A0A093Y889 · A0A093Y889_9PEZI

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 site31ATP (UniProtKB | ChEBI)
Binding site94-95ATP (UniProtKB | ChEBI)
Binding site124-127ATP (UniProtKB | ChEBI)
Binding site125Mg2+ (UniProtKB | ChEBI); catalytic
Binding site170-172substrate; ligand shared between dimeric partners; in other chain
Active site172Proton acceptor
Binding site207substrate; ligand shared between dimeric partners
Binding site214-216substrate; ligand shared between dimeric partners; in other chain
Binding site270substrate; ligand shared between dimeric partners; in other chain
Binding site300substrate; ligand shared between dimeric partners
Binding site306-309substrate; ligand shared between dimeric partners; in other chain
Binding site490beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site548-552beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site586beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site593-595beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site653beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site679beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site685-688beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site757beta-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
      V490_03985

Organism names

  • Taxonomic identifier
  • Strain
    • VKM F-3557
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Thelebolales > Thelebolaceae > Pseudogymnoascus

Accessions

  • Primary accession
    A0A093Y889

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain, compositional bias.

Type
IDPosition(s)Description
Region1-398N-terminal catalytic PFK domain 1
Domain23-331Phosphofructokinase
Domain414-710Phosphofructokinase
Region414-804C-terminal regulatory PFK domain 2
Region776-804Disordered
Compositional bias779-804Basic and acidic residues

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    804
  • Mass (Da)
    87,292
  • Last updated
    2014-11-26 v1
  • Checksum
    7DA056F87EE2C0BB
MGMLDPRPNGQKAELLPNGKRRKIAMMTSGGDAPGMNGAVRAVVRSAIDEGFDAYCIYEGYEGLVQGGDLIKQMSWGDVRGWLSEGGTLIGTARCKAFYERPGRLKAAKNMVLNGIDSLIICGGDGSLTGADKFRFEWPSLLEELVQTKELTAEEIKPFMHLTIVGLVGSIDNDMSGTDVTIGCFSALARICEMVDYIEATASSHSRAFVIEVMGRHCGWLALMAGVATGADFVFIPEKPRADNWREEMCTIIAKHRGVGKRKTIVIMAEGANDQQGNKITPEQVKDLLADPKGLALDTRITTLGHVQRGGQACSFDRTLATLQGVEAVRAVLDAKPDTPTCFIAINENKIVRKPLMQAVRDTQEVAKAIQARDFDRAMGLRDTEFAEIYASYLITTATSLDKAMHLPAEKCMRIGIIHVGAPAGGMNSATRAAVAYCQTRGHTPVGIYNGFAGFTRHHGDTPLGAVRDFDWLEVDGWASKGGSEIGTNRELPGESGMATVAELIAKYKIDAIFMVGGFEAFHAMSQLRKAKKEFPQLAIPMTLLPATISNNVPGTEYSLGSDTCLNELVRYCDTIKQSASASRRRVFVIETQGGRCGYVPVLAGLNVGATAVYTPEEGISIDMLAADIRHLRKAFAEDSGQSRAGRLLLVGEKASSVYSAKLIADIIRTEAHGRFESRDSIPGHVQQGGTPSPMDRIRAVRLSIKCMEHLEKFANASKQEIIDDALSSSVIGIRGASVTFTSMEHVEEKETDWANRRPLEVFWADIEPVVDTLSGRPEIPRPEPDLKGQRAKDIKRGLVRGPV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias779-804Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JPJS01001075
EMBL· GenBank· DDBJ
KFX95179.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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