A0AAI9WZK5 · A0AAI9WZK5_9ASCO

  • Protein
    ATP-dependent 6-phosphofructokinase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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 site200ATP (UniProtKB | ChEBI)
Binding site264-265ATP (UniProtKB | ChEBI)
Binding site294-297ATP (UniProtKB | ChEBI)
Binding site295Mg2+ (UniProtKB | ChEBI); catalytic
Binding site340-342substrate; ligand shared between dimeric partners; in other chain
Active site342Proton acceptor
Binding site377substrate; ligand shared between dimeric partners
Binding site384-386substrate; ligand shared between dimeric partners; in other chain
Binding site441substrate; ligand shared between dimeric partners; in other chain
Binding site469substrate; ligand shared between dimeric partners
Binding site475-478substrate; ligand shared between dimeric partners; in other chain
Binding site652beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site710-714beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site748beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site755-757beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site841beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site847-850beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site928beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain

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
      KGF56_000638

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CBS 10844
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Candida/Lodderomyces clade > Candida

Accessions

  • Primary accession
    A0AAI9WZK5

Proteomes

Subcellular Location

Cytoplasm

Keywords

Interaction

Subunit

Heterooctamer of 4 alpha and 4 beta chains.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-567N-terminal catalytic PFK domain 1
Domain192-500Phosphofructokinase
Region568-581Interdomain linker
Region582-959C-terminal regulatory PFK domain 2
Domain583-873Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    959
  • Mass (Da)
    105,486
  • Last updated
    2024-07-24 v1
  • Checksum
    6FF568F94A343859
MSSIINGSSTVPLIAGSQELLDDALIFYTNVLDFSEHSKKDNCVFLANRDQVVIELKLDPKKGNSAREVKERRKEILSKLNIVDWRSLDTTFVFKVGNLVDTIEILNSFKYTLQITPNELYPNEAYCVDPLGYIIGFTACNEPLTVVPPLQKANPKTDTSYLPSAMMSTTGSFSKLSESLQLSTNSLKPRRNIAIMTSGGDAPGMNASVRAVVRAAIFRGCKAFAIKEGYEGLVRGGEKYITEMKWQDVRGFLSDGGTNIGTARCMEFKKREGRLKGCRHLIEAGIDALIVCGGDGSLTGADLFRSEWPSLIAELKEQKEISEEQYEKHKHLYICGMVGSIDNDMATTDSTIGCYSALERICRAVDYIDATANSHSRAFVVEVMGRHCGWLALMAGIATSADYILIPEKPASSQDWQDQMTTIVKNHRAKGKRKTIVIVAEGAITLDLTPISSEDVKNVLVDRLGLDTRITTLGHVQRGGTAVAFDRILATVQGVEAVKAVLELEPDTPSPLIAIDENKICRRPLVEAVKITKSVAAAIAEKDFEKAMSLRDSEFKEHLSNFIAMNSACHDEPTLPLTKRKTIAIINIGAPAGGMNSATYAMATYCMSRGHTPYAIHNGFSGLSRHESVKSINWLDIEGWNSVGGSDIGTNRKTPEETDIGMIAHYFEKYKFDGLIIVGGFEAFISLHQLEKSRPMYPAFRIPMVLIPATISNNIPGTEYSLGADTCLNALMNYCDIIKQSASATRGRAFVIEAQGGNSGYIATYASLVSGAQASYVPEEGIHLTQLQMDIDSLREAFALEKSTTKTGKLIIKSSNASQVLTPQVLADIINAECKGEFDVKTAIPGHVQQGGLPSPIDRTRADRFAIKAVQFIEDHCDLMEPVRYAIDFSQDGKKYTETAAVLCLKGSHLRFSSIRRLYNFETELSKRMPKKVFWSKTRSIADDLVGRNRYKPVEEISH

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAHUZD010000023
EMBL· GenBank· DDBJ
KAI3406506.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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