Probable serine acetyltransferase CysE (sat); Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS); Belongs to the transferase hexapeptide repeat family.

O-acetylserine sulfhydrylase; Catalyzes the conversion of O-acetylserine (OAS) to cysteine through the elimination of acetate and addition of hydrogen sulfide. Belongs to the cysteine synthase/cystathionine beta- synthase family.

Probable serine acetyltransferase CysE (sat); Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS); Belongs to the transferase hexapeptide repeat family.

S-sulfocysteine synthase; Catalyzes the synthesis of S-sulfocysteine, utilizing O- phosphoserine (OPS) and thiosulfate as substrates. To a lesser extent, can also use sulfide as donor substrate, producing L-cysteine. CysK2 thus provides a third metabolic route to cysteine, either directly using sulfide as donor or indirectly via S-sulfocysteine. S- sulfocysteine might also act as a signaling molecule triggering additional responses in redox defense in the pathogen upon exposure to reactive oxygen species during intracellular survival or dormancy. Cannot utilize thiocarboxylated CysO as [...]

Probable serine acetyltransferase CysE (sat); Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS); Belongs to the transferase hexapeptide repeat family.

O-phosphoserine sulfhydrylase; Catalyzes the formation of a covalent CysO-cysteine adduct via a sulfur transfer, using the thiocarboxylated sulfur carrier protein CysO-COSH as sulfur donor and O-phospho-L-serine (OPS) as sulfur acceptor. Can also use sodium sulfide as sulfur donor in vitro, albeit with less efficiency, but not thiosulfate or thio-nitro- benzoate. O-acetylserine (OAS) is a very poor substrate in comparison with OPS. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis; Belongs to the cysteine synthase/cystathionine beta- sy [...]

Probable serine acetyltransferase CysE (sat); Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS); Belongs to the transferase hexapeptide repeat family.

Serine hydroxymethyltransferase 1 GlyA1; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L- allo-threonine; Belongs to the SHMT family.

Probable serine acetyltransferase CysE (sat); Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS); Belongs to the transferase hexapeptide repeat family.

Serine hydroxymethyltransferase GlyA2 (serine methylase 2) (SHMT 2); Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L- allo-threonine; Belongs to the SHMT family.

Probable serine acetyltransferase CysE (sat); Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS); Belongs to the transferase hexapeptide repeat family.

Probable threonine dehydratase IlvA; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA (By similarity).

Probable serine acetyltransferase CysE (sat); Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS); Belongs to the transferase hexapeptide repeat family.

Probable D-3-phosphoglycerate dehydrogenase SerA1 (PGDH); Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L- serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.

Probable serine acetyltransferase CysE (sat); Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS); Belongs to the transferase hexapeptide repeat family.

Probable phosphoserine phosphatase SerB2 (PSP) (O-phosphoserine phosphohydrolase) (pspase); Catalyzes the dephosphorylation of O-phospho-L-serine into L- serine, a step in the L-serine biosynthetic pathway. Exhibits high specificity for L-phosphoserine compared to substrates like L-phosphothreonine (5% relative activity) and L-phosphotyrosine (1.7% relative activity). Belongs to the HAD-like hydrolase superfamily. SerB family.

O-acetylserine sulfhydrylase; Catalyzes the conversion of O-acetylserine (OAS) to cysteine through the elimination of acetate and addition of hydrogen sulfide. Belongs to the cysteine synthase/cystathionine beta- synthase family.

Probable serine acetyltransferase CysE (sat); Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS); Belongs to the transferase hexapeptide repeat family.

O-acetylserine sulfhydrylase; Catalyzes the conversion of O-acetylserine (OAS) to cysteine through the elimination of acetate and addition of hydrogen sulfide. Belongs to the cysteine synthase/cystathionine beta- synthase family.

S-sulfocysteine synthase; Catalyzes the synthesis of S-sulfocysteine, utilizing O- phosphoserine (OPS) and thiosulfate as substrates. To a lesser extent, can also use sulfide as donor substrate, producing L-cysteine. CysK2 thus provides a third metabolic route to cysteine, either directly using sulfide as donor or indirectly via S-sulfocysteine. S- sulfocysteine might also act as a signaling molecule triggering additional responses in redox defense in the pathogen upon exposure to reactive oxygen species during intracellular survival or dormancy. Cannot utilize thiocarboxylated CysO as [...]

O-acetylserine sulfhydrylase; Catalyzes the conversion of O-acetylserine (OAS) to cysteine through the elimination of acetate and addition of hydrogen sulfide. Belongs to the cysteine synthase/cystathionine beta- synthase family.

Serine hydroxymethyltransferase 1 GlyA1; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L- allo-threonine; Belongs to the SHMT family.

O-acetylserine sulfhydrylase; Catalyzes the conversion of O-acetylserine (OAS) to cysteine through the elimination of acetate and addition of hydrogen sulfide. Belongs to the cysteine synthase/cystathionine beta- synthase family.

Rv0728c, (MTV041.02c), len: 326 aa. Possible serA2,D-3-phosphoglycerate dehydrogenase, similar to others e.g. AF0278|AF027868_5|YoaD D-3-phosphoglycerate dehydrogenase from Bacillus subtilis (344 aa), FASTA scores: opt: 594,E(): 3.1e-31, (35.9% identity in 309 aa overlap); etc. Also similar to Rv2996c|MTV012.10|SERA1 D-3-phosphoglycerate dehydrogenase from Mycobacterium tuberculosis (528 aa); Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.

O-acetylserine sulfhydrylase; Catalyzes the conversion of O-acetylserine (OAS) to cysteine through the elimination of acetate and addition of hydrogen sulfide. Belongs to the cysteine synthase/cystathionine beta- synthase family.

Possible phosphoserine aminotransferase SerC (PSAT); Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.

S-sulfocysteine synthase; Catalyzes the synthesis of S-sulfocysteine, utilizing O- phosphoserine (OPS) and thiosulfate as substrates. To a lesser extent, can also use sulfide as donor substrate, producing L-cysteine. CysK2 thus provides a third metabolic route to cysteine, either directly using sulfide as donor or indirectly via S-sulfocysteine. S- sulfocysteine might also act as a signaling molecule triggering additional responses in redox defense in the pathogen upon exposure to reactive oxygen species during intracellular survival or dormancy. Cannot utilize thiocarboxylated CysO as [...]

Probable serine acetyltransferase CysE (sat); Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS); Belongs to the transferase hexapeptide repeat family.

S-sulfocysteine synthase; Catalyzes the synthesis of S-sulfocysteine, utilizing O- phosphoserine (OPS) and thiosulfate as substrates. To a lesser extent, can also use sulfide as donor substrate, producing L-cysteine. CysK2 thus provides a third metabolic route to cysteine, either directly using sulfide as donor or indirectly via S-sulfocysteine. S- sulfocysteine might also act as a signaling molecule triggering additional responses in redox defense in the pathogen upon exposure to reactive oxygen species during intracellular survival or dormancy. Cannot utilize thiocarboxylated CysO as [...]

O-acetylserine sulfhydrylase; Catalyzes the conversion of O-acetylserine (OAS) to cysteine through the elimination of acetate and addition of hydrogen sulfide. Belongs to the cysteine synthase/cystathionine beta- synthase family.

S-sulfocysteine synthase; Catalyzes the synthesis of S-sulfocysteine, utilizing O- phosphoserine (OPS) and thiosulfate as substrates. To a lesser extent, can also use sulfide as donor substrate, producing L-cysteine. CysK2 thus provides a third metabolic route to cysteine, either directly using sulfide as donor or indirectly via S-sulfocysteine. S- sulfocysteine might also act as a signaling molecule triggering additional responses in redox defense in the pathogen upon exposure to reactive oxygen species during intracellular survival or dormancy. Cannot utilize thiocarboxylated CysO as [...]

O-phosphoserine sulfhydrylase; Catalyzes the formation of a covalent CysO-cysteine adduct via a sulfur transfer, using the thiocarboxylated sulfur carrier protein CysO-COSH as sulfur donor and O-phospho-L-serine (OPS) as sulfur acceptor. Can also use sodium sulfide as sulfur donor in vitro, albeit with less efficiency, but not thiosulfate or thio-nitro- benzoate. O-acetylserine (OAS) is a very poor substrate in comparison with OPS. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis; Belongs to the cysteine synthase/cystathionine beta- sy [...]

S-sulfocysteine synthase; Catalyzes the synthesis of S-sulfocysteine, utilizing O- phosphoserine (OPS) and thiosulfate as substrates. To a lesser extent, can also use sulfide as donor substrate, producing L-cysteine. CysK2 thus provides a third metabolic route to cysteine, either directly using sulfide as donor or indirectly via S-sulfocysteine. S- sulfocysteine might also act as a signaling molecule triggering additional responses in redox defense in the pathogen upon exposure to reactive oxygen species during intracellular survival or dormancy. Cannot utilize thiocarboxylated CysO as [...]

Rv0728c, (MTV041.02c), len: 326 aa. Possible serA2,D-3-phosphoglycerate dehydrogenase, similar to others e.g. AF0278|AF027868_5|YoaD D-3-phosphoglycerate dehydrogenase from Bacillus subtilis (344 aa), FASTA scores: opt: 594,E(): 3.1e-31, (35.9% identity in 309 aa overlap); etc. Also similar to Rv2996c|MTV012.10|SERA1 D-3-phosphoglycerate dehydrogenase from Mycobacterium tuberculosis (528 aa); Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.

S-sulfocysteine synthase; Catalyzes the synthesis of S-sulfocysteine, utilizing O- phosphoserine (OPS) and thiosulfate as substrates. To a lesser extent, can also use sulfide as donor substrate, producing L-cysteine. CysK2 thus provides a third metabolic route to cysteine, either directly using sulfide as donor or indirectly via S-sulfocysteine. S- sulfocysteine might also act as a signaling molecule triggering additional responses in redox defense in the pathogen upon exposure to reactive oxygen species during intracellular survival or dormancy. Cannot utilize thiocarboxylated CysO as [...]

Possible phosphoserine aminotransferase SerC (PSAT); Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.

O-phosphoserine sulfhydrylase; Catalyzes the formation of a covalent CysO-cysteine adduct via a sulfur transfer, using the thiocarboxylated sulfur carrier protein CysO-COSH as sulfur donor and O-phospho-L-serine (OPS) as sulfur acceptor. Can also use sodium sulfide as sulfur donor in vitro, albeit with less efficiency, but not thiosulfate or thio-nitro- benzoate. O-acetylserine (OAS) is a very poor substrate in comparison with OPS. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis; Belongs to the cysteine synthase/cystathionine beta- sy [...]

Probable serine acetyltransferase CysE (sat); Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS); Belongs to the transferase hexapeptide repeat family.

O-phosphoserine sulfhydrylase; Catalyzes the formation of a covalent CysO-cysteine adduct via a sulfur transfer, using the thiocarboxylated sulfur carrier protein CysO-COSH as sulfur donor and O-phospho-L-serine (OPS) as sulfur acceptor. Can also use sodium sulfide as sulfur donor in vitro, albeit with less efficiency, but not thiosulfate or thio-nitro- benzoate. O-acetylserine (OAS) is a very poor substrate in comparison with OPS. May be of particular importance for cysteine biosynthesis in the persistent phase of M.tuberculosis; Belongs to the cysteine synthase/cystathionine beta- sy [...]

S-sulfocysteine synthase; Catalyzes the synthesis of S-sulfocysteine, utilizing O- phosphoserine (OPS) and thiosulfate as substrates. To a lesser extent, can also use sulfide as donor substrate, producing L-cysteine. CysK2 thus provides a third metabolic route to cysteine, either directly using sulfide as donor or indirectly via S-sulfocysteine. S- sulfocysteine might also act as a signaling molecule triggering additional responses in redox defense in the pathogen upon exposure to reactive oxygen species during intracellular survival or dormancy. Cannot utilize thiocarboxylated CysO as [...]