Acetyl-CoA carboxylase, biotin containing enzyme; catalyzes carboxylation of cytosolic acetyl-CoA to form malonyl-CoA and regulates histone acetylation by regulating the availablity of acetyl-CoA; required for de novo biosynthesis of long-chain fatty acids; ACC1 has a paralog, HFA1, that arose from the whole genome duplication.

Bifunctional purine biosynthetic protein ADE5,7; Enzyme of the 'de novo' purine nucleotide biosynthetic pathway; contains aminoimidazole ribotide synthetase and glycinamide ribotide synthetase activities; In the C-terminal section; belongs to the AIR synthase family.

Acetyl-CoA carboxylase, biotin containing enzyme; catalyzes carboxylation of cytosolic acetyl-CoA to form malonyl-CoA and regulates histone acetylation by regulating the availablity of acetyl-CoA; required for de novo biosynthesis of long-chain fatty acids; ACC1 has a paralog, HFA1, that arose from the whole genome duplication.

Allophanate hydrolase; Urea amidolyase; contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repression and induced by allophanate, an intermediate in allantoin degradation; protein abundance increases in response to DNA replication stress.

Acetyl-CoA carboxylase, biotin containing enzyme; catalyzes carboxylation of cytosolic acetyl-CoA to form malonyl-CoA and regulates histone acetylation by regulating the availablity of acetyl-CoA; required for de novo biosynthesis of long-chain fatty acids; ACC1 has a paralog, HFA1, that arose from the whole genome duplication.

Acetyl-CoA carboxylase, mitochondrial; Mitochondrial acetyl-coenzyme A carboxylase; catalyzes production of malonyl-CoA in mitochondrial fatty acid biosynthesis; relocalizes from mitochondrion to cytoplasm upon DNA replication stress; genetic and comparative analysis suggests that translation begins at a non-canonical (Ile) start codon at -372 relative to the annotated start codon.

Acetyl-CoA carboxylase, biotin containing enzyme; catalyzes carboxylation of cytosolic acetyl-CoA to form malonyl-CoA and regulates histone acetylation by regulating the availablity of acetyl-CoA; required for de novo biosynthesis of long-chain fatty acids; ACC1 has a paralog, HFA1, that arose from the whole genome duplication.

Pyruvate carboxylase isoform; cytoplasmic enzyme that converts pyruvate to oxaloacetate; differentially regulated than isoform Pyc2p; mutations in the human homolog are associated with lactic acidosis; PYC1 has a paralog, PYC2, that arose from the whole genome duplication.

Acetyl-CoA carboxylase, biotin containing enzyme; catalyzes carboxylation of cytosolic acetyl-CoA to form malonyl-CoA and regulates histone acetylation by regulating the availablity of acetyl-CoA; required for de novo biosynthesis of long-chain fatty acids; ACC1 has a paralog, HFA1, that arose from the whole genome duplication.

Pyruvate carboxylase isoform; cytoplasmic enzyme that converts pyruvate to oxaloacetate; differentially regulated than isoform Pyc1p; mutations in the human homolog are associated with lactic acidosis; PYC2 has a paralog, PYC1, 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.

Bifunctional purine biosynthetic protein ADE5,7; Enzyme of the 'de novo' purine nucleotide biosynthetic pathway; contains aminoimidazole ribotide synthetase and glycinamide ribotide synthetase activities; In the C-terminal section; belongs to the AIR synthase family.

Bifunctional purine biosynthetic protein ADE5,7; Enzyme of the 'de novo' purine nucleotide biosynthetic pathway; contains aminoimidazole ribotide synthetase and glycinamide ribotide synthetase activities; In the C-terminal section; belongs to the AIR synthase family.

Acetyl-CoA carboxylase, biotin containing enzyme; catalyzes carboxylation of cytosolic acetyl-CoA to form malonyl-CoA and regulates histone acetylation by regulating the availablity of acetyl-CoA; required for de novo biosynthesis of long-chain fatty acids; ACC1 has a paralog, HFA1, that arose from the whole genome duplication.

Bifunctional purine biosynthetic protein ADE5,7; Enzyme of the 'de novo' purine nucleotide biosynthetic pathway; contains aminoimidazole ribotide synthetase and glycinamide ribotide synthetase activities; In the C-terminal section; belongs to the AIR synthase family.

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

Bifunctional purine biosynthetic protein ADE5,7; Enzyme of the 'de novo' purine nucleotide biosynthetic pathway; contains aminoimidazole ribotide synthetase and glycinamide ribotide synthetase activities; In the C-terminal section; belongs to the AIR synthase family.

Allophanate hydrolase; Urea amidolyase; contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repression and induced by allophanate, an intermediate in allantoin degradation; protein abundance increases in response to DNA replication stress.

Bifunctional purine biosynthetic protein ADE5,7; Enzyme of the 'de novo' purine nucleotide biosynthetic pathway; contains aminoimidazole ribotide synthetase and glycinamide ribotide synthetase activities; In the C-terminal section; belongs to the AIR synthase family.

Acetyl-CoA carboxylase, mitochondrial; Mitochondrial acetyl-coenzyme A carboxylase; catalyzes production of malonyl-CoA in mitochondrial fatty acid biosynthesis; relocalizes from mitochondrion to cytoplasm upon DNA replication stress; genetic and comparative analysis suggests that translation begins at a non-canonical (Ile) start codon at -372 relative to the annotated start codon.

Allophanate hydrolase; Urea amidolyase; contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repression and induced by allophanate, an intermediate in allantoin degradation; protein abundance increases in response to DNA replication stress.

Acetyl-CoA carboxylase, biotin containing enzyme; catalyzes carboxylation of cytosolic acetyl-CoA to form malonyl-CoA and regulates histone acetylation by regulating the availablity of acetyl-CoA; required for de novo biosynthesis of long-chain fatty acids; ACC1 has a paralog, HFA1, that arose from the whole genome duplication.

Allophanate hydrolase; Urea amidolyase; contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repression and induced by allophanate, an intermediate in allantoin degradation; protein abundance increases in response to DNA replication stress.

Bifunctional purine biosynthetic protein ADE5,7; Enzyme of the 'de novo' purine nucleotide biosynthetic pathway; contains aminoimidazole ribotide synthetase and glycinamide ribotide synthetase activities; In the C-terminal section; belongs to the AIR synthase family.

Allophanate hydrolase; Urea amidolyase; contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repression and induced by allophanate, an intermediate in allantoin degradation; protein abundance increases in response to DNA replication stress.

Acetyl-CoA carboxylase, mitochondrial; Mitochondrial acetyl-coenzyme A carboxylase; catalyzes production of malonyl-CoA in mitochondrial fatty acid biosynthesis; relocalizes from mitochondrion to cytoplasm upon DNA replication stress; genetic and comparative analysis suggests that translation begins at a non-canonical (Ile) start codon at -372 relative to the annotated start codon.

Allophanate hydrolase; Urea amidolyase; contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repression and induced by allophanate, an intermediate in allantoin degradation; protein abundance increases in response to DNA replication stress.

Pyruvate carboxylase isoform; cytoplasmic enzyme that converts pyruvate to oxaloacetate; differentially regulated than isoform Pyc2p; mutations in the human homolog are associated with lactic acidosis; PYC1 has a paralog, PYC2, that arose from the whole genome duplication.

Allophanate hydrolase; Urea amidolyase; contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repression and induced by allophanate, an intermediate in allantoin degradation; protein abundance increases in response to DNA replication stress.

Pyruvate carboxylase isoform; cytoplasmic enzyme that converts pyruvate to oxaloacetate; differentially regulated than isoform Pyc1p; mutations in the human homolog are associated with lactic acidosis; PYC2 has a paralog, PYC1, that arose from the whole genome duplication.

Acetyl-CoA carboxylase, mitochondrial; Mitochondrial acetyl-coenzyme A carboxylase; catalyzes production of malonyl-CoA in mitochondrial fatty acid biosynthesis; relocalizes from mitochondrion to cytoplasm upon DNA replication stress; genetic and comparative analysis suggests that translation begins at a non-canonical (Ile) start codon at -372 relative to the annotated start codon.

Acetyl-CoA carboxylase, biotin containing enzyme; catalyzes carboxylation of cytosolic acetyl-CoA to form malonyl-CoA and regulates histone acetylation by regulating the availablity of acetyl-CoA; required for de novo biosynthesis of long-chain fatty acids; ACC1 has a paralog, HFA1, that arose from the whole genome duplication.

Acetyl-CoA carboxylase, mitochondrial; Mitochondrial acetyl-coenzyme A carboxylase; catalyzes production of malonyl-CoA in mitochondrial fatty acid biosynthesis; relocalizes from mitochondrion to cytoplasm upon DNA replication stress; genetic and comparative analysis suggests that translation begins at a non-canonical (Ile) start codon at -372 relative to the annotated start codon.

Bifunctional purine biosynthetic protein ADE5,7; Enzyme of the 'de novo' purine nucleotide biosynthetic pathway; contains aminoimidazole ribotide synthetase and glycinamide ribotide synthetase activities; In the C-terminal section; belongs to the AIR synthase family.

Acetyl-CoA carboxylase, mitochondrial; Mitochondrial acetyl-coenzyme A carboxylase; catalyzes production of malonyl-CoA in mitochondrial fatty acid biosynthesis; relocalizes from mitochondrion to cytoplasm upon DNA replication stress; genetic and comparative analysis suggests that translation begins at a non-canonical (Ile) start codon at -372 relative to the annotated start codon.

Allophanate hydrolase; Urea amidolyase; contains both urea carboxylase and allophanate hydrolase activities, degrades urea to CO2 and NH3; expression sensitive to nitrogen catabolite repression and induced by allophanate, an intermediate in allantoin degradation; protein abundance increases in response to DNA replication stress.

Acetyl-CoA carboxylase, mitochondrial; Mitochondrial acetyl-coenzyme A carboxylase; catalyzes production of malonyl-CoA in mitochondrial fatty acid biosynthesis; relocalizes from mitochondrion to cytoplasm upon DNA replication stress; genetic and comparative analysis suggests that translation begins at a non-canonical (Ile) start codon at -372 relative to the annotated start codon.

Pyruvate carboxylase isoform; cytoplasmic enzyme that converts pyruvate to oxaloacetate; differentially regulated than isoform Pyc2p; mutations in the human homolog are associated with lactic acidosis; PYC1 has a paralog, PYC2, that arose from the whole genome duplication.

Acetyl-CoA carboxylase, mitochondrial; Mitochondrial acetyl-coenzyme A carboxylase; catalyzes production of malonyl-CoA in mitochondrial fatty acid biosynthesis; relocalizes from mitochondrion to cytoplasm upon DNA replication stress; genetic and comparative analysis suggests that translation begins at a non-canonical (Ile) start codon at -372 relative to the annotated start codon.

Pyruvate carboxylase isoform; cytoplasmic enzyme that converts pyruvate to oxaloacetate; differentially regulated than isoform Pyc1p; mutations in the human homolog are associated with lactic acidosis; PYC2 has a paralog, PYC1, that arose from the whole genome duplication.