Literature summary for 2.3.1.B34 extracted from

Favrot, L.; Blanchard, J.; Vergnolle, O.
Bacterial GCN5-related N-acetyltransferases from resistance to regulation (2016), Biochemistry, 55, 989-1002 .

Search for more literature for 2.3.1.B34

Metals/Ions

Metals/Ions	Comment	Organism
Mg2+	required	Mycobacterium tuberculosis
Mg2+	required	Mycolicibacterium smegmatis
Mg2+	required	Salmonella enterica subsp. enterica serovar Typhimurium

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
acetyl-CoA + [AceA]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [AceA]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [AceA]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [AceA]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [AceA]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [AceA]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [AceK]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium	ACS is isocitrate dehydrogenase kinase	CoA + [AceK]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [AceK]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412	ACS is isocitrate dehydrogenase kinase	CoA + [AceK]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [AceK]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720	ACS is isocitrate dehydrogenase kinase	CoA + [AceK]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium	ACS is AcCoA synthase, Nepsilon-lysine-acetylation	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium	ACS is isocitrate lyase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	Rhodopseudomonas palustris	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	r
acetyl-CoA + [ACS]-L-Lys	Streptomyces coelicolor	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	r
acetyl-CoA + [ACS]-L-Lys	Streptomyces lividans	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	Mycobacterium tuberculosis	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	Mycolicibacterium smegmatis	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	Bacillus subtilis	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	Bacillus subtilis 168	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412	ACS is AcCoA synthase, Nepsilon-lysine-acetylation	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720	ACS is AcCoA synthase, Nepsilon-lysine-acetylation	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	Mycolicibacterium smegmatis ATCC 700084	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	Mycobacterium tuberculosis H37Rv	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	Mycobacterium tuberculosis ATCC 25618	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	Mycolicibacterium smegmatis mc(2)155	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
additional information	Salmonella enterica subsp. enterica serovar Typhimurium	SePat has been reported to acetylate several metabolic enzymes, including ACS, glyceraldehyde-3-phosphate dehydrogenase (GapA), isocitrate lyase (AceA), and isocitrate dehydrogenase kinase (AceK), and to propionylate propionyl-CoA synthetase (PprE)	?	-	-
additional information	Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412	SePat has been reported to acetylate several metabolic enzymes, including ACS, glyceraldehyde-3-phosphate dehydrogenase (GapA), isocitrate lyase (AceA), and isocitrate dehydrogenase kinase (AceK), and to propionylate propionyl-CoA synthetase (PprE)	?	-	-
additional information	Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720	SePat has been reported to acetylate several metabolic enzymes, including ACS, glyceraldehyde-3-phosphate dehydrogenase (GapA), isocitrate lyase (AceA), and isocitrate dehydrogenase kinase (AceK), and to propionylate propionyl-CoA synthetase (PprE)	?	-	-
propionyl-CoA + [PprE]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium	PprE is propionyl-CoA synthetase	CoA + [PprE]-N6-propionyl-L-Lys	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	P39065	-	-
Bacillus subtilis 168	P39065	-	-
Mycobacterium tuberculosis	O05581	-	-
Mycobacterium tuberculosis ATCC 25618	O05581	-	-
Mycobacterium tuberculosis H37Rv	O05581	-	-
Mycolicibacterium smegmatis	A0R3F9	-	-
Mycolicibacterium smegmatis ATCC 700084	A0R3F9	-	-
Mycolicibacterium smegmatis mc(2)155	A0R3F9	-	-
Rhodopseudomonas palustris	-	-	-
Salmonella enterica subsp. enterica serovar Typhimurium	Q8ZMX2	-	-
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720	Q8ZMX2	-	-
Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412	Q8ZMX2	-	-
Streptomyces coelicolor	-	-	-
Streptomyces lividans	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
acetyl-CoA + [AceA]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Salmonella enterica subsp. enterica serovar Typhimurium	CoA + [AceA]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [AceA]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412	CoA + [AceA]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [AceA]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720	CoA + [AceA]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [AceK]-L-Lys	ACS is isocitrate dehydrogenase kinase	Salmonella enterica subsp. enterica serovar Typhimurium	CoA + [AceK]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [AceK]-L-Lys	ACS is isocitrate dehydrogenase kinase	Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412	CoA + [AceK]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [AceK]-L-Lys	ACS is isocitrate dehydrogenase kinase	Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720	CoA + [AceK]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	ACS is AcCoA synthase, Nepsilon-lysine-acetylation	Salmonella enterica subsp. enterica serovar Typhimurium	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	ACS is isocitrate lyase	Salmonella enterica subsp. enterica serovar Typhimurium	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Rhodopseudomonas palustris	CoA + [ACS]-N6-acetyl-L-Lys	-	r
acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Streptomyces coelicolor	CoA + [ACS]-N6-acetyl-L-Lys	-	r
acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Streptomyces lividans	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Mycobacterium tuberculosis	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Mycolicibacterium smegmatis	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Bacillus subtilis	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Bacillus subtilis 168	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	ACS is AcCoA synthase, Nepsilon-lysine-acetylation	Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	ACS is AcCoA synthase, Nepsilon-lysine-acetylation	Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Mycolicibacterium smegmatis ATCC 700084	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Mycobacterium tuberculosis H37Rv	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Mycobacterium tuberculosis ATCC 25618	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Mycolicibacterium smegmatis mc(2)155	CoA + [ACS]-N6-acetyl-L-Lys	-	?
acetyl-CoA + [GapA]-L-Lys	ACS is glyceraldehyde-3-phosphate dehydrogenase	Salmonella enterica subsp. enterica serovar Typhimurium	CoA + [GapA]-N6-acetyl-L-Lys	-	?
additional information	SePat has been reported to acetylate several metabolic enzymes, including ACS, glyceraldehyde-3-phosphate dehydrogenase (GapA), isocitrate lyase (AceA), and isocitrate dehydrogenase kinase (AceK), and to propionylate propionyl-CoA synthetase (PprE)	Salmonella enterica subsp. enterica serovar Typhimurium	?	-	-
additional information	the NDP-forming AcCoA domain is unable to produce acetyl-CoA from acetate, ATP, and CoA because the catalytic histidine, present e.g. in Escherichia coli PatZ, is replaced with an asparagine (N114) in SePat	Salmonella enterica subsp. enterica serovar Typhimurium	?	-	-
additional information	SePat has been reported to acetylate several metabolic enzymes, including ACS, glyceraldehyde-3-phosphate dehydrogenase (GapA), isocitrate lyase (AceA), and isocitrate dehydrogenase kinase (AceK), and to propionylate propionyl-CoA synthetase (PprE)	Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412	?	-	-
additional information	the NDP-forming AcCoA domain is unable to produce acetyl-CoA from acetate, ATP, and CoA because the catalytic histidine, present e.g. in Escherichia coli PatZ, is replaced with an asparagine (N114) in SePat	Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412	?	-	-
additional information	SePat has been reported to acetylate several metabolic enzymes, including ACS, glyceraldehyde-3-phosphate dehydrogenase (GapA), isocitrate lyase (AceA), and isocitrate dehydrogenase kinase (AceK), and to propionylate propionyl-CoA synthetase (PprE)	Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720	?	-	-
additional information	the NDP-forming AcCoA domain is unable to produce acetyl-CoA from acetate, ATP, and CoA because the catalytic histidine, present e.g. in Escherichia coli PatZ, is replaced with an asparagine (N114) in SePat	Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720	?	-	-
propionyl-CoA + [PprE]-L-Lys	PprE is propionyl-CoA synthetase	Salmonella enterica subsp. enterica serovar Typhimurium	CoA + [PprE]-N6-propionyl-L-Lys	-	?

Subunits

Subunits	Comment	Organism
More	enzyme SePat enzyme is composed of two domains: a GNAT acetyltransferase domain at the C-terminus and a NDP-forming AcCoA synthetase domain at the N-terminus	Salmonella enterica subsp. enterica serovar Typhimurium

Synonyms

Synonyms	Comment	Organism
acetoin utilization protein	UniProt	Bacillus subtilis
acetyltransferase Pat	-	Rhodopseudomonas palustris
acetyltransferase Pat	-	Streptomyces coelicolor
acetyltransferase Pat	-	Streptomyces lividans
acetyltransferase Pat	-	Mycobacterium tuberculosis
acetyltransferase Pat	-	Mycolicibacterium smegmatis
AcuA	-	Rhodopseudomonas palustris
AcuA	-	Streptomyces coelicolor
AcuA	-	Streptomyces lividans
AcuA	-	Mycobacterium tuberculosis
AcuA	-	Mycolicibacterium smegmatis
AcuA	-	Bacillus subtilis
BsAcuA	-	Bacillus subtilis
epsilonN-lysine acetyltransferase	-	Rhodopseudomonas palustris
epsilonN-lysine acetyltransferase	-	Streptomyces coelicolor
epsilonN-lysine acetyltransferase	-	Streptomyces lividans
epsilonN-lysine acetyltransferase	-	Mycobacterium tuberculosis
epsilonN-lysine acetyltransferase	-	Mycolicibacterium smegmatis
MSMEG_5458	-	Mycolicibacterium smegmatis
Pat	-	Rhodopseudomonas palustris
Pat	-	Streptomyces coelicolor
Pat	-	Streptomyces lividans
Pat	-	Mycobacterium tuberculosis
Pat	-	Mycolicibacterium smegmatis
Pat	-	Salmonella enterica subsp. enterica serovar Typhimurium
peptidyl-lysine N-acetyltransferase	UniProt	Salmonella enterica subsp. enterica serovar Typhimurium
Rv0998	-	Mycobacterium tuberculosis
SePat	-	Salmonella enterica subsp. enterica serovar Typhimurium
type-I bGNAT	-	Salmonella enterica subsp. enterica serovar Typhimurium
type-IV bGNAT	-	Bacillus subtilis
YhiQ	formerly	Salmonella enterica subsp. enterica serovar Typhimurium

Cofactor

Cofactor	Comment	Organism
acetyl-CoA	-	Rhodopseudomonas palustris
acetyl-CoA	-	Streptomyces coelicolor
acetyl-CoA	-	Streptomyces lividans
acetyl-CoA	-	Mycobacterium tuberculosis
acetyl-CoA	-	Mycolicibacterium smegmatis
acetyl-CoA	-	Salmonella enterica subsp. enterica serovar Typhimurium
acetyl-CoA	-	Bacillus subtilis
propionyl-CoA	-	Salmonella enterica subsp. enterica serovar Typhimurium

General Information

General Information	Comment	Organism
evolution	the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes	Rhodopseudomonas palustris
evolution	the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes	Streptomyces coelicolor
evolution	the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes	Streptomyces lividans
evolution	the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes	Mycobacterium tuberculosis
evolution	the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes	Mycolicibacterium smegmatis
evolution	the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes	Salmonella enterica subsp. enterica serovar Typhimurium
evolution	the enzyme belongs to the GCN5-related N-acetyltransferases family (GNAT) is an important family of proteins that includes more than 100000 members among eukaryotes and prokaryotes	Bacillus subtilis
metabolism	enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes	Rhodopseudomonas palustris
metabolism	enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes	Streptomyces coelicolor
metabolism	enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes	Streptomyces lividans
metabolism	enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes	Mycobacterium tuberculosis
metabolism	enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes	Mycolicibacterium smegmatis
metabolism	enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes	Salmonella enterica subsp. enterica serovar Typhimurium
metabolism	enzyme acetylation by Pat is reversed by deacetylase enzymes, including the NAD+-dependent sirtuin-like deacetylases, which allows for the rapid response and adaptation to new metabolic needs or physiological changes. The ACS gene and AcuABC operon are adjacent to each other, with AcuA functioning as the acetylase and AcuC as an NAD+-independent deacetylase	Bacillus subtilis
additional information	key determinants for protein substrate recognition and subsequent acetylation. In addition to the conserved PX4GK motif on the C-terminus of the ACS protein substrate, a trio of arginines located after the PX4GK motif also conserved in ACS homologues was shown to interact with a negative patch on Pat. Those complementary ionic interactions contribute to Pat substrate specificity	Streptomyces lividans
additional information	key determinants for protein substrate recognition and subsequent acetylation. In addition to the conserved PX4GK motif on the C-terminus of the ACS protein substrate, a trio of arginines located after the PX4GK motif also conserved in ACS homologues was shown to interact with a negative patch on Pat. Those complementary ionic interactions contribute to Pat substrate specificity	Salmonella enterica subsp. enterica serovar Typhimurium
physiological function	protein acetyltransferase, Pat, catalyzes the acetylation at the apsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition	Rhodopseudomonas palustris
physiological function	protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition	Streptomyces coelicolor
physiological function	protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition	Streptomyces lividans
physiological function	protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition	Mycolicibacterium smegmatis
physiological function	protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition. Pat acetylates acetyl-CoA synthase at high intracellular concentrations of acetyl-CoA to prevent further increases in its concentration, maintain the acetate pool, and prevent unnecessary ATP hydrolysis	Mycobacterium tuberculosis
physiological function	protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition. Pat acetylates acetyl-CoA synthase at high intracellular concentrations of acetyl-CoA to prevent further increases in its concentration, maintain the acetate pool, and prevent unnecessary ATP hydrolysis	Salmonella enterica subsp. enterica serovar Typhimurium
physiological function	protein acetyltransferase, Pat, catalyzes the acetylation at the epsilon-amino group of a lysine residue is a major post-translational protein regulation mechanism found in all kingdoms of life. ACS acetylation leads to enzyme inhibition. Pat acetylates acetyl-CoA synthase at high intracellular concentrations of acetyl-CoA to prevent further increases in its concentration, maintain the acetate pool, and prevent unnecessary ATP hydrolysis. ACS activity is also post-translationally modified by GNAT protein acetyltransferase AcuA	Bacillus subtilis