A0A4R0RCS1 · A0A4R0RCS1_9APHY

  • Protein
    ATP-dependent 6-phosphofructokinase
  • Gene
    PFK1
  • 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.

TypeIDPosition(s)Description
Binding site19ATP (UniProtKB | ChEBI)
Binding site140-141ATP (UniProtKB | ChEBI)
Binding site170-173ATP (UniProtKB | ChEBI)
Binding site171Mg2+ (UniProtKB | ChEBI); catalytic
Binding site216-218substrate; ligand shared between dimeric partners; in other chain
Active site218Proton acceptor
Binding site253substrate; ligand shared between dimeric partners
Binding site260-262substrate; ligand shared between dimeric partners; in other chain
Binding site317substrate; ligand shared between dimeric partners; in other chain
Binding site345substrate; ligand shared between dimeric partners
Binding site351-354substrate; ligand shared between dimeric partners; in other chain
Binding site526beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site583-587beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site621beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site628-630beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site688beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site714beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site797beta-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

    • Name
      PFK1
    • ORF names
      EIP91_003597

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • LE-BIN_3174
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Polyporales > Steccherinaceae > Steccherinum

Accessions

  • Primary accession
    A0A4R0RCS1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-443N-terminal catalytic PFK domain 1
Domain11-377Phosphofructokinase
Domain457-746Phosphofructokinase
Region457-831C-terminal regulatory PFK domain 2

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    831
  • Mass (Da)
    90,819
  • Last updated
    2019-07-31 v1
  • Checksum
    DE7A2D6F51019302
MTEAPRVHKLRLAVLTSGGDSAGMNAVVRAIVKTAILKGCETYVVREGYEGLVRGNSEAVSVASPPREHNHHQRKESLLVEGDADSFVHNLRFGDGELLRDGTSDHPAGRTLKGRYIVRVGWDDVRGWFTSGGTLIGTARSVAFRTYEGRLTAAHNLIKEGIDAIAVCGGDGSLTGADVFRAEWPKLVAELASTSRITEEQHKAHAHLRIVGLVGSIDNDMSMTDLTIGAPTALHRICEAIDNIDSTASSHSRAFVLEVMGRHCGWLALLAGVSGGADFIFIPERPPEADPWEDEMCRNIQRHREIGKRKTIVIVAEGAHDKHLTPIRADYVKEVLSERLGLDTRVTTLGHTQRGGRPCAFDRILPTLQGVEAVDALLEATPDTPSYMIGIAENKITRVPLMEAVKMTNEVTQAIKDKDFDKAMSLRDPEFRESLDGFYATSILEKEPRLPHHQRMRVAIMHVGAPAGGMNAATRAAVRYCIRQGHKPFAIHNGFPGLLDDNVHQLSWLGVDNWMTRGGSELGTNRKLPEVDMGAIAAKFQQYNFHALMMIGGFEAFTSLLSLENARKYYPAFHIPLVHLPATISNNVPLTEFSLGSDTSLNALVDACDAIKQSASASRNRVFVVETQGGKCGYIATMGALATGACMVYTPETGIDLDMLRNDVKFLKKRFSLDVKGRAEGRLVIKNEVASAVYTTDVITKMFKEEGGKLFDARSASLGHTLQGGIPSPIDRARAVRLSLKCMTFIEEQHAILLKQSSSGKTRQAAPDSAAVITIQGSNVIWVPVQDVVPHADMENRRGLHEHWKPIIGLVEALVARPQILEKARPGKILD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
RWJN01000213
EMBL· GenBank· DDBJ
TCD64816.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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