A0A061H3R4 · A0A061H3R4_9BASI

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.

Type
IDPosition(s)Description
Binding site20ATP (UniProtKB | ChEBI)
Binding site168-169ATP (UniProtKB | ChEBI)
Binding site198-201ATP (UniProtKB | ChEBI)
Binding site199Mg2+ (UniProtKB | ChEBI); catalytic
Binding site244-246substrate; ligand shared between dimeric partners; in other chain
Active site246Proton acceptor
Binding site281substrate; ligand shared between dimeric partners
Binding site288-290substrate; ligand shared between dimeric partners; in other chain
Binding site346substrate; ligand shared between dimeric partners; in other chain
Binding site374substrate; ligand shared between dimeric partners
Binding site380-383substrate; ligand shared between dimeric partners; in other chain
Binding site555beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site612-616beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site650beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site657-659beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site717beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site743beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site836beta-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
      PFL1_05832

Organism names

  • Taxonomic identifier
  • Strain
    • PF-1
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Ustilaginomycotina > Ustilaginomycetes > Ustilaginales > Ustilaginaceae > Pseudozyma

Accessions

  • Primary accession
    A0A061H3R4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-20Disordered
Region1-472N-terminal catalytic PFK domain 1
Domain12-58Phosphofructokinase
Domain143-405Phosphofructokinase
Domain486-775Phosphofructokinase
Region486-862C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    862
  • Mass (Da)
    92,906
  • Last updated
    2014-09-03 v1
  • Checksum
    45EC1434C537ED40
MASSSSAAPPRRLAVMTSGGDSAGMNAAVRAVVKMAIFRGCEAFVIREGWEGLVRGNHSPDGTPITTPALSRNNSGFFDSLDPRGRVDQQFGGAAQHGEAVAATAAAAAASTTVEGQFVPTYGEGEALREGVGEAQELGLRGRYIIRVGWDDVRGWMDQGGTLIGTARCKEFRTVEGREKAAYNLIVNGIDALAVCGGDGSLTGADRLRAEWPDLVASLLQKGRITDEQATRYAHLNIVGLVGSIDNDMATTDITIGASTALQRICESIDSISSTAASHSRAFVVEVMGRHCGWLAVMAGIATGADYIFIPEQPPQRGDHWSSEMCDVLRRHRELGKRKSIVIIAEGAHDRDLNEIKPEMVKDVLTHELGLDTRVTTLGHTQRGGKPDANDRILATLQGVEAVNAVLEATPETPSYVIGMTENKVTRIPLMHAVEQTQRVAAEIEAKNFDAALALRDPEFEEGLRAFKIISQITEANRLPADQRLRIGIIHIGAPAGGMNAATRTMVRYCLDRGHEPVVIYNGFNGLLEDNVSVLSWLRVDNWATRGGSELGVNRNLPDIDLGAVAAKFQQHRIEALLMIGGFEAFMSVKILDDNRERYPAFRMPIVALPATISNNVPMNEFSLGSDTSLNALVDACDAVKQSASASRNRVFVVETQGGRCGYIAVAGALAAGAVLVYTPEQGIGLQQLGKDVEFLKKRFALDVKGKSEGRLVIRNEKSSEVFTTEVITKILKEEGASLFDSRSASLGHTLQGGTPSPLDRIRATRLALKCCQFLEAKALESRRRTRRQQPGGSKADADGAAAYSDDTAVMITIQGAKICFATVKEMAKHADMKNRRAKKAWWHDLKALVELMGGRTGLGNL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KE361644
EMBL· GenBank· DDBJ
EPQ26510.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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