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A0A0L0N6Y1 · A0A0L0N6Y1_TOLOC

Function

function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.

Caution

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.

Type
IDPosition(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 site349substrate; ligand shared between dimeric partners
Binding site355-358substrate; ligand shared between dimeric partners; in other chain
Binding site538beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site596-600beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site634beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site641-643beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site701beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site727beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site733-736beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site805beta-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
      TOPH_05559

Organism names

Accessions

  • Primary accession
    A0A0L0N6Y1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-447N-terminal catalytic PFK domain 1
Domain70-380Phosphofructokinase
Region448-461Interdomain linker
Domain462-758Phosphofructokinase
Region462-848C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    848
  • Mass (Da)
    92,177
  • Last updated
    2015-11-11 v1
  • MD5 Checksum
    630BA4DF0287E98BADCF1270BC97B6D2
MPVTSYLQLLSRPVDILLASFRSIVSSSVWPAPFPGLGSSANRTATPLPPSSSKGTTTATTTAAMAPKKKIAVMTSGGDSPGMNAVVRAVVRMTIHMGCDAFAVYEGYEGLVRGGDYIRKMDWNDVRGWLSEGGTLIGTARCMAFYERPGRMAAAKNMVLHGIDALIICGGDGSLTGADRFRSEWPSLLDELVSRGELSADQVAPYMNLNIVGIVGSIDNDLSGTDATVGCYSALSRICEMVDYIEATASSHSRAFVIEVMGRHCGWLXLLAGVATGADFVFIPERPQDHDWRKDMSVVVTRHRKMGKRKTIVIVAEGARDKNGDSIRPEEIKHLLADKSEGGLGLDTRITTLGHVQRGGTAVAYDRMLGTLQGVEAVKAVLEATPETETCFIAINENKIVRKPLMKAVQETKELAAAVDAKDFERAMSLRDAEFADQYNSYITTTNVLVDDHKLPDKSRMKIGFINVGAPAGGMNAAVRAAVAYCISRGHEPIAIHNGFAGFARHHDDKPLGSVRPFDWLEVDGWASKGGSEIGTNRELPSESGMDLIANLIEQYEFDALFIVGGFEAFHSVSQLRKARDQYPSLCIPICLLPATISNNVPGTEYSLGSDTCLNELVNYCDKIKQSASATRRRVFVIETQGGRSGYIATLSGLNVGASAVYIPEEGISLEMLNTDVMHLKKVFKNDSGQSRAGRLILVNEKASKVYDAKLIASIIREEAHDRFESRESIPGHVQQGGVPSPMDRCRSVRLAIKCIQHLEDFGRNAHNRVKKDPNSTTVIGIQGSEVVFTPMKALEEQGTDWPNRRPKAAHWLGLRDVVDILGGRPDYPRPEKSLTGLIAKDTKRGIV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LFRF01000016
EMBL· GenBank· DDBJ
KND89873.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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