Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium (PubMed:12686616, PubMed:22044534). Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:12686616, PubMed:22044534). May catalyze ubiquitination of target proteins in complex with RMD5 (Probable). Required for survival upon exposure to K1 killer toxin (PubMed:12663529). S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. Protein modification; protein ubiquitination. Identified in the GID complex. In the absence of glucose, the complex contains VID30/GID1, the E3 ubiquitin-ligase RMD5/GID2, VID28/GID5, GID7, GID8, and FYV10/GID9. When cells are shifted to glucose-containing medium, VID24/GID4 is induced and becomes part of the complex (PubMed:22645139). Interacts with RMD5/GID2; the interaction is direct (PubMed:22044534). Within the GID complex, interacts directly with VID28/GID5, GID8 and RMD5/GID2 (PubMed:22645139). Present with 784 molecules/cell in log phase SD medium. Belongs to the FYV10 family. It is not certain that this protein has E3 ubiquitin-protein ligase activity by itself. Lacks a detectable RING-type zinc finger domain; the sequence in this region is highly divergent and lacks most of the expected Cys residues. Still, Cys-434 in this highly divergent region is required for ubiquitination of FBP1, suggesting a direct role in catalyzing ubiquitination.