Alanine racemase, biosynthetic, PLP-binding; Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis.

Alanine racemase, catabolic, PLP-binding; Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA.

Alanine racemase, biosynthetic, PLP-binding; Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis.

Serine hydroxymethyltransferase; 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 allothreonine and 3-phenylserine. Also catalyzes the irreversible conversion of 5,10-m [...]

Alanine racemase, biosynthetic, PLP-binding; Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis.

UPF0001 family protein, PLP-binding; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis. May have a carrier function to deliver PLP to the target enzymes or a protective function so that PLP does not inactivate essential lysines in proteins. Does not have amino acid racemase activity.

Alanine racemase, catabolic, PLP-binding; Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA.

Alanine racemase, biosynthetic, PLP-binding; Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis.

Alanine racemase, catabolic, PLP-binding; Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA.

Serine hydroxymethyltransferase; 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 allothreonine and 3-phenylserine. Also catalyzes the irreversible conversion of 5,10-m [...]

Alanine racemase, catabolic, PLP-binding; Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA.

UPF0001 family protein, PLP-binding; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis. May have a carrier function to deliver PLP to the target enzymes or a protective function so that PLP does not inactivate essential lysines in proteins. Does not have amino acid racemase activity.

Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Belongs to the thioredoxin family. DsbA subfamily.

Oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway.

Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Belongs to the thioredoxin family. DsbA subfamily.

OM lipoprotein stimulator of MrcB transpeptidase; Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b). Stimulates transpeptidase and transglycosylase activities of PBP1b in vitro. May also contribute to outer membrane constriction during cell division, in complex with PBP1b.

Oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway.

Periplasmic protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. Belongs to the thioredoxin family. DsbA subfamily.

5-formyltetrahydrofolate cyclo-ligase family protein; Involved in the removal of 5-formyltetrahydrofolate. In vitro, it is a potent inhibitor of various folate-dependent enzymes in the C1 metabolism network and in vivo it might function as a folate storage. 5-formyltetrahydrofolate is also used as an antifolate rescue agent in cancer chemotherapy. Catalyzes the irreversible ATP-dependent transformation of 5-formyltetrahydrofolate (5-CHO-THF) to form 5,10- methenyltetrahydrofolate (5,10-CH=THF). The reverse reaction is catalyzed by the serine hydroxymethyltransferase GlyA (SHMT).

Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.

5-formyltetrahydrofolate cyclo-ligase family protein; Involved in the removal of 5-formyltetrahydrofolate. In vitro, it is a potent inhibitor of various folate-dependent enzymes in the C1 metabolism network and in vivo it might function as a folate storage. 5-formyltetrahydrofolate is also used as an antifolate rescue agent in cancer chemotherapy. Catalyzes the irreversible ATP-dependent transformation of 5-formyltetrahydrofolate (5-CHO-THF) to form 5,10- methenyltetrahydrofolate (5,10-CH=THF). The reverse reaction is catalyzed by the serine hydroxymethyltransferase GlyA (SHMT).

Glycine cleavage complex lipoylprotein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.

5-formyltetrahydrofolate cyclo-ligase family protein; Involved in the removal of 5-formyltetrahydrofolate. In vitro, it is a potent inhibitor of various folate-dependent enzymes in the C1 metabolism network and in vivo it might function as a folate storage. 5-formyltetrahydrofolate is also used as an antifolate rescue agent in cancer chemotherapy. Catalyzes the irreversible ATP-dependent transformation of 5-formyltetrahydrofolate (5-CHO-THF) to form 5,10- methenyltetrahydrofolate (5,10-CH=THF). The reverse reaction is catalyzed by the serine hydroxymethyltransferase GlyA (SHMT).

Serine hydroxymethyltransferase; 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 allothreonine and 3-phenylserine. Also catalyzes the irreversible conversion of 5,10-m [...]

Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.

5-formyltetrahydrofolate cyclo-ligase family protein; Involved in the removal of 5-formyltetrahydrofolate. In vitro, it is a potent inhibitor of various folate-dependent enzymes in the C1 metabolism network and in vivo it might function as a folate storage. 5-formyltetrahydrofolate is also used as an antifolate rescue agent in cancer chemotherapy. Catalyzes the irreversible ATP-dependent transformation of 5-formyltetrahydrofolate (5-CHO-THF) to form 5,10- methenyltetrahydrofolate (5,10-CH=THF). The reverse reaction is catalyzed by the serine hydroxymethyltransferase GlyA (SHMT).

Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.

7,8-dihydropteroate synthase; Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. Belongs to the DHPS family.

Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.

Glycine cleavage complex lipoylprotein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.

Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.

Glycine decarboxylase, PLP-dependent, subunit P of glycine cleavage complex; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.

Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.

Aminomethyltransferase, tetrahydrofolate-dependent, subunit (T protein) of glycine cleavage complex; The glycine cleavage system catalyzes the degradation of glycine.

Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.

Serine hydroxymethyltransferase; 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 allothreonine and 3-phenylserine. Also catalyzes the irreversible conversion of 5,10-m [...]

7,8-dihydropteroate synthase; Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. Belongs to the DHPS family.

Dihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.

7,8-dihydropteroate synthase; Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. Belongs to the DHPS family.

Serine hydroxymethyltransferase; 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 allothreonine and 3-phenylserine. Also catalyzes the irreversible conversion of 5,10-m [...]