Actin; structural protein involved in cell polarization, endocytosis, and other cytoskeletal functions.

Enolase I, a phosphopyruvate hydratase; catalyzes conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis and the reverse reaction during gluconeogenesis; expression repressed in response to glucose; protein abundance increases in response to DNA replication stress; N-terminally propionylated in vivo; ENO1 has a paralog, ENO2, that arose from the whole genome duplication.

Actin; structural protein involved in cell polarization, endocytosis, and other cytoskeletal functions.

Ubiquitin-conjugating enzyme (E2); key E2 partner with Ubc1p for the anaphase-promoting complex (APC); mediates degradation of abnormal or excess proteins, including calmodulin and histone H3; regulates levels of DNA Polymerase-{alpha} to promote efficient and accurate DNA replication; interacts with many SCF ubiquitin protein ligases; component of the cellular stress response; UBC4 has a paralog, UBC5, that arose from the whole genome duplication.

Actin; structural protein involved in cell polarization, endocytosis, and other cytoskeletal functions.

Orotidine-5'-phosphate (OMP) decarboxylase; catalyzes the sixth enzymatic step in the de novo biosynthesis of pyrimidines, converting OMP into uridine monophosphate (UMP); converts 5-FOA into 5-fluorouracil, a toxic compound.

Alcohol dehydrogenase isoenzyme type IV; dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency.

Enolase I, a phosphopyruvate hydratase; catalyzes conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis and the reverse reaction during gluconeogenesis; expression repressed in response to glucose; protein abundance increases in response to DNA replication stress; N-terminally propionylated in vivo; ENO1 has a paralog, ENO2, that arose from the whole genome duplication.

Alcohol dehydrogenase isoenzyme type IV; dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency.

Isocitrate lyase; catalyzes the formation of succinate and glyoxylate from isocitrate, a key reaction of the glyoxylate cycle; expression of ICL1 is induced by growth on ethanol and repressed by growth on glucose.

Alcohol dehydrogenase isoenzyme type IV; dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency.

Orotidine-5'-phosphate (OMP) decarboxylase; catalyzes the sixth enzymatic step in the de novo biosynthesis of pyrimidines, converting OMP into uridine monophosphate (UMP); converts 5-FOA into 5-fluorouracil, a toxic compound.

Enolase I, a phosphopyruvate hydratase; catalyzes conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis and the reverse reaction during gluconeogenesis; expression repressed in response to glucose; protein abundance increases in response to DNA replication stress; N-terminally propionylated in vivo; ENO1 has a paralog, ENO2, that arose from the whole genome duplication.

Actin; structural protein involved in cell polarization, endocytosis, and other cytoskeletal functions.

Enolase I, a phosphopyruvate hydratase; catalyzes conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis and the reverse reaction during gluconeogenesis; expression repressed in response to glucose; protein abundance increases in response to DNA replication stress; N-terminally propionylated in vivo; ENO1 has a paralog, ENO2, that arose from the whole genome duplication.

Alcohol dehydrogenase isoenzyme type IV; dimeric enzyme demonstrated to be zinc-dependent despite sequence similarity to iron-activated alcohol dehydrogenases; transcription is induced in response to zinc deficiency.

Enolase I, a phosphopyruvate hydratase; catalyzes conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis and the reverse reaction during gluconeogenesis; expression repressed in response to glucose; protein abundance increases in response to DNA replication stress; N-terminally propionylated in vivo; ENO1 has a paralog, ENO2, that arose from the whole genome duplication.

Isocitrate lyase; catalyzes the formation of succinate and glyoxylate from isocitrate, a key reaction of the glyoxylate cycle; expression of ICL1 is induced by growth on ethanol and repressed by growth on glucose.

Enolase I, a phosphopyruvate hydratase; catalyzes conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis and the reverse reaction during gluconeogenesis; expression repressed in response to glucose; protein abundance increases in response to DNA replication stress; N-terminally propionylated in vivo; ENO1 has a paralog, ENO2, that arose from the whole genome duplication.

Malate synthase, enzyme of the glyoxylate cycle; involved in utilization of non-fermentable carbon sources; expression is subject to carbon catabolite repression; localizes in peroxisomes during growth on oleic acid, otherwise cytosolic; can accept butyryl-CoA as acyl-CoA donor in addition to traditional substrate acetyl-CoA.

Enolase I, a phosphopyruvate hydratase; catalyzes conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis and the reverse reaction during gluconeogenesis; expression repressed in response to glucose; protein abundance increases in response to DNA replication stress; N-terminally propionylated in vivo; ENO1 has a paralog, ENO2, that arose from the whole genome duplication.

Orotidine-5'-phosphate (OMP) decarboxylase; catalyzes the sixth enzymatic step in the de novo biosynthesis of pyrimidines, converting OMP into uridine monophosphate (UMP); converts 5-FOA into 5-fluorouracil, a toxic compound.

Protein FYV10; Subunit of GID complex; involved in proteasome-dependent catabolite inactivation of gluconeogenic enzymes FBPase, PEPCK, and c-MDH; forms dimer with Rmd5p that is then recruited to GID Complex by Gid8p; contains a degenerate RING finger motif needed for GID complex ubiquitin ligase activity in vivo, as well as CTLH and CRA domains; plays role in anti-apoptosis; required for survival upon exposure to K1 killer toxin; Belongs to the FYV10 family.

Glucose-induced degradation protein 7; Subunit of GID Complex that binds directly to central component Vid30p; GID complex is involved in proteasome-dependent catabolite inactivation of fructose-1,6-bisphosphatase; Gid7p contains six WD40 repeats; computational analysis suggests that Gid7p and Moh1p have similar functions.

Protein FYV10; Subunit of GID complex; involved in proteasome-dependent catabolite inactivation of gluconeogenic enzymes FBPase, PEPCK, and c-MDH; forms dimer with Rmd5p that is then recruited to GID Complex by Gid8p; contains a degenerate RING finger motif needed for GID complex ubiquitin ligase activity in vivo, as well as CTLH and CRA domains; plays role in anti-apoptosis; required for survival upon exposure to K1 killer toxin; Belongs to the FYV10 family.

Glucose-induced degradation protein 8; Subunit of GID Complex, binds strongly to central component Vid30p; GID Complex is involved in proteasome-dependent catabolite inactivation of fructose-1,6-bisphosphatase; recruits Rmd5p, Fyv10 and Vid28p to GID Complex; contains LisH, CTLH, and CRA domains that mediate binding to Vid30p (LisH) and Rmd5p and Vid28p (CTLH and CRA); dosage-dependent regulator of START.

Protein FYV10; Subunit of GID complex; involved in proteasome-dependent catabolite inactivation of gluconeogenic enzymes FBPase, PEPCK, and c-MDH; forms dimer with Rmd5p that is then recruited to GID Complex by Gid8p; contains a degenerate RING finger motif needed for GID complex ubiquitin ligase activity in vivo, as well as CTLH and CRA domains; plays role in anti-apoptosis; required for survival upon exposure to K1 killer toxin; Belongs to the FYV10 family.

E3 ubiquitin-protein ligase RMD5; Component of GID Complex that confers ubiquitin ligase (U3) activity; necessary for polyubiquitination and degradation of the gluconeogenic enzyme fructose-1,6-bisphosphatase; forms dimer with Fyv10p that is then recruited to GID Complex by Gid8p; also required for sporulation; conserved protein that has a degenerate RING finger domain.

Protein FYV10; Subunit of GID complex; involved in proteasome-dependent catabolite inactivation of gluconeogenic enzymes FBPase, PEPCK, and c-MDH; forms dimer with Rmd5p that is then recruited to GID Complex by Gid8p; contains a degenerate RING finger motif needed for GID complex ubiquitin ligase activity in vivo, as well as CTLH and CRA domains; plays role in anti-apoptosis; required for survival upon exposure to K1 killer toxin; Belongs to the FYV10 family.

Vacuolar import and degradation protein 24; GID Complex regulatory subunit; binds GID Complex in response to glucose through interactions with complex member Vid28p; regulates fructose-1,6-bisphosphatase (FBPase) targeting to the vacuole; promotes proteasome-dependent catabolite degradation of FBPase; peripheral membrane protein located at Vid (vacuole import and degradation) vesicles; Belongs to the GID4/VID24 family.

Protein FYV10; Subunit of GID complex; involved in proteasome-dependent catabolite inactivation of gluconeogenic enzymes FBPase, PEPCK, and c-MDH; forms dimer with Rmd5p that is then recruited to GID Complex by Gid8p; contains a degenerate RING finger motif needed for GID complex ubiquitin ligase activity in vivo, as well as CTLH and CRA domains; plays role in anti-apoptosis; required for survival upon exposure to K1 killer toxin; Belongs to the FYV10 family.

Vacuolar import and degradation protein 28; GID Complex subunit, serves as adaptor for regulatory subunit Vid24p; protein involved in proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBPase); localized to the nucleus and the cytoplasm.

Protein FYV10; Subunit of GID complex; involved in proteasome-dependent catabolite inactivation of gluconeogenic enzymes FBPase, PEPCK, and c-MDH; forms dimer with Rmd5p that is then recruited to GID Complex by Gid8p; contains a degenerate RING finger motif needed for GID complex ubiquitin ligase activity in vivo, as well as CTLH and CRA domains; plays role in anti-apoptosis; required for survival upon exposure to K1 killer toxin; Belongs to the FYV10 family.

Vacuolar import and degradation protein 30; Central component of GID Complex, involved in FBPase degradation; interacts strongly with Gid8p to serve as a scaffold for other GID Complex subunits; contains SPRY domain and 3 domains that are also found in Gid8p - LisH, CTLH, and CRA; required for association of Vid vesicles and actin patches in vacuole import and degradation pathway; shifts the balance of nitrogen metabolism toward glutamate production; localizes to the nucleus and the cytoplasm.

Glucose-induced degradation protein 7; Subunit of GID Complex that binds directly to central component Vid30p; GID complex is involved in proteasome-dependent catabolite inactivation of fructose-1,6-bisphosphatase; Gid7p contains six WD40 repeats; computational analysis suggests that Gid7p and Moh1p have similar functions.

Protein FYV10; Subunit of GID complex; involved in proteasome-dependent catabolite inactivation of gluconeogenic enzymes FBPase, PEPCK, and c-MDH; forms dimer with Rmd5p that is then recruited to GID Complex by Gid8p; contains a degenerate RING finger motif needed for GID complex ubiquitin ligase activity in vivo, as well as CTLH and CRA domains; plays role in anti-apoptosis; required for survival upon exposure to K1 killer toxin; Belongs to the FYV10 family.

Glucose-induced degradation protein 7; Subunit of GID Complex that binds directly to central component Vid30p; GID complex is involved in proteasome-dependent catabolite inactivation of fructose-1,6-bisphosphatase; Gid7p contains six WD40 repeats; computational analysis suggests that Gid7p and Moh1p have similar functions.

Glucose-induced degradation protein 8; Subunit of GID Complex, binds strongly to central component Vid30p; GID Complex is involved in proteasome-dependent catabolite inactivation of fructose-1,6-bisphosphatase; recruits Rmd5p, Fyv10 and Vid28p to GID Complex; contains LisH, CTLH, and CRA domains that mediate binding to Vid30p (LisH) and Rmd5p and Vid28p (CTLH and CRA); dosage-dependent regulator of START.

Glucose-induced degradation protein 7; Subunit of GID Complex that binds directly to central component Vid30p; GID complex is involved in proteasome-dependent catabolite inactivation of fructose-1,6-bisphosphatase; Gid7p contains six WD40 repeats; computational analysis suggests that Gid7p and Moh1p have similar functions.

E3 ubiquitin-protein ligase RMD5; Component of GID Complex that confers ubiquitin ligase (U3) activity; necessary for polyubiquitination and degradation of the gluconeogenic enzyme fructose-1,6-bisphosphatase; forms dimer with Fyv10p that is then recruited to GID Complex by Gid8p; also required for sporulation; conserved protein that has a degenerate RING finger domain.