node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
fdhE | fdhF | b3891 | b4079 | Formate dehydrogenase formation protein; Necessary for formate dehydrogenase activity. | Formate dehydrogenase-H, selenopolypeptide subunit; Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. | 0.846 |
fdhE | fdnG | b3891 | b1474 | Formate dehydrogenase formation protein; Necessary for formate dehydrogenase activity. | Formate dehydrogenase-N, alpha 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. The alpha subunit FdnG contains the formate oxidation site. Electrons are transferred from formate to menaquinone in the gamma subunit (FdnI), through the 4Fe-4S clusters in the beta subunit (FdnH). Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar). | 0.992 |
fdhE | fdnH | b3891 | b1475 | Formate dehydrogenase formation protein; Necessary for formate dehydrogenase activity. | Formate dehydrogenase-N, Fe-S (beta) 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. The beta subunit FdnH is an electron transfer unit containing 4 iron-sulfur clusters; it serves as a conduit for electrons that are transferred from the formate oxidation site in the alpha subunit (FdnG) to the menaquinone associated with the gamma subunit (FdnI) of formate dehydrogenase-N. Formate dehydrogenase-N is part of a system that generates proton motive force, togethe [...] | 0.942 |
fdhE | fdnI | b3891 | b1476 | Formate dehydrogenase formation protein; Necessary for formate dehydrogenase activity. | 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). | 0.895 |
fdhE | fdoG | b3891 | b3894 | Formate dehydrogenase formation protein; Necessary for formate dehydrogenase activity. | 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. | 0.998 |
fdhE | fdoH | b3891 | b3893 | Formate dehydrogenase formation protein; Necessary for formate dehydrogenase activity. | Formate dehydrogenase-O, Fe-S subunit; Allows to use formate as major electron donor during aerobic respiration. The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit (By similarity). | 0.981 |
fdhE | fdoI | b3891 | b3892 | Formate dehydrogenase formation protein; Necessary for formate dehydrogenase activity. | Formate dehydrogenase-O, cytochrome b556 subunit; Allows to use formate as major electron donor during aerobic respiration. Subunit gamma is probably the cytochrome b556(FDO) component of the formate dehydrogenase. | 0.992 |
fdhE | hycB | b3891 | b2724 | Formate dehydrogenase formation protein; Necessary for formate dehydrogenase activity. | Hydrogenase 3, Fe-S subunit; Probable electron transfer protein for hydrogenase 3. | 0.529 |
fdhF | fdhE | b4079 | b3891 | Formate dehydrogenase-H, selenopolypeptide subunit; Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. | Formate dehydrogenase formation protein; Necessary for formate dehydrogenase activity. | 0.846 |
fdhF | fdnG | b4079 | b1474 | Formate dehydrogenase-H, selenopolypeptide subunit; Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. | Formate dehydrogenase-N, alpha 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. The alpha subunit FdnG contains the formate oxidation site. Electrons are transferred from formate to menaquinone in the gamma subunit (FdnI), through the 4Fe-4S clusters in the beta subunit (FdnH). Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar). | 0.744 |
fdhF | fdnH | b4079 | b1475 | Formate dehydrogenase-H, selenopolypeptide subunit; Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. | Formate dehydrogenase-N, Fe-S (beta) 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. The beta subunit FdnH is an electron transfer unit containing 4 iron-sulfur clusters; it serves as a conduit for electrons that are transferred from the formate oxidation site in the alpha subunit (FdnG) to the menaquinone associated with the gamma subunit (FdnI) of formate dehydrogenase-N. Formate dehydrogenase-N is part of a system that generates proton motive force, togethe [...] | 0.866 |
fdhF | fdnI | b4079 | b1476 | Formate dehydrogenase-H, selenopolypeptide subunit; Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. | 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). | 0.906 |
fdhF | fdoG | b4079 | b3894 | Formate dehydrogenase-H, selenopolypeptide subunit; Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. | 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. | 0.730 |
fdhF | fdoH | b4079 | b3893 | Formate dehydrogenase-H, selenopolypeptide subunit; Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. | Formate dehydrogenase-O, Fe-S subunit; Allows to use formate as major electron donor during aerobic respiration. The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit (By similarity). | 0.866 |
fdhF | fdoI | b4079 | b3892 | Formate dehydrogenase-H, selenopolypeptide subunit; Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. | Formate dehydrogenase-O, cytochrome b556 subunit; Allows to use formate as major electron donor during aerobic respiration. Subunit gamma is probably the cytochrome b556(FDO) component of the formate dehydrogenase. | 0.920 |
fdhF | hybB | b4079 | b2995 | Formate dehydrogenase-H, selenopolypeptide subunit; Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. | Putative hydrogenase 2 cytochrome b type component; Probable b-type cytochrome; Belongs to the NrfD family. | 0.666 |
fdhF | hycB | b4079 | b2724 | Formate dehydrogenase-H, selenopolypeptide subunit; Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. | Hydrogenase 3, Fe-S subunit; Probable electron transfer protein for hydrogenase 3. | 0.999 |
fdnG | fdhE | b1474 | b3891 | Formate dehydrogenase-N, alpha 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. The alpha subunit FdnG contains the formate oxidation site. Electrons are transferred from formate to menaquinone in the gamma subunit (FdnI), through the 4Fe-4S clusters in the beta subunit (FdnH). Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar). | Formate dehydrogenase formation protein; Necessary for formate dehydrogenase activity. | 0.992 |
fdnG | fdhF | b1474 | b4079 | Formate dehydrogenase-N, alpha 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. The alpha subunit FdnG contains the formate oxidation site. Electrons are transferred from formate to menaquinone in the gamma subunit (FdnI), through the 4Fe-4S clusters in the beta subunit (FdnH). Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar). | Formate dehydrogenase-H, selenopolypeptide subunit; Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. | 0.744 |
fdnG | fdnH | b1474 | b1475 | Formate dehydrogenase-N, alpha 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. The alpha subunit FdnG contains the formate oxidation site. Electrons are transferred from formate to menaquinone in the gamma subunit (FdnI), through the 4Fe-4S clusters in the beta subunit (FdnH). Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar). | Formate dehydrogenase-N, Fe-S (beta) 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. The beta subunit FdnH is an electron transfer unit containing 4 iron-sulfur clusters; it serves as a conduit for electrons that are transferred from the formate oxidation site in the alpha subunit (FdnG) to the menaquinone associated with the gamma subunit (FdnI) of formate dehydrogenase-N. Formate dehydrogenase-N is part of a system that generates proton motive force, togethe [...] | 0.999 |