A0A8K0YFP3 · A0A8K0YFP3_9EUCA

  • Protein
    ATP-dependent 6-phosphofructokinase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • 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.

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 site224ATP (UniProtKB | ChEBI)
Binding site287-288ATP (UniProtKB | ChEBI)
Binding site317-320ATP (UniProtKB | ChEBI)
Binding site318Mg2+ (UniProtKB | ChEBI); catalytic
Binding site363-365substrate; ligand shared between dimeric partners; in other chain
Active site365Proton acceptor
Binding site400substrate; ligand shared between dimeric partners
Binding site407-409substrate; ligand shared between dimeric partners; in other chain
Binding site463substrate; ligand shared between dimeric partners; in other chain
Binding site491substrate; ligand shared between dimeric partners
Binding site497-500substrate; ligand shared between dimeric partners; in other chain
Binding site672beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site729-733beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site767beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site774-776beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site830beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site856beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site862-865beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site937beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Component6-phosphofructokinase complex
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

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Crustacea > Multicrustacea > Malacostraca > Eumalacostraca > Eucarida > Decapoda > Pleocyemata > Caridea > Atyoidea > Atyidae > Neocaridina

Accessions

  • Primary accession
    A0A8K0YFP3

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-589N-terminal catalytic PFK domain 1
Domain217-522Phosphofructokinase
Region603-976C-terminal regulatory PFK domain 2
Domain604-887Phosphofructokinase

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    976
  • Mass (Da)
    108,572
  • Last updated
    2022-08-03 v1
  • Checksum
    06856AFB06038481
MELQLVDQLREKLEKAKLSREELRRVFPPTLFKKDSHSAPPYVPYSFQRQKLDALKRLNQPGIPVKPRIPKSQVKKYLQEFENAKAAGRFAHLPVDQLEKLEKEVKAAATDADKASELEEFLRAVREEELSEDEGNEGYERAPPQVPVFGAEKTFEQSQQQFFQTPYEEIIPPPPTFPEDPWQAFLDYMAAAEGQENLILGQEGQVIERGMHKGKGIAVLTSGGDSQGMNAAVRAVVRMSLYVGARVFFIKEGYQGMVDGGDNIVEASWSSVSGIIHKGGTVIGSARCKDFRDREGRMKAAKNLIKRGITNLVIIGGDGSLTGANLFKQDWPALLALLIKKGEITEEERKAYSFINIVGMVGSIDNDFCGTDMTIGTDSALHRIIEAVDAISSTAYSHQRCFILEVMGRHCGYLCLSASIACEADYMFIPEFPPDHNWEERLCEKLESERSMGQRLNIIIVAEGAIDREGEAITAEGVRKVIADNLGFDTRITVLGHVQRGGSPSAFDRLLGCRMGAEAVLALMEATQETEPCVISLDGNQAVRVPLMGCVLKTQAVAQAMKDRNWDQAVQMRGRSFARNLETYKMLTRLKPPKPVEGKGGFNLGVMHIGAPACGMNAALRSFVRNCIYRGDIVYGIHDGIDGLVEGNIQEMKWSEVSGWVGQGGAFLGTKRTLPDKYLDQVAARLREYKMHSLLIVGGFEAYHALLQLYEARGKYKEFCIPMVVIPSTISNNVPGSDFSLGCDTALNEITEICDRIRQSAQGTKRRVFVVETMGGYCGYLATLAGLAGGADAAYIYEEQFGIQELQLDVYHMAAKMAEGVQRGLVLRNENANENYSTEFIYRLYSEEGKGIFSCRKNVLGHMQQGGSPSVFDRNMGTKMAAKAVNWMTEQMLQHRQDDGSVVCDEANTAVLLGLQKRSYVFQPVSELKRKTDWDRRIPVNQWWLKLRPLLRILAKHDGAYEEEGINVKEVEEALD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MK685666
EMBL· GenBank· DDBJ
QID05234.1
EMBL· GenBank· DDBJ
mRNA

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