In Toxoplasma gondii, MPC1 is a subunit of the mitochondrial pyruvate carrier that couples cytosolic glycolysis to the mitochondrial TCA cycle by importing pyruvate into the mitochondrion (PMID:36920199). MPC1 assembles with MPC2 into a heteromeric carrier complex whose transport function is conserved, as both subunits restore growth on leucine and valine in a transport-deficient yeast mutant (PMID:36920199). Genetic ablation of MPC1 impairs the synthesis of acetyl-CoA from glucose and reduces carbon flux through glycolysis and the TCA cycle, phenocopying loss of branched-chain ketoacid dehydrogenase and thereby placing the carrier at the junction between cytosolic and mitochondrial carbon metabolism, with a corresponding reduction in asexual parasite growth (PMID:36920199). Despite this metabolic role, MPC1 disruption has only a modest effect on virulence in mice, indicating that the parasite compensates for loss of cytosolic pyruvate import through broader metabolic plasticity (PMID:36920199). Beyond these findings, no structural model or in vitro reconstitution of the carrier has been characterized in the available corpus.