Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

Plasma membrane arginine permease; requires phosphatidyl ethanolamine (PE) for localization, exclusively associated with lipid rafts; mutation confers canavanine resistance; CAN1 has a paralog, ALP1, that arose from the whole genome duplication.

Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

Imidazoleglycerol-phosphate dehydratase; catalyzes the sixth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; transcription is regulated by general amino acid control via Gcn4p.

Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication.

Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication.

Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

Beta-isopropylmalate dehydrogenase (IMDH); catalyzes the third step in the leucine biosynthesis pathway; can additionally catalyze the conversion of beta-ethylmalate into alpha-ketovalerate; Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

Phosphoribosylanthranilate isomerase; catalyzes the third step in tryptophan biosynthesis; in 2004, the sequence of TRP1 from strain S228C was updated by changing the previously annotated internal STOP (TAA) to serine (TCA); enhances vegetative growth at low and high temperatures when used as an auxotrophic marker in strains such as W303.

Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

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.

Plasma membrane arginine permease; requires phosphatidyl ethanolamine (PE) for localization, exclusively associated with lipid rafts; mutation confers canavanine resistance; CAN1 has a paralog, ALP1, that arose from the whole genome duplication.

Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

Plasma membrane arginine permease; requires phosphatidyl ethanolamine (PE) for localization, exclusively associated with lipid rafts; mutation confers canavanine resistance; CAN1 has a paralog, ALP1, that arose from the whole genome duplication.

Imidazoleglycerol-phosphate dehydratase; catalyzes the sixth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; transcription is regulated by general amino acid control via Gcn4p.

Plasma membrane arginine permease; requires phosphatidyl ethanolamine (PE) for localization, exclusively associated with lipid rafts; mutation confers canavanine resistance; CAN1 has a paralog, ALP1, that arose from the whole genome duplication.

Beta-isopropylmalate dehydrogenase (IMDH); catalyzes the third step in the leucine biosynthesis pathway; can additionally catalyze the conversion of beta-ethylmalate into alpha-ketovalerate; Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Plasma membrane arginine permease; requires phosphatidyl ethanolamine (PE) for localization, exclusively associated with lipid rafts; mutation confers canavanine resistance; CAN1 has a paralog, ALP1, that arose from the whole genome duplication.

Phosphoribosylanthranilate isomerase; catalyzes the third step in tryptophan biosynthesis; in 2004, the sequence of TRP1 from strain S228C was updated by changing the previously annotated internal STOP (TAA) to serine (TCA); enhances vegetative growth at low and high temperatures when used as an auxotrophic marker in strains such as W303.

Plasma membrane arginine permease; requires phosphatidyl ethanolamine (PE) for localization, exclusively associated with lipid rafts; mutation confers canavanine resistance; CAN1 has a paralog, ALP1, 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.

Essential Hsp90p co-chaperone; necessary for passage through the START phase of the cell cycle; stabilizes protein kinase nascent chains and participates along with Hsp90p in their folding; Belongs to the CDC37 family.

ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication.

Essential Hsp90p co-chaperone; necessary for passage through the START phase of the cell cycle; stabilizes protein kinase nascent chains and participates along with Hsp90p in their folding; Belongs to the CDC37 family.

Trimeric heat shock transcription factor; activates multiple genes in response to highly diverse stresses; recognizes variable heat shock elements (HSEs) consisting of inverted NGAAN repeats; monitors translational status of cell through an RQC (Ribosomal Quality Control)-mediated translation-stress signal; involved in diauxic shift; posttranslationally regulated; human homolog HSF1 with linker region mutations can complement yeast hsf1 mutant; Belongs to the HSF family.

Essential Hsp90p co-chaperone; necessary for passage through the START phase of the cell cycle; stabilizes protein kinase nascent chains and participates along with Hsp90p in their folding; Belongs to the CDC37 family.

ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication.

Imidazoleglycerol-phosphate dehydratase; catalyzes the sixth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; transcription is regulated by general amino acid control via Gcn4p.

Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine.

Imidazoleglycerol-phosphate dehydratase; catalyzes the sixth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; transcription is regulated by general amino acid control via Gcn4p.

Plasma membrane arginine permease; requires phosphatidyl ethanolamine (PE) for localization, exclusively associated with lipid rafts; mutation confers canavanine resistance; CAN1 has a paralog, ALP1, that arose from the whole genome duplication.

Imidazoleglycerol-phosphate dehydratase; catalyzes the sixth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; transcription is regulated by general amino acid control via Gcn4p.

ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication.

Imidazoleglycerol-phosphate dehydratase; catalyzes the sixth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; transcription is regulated by general amino acid control via Gcn4p.

Beta-isopropylmalate dehydrogenase (IMDH); catalyzes the third step in the leucine biosynthesis pathway; can additionally catalyze the conversion of beta-ethylmalate into alpha-ketovalerate; Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Imidazoleglycerol-phosphate dehydratase; catalyzes the sixth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; transcription is regulated by general amino acid control via Gcn4p.

Phosphoribosylanthranilate isomerase; catalyzes the third step in tryptophan biosynthesis; in 2004, the sequence of TRP1 from strain S228C was updated by changing the previously annotated internal STOP (TAA) to serine (TCA); enhances vegetative growth at low and high temperatures when used as an auxotrophic marker in strains such as W303.