Application | Comment | Organism |
---|---|---|
drug development | the enzyme represents a potential target for chemotherapeutics | Mycobacterium tuberculosis |
drug development | the enzyme represents a potential target for chemotherapeutics | Escherichia coli |
drug development | the enzyme represents a potential target for chemotherapeutics | Geobacillus stearothermophilus |
drug development | the enzyme represents a potential target for chemotherapeutics | Psychromonas ingrahamii |
drug development | the enzyme represents a potential target for chemotherapeutics | Staphylococcus aureus |
drug development | the enzyme represents a potential target for chemotherapeutics | Thermus thermophilus |
drug development | the enzyme represents a potential target for chemotherapeutics | Burkholderia pseudomallei |
drug development | the enzyme represents a potential target for chemotherapeutics | Salmonella enterica subsp. enterica serovar Typhimurium |
drug development | the enzyme represents a potential target for chemotherapeutics | Campylobacter jejuni |
drug development | the enzyme represents a potential target for chemotherapeutics | Rickettsia rickettsii |
drug development | the enzyme represents a potential target for chemotherapeutics | Burkholderia cenocepacia |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
5,10-methylenetetrahydrofolate + glycine + H2O | Mycobacterium tuberculosis | - |
tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | Escherichia coli | - |
tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | Geobacillus stearothermophilus | - |
tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | Psychromonas ingrahamii | - |
tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | Staphylococcus aureus | - |
tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | Thermus thermophilus | - |
tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | Burkholderia pseudomallei | - |
tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | Salmonella enterica subsp. enterica serovar Typhimurium | - |
tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | Campylobacter jejuni | - |
tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | Rickettsia rickettsii | - |
tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | Burkholderia cenocepacia | - |
tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | Campylobacter jejuni ATCC 33560 | - |
tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | Psychromonas ingrahamii 37 | - |
tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | Mycobacterium tuberculosis H37Rv | - |
tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | Staphylococcus aureus COL | - |
tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | Burkholderia pseudomallei ATCC 23343 | - |
tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | Rickettsia rickettsii Sheila Smith | - |
tetrahydrofolate + L-serine | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Burkholderia cenocepacia | B4ECY9 | gene glyA | - |
Burkholderia pseudomallei | A0A069BAT4 | gene glyA | - |
Burkholderia pseudomallei ATCC 23343 | A0A069BAT4 | gene glyA | - |
Campylobacter jejuni | Q9S6K1 | gene glyA | - |
Campylobacter jejuni ATCC 33560 | Q9S6K1 | gene glyA | - |
Escherichia coli | P0A825 | gene glyA | - |
Geobacillus stearothermophilus | Q7SIB6 | gene glyA | - |
Mycobacterium tuberculosis | P9WGI9 | gene glyA1 | - |
Mycobacterium tuberculosis H37Rv | P9WGI9 | gene glyA1 | - |
Psychromonas ingrahamii | A1SUU0 | gene glyA | - |
Psychromonas ingrahamii 37 | A1SUU0 | gene glyA | - |
Rickettsia rickettsii | A8GTI9 | gene glyA | - |
Rickettsia rickettsii Sheila Smith | A8GTI9 | gene glyA | - |
Salmonella enterica subsp. enterica serovar Typhimurium | P0A2E1 | gene glyA | - |
Staphylococcus aureus | Q5HE87 | gene glyA | - |
Staphylococcus aureus COL | Q5HE87 | gene glyA | - |
Thermus thermophilus | Q5SI56 | gene glyA | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Mycobacterium tuberculosis | tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Escherichia coli | tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Geobacillus stearothermophilus | tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Psychromonas ingrahamii | tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Staphylococcus aureus | tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Thermus thermophilus | tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Burkholderia pseudomallei | tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Salmonella enterica subsp. enterica serovar Typhimurium | tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Campylobacter jejuni | tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Rickettsia rickettsii | tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Burkholderia cenocepacia | tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Campylobacter jejuni ATCC 33560 | tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Psychromonas ingrahamii 37 | tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Mycobacterium tuberculosis H37Rv | tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Staphylococcus aureus COL | tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Burkholderia pseudomallei ATCC 23343 | tetrahydrofolate + L-serine | - |
r | |
5,10-methylenetetrahydrofolate + glycine + H2O | - |
Rickettsia rickettsii Sheila Smith | tetrahydrofolate + L-serine | - |
r |
Subunits | Comment | Organism |
---|---|---|
dimer | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview | Mycobacterium tuberculosis |
dimer | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview | Escherichia coli |
dimer | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview | Geobacillus stearothermophilus |
dimer | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview | Psychromonas ingrahamii |
dimer | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview | Staphylococcus aureus |
dimer | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview | Thermus thermophilus |
dimer | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview | Burkholderia pseudomallei |
dimer | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview | Salmonella enterica subsp. enterica serovar Typhimurium |
dimer | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview | Campylobacter jejuni |
dimer | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview | Rickettsia rickettsii |
dimer | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview | Burkholderia cenocepacia |
Synonyms | Comment | Organism |
---|---|---|
serine hydroxymethyltransferase | - |
Mycobacterium tuberculosis |
serine hydroxymethyltransferase | - |
Escherichia coli |
serine hydroxymethyltransferase | - |
Geobacillus stearothermophilus |
serine hydroxymethyltransferase | - |
Psychromonas ingrahamii |
serine hydroxymethyltransferase | - |
Staphylococcus aureus |
serine hydroxymethyltransferase | - |
Thermus thermophilus |
serine hydroxymethyltransferase | - |
Burkholderia pseudomallei |
serine hydroxymethyltransferase | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
serine hydroxymethyltransferase | - |
Campylobacter jejuni |
serine hydroxymethyltransferase | - |
Rickettsia rickettsii |
serine hydroxymethyltransferase | - |
Burkholderia cenocepacia |
SHMT | - |
Mycobacterium tuberculosis |
SHMT | - |
Escherichia coli |
SHMT | - |
Geobacillus stearothermophilus |
SHMT | - |
Psychromonas ingrahamii |
SHMT | - |
Staphylococcus aureus |
SHMT | - |
Thermus thermophilus |
SHMT | - |
Burkholderia pseudomallei |
SHMT | - |
Salmonella enterica subsp. enterica serovar Typhimurium |
SHMT | - |
Campylobacter jejuni |
SHMT | - |
Rickettsia rickettsii |
SHMT | - |
Burkholderia cenocepacia |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
5,10-methylenetetrahydrofolate | - |
Mycobacterium tuberculosis | |
5,10-methylenetetrahydrofolate | - |
Escherichia coli | |
5,10-methylenetetrahydrofolate | - |
Geobacillus stearothermophilus | |
5,10-methylenetetrahydrofolate | - |
Psychromonas ingrahamii | |
5,10-methylenetetrahydrofolate | - |
Staphylococcus aureus | |
5,10-methylenetetrahydrofolate | - |
Thermus thermophilus | |
5,10-methylenetetrahydrofolate | - |
Burkholderia pseudomallei | |
5,10-methylenetetrahydrofolate | - |
Salmonella enterica subsp. enterica serovar Typhimurium | |
5,10-methylenetetrahydrofolate | - |
Campylobacter jejuni | |
5,10-methylenetetrahydrofolate | - |
Rickettsia rickettsii | |
5,10-methylenetetrahydrofolate | - |
Burkholderia cenocepacia | |
pyridoxal 5'-phosphate | dependent on | Mycobacterium tuberculosis | |
pyridoxal 5'-phosphate | dependent on | Escherichia coli | |
pyridoxal 5'-phosphate | dependent on | Geobacillus stearothermophilus | |
pyridoxal 5'-phosphate | dependent on | Psychromonas ingrahamii | |
pyridoxal 5'-phosphate | dependent on | Staphylococcus aureus | |
pyridoxal 5'-phosphate | dependent on | Thermus thermophilus | |
pyridoxal 5'-phosphate | dependent on | Burkholderia pseudomallei | |
pyridoxal 5'-phosphate | dependent on | Salmonella enterica subsp. enterica serovar Typhimurium | |
pyridoxal 5'-phosphate | dependent on | Campylobacter jejuni | |
pyridoxal 5'-phosphate | dependent on | Rickettsia rickettsii | |
pyridoxal 5'-phosphate | dependent on | Burkholderia cenocepacia | |
tetrahydrofolate | - |
Mycobacterium tuberculosis | |
tetrahydrofolate | - |
Escherichia coli | |
tetrahydrofolate | - |
Geobacillus stearothermophilus | |
tetrahydrofolate | - |
Psychromonas ingrahamii | |
tetrahydrofolate | - |
Staphylococcus aureus | |
tetrahydrofolate | - |
Thermus thermophilus | |
tetrahydrofolate | - |
Burkholderia pseudomallei | |
tetrahydrofolate | - |
Salmonella enterica subsp. enterica serovar Typhimurium | |
tetrahydrofolate | - |
Campylobacter jejuni | |
tetrahydrofolate | - |
Rickettsia rickettsii | |
tetrahydrofolate | - |
Burkholderia cenocepacia |
General Information | Comment | Organism |
---|---|---|
evolution | SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process | Mycobacterium tuberculosis |
evolution | SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process | Escherichia coli |
evolution | SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process | Geobacillus stearothermophilus |
evolution | SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process | Psychromonas ingrahamii |
evolution | SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process | Staphylococcus aureus |
evolution | SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process | Thermus thermophilus |
evolution | SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process | Burkholderia pseudomallei |
evolution | SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process | Salmonella enterica subsp. enterica serovar Typhimurium |
evolution | SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process | Campylobacter jejuni |
evolution | SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process | Rickettsia rickettsii |
evolution | SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process | Burkholderia cenocepacia |
additional information | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 1DFO, molecular dynamics, overview | Escherichia coli |
additional information | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 1KKJ, molecular dynamics, overview | Geobacillus stearothermophilus |
additional information | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 2DKJ, molecular dynamics, overview | Thermus thermophilus |
additional information | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3ECD, molecular dynamics, overview | Burkholderia pseudomallei |
additional information | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3GBX, molecular dynamics, overview | Salmonella enterica subsp. enterica serovar Typhimurium |
additional information | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3H7F, molecular dynamics, overview | Mycobacterium tuberculosis |
additional information | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3N0L, molecular dynamics, overview | Campylobacter jejuni |
additional information | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 3PGY, molecular dynamics, overview | Staphylococcus aureus |
additional information | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4J5U, molecular dynamics, overview | Rickettsia rickettsii |
additional information | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4N0W, molecular dynamics, overview | Burkholderia cenocepacia |
additional information | analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 4P3M, molecular dynamics, overview | Psychromonas ingrahamii |
physiological function | SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the 5,10-methylenetetrahydropteroylglutamate-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage | Escherichia coli |
physiological function | SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage | Mycobacterium tuberculosis |
physiological function | SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage | Geobacillus stearothermophilus |
physiological function | SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage | Psychromonas ingrahamii |
physiological function | SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage | Staphylococcus aureus |
physiological function | SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage | Thermus thermophilus |
physiological function | SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage | Burkholderia pseudomallei |
physiological function | SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage | Salmonella enterica subsp. enterica serovar Typhimurium |
physiological function | SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage | Campylobacter jejuni |
physiological function | SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage | Rickettsia rickettsii |
physiological function | SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage | Burkholderia cenocepacia |