A2RV78 · A2RV78_XENLA

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 site26ATP (UniProtKB | ChEBI)
Binding site89-90ATP (UniProtKB | ChEBI)
Binding site119-122ATP (UniProtKB | ChEBI)
Binding site120Mg2+ (UniProtKB | ChEBI); catalytic
Binding site165-167substrate; ligand shared between dimeric partners; in other chain
Active site167Proton acceptor
Binding site202substrate; ligand shared between dimeric partners
Binding site209-211substrate; ligand shared between dimeric partners; in other chain
Binding site265substrate; ligand shared between dimeric partners; in other chain
Binding site293substrate; ligand shared between dimeric partners
Binding site299-302substrate; ligand shared between dimeric partners; in other chain
Binding site473beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site530-534beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site568beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site575-577beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site631beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site657beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site663-666beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site739beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function6-phosphofructokinase activity
Molecular FunctionATP binding
Molecular Functionmetal ion binding
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
      pfkp.S
    • Synonyms
      LOC100037146
      , pfk
      , pfk-c
      , pfk1
      , pfkf
      , pfkp

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus

Accessions

  • Primary accession
    A2RV78

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Keywords

Expression

Gene expression databases

    • 100037146Expressed in brain and 19 other cell types or tissues

Interaction

Subunit

Homo- and heterotetramers.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-391N-terminal catalytic PFK domain 1
Domain19-324Phosphofructokinase
Domain404-689Phosphofructokinase
Region404-786C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    786
  • Mass (Da)
    86,641
  • Last updated
    2007-03-06 v1
  • Checksum
    C4A3B826DDEE3965
MAQPDKRLFENLSGKGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVQAKVYFIYEGYQGMVDGGDNIEEVSWESVSSILQVGGTVIGSARCKSFRTREGRLQAANNLVQRGITNLCVIGGDGSLTGANLFREEWSGLLDELVQNGKIEAEATKQYAHLNIVGMVGSIDNDFCGTDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFIPEYPPEEGWEDTMCNKLSENRARKKRLNIIIVSEGAIDCHNKPITSDLVKDLVMKRLGFDTRVTILGHVQRGGTPSAFDRILASRMGVDCVLALLEATPETPACVVSLCGNQAVRLPLMECVQMTQEVQKAMDERRFDDAVRLRGRSFENNLNTYKLLSHKKNVSELPKSNFNVAVLNVGAPAAGMNAAVRSAVRVGITEGHKMFAVNDGFEGFAKGQIKEIKWGDVGGYTGQGGSLLGTKRTLPAKYFDQIAEQLRTHKINALLVIGGFEAYLGLLEMVEGRGKYDEFCIPMVMVPATVSNNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGADAAYIFEESFDIRELQANVEHLTEKMKTSIQRGLVLRNENSNENYTTDFIYQLYSEEGRGVFDCRKNVLGHMQQGGAPSPFDRNFGTKISAKAVQWISKKLVETYRKDEGRVFANTDDSVCLLGMRRRNLLFQPVTQLKDETDFKHRIPKEQWWLKMRPLMKILAKYKTSYDISDAGKLEHVNMCRRTDEAVAI

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8J1L0B3A0A8J1L0B3_XENLApfkp.S835
A0A8J0VII5A0A8J0VII5_XENLApfkp.S786
A0A8J0VKV2A0A8J0VKV2_XENLApfkp.S784
A0A8J0VM01A0A8J0VM01_XENLApfkp.S784

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BC133214
EMBL· GenBank· DDBJ
AAI33215.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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