Literature summary extracted from

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

Metals/Ions

EC Number	Metals/Ions	Comment	Organism
2.3.1.B34	Mg2+	required	Mycobacterium tuberculosis
2.3.1.B34	Mg2+	required	Mycolicibacterium smegmatis
2.3.1.B34	Mg2+	required	Salmonella enterica subsp. enterica serovar Typhimurium

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
2.3.1.B34	acetyl-CoA + [AceA]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [AceA]-N6-acetyl-L-Lys	-	?
2.3.1.B34	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	-	?
2.3.1.B34	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	-	?
2.3.1.B34	acetyl-CoA + [AceK]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium	ACS is isocitrate dehydrogenase kinase	CoA + [AceK]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [AceK]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412	ACS is isocitrate dehydrogenase kinase	CoA + [AceK]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [AceK]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720	ACS is isocitrate dehydrogenase kinase	CoA + [AceK]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium	ACS is AcCoA synthase, Nepsilon-lysine-acetylation	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium	ACS is isocitrate lyase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	Rhodopseudomonas palustris	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	r
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	Streptomyces coelicolor	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	r
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	Streptomyces lividans	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	Mycobacterium tuberculosis	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	Mycolicibacterium smegmatis	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	Bacillus subtilis	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	Bacillus subtilis 168	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	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	-	?
2.3.1.B34	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	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	Mycolicibacterium smegmatis ATCC 700084	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	Mycobacterium tuberculosis H37Rv	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	Mycobacterium tuberculosis ATCC 25618	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	Mycolicibacterium smegmatis mc(2)155	ACS is Nepsilon-lysine-acetylated AcCoA synthase	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	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)	?	-	-
2.3.1.B34	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)	?	-	-
2.3.1.B34	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)	?	-	-
2.3.1.B34	propionyl-CoA + [PprE]-L-Lys	Salmonella enterica subsp. enterica serovar Typhimurium	PprE is propionyl-CoA synthetase	CoA + [PprE]-N6-propionyl-L-Lys	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.3.1.B34	Bacillus subtilis	P39065	-	-
2.3.1.B34	Bacillus subtilis 168	P39065	-	-
2.3.1.B34	Mycobacterium tuberculosis	O05581	-	-
2.3.1.B34	Mycobacterium tuberculosis ATCC 25618	O05581	-	-
2.3.1.B34	Mycobacterium tuberculosis H37Rv	O05581	-	-
2.3.1.B34	Mycolicibacterium smegmatis	A0R3F9	-	-
2.3.1.B34	Mycolicibacterium smegmatis ATCC 700084	A0R3F9	-	-
2.3.1.B34	Mycolicibacterium smegmatis mc(2)155	A0R3F9	-	-
2.3.1.B34	Rhodopseudomonas palustris	-	-	-
2.3.1.B34	Salmonella enterica subsp. enterica serovar Typhimurium	Q8ZMX2	-	-
2.3.1.B34	Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720	Q8ZMX2	-	-
2.3.1.B34	Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412	Q8ZMX2	-	-
2.3.1.B34	Streptomyces coelicolor	-	-	-
2.3.1.B34	Streptomyces lividans	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
2.3.1.B34	acetyl-CoA + [AceA]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Salmonella enterica subsp. enterica serovar Typhimurium	CoA + [AceA]-N6-acetyl-L-Lys	-	?
2.3.1.B34	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	-	?
2.3.1.B34	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	-	?
2.3.1.B34	acetyl-CoA + [AceK]-L-Lys	ACS is isocitrate dehydrogenase kinase	Salmonella enterica subsp. enterica serovar Typhimurium	CoA + [AceK]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [AceK]-L-Lys	ACS is isocitrate dehydrogenase kinase	Salmonella enterica subsp. enterica serovar Typhimurium SGSC1412	CoA + [AceK]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [AceK]-L-Lys	ACS is isocitrate dehydrogenase kinase	Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720	CoA + [AceK]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	ACS is AcCoA synthase, Nepsilon-lysine-acetylation	Salmonella enterica subsp. enterica serovar Typhimurium	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	ACS is isocitrate lyase	Salmonella enterica subsp. enterica serovar Typhimurium	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Rhodopseudomonas palustris	CoA + [ACS]-N6-acetyl-L-Lys	-	r
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Streptomyces coelicolor	CoA + [ACS]-N6-acetyl-L-Lys	-	r
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Streptomyces lividans	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Mycobacterium tuberculosis	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Mycolicibacterium smegmatis	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Bacillus subtilis	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Bacillus subtilis 168	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	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	-	?
2.3.1.B34	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	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Mycolicibacterium smegmatis ATCC 700084	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Mycobacterium tuberculosis H37Rv	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Mycobacterium tuberculosis ATCC 25618	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [ACS]-L-Lys	ACS is Nepsilon-lysine-acetylated AcCoA synthase	Mycolicibacterium smegmatis mc(2)155	CoA + [ACS]-N6-acetyl-L-Lys	-	?
2.3.1.B34	acetyl-CoA + [GapA]-L-Lys	ACS is glyceraldehyde-3-phosphate dehydrogenase	Salmonella enterica subsp. enterica serovar Typhimurium	CoA + [GapA]-N6-acetyl-L-Lys	-	?
2.3.1.B34	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	?	-	-
2.3.1.B34	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	?	-	-
2.3.1.B34	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	?	-	-
2.3.1.B34	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	?	-	-
2.3.1.B34	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	?	-	-
2.3.1.B34	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	?	-	-
2.3.1.B34	propionyl-CoA + [PprE]-L-Lys	PprE is propionyl-CoA synthetase	Salmonella enterica subsp. enterica serovar Typhimurium	CoA + [PprE]-N6-propionyl-L-Lys	-	?

Subunits

EC Number	Subunits	Comment	Organism
2.3.1.B34	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

EC Number	Synonyms	Comment	Organism
2.3.1.B34	acetoin utilization protein	UniProt	Bacillus subtilis
2.3.1.B34	acetyltransferase Pat	-	Rhodopseudomonas palustris
2.3.1.B34	acetyltransferase Pat	-	Streptomyces coelicolor
2.3.1.B34	acetyltransferase Pat	-	Streptomyces lividans
2.3.1.B34	acetyltransferase Pat	-	Mycobacterium tuberculosis
2.3.1.B34	acetyltransferase Pat	-	Mycolicibacterium smegmatis
2.3.1.B34	AcuA	-	Rhodopseudomonas palustris
2.3.1.B34	AcuA	-	Streptomyces coelicolor
2.3.1.B34	AcuA	-	Streptomyces lividans
2.3.1.B34	AcuA	-	Mycobacterium tuberculosis
2.3.1.B34	AcuA	-	Mycolicibacterium smegmatis
2.3.1.B34	AcuA	-	Bacillus subtilis
2.3.1.B34	BsAcuA	-	Bacillus subtilis
2.3.1.B34	epsilonN-lysine acetyltransferase	-	Rhodopseudomonas palustris
2.3.1.B34	epsilonN-lysine acetyltransferase	-	Streptomyces coelicolor
2.3.1.B34	epsilonN-lysine acetyltransferase	-	Streptomyces lividans
2.3.1.B34	epsilonN-lysine acetyltransferase	-	Mycobacterium tuberculosis
2.3.1.B34	epsilonN-lysine acetyltransferase	-	Mycolicibacterium smegmatis
2.3.1.B34	MSMEG_5458	-	Mycolicibacterium smegmatis
2.3.1.B34	Pat	-	Rhodopseudomonas palustris
2.3.1.B34	Pat	-	Streptomyces coelicolor
2.3.1.B34	Pat	-	Streptomyces lividans
2.3.1.B34	Pat	-	Mycobacterium tuberculosis
2.3.1.B34	Pat	-	Mycolicibacterium smegmatis
2.3.1.B34	Pat	-	Salmonella enterica subsp. enterica serovar Typhimurium
2.3.1.B34	peptidyl-lysine N-acetyltransferase	UniProt	Salmonella enterica subsp. enterica serovar Typhimurium
2.3.1.B34	Rv0998	-	Mycobacterium tuberculosis
2.3.1.B34	SePat	-	Salmonella enterica subsp. enterica serovar Typhimurium
2.3.1.B34	type-I bGNAT	-	Salmonella enterica subsp. enterica serovar Typhimurium
2.3.1.B34	type-IV bGNAT	-	Bacillus subtilis
2.3.1.B34	YhiQ	formerly	Salmonella enterica subsp. enterica serovar Typhimurium

Cofactor

EC Number	Cofactor	Comment	Organism
2.3.1.B34	acetyl-CoA	-	Rhodopseudomonas palustris
2.3.1.B34	acetyl-CoA	-	Streptomyces coelicolor
2.3.1.B34	acetyl-CoA	-	Streptomyces lividans
2.3.1.B34	acetyl-CoA	-	Mycobacterium tuberculosis
2.3.1.B34	acetyl-CoA	-	Mycolicibacterium smegmatis
2.3.1.B34	acetyl-CoA	-	Salmonella enterica subsp. enterica serovar Typhimurium
2.3.1.B34	acetyl-CoA	-	Bacillus subtilis
2.3.1.B34	propionyl-CoA	-	Salmonella enterica subsp. enterica serovar Typhimurium

General Information

EC Number	General Information	Comment	Organism
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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
2.3.1.B34	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