3-hydroxyanthranilate 3,4-dioxygenase; 3-hydroxyanthranilic acid dioxygenase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p.

Tryptophan 2,3-dioxygenase or indoleamine 2,3-dioxygenase; required for de novo biosynthesis of NAD from tryptophan via kynurenine; interacts genetically with telomere capping gene CDC13; regulated by Hst1p and Aftp.

3-hydroxyanthranilate 3,4-dioxygenase; 3-hydroxyanthranilic acid dioxygenase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p.

Kynurenine 3-monooxygenase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p; putative therapeutic target for Huntington disease.

3-hydroxyanthranilate 3,4-dioxygenase; 3-hydroxyanthranilic acid dioxygenase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p.

Kynureninase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p.

Tryptophan 2,3-dioxygenase or indoleamine 2,3-dioxygenase; required for de novo biosynthesis of NAD from tryptophan via kynurenine; interacts genetically with telomere capping gene CDC13; regulated by Hst1p and Aftp.

3-hydroxyanthranilate 3,4-dioxygenase; 3-hydroxyanthranilic acid dioxygenase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p.

Tryptophan 2,3-dioxygenase or indoleamine 2,3-dioxygenase; required for de novo biosynthesis of NAD from tryptophan via kynurenine; interacts genetically with telomere capping gene CDC13; regulated by Hst1p and Aftp.

Kynurenine 3-monooxygenase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p; putative therapeutic target for Huntington disease.

Tryptophan 2,3-dioxygenase or indoleamine 2,3-dioxygenase; required for de novo biosynthesis of NAD from tryptophan via kynurenine; interacts genetically with telomere capping gene CDC13; regulated by Hst1p and Aftp.

Kynureninase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p.

Kynurenine 3-monooxygenase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p; putative therapeutic target for Huntington disease.

3-hydroxyanthranilate 3,4-dioxygenase; 3-hydroxyanthranilic acid dioxygenase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p.

Kynurenine 3-monooxygenase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p; putative therapeutic target for Huntington disease.

Tryptophan 2,3-dioxygenase or indoleamine 2,3-dioxygenase; required for de novo biosynthesis of NAD from tryptophan via kynurenine; interacts genetically with telomere capping gene CDC13; regulated by Hst1p and Aftp.

Kynurenine 3-monooxygenase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p; putative therapeutic target for Huntington disease.

Kynureninase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p.

Kynureninase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p.

3-hydroxyanthranilate 3,4-dioxygenase; 3-hydroxyanthranilic acid dioxygenase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p.

Kynureninase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p.

Tryptophan 2,3-dioxygenase or indoleamine 2,3-dioxygenase; required for de novo biosynthesis of NAD from tryptophan via kynurenine; interacts genetically with telomere capping gene CDC13; regulated by Hst1p and Aftp.

Kynureninase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p.

Kynurenine 3-monooxygenase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p; putative therapeutic target for Huntington disease.

Cytochrome c, isoform 1; also known as iso-1-cytochrome c; electron carrier of mitochondrial intermembrane space that transfers electrons from ubiquinone-cytochrome c oxidoreductase to cytochrome c oxidase during cellular respiration; CYC1 has a paralog, CYC7, that arose from the whole genome duplication; human homolog CYC1 can complement yeast null mutant; mutations in human CYC1 cause insulin-responsive hyperglycemia.

Cytochrome c isoform 2, expressed under hypoxic conditions; also known as iso-2-cytochrome c; electron carrier of the mitochondrial intermembrane space that transfers electrons from ubiquinone-cytochrome c oxidoreductase to cytochrome c oxidase during cellular respiration; protein abundance increases in response to DNA replication stress; CYC7 has a paralog, CYC1, that arose from the whole genome duplication.

Cytochrome c isoform 2, expressed under hypoxic conditions; also known as iso-2-cytochrome c; electron carrier of the mitochondrial intermembrane space that transfers electrons from ubiquinone-cytochrome c oxidoreductase to cytochrome c oxidase during cellular respiration; protein abundance increases in response to DNA replication stress; CYC7 has a paralog, CYC1, that arose from the whole genome duplication.

Cytochrome c, isoform 1; also known as iso-1-cytochrome c; electron carrier of mitochondrial intermembrane space that transfers electrons from ubiquinone-cytochrome c oxidoreductase to cytochrome c oxidase during cellular respiration; CYC1 has a paralog, CYC7, that arose from the whole genome duplication; human homolog CYC1 can complement yeast null mutant; mutations in human CYC1 cause insulin-responsive hyperglycemia.

Long-chain-fatty-acid--CoA ligase 1; Long chain fatty acyl-CoA synthetase; activates fatty acids with a preference for C12:0-C16:0 chain lengths; role in the competitive import of long-chain fatty acids and sphingoid long-chain bases; accounts for most acyl-CoA synthetase activity; localizes to lipid particles and the plasma membrane; role in sphingolipid-to-glycerolipid metabolism; forms ER foci upon replication stress; faa1 faa4 double null complemented by any of human ACSBG1, ACSL1, 3, 4, 5, 6, SLC27A2, or 4.

Long-chain-fatty-acid--CoA ligase 2; Medium chain fatty acyl-CoA synthetase; activates imported fatty acids; accepts a wide range of fatty acid chain lengths with a preference for medium chains, C9:0-C13:0; localized to the peroxisome; comparative analysis suggests that a mitochondrially targeted form may result from translation starting at a non-canonical codon upstream of the annotated start codon.

Long-chain-fatty-acid--CoA ligase 1; Long chain fatty acyl-CoA synthetase; activates fatty acids with a preference for C12:0-C16:0 chain lengths; role in the competitive import of long-chain fatty acids and sphingoid long-chain bases; accounts for most acyl-CoA synthetase activity; localizes to lipid particles and the plasma membrane; role in sphingolipid-to-glycerolipid metabolism; forms ER foci upon replication stress; faa1 faa4 double null complemented by any of human ACSBG1, ACSL1, 3, 4, 5, 6, SLC27A2, or 4.

Long-chain-fatty-acid--CoA ligase 3; Long chain fatty acyl-CoA synthetase; activates imported fatty acids with a preference for C16:0-C18:0 chain lengths; green fluorescent protein (GFP)-fusion protein localizes to the cell periphery; Belongs to the ATP-dependent AMP-binding enzyme family.

Long-chain-fatty-acid--CoA ligase 1; Long chain fatty acyl-CoA synthetase; activates fatty acids with a preference for C12:0-C16:0 chain lengths; role in the competitive import of long-chain fatty acids and sphingoid long-chain bases; accounts for most acyl-CoA synthetase activity; localizes to lipid particles and the plasma membrane; role in sphingolipid-to-glycerolipid metabolism; forms ER foci upon replication stress; faa1 faa4 double null complemented by any of human ACSBG1, ACSL1, 3, 4, 5, 6, SLC27A2, or 4.

Long-chain-fatty-acid--CoA ligase 4; Long chain fatty acyl-CoA synthetase; activates fatty acids with a preference for C12:0-C16:0 chain lengths; role in the competitive import of long-chain fatty acids and sphingoid long-chain bases; role in stationary phase survival; localizes to lipid particles and the plasma membrane; role in sphingolipid-to-glycerolipid metabolism; forms cytoplasmic foci upon replication stress; faa1 faa4 double null complemented by any of human ACSBG1, ACSL1, 3, 4, 5, 6, SLC27A2, or 4; Belongs to the ATP-dependent AMP-binding enzyme family.

Long-chain-fatty-acid--CoA ligase 1; Long chain fatty acyl-CoA synthetase; activates fatty acids with a preference for C12:0-C16:0 chain lengths; role in the competitive import of long-chain fatty acids and sphingoid long-chain bases; accounts for most acyl-CoA synthetase activity; localizes to lipid particles and the plasma membrane; role in sphingolipid-to-glycerolipid metabolism; forms ER foci upon replication stress; faa1 faa4 double null complemented by any of human ACSBG1, ACSL1, 3, 4, 5, 6, SLC27A2, or 4.

Glycerol kinase; converts glycerol to glycerol-3-phosphate; glucose repression of expression is mediated by Adr1p and Ino2p-Ino4p; derepression of expression on non-fermentable carbon sources is mediated by Opi1p and Rsf1p; Belongs to the FGGY kinase family.

Long-chain-fatty-acid--CoA ligase 1; Long chain fatty acyl-CoA synthetase; activates fatty acids with a preference for C12:0-C16:0 chain lengths; role in the competitive import of long-chain fatty acids and sphingoid long-chain bases; accounts for most acyl-CoA synthetase activity; localizes to lipid particles and the plasma membrane; role in sphingolipid-to-glycerolipid metabolism; forms ER foci upon replication stress; faa1 faa4 double null complemented by any of human ACSBG1, ACSL1, 3, 4, 5, 6, SLC27A2, or 4.

Beta 6 subunit of the 20S proteasome.

Long-chain-fatty-acid--CoA ligase 2; Medium chain fatty acyl-CoA synthetase; activates imported fatty acids; accepts a wide range of fatty acid chain lengths with a preference for medium chains, C9:0-C13:0; localized to the peroxisome; comparative analysis suggests that a mitochondrially targeted form may result from translation starting at a non-canonical codon upstream of the annotated start codon.

Long-chain-fatty-acid--CoA ligase 1; Long chain fatty acyl-CoA synthetase; activates fatty acids with a preference for C12:0-C16:0 chain lengths; role in the competitive import of long-chain fatty acids and sphingoid long-chain bases; accounts for most acyl-CoA synthetase activity; localizes to lipid particles and the plasma membrane; role in sphingolipid-to-glycerolipid metabolism; forms ER foci upon replication stress; faa1 faa4 double null complemented by any of human ACSBG1, ACSL1, 3, 4, 5, 6, SLC27A2, or 4.