Formate dehydrogenase-N, cytochrome B556 (gamma) subunit, nitrate-inducible; Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. Subunit gamma is the cytochrome b556 component of the formate dehydrogenase-N, and also contains a menaquinone reduction site that receives electrons from the beta subunit (FdnH), through its hemes. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar).

Formate dehydrogenase-O, large subunit; Allows to use formate as major electron donor during aerobic respiration. Subunit alpha possibly forms the active site; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Formate dehydrogenase-N, cytochrome B556 (gamma) subunit, nitrate-inducible; Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. Subunit gamma is the cytochrome b556 component of the formate dehydrogenase-N, and also contains a menaquinone reduction site that receives electrons from the beta subunit (FdnH), through its hemes. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar).

Nitrate reductase 1, alpha subunit; The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.

Formate dehydrogenase-O, large subunit; Allows to use formate as major electron donor during aerobic respiration. Subunit alpha possibly forms the active site; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Formate dehydrogenase-N, cytochrome B556 (gamma) subunit, nitrate-inducible; Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. Subunit gamma is the cytochrome b556 component of the formate dehydrogenase-N, and also contains a menaquinone reduction site that receives electrons from the beta subunit (FdnH), through its hemes. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar).

Formate dehydrogenase-O, large subunit; Allows to use formate as major electron donor during aerobic respiration. Subunit alpha possibly forms the active site; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.

Nitrate reductase 1, alpha subunit; The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.

Hybrid-cluster [4Fe-2S-2O] subunit of anaerobic terminal reductases; Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. Is also able to reduce hydroxylamine analogs such as methylhydroxylamine and hydroxyquinone. Might have a role as a scavenger of potentially toxic by-products of nitrate metabolism. Belongs to the HCP family.

HCP oxidoreductase, NADH-dependent; NADH oxidoreductase acting in concert with HCP.

Hybrid-cluster [4Fe-2S-2O] subunit of anaerobic terminal reductases; Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. Is also able to reduce hydroxylamine analogs such as methylhydroxylamine and hydroxyquinone. Might have a role as a scavenger of potentially toxic by-products of nitrate metabolism. Belongs to the HCP family.

Fused nitric oxide dioxygenase/dihydropteridine reductase 2; Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. Various electron acceptors are also reduced by HMP in vitro, including dihydropterine, ferrisiderophores, ferric citrate, cytochrome c, nitrite, S-nitrosoglutathione, and alkylhydroperoxides. However, it is unknown if th [...]

Hybrid-cluster [4Fe-2S-2O] subunit of anaerobic terminal reductases; Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. Is also able to reduce hydroxylamine analogs such as methylhydroxylamine and hydroxyquinone. Might have a role as a scavenger of potentially toxic by-products of nitrate metabolism. Belongs to the HCP family.

Nitrate reductase 1, alpha subunit; The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.

Hybrid-cluster [4Fe-2S-2O] subunit of anaerobic terminal reductases; Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. Is also able to reduce hydroxylamine analogs such as methylhydroxylamine and hydroxyquinone. Might have a role as a scavenger of potentially toxic by-products of nitrate metabolism. Belongs to the HCP family.

Nitrite reductase, large subunit, NAD(P)H-binding; Nitrite reductase (NAD(P)H) subunit; Protein involved in anaerobic respiration; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.

Hybrid-cluster [4Fe-2S-2O] subunit of anaerobic terminal reductases; Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. Is also able to reduce hydroxylamine analogs such as methylhydroxylamine and hydroxyquinone. Might have a role as a scavenger of potentially toxic by-products of nitrate metabolism. Belongs to the HCP family.

Anaerobic nitric oxide reductase flavorubredoxin; Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the reductase at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase; In the N-terminal section; belongs to the zinc metallo- hydrolase group 3 family.

Hybrid-cluster [4Fe-2S-2O] subunit of anaerobic terminal reductases; Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. Is also able to reduce hydroxylamine analogs such as methylhydroxylamine and hydroxyquinone. Might have a role as a scavenger of potentially toxic by-products of nitrate metabolism. Belongs to the HCP family.

Nitrite reductase, formate-dependent, cytochrome; Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process. Has very low activity toward hydroxylamine. Has even lower activity toward sulfite. Sulfite reductase activity is maximal at neutral pH (By similarity).

Hybrid-cluster [4Fe-2S-2O] subunit of anaerobic terminal reductases; Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. Is also able to reduce hydroxylamine analogs such as methylhydroxylamine and hydroxyquinone. Might have a role as a scavenger of potentially toxic by-products of nitrate metabolism. Belongs to the HCP family.

Iron-sulfur cluster repair protein RIC; Di-iron-containing protein involved in the repair of iron- sulfur clusters damaged by oxidative and nitrosative stress conditions.

HCP oxidoreductase, NADH-dependent; NADH oxidoreductase acting in concert with HCP.

Hybrid-cluster [4Fe-2S-2O] subunit of anaerobic terminal reductases; Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. Is also able to reduce hydroxylamine analogs such as methylhydroxylamine and hydroxyquinone. Might have a role as a scavenger of potentially toxic by-products of nitrate metabolism. Belongs to the HCP family.

HCP oxidoreductase, NADH-dependent; NADH oxidoreductase acting in concert with HCP.

Fused nitric oxide dioxygenase/dihydropteridine reductase 2; Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. Various electron acceptors are also reduced by HMP in vitro, including dihydropterine, ferrisiderophores, ferric citrate, cytochrome c, nitrite, S-nitrosoglutathione, and alkylhydroperoxides. However, it is unknown if th [...]

HCP oxidoreductase, NADH-dependent; NADH oxidoreductase acting in concert with HCP.

Nitrite reductase, large subunit, NAD(P)H-binding; Nitrite reductase (NAD(P)H) subunit; Protein involved in anaerobic respiration; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.

HCP oxidoreductase, NADH-dependent; NADH oxidoreductase acting in concert with HCP.

Anaerobic nitric oxide reductase flavorubredoxin; Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the reductase at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase; In the N-terminal section; belongs to the zinc metallo- hydrolase group 3 family.

HCP oxidoreductase, NADH-dependent; NADH oxidoreductase acting in concert with HCP.

Nitrite reductase, formate-dependent, cytochrome; Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process. Has very low activity toward hydroxylamine. Has even lower activity toward sulfite. Sulfite reductase activity is maximal at neutral pH (By similarity).

HCP oxidoreductase, NADH-dependent; NADH oxidoreductase acting in concert with HCP.

Iron-sulfur cluster repair protein RIC; Di-iron-containing protein involved in the repair of iron- sulfur clusters damaged by oxidative and nitrosative stress conditions.

Fused nitric oxide dioxygenase/dihydropteridine reductase 2; Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. Various electron acceptors are also reduced by HMP in vitro, including dihydropterine, ferrisiderophores, ferric citrate, cytochrome c, nitrite, S-nitrosoglutathione, and alkylhydroperoxides. However, it is unknown if th [...]

Hybrid-cluster [4Fe-2S-2O] subunit of anaerobic terminal reductases; Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. Is also able to reduce hydroxylamine analogs such as methylhydroxylamine and hydroxyquinone. Might have a role as a scavenger of potentially toxic by-products of nitrate metabolism. Belongs to the HCP family.

Fused nitric oxide dioxygenase/dihydropteridine reductase 2; Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. Various electron acceptors are also reduced by HMP in vitro, including dihydropterine, ferrisiderophores, ferric citrate, cytochrome c, nitrite, S-nitrosoglutathione, and alkylhydroperoxides. However, it is unknown if th [...]

HCP oxidoreductase, NADH-dependent; NADH oxidoreductase acting in concert with HCP.

Fused nitric oxide dioxygenase/dihydropteridine reductase 2; Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. Various electron acceptors are also reduced by HMP in vitro, including dihydropterine, ferrisiderophores, ferric citrate, cytochrome c, nitrite, S-nitrosoglutathione, and alkylhydroperoxides. However, it is unknown if th [...]

Nitrate reductase 1, alpha subunit; The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.