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A0A1B9ITA2 · A0A1B9ITA2_9TREE

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 site90ATP (UniProtKB | ChEBI)
Binding site275-276ATP (UniProtKB | ChEBI)
Binding site305-308ATP (UniProtKB | ChEBI)
Binding site306Mg2+ (UniProtKB | ChEBI); catalytic
Binding site351-353substrate; ligand shared between dimeric partners; in other chain
Active site353Proton acceptor
Binding site388substrate; ligand shared between dimeric partners
Binding site395-397substrate; ligand shared between dimeric partners; in other chain
Binding site452substrate; ligand shared between dimeric partners; in other chain
Binding site480substrate; ligand shared between dimeric partners
Binding site486-489substrate; ligand shared between dimeric partners; in other chain
Binding site661beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site718-722beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site756beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site763-765beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site823beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site849beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site941beta-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
      L486_03262

Organism names

  • Taxonomic identifier
  • Strain
    • CBS 10435
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Tremellomycetes > Tremellales > Cryptococcaceae > Kwoniella

Accessions

  • Primary accession
    A0A1B9ITA2

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-37Polar residues
Region1-49Disordered
Region1-578N-terminal catalytic PFK domain 1
Domain82-129Phosphofructokinase
Region125-166Disordered
Compositional bias128-166Polar residues
Domain252-512Phosphofructokinase
Domain592-881Phosphofructokinase
Region592-967C-terminal regulatory PFK domain 2
Region889-908Disordered

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    967
  • Mass (Da)
    105,052
  • Last updated
    2016-11-02 v1
  • MD5 Checksum
    FD75E4D024EEE7E4D7A06393C2F83CDB
MLSSKTIDSVVQDTASNPKHVVDQQSQAMSPIPQDQDQEDIQTKDLEGIPEGLVDKAEGITVPTVREDGMRSPAARNKKQKNVAVLTSGGDSAGMNAAVRAVVRQSIARGCQAYIIREGWEGLVRGNTTDPTPFTTPRRTPSASANQSPVLQPAKSVSFSSLPPSKQMDLEKATHELNEQAEEDFEKNRVNFTDPSGVAPLSNAPLSFGFGELLKDGAGEGDIEEMQAHGLQSMVIVDEEDEKGKSLKGRYIVRVGWDDVRGWLGEGGTLIGSSRCPSFRERSGRLQAAHNLIKYGIDCLAVCGGDGSLTGADKLRGEWPSLMDELLVTGKIDEEQRETYRHLNIVGLVGSIDNDMSMTDLTIGAPTALHRICESIDSIASTASSHSRAFVIEVMGRHCGWLALLAGVAMGADFIFIPESPPETDDWETEMCNLLQSHRKVGKRKSIVIVAEGALDRNLKPIKPDYVKDILVDRLGLDTRVTTLGHTQRGGRPCAYDRILPTLQGVQAVQALLEATPETPSYMIGTRENKIIKVPLLEAVAETQAVAKAIENRDFATAMSHRDSEFREMLQAFQISSSLAINEEAPKDKRLRIGIVHVGAPAGGMNAATRQAVRFCHHRGHTPVAIYNGFEGLLDDNVAELSWLRVDTWTTRGGSELGTNRTLPSIDLGSVAAGFQRHALDGLLVIGGFEAFHSLMILEQNRANYPSFQIPMVHLPATISNNVPMTDFSLGSDTSLNALVDACDAIRQSASASRNRVFVVETQGGMSGYLATMGALAVGAVLVYTPEDGISLKLLQADVEFLTKRYSLDAKGKSEGRLVIKSEKSSSIYTTEVLTKIFKEEGKELFDARSASLGHTLQGGTPSPMDRTRAARLALRCMQFLEQHAVPNSQTSSIAHRGGSGAKHKKPSYSTETATMIAIRGSKIVYATMEEVLKHTDMKLRRGKDEWWSDIKRLAEIMGGRQGLISS

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-37Polar residues
Compositional bias128-166Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KI669461
EMBL· GenBank· DDBJ
OCF58772.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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