A0A166M9H0 · A0A166M9H0_9AGAM

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 site16ATP (UniProtKB | ChEBI)
Binding site132-133ATP (UniProtKB | ChEBI)
Binding site162-165ATP (UniProtKB | ChEBI)
Binding site163Mg2+ (UniProtKB | ChEBI); catalytic
Binding site208-210substrate; ligand shared between dimeric partners; in other chain
Active site210Proton acceptor
Binding site245substrate; ligand shared between dimeric partners
Binding site252-254substrate; ligand shared between dimeric partners; in other chain
Binding site312substrate; ligand shared between dimeric partners; in other chain
Binding site340substrate; ligand shared between dimeric partners
Binding site346-349substrate; ligand shared between dimeric partners; in other chain
Binding site521beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site578-582beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site616beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site623-625beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site683beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site709beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site790beta-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
      FIBSPDRAFT_822899

Organism names

  • Taxonomic identifier
  • Strain
    • CBS 109695
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Atheliales > Atheliaceae > Fibularhizoctonia

Accessions

  • Primary accession
    A0A166M9H0

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-438N-terminal catalytic PFK domain 1
Domain8-372Phosphofructokinase
Domain452-741Phosphofructokinase
Region452-816C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    816
  • Mass (Da)
    88,178
  • Last updated
    2016-07-06 v1
  • Checksum
    3F55D838D62DDBA4
MADQGNIRLAVLTSGGDSAGMNGVVRAVVKAGILKGCETYIVREGYEGLVRGNGEGHHSKPGSPILASGHIIKDTDPTLVHNLRFGDGDLLKDGTGDYQSARSLKGRYIVRVGWDDVRGWLAEGGTLIGTARSAAFRTPEGRLAAANNLIKEGIDCLAVCGGDGSLTGADVFRSEWPKLVDDLLNAGKITKDQATKHGHLKIVGLVGSIDNDMSMTDLTIGAPTALHRICEAIDNINSTAASHSRAFVLEVMGRYCGWLALLAGVAQVFGGADFIFIPERPPVGDPWEDEMCQAIQRHREVGKRKTIVIVSEGAHDSKLNPIRAEHVKDILTERLGLDTRVTTLGHTQRGGRPCAFDRILPTLQGVEAVNALLEATPDTPSYMIGISENKITRVPLMEAVAMTKAVAEAISAKDFAKAMELRDPEFAESLEGFISTSTLSQDKRLPKNQRIRVAIMHTGAPAGGMNAATRAAVRYCIRQGHHPLAVHNGFRGLLDDSIHELSWLGVDNWMARGGSELGTNRTLPDIDLGAVAAKFQQHNVQALLMIGGFEAFTSLSIMEQGRKHYPAFHIPMVHLPATISNNVPMTEFSLGSDTSLNALVDACDAIKQSASASRNRVFVVETQGGKCGYVATMGALATGASLVYTPEVGMNLDMLRSDVKFLKNRYGVDVKGKSEGRLVIRNEQASSVYTTEFITKMLKEEGGELFDARSASLGHTLQGGVPSPMDRARAVRLSLKCMSFIEKEYDIIHKQKSKTKIASPHSAAIITIQGSSIKWVPVKEMLEHADLKNRRGKTQWWTEYKGLAEALAGLPQLTDL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KV417530
EMBL· GenBank· DDBJ
KZP23770.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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