Literature summary for 2.1.2.1 extracted from

Milano, T.; Di Salvo, M.L.; Angelaccio, S.; Pascarella, S.
Conserved water molecules in bacterial serine hydroxymethyltransferases (2015), Protein Eng. Des. Sel., 28, 415-426.

Application

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/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
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

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 and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
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

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

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

Cofactor	Comment	Organism
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

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