A0A5F9D5Z9 · A0A5F9D5Z9_RABIT

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 site96ATP (UniProtKB | ChEBI)
Binding site159-160ATP (UniProtKB | ChEBI)
Binding site189-192ATP (UniProtKB | ChEBI)
Binding site190Mg2+ (UniProtKB | ChEBI); catalytic
Binding site235-237substrate; ligand shared between dimeric partners; in other chain
Active site237Proton acceptor
Binding site272substrate; ligand shared between dimeric partners
Binding site279-281substrate; ligand shared between dimeric partners; in other chain
Binding site335substrate; ligand shared between dimeric partners; in other chain
Binding site363substrate; ligand shared between dimeric partners
Binding site369-372substrate; ligand shared between dimeric partners; in other chain
Binding site492beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site549-553beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site587beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site594-596beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site650beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site676beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site682-685beta-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; in other chain

GO annotations

AspectTerm
Cellular Component6-phosphofructokinase complex
Cellular Componentmembrane
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

    • Name
      PFKM

Organism names

  • Taxonomic identifier
  • Strain
    • Thorbecke
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus

Accessions

  • Primary accession
    A0A5F9D5Z9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Expression

Gene expression databases

Interaction

Subunit

Homo- and heterotetramers.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-461N-terminal catalytic PFK domain 1
Region22-62Disordered
Domain89-394Phosphofructokinase
Domain468-707Phosphofructokinase
Region468-801C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    801
  • Mass (Da)
    88,290
  • Last updated
    2019-12-11 v1
  • Checksum
    F60A5395AC04317F
MREEEFHLKFFMCVIRSHQVVRTPQSTAAEASTSNRLIPRPPPKTDASQSLYTDDDPGTEEGIPHLQTEWIMTHEEHHAARTLGVGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVDGGDHIREATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAHNLVKRGITNLCVIGGDGSLTGADTFRSEWSDLLSDLQKAGKITAEEATRSSYLNIVGLVGSIDNDFCGTDMTIGTDSALHRITEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDNWEDHLCRRLSETRTRGSRLNIIIVAEGAIDRNGKPITSEGVKDLVVKRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTKAMDEKRFDEAMKLRGRSFMNNWEVYKLLAHIRPPAPKIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSVGADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPFTIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLGHMQQGGSPTPFDRNFATKMGAKAMNWMAGKIKESYRNGRIFANTPDSGCVLGMRKRALVFQPVTELQNQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSEHAHLEHISRKRSGEATV

Computationally mapped potential isoform sequences

There are 7 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A5F9DGX0A0A5F9DGX0_RABITPFKM851
A0A5F9CE16A0A5F9CE16_RABITPFKM694
A0A5F9DKQ9A0A5F9DKQ9_RABITPFKM94
G1TDQ5G1TDQ5_RABITPFKM749
A0A5F9DCR3A0A5F9DCR3_RABITPFKM816
A0A5F9D2K9A0A5F9D2K9_RABITPFKM753
A0A5F9CT34A0A5F9CT34_RABITPFKM758

Keywords

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help