C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

Thymidylate synthase; required for de novo biosynthesis of pyrimidine deoxyribonucleotides; expression is induced at G1/S; human homolog TYMSOS can complement yeast cdc21 temperature-sensitive mutant at restrictive temperature.

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

Dihydrofolate reductase involved in tetrahydrofolate biosynthesis; required for respiratory metabolism; mutation is functionally complemented by human DHFR.

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

5-formyltetrahydrofolate cyclo-ligase; 5,10-methenyltetrahydrofolate synthetase; involved in folic acid biosynthesis.

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

Methionyl-tRNA formyltransferase, mitochondrial; Methionyl-tRNA formyltransferase; catalyzes the formylation of initiator Met-tRNA in mitochondria; potential Cdc28p substrate.

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase; Multifunctional enzyme of the folic acid biosynthesis pathway; has dihydropteroate synthetase, dihydro-6-hydroxymethylpterin pyrophosphokinase, and dihydroneopterin aldolase activities; In the central section; belongs to the HPPK family.

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

GTP-cyclohydrolase I, catalyzes first step in folic acid biosynthesis; human homolog GCH1 is implicated in dopa-responsive dystonia (DRD), and can complement yeast null mutant.

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

Dihydrofolate synthetase, involved in folic acid biosynthesis; catalyzes conversion of dihydropteroate to dihydrofolate in folate coenzyme biosynthesis; FOL3 has a paralog, RMA1, that arose from the whole genome duplication.

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

T subunit of the mitochondrial glycine decarboxylase complex; glycine decarboxylase is required for the catabolism of glycine to 5,10-methylene-THF; expression is regulated by levels of levels of 5,10-methylene-THF in the cytoplasm.

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

P subunit of the mitochondrial glycine decarboxylase complex; glycine decarboxylase is required for the catabolism of glycine to 5,10-methylene-THF; expression is regulated by levels of 5,10-methylene-THF in the cytoplasm.

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

H subunit of the mitochondrial glycine decarboxylase complex; glycine decarboxylase is required for the catabolism of glycine to 5,10-methylene-THF; also required for all protein lipoylation; expression is regulated by levels of 5,10-methylene-THF; Belongs to the GcvH family.

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

Methylenetetrahydrofolate reductase 1; Protein with MTHFR activity in vitro; null mutant has no phenotype and is prototrophic for methionine; MET13 encodes major isozyme of methylenetetrahydrofolate reductase (MTHFR).

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

Major isozyme of methylenetetrahydrofolate reductase; catalyzes the reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate in the methionine biosynthesis pathway.

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

Folylpolyglutamate synthetase; catalyzes extension of the glutamate chains of the folate coenzymes, required for methionine synthesis and for maintenance of mitochondrial DNA; protein abundance increases in response to DNA replication stress.

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

C-1-tetrahydrofolate synthase, mitochondrial; Mitochondrial C1-tetrahydrofolate synthase; involved in interconversion between different oxidation states of tetrahydrofolate (THF); provides activities of formyl-THF synthetase, methenyl-THF cyclohydrolase, and methylene-THF dehydrogenase.

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

Methylenetetrahydrofolate dehydrogenase [NAD(+)]; NAD-dependent 5,10-methylenetetrahydrafolate dehydrogenase; plays a catalytic role in oxidation of cytoplasmic one-carbon units; expression is regulated by Bas1p and Bas2p, repressed by adenine, and may be induced by inositol and choline; Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family.

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

Probable folylpolyglutamate synthase; Putative dihydrofolate synthetase; similar to E. coli folylpolyglutamate synthetase/dihydrofolate synthetase; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; RMA1 has a paralog, FOL3, that arose from the whole genome duplication.

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

Mitochondrial serine hydroxymethyltransferase; converts serine to glycine plus 5,10 methylenetetrahydrofolate; involved in generating precursors for purine, pyrimidine, amino acid, and lipid biosynthesis; reverse reaction generates serine; Belongs to the SHMT family.

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

Cytosolic serine hydroxymethyltransferase; converts serine to glycine plus 5,10 methylenetetrahydrofolate; major isoform involved in generating precursors for purine, pyrimidine, amino acid, and lipid biosynthesis; Belongs to the SHMT family.

Thymidylate synthase; required for de novo biosynthesis of pyrimidine deoxyribonucleotides; expression is induced at G1/S; human homolog TYMSOS can complement yeast cdc21 temperature-sensitive mutant at restrictive temperature.

C-1-tetrahydrofolate synthase, cytoplasmic; Cytoplasmic trifunctional enzyme C1-tetrahydrofolate synthase; involved in single carbon metabolism and required for biosynthesis of purines, thymidylate, methionine, and histidine; null mutation causes auxotrophy for adenine and histidine.

Thymidylate synthase; required for de novo biosynthesis of pyrimidine deoxyribonucleotides; expression is induced at G1/S; human homolog TYMSOS can complement yeast cdc21 temperature-sensitive mutant at restrictive temperature.

Dihydrofolate reductase involved in tetrahydrofolate biosynthesis; required for respiratory metabolism; mutation is functionally complemented by human DHFR.