E3 ubiquitin-protein ligase component of the GID complex (PubMed:12686616, PubMed:18508925). 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:9737955, PubMed:18508925). Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:9737955, PubMed:12686616, PubMed:18508925, PubMed:28126757). 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 FYV10/GID9; the interaction is direct (PubMed:22044534). Within the GID complex, interacts directly with GID8, FYV10/GID9 and VID28/GID5 (PubMed:22645139).