Homologous Superfamily

Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily (IPR015813)

Short name: Pyrv/PenolPyrv_Kinase-like_dom

Overlapping entries



Pyruvate kinase controls the exit from the glysolysis pathway, catalysing the transfer of phosphate from phosphooenolpyruvate (PEP) to ADP. Mammalian pyruvate kinase is a homotetramer, where each polypeptide subunit consists of four domains: N-terminal, A domain, B domain and C-terminal. Activation of the enzyme is believed to occur via the clamping down of the B domain onto the A domain to dehydrate the active site cleft. The N- and C-terminal domains are situated at inter-subunit contact sites, and could be involved in assembly and communication within the complex. The N-terminal domain has a TIM beta/alpha-barrel structure. Homologous TIM-barrel domains are found in the following proteins:

  • N-terminal of pyruvate kinase (EC:, which is interrupted by an all-beta domain [PMID: 11563914].
  • C-terminal of pyruvate phosphate dikinase (EC:, which has a similar mode of substrate binding to pyruvate kinase [PMID: 11790099].
  • Phosphoenolpyruvate carboxylase (EC:; this domain has additional helices [PMID: 12467579].
  • Phosphenolpyruvate mutase(EC: lyase (EC:, where it forms a swapped dimer [PMID: 11526312].
  • HpcH/HpaI aldolases, such as the beta subunit of citrate lyase, where it forms a swapped dimer, and contains a pyruvate kinase-type metal binding site [PMID: 7064730].
  • Ketopantoate hydroxymethyltransferase PanB (EC:, where a C-terminal helix exchange is observed in some enzymes [PMID: 12906829].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0003824 catalytic activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.