex
Cellular Componentmembrane
Cellular Componentmitochondrion
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

    • ORF names
      PODANS_1_14910

Organism names

Accessions

  • Primary accession
    B2AT75

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane9-28Helical

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-445N-terminal catalytic PFK domain 1
Domain70-378Phosphofructokinase
Domain461-756Phosphofructokinase
Region461-848C-terminal regulatory PFK domain 2

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    848
  • Mass (Da)
    93,016
  • Last updated
    2008-05-20 v1
  • Checksum
    ECE40892D2B8A31A
MPLPDTRFLLRPFSIVIYPIWTLLAFFYRHSPLRFLSSTLQPLFGLRNTTDIDPETPEPTSTTNMSAKKKIAIMTSGGDSPGMNGVVRACVRMAIHMGCDAYCIYEGYEGLVRGGDLIRKMNWYDVRGWLSEGGTLIGTARCMAFFERAGRLAAAKNMILHGIDALIICGGDGSLTGADRFRAEWPSLLDELAANGEFTTQELQPFRHLNIVGLVGSIDNDLSGTDATIGCYSALARICYAVDLIEATASSHSRAFVVEVMGRHCGWLALMAGVATGADFIFIPEKPREDNWREEMCSIVEHHRKIGKRKTIVIIAEGALDREGNKITPAMVKDLLADKDGLGLDTRITTLGHVQRGGTAVAYDRMLATLQGVEAVKAVLEATPETKTCVIAITENKIVRKPLMDAVQDTKKVAKAIERQDFEEAMGLRDAEFSEQYKSFMMTTAVQVDKELLLPEKERMRIGFINVGAPAGGMNAAVRAGVAYCLSRGHEPMAIYNGFAGFARHHADNPGAVRPFNWLEVDGWASKGGSEIGTNRELPGESGMETIANLIEQYKFDALFLIGGFEAFHAVSQLRKARDQYPSLCIPMTLLPATISNNVPGTEYSLGSDTCLNELVEYCDKIKQSASATRRRVFVIETQGGRSGYVATLGGLGVGASAVYTPEEGVSLDMLAADVRHLKNVFAHDQGQSRAGRLILINEKASKVYNAKLIADILREESHGRFESREGIPGHMQQGGVPSPMDRCRAVRLAIRCIQHLEQFGRNVHNRVKVDPMSTTVIGIKGASVVFTPVKQVEEEETDWPNRRPKAAYWLGMKEIVDILGGRPKYELPESDLTGIKAKDVKRGIVPP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CU633899
EMBL· GenBank· DDBJ
CAP67598.1
EMBL· GenBank· DDBJ
Genomic DNA
FO904936
EMBL· GenBank· DDBJ
CDP23859.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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