The Saccharomyces cerevisiae general amino-acid permease Gap1 not only mediates the uptake of most amino acids, it also functions as a receptor for the activation of protein kinase A. Fungal pathogens can colonize different niches in the host, each containing various levels of different amino acids and sugars. The Candida albicans genome contains six genes homologous to the S. cerevisiae GAP1. The expression of these six genes in S. cerevisiae showed that the products of all six C. albicans genes differ in their transport capacities. CaGap2 is the true orthologue of ScGap1, as it transports all tested amino acids. The other CaGap proteins have narrower substrate specificities, though CaGap1 and CaGap6 transport several structurally unrelated amino acids. CaGap1, CaGap2, and CaGap6 also function as transceptors. Upon detecting some amino acids, e.g. methionine, they are involved in a rapid activation of trehalase, a downstream target of PKA. Our data shows that CaGAP genes can be functionally expressed in S. cerevisiae and that CaGap permeases communicate to the intracellular signal transduction pathway similarly to S. cerevisiae's own Gap1.