Argininosuccinate lyase; catalyzes the final step in the arginine biosynthesis pathway; Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.

Porphobilinogen deaminase; catalyzes the conversion of 4-porphobilinogen to hydroxymethylbilane, the third step in heme biosynthesis; localizes to the cytoplasm and nucleus; expression is regulated by Hap2p-Hap3p, but not by levels of heme; human homolog HMBS can complement yeast mutant and allow growth of haploid null after sporulation of a heterozygous diploid.

ER-retained PMA1-suppressing protein 1; ER protein with chaperone and co-chaperone activity; involved in retention of resident ER proteins; has a role in recognizing proteins targeted for ER-associated degradation (ERAD), member of the protein disulfide isomerase family.

Endoplasmic reticulum chaperone BiP; ATPase involved in protein import into the ER; also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p.

ER-retained PMA1-suppressing protein 1; ER protein with chaperone and co-chaperone activity; involved in retention of resident ER proteins; has a role in recognizing proteins targeted for ER-associated degradation (ERAD), member of the protein disulfide isomerase family.

Methionine-S-sulfoxide reductase; involved in the response to oxidative stress; protects iron-sulfur clusters from oxidative inactivation along with MXR2; involved in the regulation of lifespan; reduced activity of human homolog implicated in Alzheimer disease.

ER-retained PMA1-suppressing protein 1; ER protein with chaperone and co-chaperone activity; involved in retention of resident ER proteins; has a role in recognizing proteins targeted for ER-associated degradation (ERAD), member of the protein disulfide isomerase family.

Protein disulfide isomerase; multifunctional oxidoreductase of the ER lumen, essential for disulfide bond formation in secretory and cell-surface proteins, processing of non-native disulfide bonds; Ero1p activator; complexes with exomannosidase, Mnl1p to facilitate the recognition of misfolded glycoproteins and the trimming of glycan Man8GlcNAc2 to Man7GlcNAc2 on substrates, thereby accelerating ERAD; PDI1 has a paralog, EUG1, that arose from the whole genome duplication.

5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Uroporphyrinogen decarboxylase; catalyzes the fifth step in the heme biosynthetic pathway; localizes to both the cytoplasm and nucleus; a hem12 mutant has phenotypes similar to patients with porphyria cutanea tarda.

5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Oxygen-dependent coproporphyrinogen-III oxidase; Coproporphyrinogen III oxidase; oxygen-requiring enzyme that catalyzes sixth step in heme biosynthetic pathway; transcription is repressed by oxygen and heme (via Rox1p and Hap1p); human homolog CPOX can complement yeast mutant and allow growth of haploid null after sporulation of a heterozygous diploid; Belongs to the aerobic coproporphyrinogen-III oxidase family.

5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Protoporphyrinogen oxidase; a mitochondrial enzyme that catalyzes the seventh step in the heme biosynthetic pathway, converting protoporphyrinogen IX to protoporphyrin IX; inhibited by diphenyl ether-type herbicides.

5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Ferrochelatase; a mitochondrial inner membrane protein, catalyzes insertion of ferrous iron into protoporphyrin IX, the eighth and final step in the heme biosynthetic pathway; human homolog FECH can complement yeast mutant and allow growth of haploid null after sporulation of a heterozygous diploid.

5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Delta-aminolevulinic acid dehydratase; Aminolevulinate dehydratase; a homo-octameric enzyme, catalyzes the conversion of 5-aminolevulinate to porphobilinogen, the second step in heme biosynthesis; enzymatic activity is zinc-dependent; localizes to the cytoplasm and nucleus; human homolog ALAD can complement yeast hem2 mutant.

5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Porphobilinogen deaminase; catalyzes the conversion of 4-porphobilinogen to hydroxymethylbilane, the third step in heme biosynthesis; localizes to the cytoplasm and nucleus; expression is regulated by Hap2p-Hap3p, but not by levels of heme; human homolog HMBS can complement yeast mutant and allow growth of haploid null after sporulation of a heterozygous diploid.

5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Uroporphyrinogen III synthase; catalyzes the conversion of hydroxymethylbilane to uroporphyrinogen III, the fourth step in heme biosynthesis; deficiency in the human homolog can result in the disease congenital erythropoietic porphyria.

Uroporphyrinogen decarboxylase; catalyzes the fifth step in the heme biosynthetic pathway; localizes to both the cytoplasm and nucleus; a hem12 mutant has phenotypes similar to patients with porphyria cutanea tarda.

5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Uroporphyrinogen decarboxylase; catalyzes the fifth step in the heme biosynthetic pathway; localizes to both the cytoplasm and nucleus; a hem12 mutant has phenotypes similar to patients with porphyria cutanea tarda.

Oxygen-dependent coproporphyrinogen-III oxidase; Coproporphyrinogen III oxidase; oxygen-requiring enzyme that catalyzes sixth step in heme biosynthetic pathway; transcription is repressed by oxygen and heme (via Rox1p and Hap1p); human homolog CPOX can complement yeast mutant and allow growth of haploid null after sporulation of a heterozygous diploid; Belongs to the aerobic coproporphyrinogen-III oxidase family.

Uroporphyrinogen decarboxylase; catalyzes the fifth step in the heme biosynthetic pathway; localizes to both the cytoplasm and nucleus; a hem12 mutant has phenotypes similar to patients with porphyria cutanea tarda.

Protoporphyrinogen oxidase; a mitochondrial enzyme that catalyzes the seventh step in the heme biosynthetic pathway, converting protoporphyrinogen IX to protoporphyrin IX; inhibited by diphenyl ether-type herbicides.

Uroporphyrinogen decarboxylase; catalyzes the fifth step in the heme biosynthetic pathway; localizes to both the cytoplasm and nucleus; a hem12 mutant has phenotypes similar to patients with porphyria cutanea tarda.

Ferrochelatase; a mitochondrial inner membrane protein, catalyzes insertion of ferrous iron into protoporphyrin IX, the eighth and final step in the heme biosynthetic pathway; human homolog FECH can complement yeast mutant and allow growth of haploid null after sporulation of a heterozygous diploid.

Uroporphyrinogen decarboxylase; catalyzes the fifth step in the heme biosynthetic pathway; localizes to both the cytoplasm and nucleus; a hem12 mutant has phenotypes similar to patients with porphyria cutanea tarda.

Delta-aminolevulinic acid dehydratase; Aminolevulinate dehydratase; a homo-octameric enzyme, catalyzes the conversion of 5-aminolevulinate to porphobilinogen, the second step in heme biosynthesis; enzymatic activity is zinc-dependent; localizes to the cytoplasm and nucleus; human homolog ALAD can complement yeast hem2 mutant.

Uroporphyrinogen decarboxylase; catalyzes the fifth step in the heme biosynthetic pathway; localizes to both the cytoplasm and nucleus; a hem12 mutant has phenotypes similar to patients with porphyria cutanea tarda.

Porphobilinogen deaminase; catalyzes the conversion of 4-porphobilinogen to hydroxymethylbilane, the third step in heme biosynthesis; localizes to the cytoplasm and nucleus; expression is regulated by Hap2p-Hap3p, but not by levels of heme; human homolog HMBS can complement yeast mutant and allow growth of haploid null after sporulation of a heterozygous diploid.

Uroporphyrinogen decarboxylase; catalyzes the fifth step in the heme biosynthetic pathway; localizes to both the cytoplasm and nucleus; a hem12 mutant has phenotypes similar to patients with porphyria cutanea tarda.

Uroporphyrinogen III synthase; catalyzes the conversion of hydroxymethylbilane to uroporphyrinogen III, the fourth step in heme biosynthesis; deficiency in the human homolog can result in the disease congenital erythropoietic porphyria.

Uroporphyrinogen decarboxylase; catalyzes the fifth step in the heme biosynthetic pathway; localizes to both the cytoplasm and nucleus; a hem12 mutant has phenotypes similar to patients with porphyria cutanea tarda.

Heme-binding protein HMX1; ER localized heme oxygenase; involved in heme degradation during iron starvation and in the oxidative stress response; expression is regulated by AFT1 and oxidative stress; relocates to the perinuclear region in the presence of oxidants.

Oxygen-dependent coproporphyrinogen-III oxidase; Coproporphyrinogen III oxidase; oxygen-requiring enzyme that catalyzes sixth step in heme biosynthetic pathway; transcription is repressed by oxygen and heme (via Rox1p and Hap1p); human homolog CPOX can complement yeast mutant and allow growth of haploid null after sporulation of a heterozygous diploid; Belongs to the aerobic coproporphyrinogen-III oxidase family.

5-aminolevulinate synthase, mitochondrial; 5-aminolevulinate synthase; catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; has a pyridoxal phosphate cofactor whose insertion is mediated by Mcx1p; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.