LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Homologous_superfamily |
| Description | 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/α-barrel structure. Homologous TIM-barrel domains are found in the following proteins:N-terminal of pyruvate kinase ( ), which is interrupted by an all-beta domain [ ].C-terminal of pyruvate phosphate dikinase ( ), which has a similar mode of substrate binding to pyruvate kinase [ ].Phosphoenolpyruvate carboxylase ( ); this domain has additional helices [ ].Phosphenolpyruvate mutase( )/Isocitrate lyase ( ), where it forms a swapped dimer [ ].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 [ ].Ketopantoate hydroxymethyltransferase PanB ( ), where a C-terminal helix exchange is observed in some enzymes [ ]. |
| Short Name | Pyrv/PenolPyrv_Kinase-like_dom |
