A0A9Q5I2V3 · A0A9Q5I2V3_SANBA

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, 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 site15ATP (UniProtKB | ChEBI)
Binding site137-138ATP (UniProtKB | ChEBI)
Binding site167-170ATP (UniProtKB | ChEBI)
Binding site168Mg2+ (UniProtKB | ChEBI); catalytic
Binding site213-215substrate; ligand shared between dimeric partners; in other chain
Active site215Proton acceptor
Binding site250substrate; ligand shared between dimeric partners
Binding site257-259substrate; ligand shared between dimeric partners; in other chain
Binding site314substrate; ligand shared between dimeric partners; in other chain
Binding site342substrate; ligand shared between dimeric partners
Binding site348-351substrate; ligand shared between dimeric partners; in other chain
Binding site523beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site580-584beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site618beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site625-627beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site685beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site711beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site792beta-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 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
      A7U60_g2287

Organism names

Accessions

  • Primary accession
    A0A9Q5I2V3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-440N-terminal catalytic PFK domain 1
Domain7-56Phosphofructokinase
Domain113-374Phosphofructokinase
Domain454-742Phosphofructokinase
Region454-826C-terminal regulatory PFK domain 2

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    826
  • Mass (Da)
    90,842
  • Last updated
    2023-09-13 v1
  • Checksum
    C9ABC0765257C237
MSKIKRKIAVLTSGGDSAGMNACVRAVVKYGIIRGCEVYVVREGYEGLVRGNVDAPKRKVAFNDSNNDKHHHGDDSAEDKLINNLRFGDGNLLKEGEGDAIEHPGGRSLKGRYIIRVGWDDVRAWFAEGGTLIGTARSAAFRTKEGRLAAANNLITEGIDSIVVCGGDGSLTGADVFRAEWPSLVNELRQSNTITSEQAERYAHLNIAGTVGSIDNDMSMTDITIGAYTALHRICESIDNINSTAFSHSRAFVVEVMGRHCGWLALMAGVSAGADFIFIPERPPVADPWEDDMCKNIQNHRDIGKRKTIVIVAEGAIDANLNPIRAEYVKDVLTERLGLDTRVTCLGHTQRGGRPCAYDRLLPTMQGVEAVDALLESTPESPSYMIAIHENKISRVPLVEAVAQTRAVAKAISEKDFERAMSYRDPEFREMLDGFVAVSSLDYTKKLPKEQRMRVAIINMGAPAGGMNAATRTATRYCIRRGHKPIAIYNGFRGLLEDNVEDLSWLRVDNWMTRGGSELGTNRTLPDIDLGAVASQFQKHRFDAFFLIGGFEAFRSLQILEEARGLYPAFHIPMVCVPATISNNVPVTDYSLGCDTSLNALVEACDAIKQSASASRNRVFVVETQGGKCGYIATMGALATGAVCYYTPEDGITLDGLRKDVEFLKLRYSLDEKGKAEGRLILRNEASSNVFTTDFIQKMLQEEGGSLFDSRMASLGHTLQGGIPSPMDRARAVRFSLKCMAFLERHHISLLAQPELKRKAPEESAAVITIQRNEVGFTPVKCMLARADVKNRRGNKTWWEEYKPMVSMLGGRTALVEEEVDPKLKK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LNZH02000128
EMBL· GenBank· DDBJ
OCB90494.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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