node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
azoR | yqjF | b1412 | b3101 | NADH-azoreductase, FMN-dependent; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. The enzyme can reduce ethyl red and methyl red, but is not able to convert sulfonated azo dyes; Belongs to the azoreductase type 1 family. | Putative quinol oxidase subunit. | 0.690 |
azoR | yqjG | b1412 | b3102 | NADH-azoreductase, FMN-dependent; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity. The enzyme can reduce ethyl red and methyl red, but is not able to convert sulfonated azo dyes; Belongs to the azoreductase type 1 family. | Putative S-transferase; Catalyzes glutathione (GSH)-dependent reduction of glutathionyl-hydroquinones (GS-HQs) to the corresponding hydroquinones. Can use a variety of GS-HQs as substrates, such as GS-p-hydroquinone (GS-HQ), GS-hydroxy-p-hydroquinone (GS-HHQ), GS-methyl-p-hydroquinone (GS-MHQ), GS-menadiol, and GS-trichloro-p-hydroquinone (GS-TriCH). Also displays GSH-dependent disulfide-bond reduction activity toward HED (2- hydroxyethyl disulfide), and is able to catalyze DMA (dimethylarsinate) reduction. Exhibits no GSH transferase activity with 1-chloro-2,4- dinitrobenzene (CDNB). | 0.676 |
dhaR | yqjG | b1201 | b3102 | dhaKLM operon transcription activator; Positively regulates the dhaKLM operon from a sigma-70 promoter. Represses its own expression. | Putative S-transferase; Catalyzes glutathione (GSH)-dependent reduction of glutathionyl-hydroquinones (GS-HQs) to the corresponding hydroquinones. Can use a variety of GS-HQs as substrates, such as GS-p-hydroquinone (GS-HQ), GS-hydroxy-p-hydroquinone (GS-HHQ), GS-methyl-p-hydroquinone (GS-MHQ), GS-menadiol, and GS-trichloro-p-hydroquinone (GS-TriCH). Also displays GSH-dependent disulfide-bond reduction activity toward HED (2- hydroxyethyl disulfide), and is able to catalyze DMA (dimethylarsinate) reduction. Exhibits no GSH transferase activity with 1-chloro-2,4- dinitrobenzene (CDNB). | 0.623 |
dkgA | yqjD | b3012 | b3098 | 2,5-diketo-D-gluconate reductase A; Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives; Belongs to the aldo/keto reductase family. | Membrane-anchored ribosome-binding protein; Upon overexpression inhibits growth. | 0.796 |
dkgA | yqjG | b3012 | b3102 | 2,5-diketo-D-gluconate reductase A; Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives; Belongs to the aldo/keto reductase family. | Putative S-transferase; Catalyzes glutathione (GSH)-dependent reduction of glutathionyl-hydroquinones (GS-HQs) to the corresponding hydroquinones. Can use a variety of GS-HQs as substrates, such as GS-p-hydroquinone (GS-HQ), GS-hydroxy-p-hydroquinone (GS-HHQ), GS-methyl-p-hydroquinone (GS-MHQ), GS-menadiol, and GS-trichloro-p-hydroquinone (GS-TriCH). Also displays GSH-dependent disulfide-bond reduction activity toward HED (2- hydroxyethyl disulfide), and is able to catalyze DMA (dimethylarsinate) reduction. Exhibits no GSH transferase activity with 1-chloro-2,4- dinitrobenzene (CDNB). | 0.556 |
gstA | yfcF | b1635 | b2301 | Glutathionine S-transferase; Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity. Belongs to the GST superfamily. Beta family. | Glutathione S-transferase; Exhibits glutathione (GSH) S-transferase activity toward 1- chloro-2,4-dinitrobenzene (CDNB); however this activity is as low as 1% of that of GstA. Also displays a GSH-dependent peroxidase activity toward cumene hydroperoxide. Is involved in defense against oxidative stress, probably via its peroxidase activity. | 0.938 |
gstA | yfcG | b1635 | b2302 | Glutathionine S-transferase; Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity. Belongs to the GST superfamily. Beta family. | GSH-dependent disulfide bond oxidoreductase; Exhibits a very robust glutathione (GSH)-dependent disulfide- bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Has also a low GSH-dependent hydroperoxidase activity toward cumene hydroperoxide, but does not reduce H(2)O(2), tert-butyl hydroperoxide, benzyl peroxide, or lauroyl peroxide. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity using glutathionylspermidine (GspSH) as the n [...] | 0.720 |
gstA | yghU | b1635 | b2989 | Glutathionine S-transferase; Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity. Belongs to the GST superfamily. Beta family. | Putative S-transferase; Exhibits a robust glutathione (GSH)-dependent disulfide-bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Also displays a modest GSH-dependent peroxidase activity toward several organic hydroperoxides, such as cumene hydroperoxide and linoleic acid 13(S)-hydroperoxide, but does not reduce H(2)O(2) or tert-butyl hydroperoxide at appreciable rates. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity toward [...] | 0.560 |
gstA | yibF | b1635 | b3592 | Glutathionine S-transferase; Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity. Belongs to the GST superfamily. Beta family. | Glutathione S-transferase homolog; Glutathione (GSH) transferase homolog, that might be involved in selenium metabolism. | 0.583 |
gstA | yqjG | b1635 | b3102 | Glutathionine S-transferase; Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity. Belongs to the GST superfamily. Beta family. | Putative S-transferase; Catalyzes glutathione (GSH)-dependent reduction of glutathionyl-hydroquinones (GS-HQs) to the corresponding hydroquinones. Can use a variety of GS-HQs as substrates, such as GS-p-hydroquinone (GS-HQ), GS-hydroxy-p-hydroquinone (GS-HHQ), GS-methyl-p-hydroquinone (GS-MHQ), GS-menadiol, and GS-trichloro-p-hydroquinone (GS-TriCH). Also displays GSH-dependent disulfide-bond reduction activity toward HED (2- hydroxyethyl disulfide), and is able to catalyze DMA (dimethylarsinate) reduction. Exhibits no GSH transferase activity with 1-chloro-2,4- dinitrobenzene (CDNB). | 0.556 |
yfcF | gstA | b2301 | b1635 | Glutathione S-transferase; Exhibits glutathione (GSH) S-transferase activity toward 1- chloro-2,4-dinitrobenzene (CDNB); however this activity is as low as 1% of that of GstA. Also displays a GSH-dependent peroxidase activity toward cumene hydroperoxide. Is involved in defense against oxidative stress, probably via its peroxidase activity. | Glutathionine S-transferase; Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity. Belongs to the GST superfamily. Beta family. | 0.938 |
yfcF | yfcG | b2301 | b2302 | Glutathione S-transferase; Exhibits glutathione (GSH) S-transferase activity toward 1- chloro-2,4-dinitrobenzene (CDNB); however this activity is as low as 1% of that of GstA. Also displays a GSH-dependent peroxidase activity toward cumene hydroperoxide. Is involved in defense against oxidative stress, probably via its peroxidase activity. | GSH-dependent disulfide bond oxidoreductase; Exhibits a very robust glutathione (GSH)-dependent disulfide- bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Has also a low GSH-dependent hydroperoxidase activity toward cumene hydroperoxide, but does not reduce H(2)O(2), tert-butyl hydroperoxide, benzyl peroxide, or lauroyl peroxide. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity using glutathionylspermidine (GspSH) as the n [...] | 0.860 |
yfcF | yghU | b2301 | b2989 | Glutathione S-transferase; Exhibits glutathione (GSH) S-transferase activity toward 1- chloro-2,4-dinitrobenzene (CDNB); however this activity is as low as 1% of that of GstA. Also displays a GSH-dependent peroxidase activity toward cumene hydroperoxide. Is involved in defense against oxidative stress, probably via its peroxidase activity. | Putative S-transferase; Exhibits a robust glutathione (GSH)-dependent disulfide-bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Also displays a modest GSH-dependent peroxidase activity toward several organic hydroperoxides, such as cumene hydroperoxide and linoleic acid 13(S)-hydroperoxide, but does not reduce H(2)O(2) or tert-butyl hydroperoxide at appreciable rates. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity toward [...] | 0.557 |
yfcF | yibF | b2301 | b3592 | Glutathione S-transferase; Exhibits glutathione (GSH) S-transferase activity toward 1- chloro-2,4-dinitrobenzene (CDNB); however this activity is as low as 1% of that of GstA. Also displays a GSH-dependent peroxidase activity toward cumene hydroperoxide. Is involved in defense against oxidative stress, probably via its peroxidase activity. | Glutathione S-transferase homolog; Glutathione (GSH) transferase homolog, that might be involved in selenium metabolism. | 0.686 |
yfcF | yqjG | b2301 | b3102 | Glutathione S-transferase; Exhibits glutathione (GSH) S-transferase activity toward 1- chloro-2,4-dinitrobenzene (CDNB); however this activity is as low as 1% of that of GstA. Also displays a GSH-dependent peroxidase activity toward cumene hydroperoxide. Is involved in defense against oxidative stress, probably via its peroxidase activity. | Putative S-transferase; Catalyzes glutathione (GSH)-dependent reduction of glutathionyl-hydroquinones (GS-HQs) to the corresponding hydroquinones. Can use a variety of GS-HQs as substrates, such as GS-p-hydroquinone (GS-HQ), GS-hydroxy-p-hydroquinone (GS-HHQ), GS-methyl-p-hydroquinone (GS-MHQ), GS-menadiol, and GS-trichloro-p-hydroquinone (GS-TriCH). Also displays GSH-dependent disulfide-bond reduction activity toward HED (2- hydroxyethyl disulfide), and is able to catalyze DMA (dimethylarsinate) reduction. Exhibits no GSH transferase activity with 1-chloro-2,4- dinitrobenzene (CDNB). | 0.565 |
yfcG | gstA | b2302 | b1635 | GSH-dependent disulfide bond oxidoreductase; Exhibits a very robust glutathione (GSH)-dependent disulfide- bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Has also a low GSH-dependent hydroperoxidase activity toward cumene hydroperoxide, but does not reduce H(2)O(2), tert-butyl hydroperoxide, benzyl peroxide, or lauroyl peroxide. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity using glutathionylspermidine (GspSH) as the n [...] | Glutathionine S-transferase; Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity. Belongs to the GST superfamily. Beta family. | 0.720 |
yfcG | yfcF | b2302 | b2301 | GSH-dependent disulfide bond oxidoreductase; Exhibits a very robust glutathione (GSH)-dependent disulfide- bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Has also a low GSH-dependent hydroperoxidase activity toward cumene hydroperoxide, but does not reduce H(2)O(2), tert-butyl hydroperoxide, benzyl peroxide, or lauroyl peroxide. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity using glutathionylspermidine (GspSH) as the n [...] | Glutathione S-transferase; Exhibits glutathione (GSH) S-transferase activity toward 1- chloro-2,4-dinitrobenzene (CDNB); however this activity is as low as 1% of that of GstA. Also displays a GSH-dependent peroxidase activity toward cumene hydroperoxide. Is involved in defense against oxidative stress, probably via its peroxidase activity. | 0.860 |
yfcG | yqjD | b2302 | b3098 | GSH-dependent disulfide bond oxidoreductase; Exhibits a very robust glutathione (GSH)-dependent disulfide- bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Has also a low GSH-dependent hydroperoxidase activity toward cumene hydroperoxide, but does not reduce H(2)O(2), tert-butyl hydroperoxide, benzyl peroxide, or lauroyl peroxide. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity using glutathionylspermidine (GspSH) as the n [...] | Membrane-anchored ribosome-binding protein; Upon overexpression inhibits growth. | 0.432 |
yfcG | yqjG | b2302 | b3102 | GSH-dependent disulfide bond oxidoreductase; Exhibits a very robust glutathione (GSH)-dependent disulfide- bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Has also a low GSH-dependent hydroperoxidase activity toward cumene hydroperoxide, but does not reduce H(2)O(2), tert-butyl hydroperoxide, benzyl peroxide, or lauroyl peroxide. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity using glutathionylspermidine (GspSH) as the n [...] | Putative S-transferase; Catalyzes glutathione (GSH)-dependent reduction of glutathionyl-hydroquinones (GS-HQs) to the corresponding hydroquinones. Can use a variety of GS-HQs as substrates, such as GS-p-hydroquinone (GS-HQ), GS-hydroxy-p-hydroquinone (GS-HHQ), GS-methyl-p-hydroquinone (GS-MHQ), GS-menadiol, and GS-trichloro-p-hydroquinone (GS-TriCH). Also displays GSH-dependent disulfide-bond reduction activity toward HED (2- hydroxyethyl disulfide), and is able to catalyze DMA (dimethylarsinate) reduction. Exhibits no GSH transferase activity with 1-chloro-2,4- dinitrobenzene (CDNB). | 0.680 |
yghU | gstA | b2989 | b1635 | Putative S-transferase; Exhibits a robust glutathione (GSH)-dependent disulfide-bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Also displays a modest GSH-dependent peroxidase activity toward several organic hydroperoxides, such as cumene hydroperoxide and linoleic acid 13(S)-hydroperoxide, but does not reduce H(2)O(2) or tert-butyl hydroperoxide at appreciable rates. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity toward [...] | Glutathionine S-transferase; Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity. Belongs to the GST superfamily. Beta family. | 0.560 |