node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
cysI | cysJ | b2763 | b2764 | Sulfite reductase, beta subunit, NAD(P)-binding, heme-binding; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | Sulfite reductase, alpha subunit, flavoprotein; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component; In the N-terminal section; belongs to the flavodoxin family. | 0.999 |
cysI | cysK | b2763 | b2414 | Sulfite reductase, beta subunit, NAD(P)-binding, heme-binding; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | Cysteine synthase A, O-acetylserine sulfhydrolase A subunit; (Microbial infection) In addition to its role in cysteine synthesis, stimulates the tRNase activity of CdiA-CT from E.coli strain 536 / UPEC; stimulation does not require O-acetylserine sulfhydrylase activity. CdiA is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (experiments done in strains BW25113 [...] | 0.995 |
cysI | glpE | b2763 | b3425 | Sulfite reductase, beta subunit, NAD(P)-binding, heme-binding; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | Thiosulfate:cyanide sulfurtransferase (rhodanese); Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide. The relatively low affinity of GlpE for both thiosulfate and cyanide suggests that these compounds are not the physiological substrates. Thioredoxin 1 or related dithiol proteins could instead be the physiological sulfur-acceptor substrate. Possible association with the metabolism of glycerol-phosphate remains to be elucidated. | 0.913 |
cysI | metB | b2763 | b3939 | Sulfite reductase, beta subunit, NAD(P)-binding, heme-binding; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | Cystathionine gamma-synthase, PLP-dependent; Catalyzes the formation of L-cystathionine from O-succinyl-L- homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2- oxobutanoate, succinate and ammonia. | 0.945 |
cysI | sseA | b2763 | b2521 | Sulfite reductase, beta subunit, NAD(P)-binding, heme-binding; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | 3-mercaptopyruvate sulfurtransferase; Transfers a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity (130-fold lower). Its participation in detoxification of cyanide may be small. May be involved in the enhancement of serine sensitivity. | 0.917 |
cysI | ydhU | b2763 | b1670 | Sulfite reductase, beta subunit, NAD(P)-binding, heme-binding; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | Putative cytochrome b subunit of YdhYVWXUT oxidoreductase complex. | 0.900 |
cysJ | cysI | b2764 | b2763 | Sulfite reductase, alpha subunit, flavoprotein; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component; In the N-terminal section; belongs to the flavodoxin family. | Sulfite reductase, beta subunit, NAD(P)-binding, heme-binding; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | 0.999 |
cysJ | cysK | b2764 | b2414 | Sulfite reductase, alpha subunit, flavoprotein; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component; In the N-terminal section; belongs to the flavodoxin family. | Cysteine synthase A, O-acetylserine sulfhydrolase A subunit; (Microbial infection) In addition to its role in cysteine synthesis, stimulates the tRNase activity of CdiA-CT from E.coli strain 536 / UPEC; stimulation does not require O-acetylserine sulfhydrylase activity. CdiA is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (experiments done in strains BW25113 [...] | 0.999 |
cysJ | glpE | b2764 | b3425 | Sulfite reductase, alpha subunit, flavoprotein; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component; In the N-terminal section; belongs to the flavodoxin family. | Thiosulfate:cyanide sulfurtransferase (rhodanese); Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide. The relatively low affinity of GlpE for both thiosulfate and cyanide suggests that these compounds are not the physiological substrates. Thioredoxin 1 or related dithiol proteins could instead be the physiological sulfur-acceptor substrate. Possible association with the metabolism of glycerol-phosphate remains to be elucidated. | 0.917 |
cysJ | metB | b2764 | b3939 | Sulfite reductase, alpha subunit, flavoprotein; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component; In the N-terminal section; belongs to the flavodoxin family. | Cystathionine gamma-synthase, PLP-dependent; Catalyzes the formation of L-cystathionine from O-succinyl-L- homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2- oxobutanoate, succinate and ammonia. | 0.922 |
cysJ | sseA | b2764 | b2521 | Sulfite reductase, alpha subunit, flavoprotein; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component; In the N-terminal section; belongs to the flavodoxin family. | 3-mercaptopyruvate sulfurtransferase; Transfers a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity (130-fold lower). Its participation in detoxification of cyanide may be small. May be involved in the enhancement of serine sensitivity. | 0.914 |
cysJ | ydhU | b2764 | b1670 | Sulfite reductase, alpha subunit, flavoprotein; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component; In the N-terminal section; belongs to the flavodoxin family. | Putative cytochrome b subunit of YdhYVWXUT oxidoreductase complex. | 0.906 |
cysK | cysI | b2414 | b2763 | Cysteine synthase A, O-acetylserine sulfhydrolase A subunit; (Microbial infection) In addition to its role in cysteine synthesis, stimulates the tRNase activity of CdiA-CT from E.coli strain 536 / UPEC; stimulation does not require O-acetylserine sulfhydrylase activity. CdiA is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (experiments done in strains BW25113 [...] | Sulfite reductase, beta subunit, NAD(P)-binding, heme-binding; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | 0.995 |
cysK | cysJ | b2414 | b2764 | Cysteine synthase A, O-acetylserine sulfhydrolase A subunit; (Microbial infection) In addition to its role in cysteine synthesis, stimulates the tRNase activity of CdiA-CT from E.coli strain 536 / UPEC; stimulation does not require O-acetylserine sulfhydrylase activity. CdiA is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (experiments done in strains BW25113 [...] | Sulfite reductase, alpha subunit, flavoprotein; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component; In the N-terminal section; belongs to the flavodoxin family. | 0.999 |
cysK | metB | b2414 | b3939 | Cysteine synthase A, O-acetylserine sulfhydrolase A subunit; (Microbial infection) In addition to its role in cysteine synthesis, stimulates the tRNase activity of CdiA-CT from E.coli strain 536 / UPEC; stimulation does not require O-acetylserine sulfhydrylase activity. CdiA is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (experiments done in strains BW25113 [...] | Cystathionine gamma-synthase, PLP-dependent; Catalyzes the formation of L-cystathionine from O-succinyl-L- homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2- oxobutanoate, succinate and ammonia. | 0.990 |
cysK | sseA | b2414 | b2521 | Cysteine synthase A, O-acetylserine sulfhydrolase A subunit; (Microbial infection) In addition to its role in cysteine synthesis, stimulates the tRNase activity of CdiA-CT from E.coli strain 536 / UPEC; stimulation does not require O-acetylserine sulfhydrylase activity. CdiA is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (experiments done in strains BW25113 [...] | 3-mercaptopyruvate sulfurtransferase; Transfers a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity (130-fold lower). Its participation in detoxification of cyanide may be small. May be involved in the enhancement of serine sensitivity. | 0.870 |
cysK | ydhU | b2414 | b1670 | Cysteine synthase A, O-acetylserine sulfhydrolase A subunit; (Microbial infection) In addition to its role in cysteine synthesis, stimulates the tRNase activity of CdiA-CT from E.coli strain 536 / UPEC; stimulation does not require O-acetylserine sulfhydrylase activity. CdiA is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (experiments done in strains BW25113 [...] | Putative cytochrome b subunit of YdhYVWXUT oxidoreductase complex. | 0.900 |
glpE | cysI | b3425 | b2763 | Thiosulfate:cyanide sulfurtransferase (rhodanese); Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide. The relatively low affinity of GlpE for both thiosulfate and cyanide suggests that these compounds are not the physiological substrates. Thioredoxin 1 or related dithiol proteins could instead be the physiological sulfur-acceptor substrate. Possible association with the metabolism of glycerol-phosphate remains to be elucidated. | Sulfite reductase, beta subunit, NAD(P)-binding, heme-binding; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. | 0.913 |
glpE | cysJ | b3425 | b2764 | Thiosulfate:cyanide sulfurtransferase (rhodanese); Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide. The relatively low affinity of GlpE for both thiosulfate and cyanide suggests that these compounds are not the physiological substrates. Thioredoxin 1 or related dithiol proteins could instead be the physiological sulfur-acceptor substrate. Possible association with the metabolism of glycerol-phosphate remains to be elucidated. | Sulfite reductase, alpha subunit, flavoprotein; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component; In the N-terminal section; belongs to the flavodoxin family. | 0.917 |
glpE | sseA | b3425 | b2521 | Thiosulfate:cyanide sulfurtransferase (rhodanese); Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide. The relatively low affinity of GlpE for both thiosulfate and cyanide suggests that these compounds are not the physiological substrates. Thioredoxin 1 or related dithiol proteins could instead be the physiological sulfur-acceptor substrate. Possible association with the metabolism of glycerol-phosphate remains to be elucidated. | 3-mercaptopyruvate sulfurtransferase; Transfers a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity (130-fold lower). Its participation in detoxification of cyanide may be small. May be involved in the enhancement of serine sensitivity. | 0.976 |