Literature summary for 2.5.1.47 extracted from

Campanini, B.; Benoni, R.; Bettati, S.; Beck, C.M.; Hayes, C.S.; Mozzarelli, A.
Moonlighting O-acetylserine sulfhydrylase: new functions for an old protein (2015), Biochim. Biophys. Acta, 1854, 1184-1193.

Activating Compound

Activating Compound	Comment	Organism
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site	Staphylococcus aureus
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site	Salmonella enterica subsp. enterica serovar Typhimurium
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site	Haemophilus influenzae
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site	Arabidopsis thaliana
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site	Mycobacterium tuberculosis
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site	Bacillus subtilis
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site	Escherichia coli
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site	Caenorhabditis elegans
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site	Entamoeba histolytica
serine acetyltransferase	CysE, each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. 20fold increase in catalytic efficiency upon binding of CysE to CysK as a result of both decreased KM for acetyl-CoA and increased kcat. Free CysE enzyme is less active and more susceptible to aggregation, inactivation and proteolysis	Glycine max

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	CysK is competitively inhibited within the cysteine synthase complex	Glycine max

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
O-acetyl-L-serine + hydrogen sulfide	Staphylococcus aureus	-	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	Salmonella enterica subsp. enterica serovar Typhimurium	-	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	Glycine max	-	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	Haemophilus influenzae	-	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	Arabidopsis thaliana	-	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	Mycobacterium tuberculosis	-	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	Bacillus subtilis	-	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	Escherichia coli	-	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	Caenorhabditis elegans	-	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	Entamoeba histolytica	-	L-cysteine + acetate	-	?

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	P47998	gene cysK	-
Bacillus subtilis	P37887	gene cysK	-
Caenorhabditis elegans	Q93244	gene cysK	-
Entamoeba histolytica	Q401L7	-	-
Escherichia coli	P0ABK5	gene cysK	-
Glycine max	A3RM03	gene cysK	-
Haemophilus influenzae	P45040	-	-
Mycobacterium tuberculosis	P9WP55	-	-
Salmonella enterica subsp. enterica serovar Typhimurium	P0A1E3	gene cysK	-
Staphylococcus aureus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
O-acetyl-L-serine + hydrogen sulfide	-	Staphylococcus aureus	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	-	Salmonella enterica subsp. enterica serovar Typhimurium	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	-	Glycine max	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	-	Haemophilus influenzae	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	-	Arabidopsis thaliana	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	-	Mycobacterium tuberculosis	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	-	Bacillus subtilis	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	-	Escherichia coli	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	-	Caenorhabditis elegans	L-cysteine + acetate	-	?
O-acetyl-L-serine + hydrogen sulfide	-	Entamoeba histolytica	L-cysteine + acetate	-	?

Synonyms

Synonyms	Comment	Organism
cysK	-	Staphylococcus aureus
cysK	-	Salmonella enterica subsp. enterica serovar Typhimurium
cysK	-	Glycine max
cysK	-	Haemophilus influenzae
cysK	-	Arabidopsis thaliana
cysK	-	Mycobacterium tuberculosis
cysK	-	Bacillus subtilis
cysK	-	Escherichia coli
cysK	-	Caenorhabditis elegans
cysK	-	Entamoeba histolytica
O-acetylserine sulfhydrylase	-	Staphylococcus aureus
O-acetylserine sulfhydrylase	-	Salmonella enterica subsp. enterica serovar Typhimurium
O-acetylserine sulfhydrylase	-	Glycine max
O-acetylserine sulfhydrylase	-	Haemophilus influenzae
O-acetylserine sulfhydrylase	-	Arabidopsis thaliana
O-acetylserine sulfhydrylase	-	Mycobacterium tuberculosis
O-acetylserine sulfhydrylase	-	Bacillus subtilis
O-acetylserine sulfhydrylase	-	Escherichia coli
O-acetylserine sulfhydrylase	-	Caenorhabditis elegans
O-acetylserine sulfhydrylase	-	Entamoeba histolytica
O-acetylserine sulfhydrylase A	-	Staphylococcus aureus
O-acetylserine sulfhydrylase A	-	Salmonella enterica subsp. enterica serovar Typhimurium
O-acetylserine sulfhydrylase A	-	Glycine max
O-acetylserine sulfhydrylase A	-	Haemophilus influenzae
O-acetylserine sulfhydrylase A	-	Arabidopsis thaliana
O-acetylserine sulfhydrylase A	-	Mycobacterium tuberculosis
O-acetylserine sulfhydrylase A	-	Bacillus subtilis
O-acetylserine sulfhydrylase A	-	Escherichia coli
O-acetylserine sulfhydrylase A	-	Caenorhabditis elegans
O-acetylserine sulfhydrylase A	-	Entamoeba histolytica
OASS	-	Staphylococcus aureus
OASS	-	Salmonella enterica subsp. enterica serovar Typhimurium
OASS	-	Glycine max
OASS	-	Haemophilus influenzae
OASS	-	Arabidopsis thaliana
OASS	-	Mycobacterium tuberculosis
OASS	-	Bacillus subtilis
OASS	-	Escherichia coli
OASS	-	Caenorhabditis elegans
OASS	-	Entamoeba histolytica

Cofactor

Cofactor	Comment	Organism
pyridoxal 5'-phosphate	dependent on	Staphylococcus aureus
pyridoxal 5'-phosphate	dependent on	Salmonella enterica subsp. enterica serovar Typhimurium
pyridoxal 5'-phosphate	dependent on	Glycine max
pyridoxal 5'-phosphate	dependent on	Haemophilus influenzae
pyridoxal 5'-phosphate	dependent on	Arabidopsis thaliana
pyridoxal 5'-phosphate	dependent on	Mycobacterium tuberculosis
pyridoxal 5'-phosphate	dependent on	Bacillus subtilis
pyridoxal 5'-phosphate	dependent on	Escherichia coli
pyridoxal 5'-phosphate	dependent on	Caenorhabditis elegans
pyridoxal 5'-phosphate	dependent on	Entamoeba histolytica

General Information

General Information	Comment	Organism
evolution	the CysK/CysE binding interaction is conserved in most bacterial and plant systems	Staphylococcus aureus
evolution	the CysK/CysE binding interaction is conserved in most bacterial and plant systems	Salmonella enterica subsp. enterica serovar Typhimurium
evolution	the CysK/CysE binding interaction is conserved in most bacterial and plant systems	Glycine max
evolution	the CysK/CysE binding interaction is conserved in most bacterial and plant systems	Haemophilus influenzae
evolution	the CysK/CysE binding interaction is conserved in most bacterial and plant systems	Arabidopsis thaliana
evolution	the CysK/CysE binding interaction is conserved in most bacterial and plant systems	Mycobacterium tuberculosis
evolution	the CysK/CysE binding interaction is conserved in most bacterial and plant systems	Bacillus subtilis
evolution	the CysK/CysE binding interaction is conserved in most bacterial and plant systems	Escherichia coli
evolution	the CysK/CysE binding interaction is conserved in most bacterial and plant systems	Caenorhabditis elegans
evolution	the CysK/CysE binding interaction is conserved in most bacterial and plant systems	Entamoeba histolytica
malfunction	deletion of the C-terminal Ile, or substitution with Ala or Glu, in CysE consistently impairs complex formation with CysK	Mycobacterium tuberculosis
metabolism	the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview	Staphylococcus aureus
metabolism	the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview	Salmonella enterica subsp. enterica serovar Typhimurium
metabolism	the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview	Glycine max
metabolism	the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview	Haemophilus influenzae
metabolism	the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview	Arabidopsis thaliana
metabolism	the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview	Mycobacterium tuberculosis
metabolism	the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview	Bacillus subtilis
metabolism	the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview	Escherichia coli
metabolism	the enzyme catalyzes the final reaction of cysteine biosynthesis in bacteria. Biological roles of known CysK complexes in the context of cysteine metabolism, overview	Entamoeba histolytica
metabolism	the enzyme catalyzes the final reaction of cysteine biosynthesis. Biological roles of known CysK complexes in the context of cysteine metabolism, overview	Caenorhabditis elegans
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific	Staphylococcus aureus
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific	Salmonella enterica subsp. enterica serovar Typhimurium
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific	Bacillus subtilis
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific	Escherichia coli
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific	Caenorhabditis elegans
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific, interaction analysis and binding structure	Glycine max
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific, interaction analysis and binding structure. Negative cooperativity with decapeptide binding to AtCysK	Arabidopsis thaliana
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific, the C-terminal Ile (residue P4) is fundamental for the CysE/CysK binding interaction	Mycobacterium tuberculosis
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific. The P4 Ile residue accounts for about 80% of total binding energy. The P2 and P3 positions account for about 10% each, and the P1 residue negatively impacts binding, interaction analysis	Entamoeba histolytica
additional information	each CysK enzyme activity requires a binding partner that invariably mimics the C-terminus of serine acetyltransferase, CysE, to interact with the CysK active site. The CysK-CysE interaction is specific. The P4 Ile residue accounts for about 80% of total binding energy. The P2 and P3 positions account for about 10% each, and the P1 residue negatively impacts binding, interaction analysis. No negative cooperativity	Haemophilus influenzae
physiological function	CysK influences transcription in Caenorhabditis elegans. The enzyme from Caenorhabditis elegans interacts with EGL-9 in regulation of O2-dependent behavioral plasticity	Caenorhabditis elegans
physiological function	enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK	Salmonella enterica subsp. enterica serovar Typhimurium
physiological function	enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK	Haemophilus influenzae
physiological function	enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK	Mycobacterium tuberculosis
physiological function	enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK	Entamoeba histolytica
physiological function	enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. CysK influences transcription in Gram-positive bacteria. The enzyme from Staphylococcus aureus interacts with CymR in transcription repression	Staphylococcus aureus
physiological function	enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. Regulatory function of CysK/CysE interaction in plants, overview	Arabidopsis thaliana
physiological function	enzyme CysK is organized in a complex with serine acetyltransferase (CysE) and can physically associate CysE, which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. Regulatory function of CysK/CysE interaction in plants, overview. Productive cysteine biosynthesis requires a high CysK to CysE ratio	Glycine max
physiological function	enzyme CysK is organized in a complex with serine acetyltransferase (CysE), which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. CysK also activates an antibacterial nuclease toxin produced by uropathogenic Escherichia coli. Role for CysK during bacterial contact-dependent growth inhibition involving the CDI system from uropathogenic Escherichi coli, overview. CysK-binding provides a mechanism to protect the bacterial CysE from cold-inactivation and proteolysis. Escherichia coli CysK acts as a so-called permissive factor to activate an antibacterial contact-dependent growth inhibition (CDI) toxin, and interacts with CdiA-CTUPEC536 in toxin activation	Escherichia coli
physiological function	enzyme CysK is organized in a complex with serine acetyltransferase (CysE), which catalyzes the penultimate reaction in the synthetic pathway. This cysteine synthase complex is stabilized by insertion of the CysE C-terminus into the active-site of CysK. CysK influences transcription in Gram-positive bacteria. In Bacillus subtilis, CysK modulates the affinity of an Rrf2-type transcription factor for its operator sequences, thereby regulating expression of the cysteine regulon. The enzyme from Bacillus subtilis interacts with CymR in transcription repression. CdiA-CT toxins are activated by CysK, also from other species	Bacillus subtilis