A0AAE0JPJ4 · A0AAE0JPJ4_9PEZI

  • Protein
    ATP-dependent 6-phosphofructokinase
  • 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.

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.

Type
IDPosition(s)Description
Binding site73ATP (UniProtKB | ChEBI)
Binding site136-137ATP (UniProtKB | ChEBI)
Binding site166-169ATP (UniProtKB | ChEBI)
Binding site167Mg2+ (UniProtKB | ChEBI); catalytic
Binding site212-214substrate; ligand shared between dimeric partners; in other chain
Active site214Proton acceptor
Binding site249substrate; ligand shared between dimeric partners
Binding site256-258substrate; ligand shared between dimeric partners; in other chain
Binding site312substrate; 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 site531beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site589-593beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site627beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site634-636beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site694beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site720beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site726-729beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site798beta-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
      B0H65DRAFT_44175

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CBS 560.94
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Sordariales > Sordariaceae > Neurospora

Accessions

  • Primary accession
    A0AAE0JPJ4

Proteomes

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane20-40Helical

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-440N-terminal catalytic PFK domain 1
Domain65-373Phosphofructokinase
Domain456-751Phosphofructokinase
Region456-844C-terminal regulatory PFK domain 2

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    844
  • Mass (Da)
    91,956
  • Last updated
    2024-05-29 v1
  • Checksum
    DB0FAC8E7266C25C
MPIFDRAILSRPLSILYNPFPALFALVLLSASSLGIRLLLSSTTPRKVLPTKMSPASNKMAPRKKIAIMTSGGDSPGMNAVVRACVRMAIHMGCDAYCVYEGYEGLVRGGDLIKKMDWYDVRGWLSEGGTLIGTARCMAFYERAGRLTAAKNLILSGIDALIICGGDGSLTGADRFRAEWPSLLEELVSTGELTAEQIHSYKHLNIVGIVGSIDNDLSGTDATVGCYSALARICMCVDMIEATASSHSRAFVVEVMGRHCGWLALMAGVATGADFIFIPEKPREDNWREEMCGVVQEHRKRGKRKTIVIIAEGALDKFGNKITPEQVRDLLADKNGLALDTRITTLGHVQRGGTAVAYDRMLATLQGVEAVKAVLEATPETKTCFIAITENKIVRKPLMEAVLDTKQVAKAIESQDFDGAIGLRDAEFGEQYKSFMMTTAGQIDHEKMLPVKERMKIGFINVGAPAGGMNAAVRAGVSYCLSRGHEPIAIHNGFAGFARHHADTPSAVRPFDWLEVDGWASKGGSEIGTNRELPSESGMETIANLIEQYQFDALFLIGGFEAFHAVAEMRKARDQYPSLCIPMALLPATISNNVPGTEYSLGSDTCLNELVDYCDKIKQSASATRRRVFVIETQGGRSGYIATLAGLGVGASAVYLPEEGLSLEMLSEDVRHLKEVFAQDKGQSRAGRLILINEKASKVYSAKLIADILRDEAHGRFESREGIPGHMQQGGVPSGMDRCRAVRLAIKCIQQLEKYGRNVHNRVKMDPMSASVIGIKGASVVFTPVQKLEEEETDWPNRRPKAAHWLSMKEIVDILGGRPRHTLPEPDLTGVKAKDVKRGLEPVN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAUEPP010000001
EMBL· GenBank· DDBJ
KAK3355331.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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