The atToc33 protein is an import receptor in the outer envelope of Arabidopsis chloroplasts. It is a GTPase with motifs characteristic of such proteins, and its loss in the plastid protein import 1 (ppi1) mutant interferes with the import of photosynthesis-related preproteins, causing a chlorotic phenotype in mutant plants. To assess the significance of GTPase cycling by atToc33, we generated several atToc33 point mutants with predicted effects on GTP binding (K49R, S50N, S50N/S51N), GTP hydrolysis (G45R, G45V, Q68A, N101A), both binding and hydrolysis (G45R/K49N/S50R), and dimerization or functional interaction between dimeric partners (R125A, R130A, R130K). First, a selection of these mutants was assessed in vitro or in yeast, to confirm that the mutations have the desired effects: in relation to nucleotide binding and dimerization, the mutants behaved as expected. Then, activities of selected mutants were tested in vivo, by assessing for complementation of ppi1 in transgenic plants. Remarkably, all tested mutants mediated high levels of complementation: complemented plants were similar to wild type in growth rate, chlorophyll accumulation, photosynthetic performance, and chloroplast ultrastructure. Protein import into mutant chloroplasts was also complemented to a considerable degree. Overall, the data indicate that neither nucleotide binding nor dimerization at atToc33 is essential for the receptor’s activity in import. Absence of atToc33 GTPase activity might somehow be compensated for by that of another receptor, Toc159. However, overexpression of atToc33 (or its close relative, atToc34) in Toc159-deficient plants did not mediate complementation, indicating that the receptors do not share functional redundancy in the conventional sense.