node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
cheY | nhoA | b1882 | b1463 | Chemotaxis regulator transmitting signal to flagellar motor component; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and th [...] | N-hydroxyarylamine O-acetyltransferase; Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene. N-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O- acetyltransferase activity (Probable). | 0.504 |
cheY | pka | b1882 | b2584 | Chemotaxis regulator transmitting signal to flagellar motor component; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and th [...] | Protein lysine acetyltransferase; Catalyzes the acetyl-CoA-dependent acetylation of lysine residues of a large number of target proteins. Acetylates RNase R in exponential phase cells and RNase II. Required for the glucose-dependent acetylation on multiple lysines of alpha, beta and beta' RNAP subunits. Also acetylates acetyl-coenzyme A synthetase (Acs) and the chromosomal replication initiator protein DnaA, and inhibits their activity. Overexpression leads to the acetylation of a large number of additional proteins and inhibits motility. | 0.456 |
cobB | dhaM | b1120 | b1198 | Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily. | Putative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone. | 0.783 |
cobB | nhoA | b1120 | b1463 | Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily. | N-hydroxyarylamine O-acetyltransferase; Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene. N-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O- acetyltransferase activity (Probable). | 0.806 |
cobB | nudC | b1120 | b3996 | Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily. | NADH pyrophosphatase; Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates, but uniquely prefers the reduced form of NADH. | 0.905 |
cobB | pka | b1120 | b2584 | Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily. | Protein lysine acetyltransferase; Catalyzes the acetyl-CoA-dependent acetylation of lysine residues of a large number of target proteins. Acetylates RNase R in exponential phase cells and RNase II. Required for the glucose-dependent acetylation on multiple lysines of alpha, beta and beta' RNAP subunits. Also acetylates acetyl-coenzyme A synthetase (Acs) and the chromosomal replication initiator protein DnaA, and inhibits their activity. Overexpression leads to the acetylation of a large number of additional proteins and inhibits motility. | 0.933 |
cobB | yiaC | b1120 | b3550 | Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily. | GNAT family putative N-acetyltransferase; N-epsilon-lysine acetyltransferase that catalyzes acetylation of a large number of proteins. Overexpression inhibits motility. | 0.512 |
dhaM | cobB | b1198 | b1120 | Putative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone. | Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily. | 0.783 |
dhaM | elbB | b1198 | b3209 | Putative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone. | Isoprenoid biosynthesis protein with amidotransferase-like domain; Displays glyoxalase activity, catalyzing the conversion of glyoxal to glycolate. However, this apparent glyoxalase activity may reflect a protein deglycase activity, which could be the primary function of this protein like other DJ-1 superfamily members such as PARK7, YajL, YhbO and HchA (Probable). Is not able to use methylglyoxal as substrate. Belongs to the peptidase C56 family. | 0.401 |
dhaM | nhoA | b1198 | b1463 | Putative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone. | N-hydroxyarylamine O-acetyltransferase; Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene. N-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O- acetyltransferase activity (Probable). | 0.556 |
dhaM | pka | b1198 | b2584 | Putative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone. | Protein lysine acetyltransferase; Catalyzes the acetyl-CoA-dependent acetylation of lysine residues of a large number of target proteins. Acetylates RNase R in exponential phase cells and RNase II. Required for the glucose-dependent acetylation on multiple lysines of alpha, beta and beta' RNAP subunits. Also acetylates acetyl-coenzyme A synthetase (Acs) and the chromosomal replication initiator protein DnaA, and inhibits their activity. Overexpression leads to the acetylation of a large number of additional proteins and inhibits motility. | 0.780 |
elbB | dhaM | b3209 | b1198 | Isoprenoid biosynthesis protein with amidotransferase-like domain; Displays glyoxalase activity, catalyzing the conversion of glyoxal to glycolate. However, this apparent glyoxalase activity may reflect a protein deglycase activity, which could be the primary function of this protein like other DJ-1 superfamily members such as PARK7, YajL, YhbO and HchA (Probable). Is not able to use methylglyoxal as substrate. Belongs to the peptidase C56 family. | Putative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone. | 0.401 |
elbB | nhoA | b3209 | b1463 | Isoprenoid biosynthesis protein with amidotransferase-like domain; Displays glyoxalase activity, catalyzing the conversion of glyoxal to glycolate. However, this apparent glyoxalase activity may reflect a protein deglycase activity, which could be the primary function of this protein like other DJ-1 superfamily members such as PARK7, YajL, YhbO and HchA (Probable). Is not able to use methylglyoxal as substrate. Belongs to the peptidase C56 family. | N-hydroxyarylamine O-acetyltransferase; Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene. N-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O- acetyltransferase activity (Probable). | 0.491 |
fpr | nhoA | b3924 | b1463 | ferredoxin-NADP reductase; Transports electrons between flavodoxin or ferredoxin and NADPH. Reduces flavodoxin 1, flavodoxin 2 and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner. Required for the activation of several enzymes such as pyruvate formate-lyase, anaerobic ribonucleotide reductase and cobalamin-dependent methionine synthase. Belongs to the ferredoxin--NADP reductase type 1 family. | N-hydroxyarylamine O-acetyltransferase; Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene. N-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O- acetyltransferase activity (Probable). | 0.443 |
nhoA | cheY | b1463 | b1882 | N-hydroxyarylamine O-acetyltransferase; Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene. N-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O- acetyltransferase activity (Probable). | Chemotaxis regulator transmitting signal to flagellar motor component; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and th [...] | 0.504 |
nhoA | cobB | b1463 | b1120 | N-hydroxyarylamine O-acetyltransferase; Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene. N-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O- acetyltransferase activity (Probable). | Deacetylase of acs and cheY, chemotaxis regulator; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Belongs to the sirtuin family. Class III subfamily. | 0.806 |
nhoA | dhaM | b1463 | b1198 | N-hydroxyarylamine O-acetyltransferase; Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene. N-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O- acetyltransferase activity (Probable). | Putative dihydroxyacetone-specific PTS enzymes: HPr, EI components; Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone. | 0.556 |
nhoA | elbB | b1463 | b3209 | N-hydroxyarylamine O-acetyltransferase; Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene. N-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O- acetyltransferase activity (Probable). | Isoprenoid biosynthesis protein with amidotransferase-like domain; Displays glyoxalase activity, catalyzing the conversion of glyoxal to glycolate. However, this apparent glyoxalase activity may reflect a protein deglycase activity, which could be the primary function of this protein like other DJ-1 superfamily members such as PARK7, YajL, YhbO and HchA (Probable). Is not able to use methylglyoxal as substrate. Belongs to the peptidase C56 family. | 0.491 |
nhoA | fpr | b1463 | b3924 | N-hydroxyarylamine O-acetyltransferase; Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene. N-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O- acetyltransferase activity (Probable). | ferredoxin-NADP reductase; Transports electrons between flavodoxin or ferredoxin and NADPH. Reduces flavodoxin 1, flavodoxin 2 and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner. Required for the activation of several enzymes such as pyruvate formate-lyase, anaerobic ribonucleotide reductase and cobalamin-dependent methionine synthase. Belongs to the ferredoxin--NADP reductase type 1 family. | 0.443 |
nhoA | nudC | b1463 | b3996 | N-hydroxyarylamine O-acetyltransferase; Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene. N-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O- acetyltransferase activity (Probable). | NADH pyrophosphatase; Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates, but uniquely prefers the reduced form of NADH. | 0.410 |