A0A6A5U354 · A0A6A5U354_9PLEO

  • 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.

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 site23ATP (UniProtKB | ChEBI)
Binding site86-87ATP (UniProtKB | ChEBI)
Binding site116-119ATP (UniProtKB | ChEBI)
Binding site117Mg2+ (UniProtKB | ChEBI); catalytic
Binding site162-164substrate; ligand shared between dimeric partners; in other chain
Active site164Proton acceptor
Binding site199substrate; ligand shared between dimeric partners
Binding site206-208substrate; ligand shared between dimeric partners; in other chain
Binding site262substrate; ligand shared between dimeric partners; in other chain
Binding site307substrate; ligand shared between dimeric partners
Binding site313-316substrate; ligand shared between dimeric partners; in other chain
Binding site496beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site553-557beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site591beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site598-600beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site658beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site684beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site690-693beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site762beta-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
      CC80DRAFT_501768

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CBS 675.92
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Pleosporomycetidae > Pleosporales > Massarineae > Massarinaceae > Byssothecium

Accessions

  • Primary accession
    A0A6A5U354

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-405N-terminal catalytic PFK domain 1
Domain15-338Phosphofructokinase
Region406-419Interdomain linker
Domain420-715Phosphofructokinase
Region420-801C-terminal regulatory PFK domain 2
Region782-801Disordered

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    801
  • Mass (Da)
    87,889
  • Last updated
    2020-06-17 v1
  • Checksum
    9DD786799881AB77
MAPTPPPPLEGKRRRIAVMTSGGDAPGMNGAVRAVVRMALHQKCDAFAIYEGYDGLVKGGDMIKEMKWEDVRGFLSEGGTLIGTARCKEFMERDGRRKAAKNMIVKGIDALVICGGDGSLTGADKFRGEWPELLNELVQAKELTHEQIQPFKHLNIVGLVGSIDNDLSMTDATIGCYSSLARICEAIDSVDTTATSHQRAFVVETMGRHCGWLTLMAGVATGSDFIFIPEQPAQNGWQEEMLATIRKHRSLGKRKTIVIVAEGVSSAHTSPFFESWLTFYTIDADLNPITPSQIKDILTNEAHLDTRVTTLGHVQRGGQPAAYDRMLSTLQGVEAVKAVLEATPDTPSPVICMIENKIVRRPLLEAVAQTKKVAEAIAQKDFQTAMTLRNAEFAEYFRSYQITTSSDQPELMLPEEKRMRIGIIHVGAPAGGMNAATRAAVAYCLARGHTPIALHNGFPGLIRHHSDEPIGAVREIKWLDAEGWANKGGSEIGTNRGLPSEDLETVAFVFKKYNIQSLFVVGGFEAFTAVSELRKGREHYKAFKIPMVVLPATISNNVPGTEYSIGSDTCLNALIEYCDACRQSASASRRRVFVIETQGGKSGYVATIAGLSIGAFAVYTPEDGINLKMLDRDIDVLRDVFLADKGQSRAGKIILVNEQASKTYSVQIIADMIAEAGKGKFESRHGVPGHFQQGTTPSPMDRIRAVRFAFRSMQHLEQYAGWSRDDIDDEPLTSAVIGIKGAKVLFSPMHDIEKRETDWNRRRPKNEFWMNTKQIVNILSGRPEQLPGAVQPDTLGGRPKQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ML976984
EMBL· GenBank· DDBJ
KAF1959563.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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