A0A3Q1NJ70 · A0A3Q1NJ70_BOVIN

  • Protein
    ATP-dependent 6-phosphofructokinase
  • Gene
    PFKP
  • 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.

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 site35ATP (UniProtKB | ChEBI)
Binding site98-99ATP (UniProtKB | ChEBI)
Binding site128-131ATP (UniProtKB | ChEBI)
Binding site129Mg2+ (UniProtKB | ChEBI); catalytic
Binding site174-176substrate; ligand shared between dimeric partners; in other chain
Active site176Proton acceptor
Binding site211substrate; ligand shared between dimeric partners
Binding site218-220substrate; ligand shared between dimeric partners; in other chain
Binding site274substrate; ligand shared between dimeric partners; in other chain
Binding site302substrate; ligand shared between dimeric partners
Binding site308-311substrate; ligand shared between dimeric partners; in other chain
Binding site482beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site590-594beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site628beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site635-637beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site691beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site717beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site723-726beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site796beta-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

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Hereford
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    A0A3Q1NJ70

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Homo- and heterotetramers.

Structure

3D structure databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-400N-terminal catalytic PFK domain 1
Domain28-333Phosphofructokinase
Region413-842C-terminal regulatory PFK domain 2
Domain563-749Phosphofructokinase

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    842
  • Mass (Da)
    91,476
  • Last updated
    2024-05-29 v2
  • Checksum
    410E72BFAE22E31D
MDGHDSPQTPKGSLRKFLEQLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFIYEGYQGMVDGGSNIVEADWESVSSILQVGGTIIGSARCQDFRTREGRLKAACNLVQLGITSLCVIGGDGSLTGAHIFQTEWSGLLEELARDGKISTEQVQKHGHLNVVGMVGSIDNDFCGTDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLPESPPEEGWQENMCIKLSENRARKKRLNIIIVAEGAIDTQNKPITSEQIKELVVTQLGYDTRVTILGHVQRGGTPSAFDRILASRMGVEAVVALLQATPETPACVVSLSGNQAVRLPLMECVQMTQEVQKAMDERRFKDAVRLRGRSFENNLNTYKRLAIKLPDSEIPKSNCNVGVVNVGAPAAGMNAAVRAAVRVGISEGHKMFAVYDGFEGFAKGQIKEIGWGDVGGWTGQGGSILGTKRTLPGKYLEDIAAQMRTHGISALLIIGGFEAYLGLLELLAARQKHEEFCVPMVMVPATVSNNVPGSDFSIGADTALNTITDAFRSLLELSKKRDSHPEFCIPVCMVPATISNNVPGTDLSIGCDTGLNVIVETCDRIKQSASGTKRRVFIIETMGGFCGYLANMGGLAAGADAAYIFEEPFDIRDLQSNVEHLTEKMKTSIQRGLVLRNESCSENYTTDFIYQLYSEEGKGVFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMQWISSKLRESVGKGKKFLSEDCVCVLGISKRTLLFQPVAELKKETDFEHRIPKEQWWLKLRPLMKILAKYKVSFEVSDASQLEPVQPRGPEEPAAI

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
E1BCW3E1BCW3_BOVINPFKP909
A0AAA9SFJ5A0AAA9SFJ5_BOVINPFKP714
A0AAA9TNU4A0AAA9TNU4_BOVINPFKP740
A0AAA9TMI3A0AAA9TMI3_BOVINPFKP738

Keywords

Genome annotation databases

Similar Proteins

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