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| | frdA | Anaerobic fumarate reductase catalytic and NAD/flavoprotein subunit; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (602 aa) |
| | nrdG | Anaerobic ribonucleoside-triphosphate reductase-activating protein; Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine; Belongs to the organic radical-activating enzymes family. (154 aa) |
| | cydX | Cytochrome d (bd-I) ubiquinol oxidase subunit X; Required for correct functioning of cytochrome bd-I oxidase. This protein and AppX may have some functional overlap. (37 aa) |
| | hybO | Hydrogenase 2, small subunit; This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake; Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit family. (372 aa) |
| | fixA | Anaerobic carnitine reduction putative electron transfer flavoprotein subunit; Required for anaerobic carnitine reduction. May bring reductant to CaiA; Belongs to the ETF beta-subunit/FixA family. (256 aa) |
| | fixB | Protein FixB; Required for anaerobic carnitine reduction. May bring reductant to CaiA; Belongs to the ETF alpha-subunit/FixB family. (313 aa) |
| | kefF | Potassium-efflux system ancillary protein for KefC, glutathione-regulated; Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefC. Shows redox enzymatic activity, but this enzymatic activity is not required for activation of KefC. Can use a wide range of substrates, including electrophilic quinones, and its function could be to reduce the redox toxicity of electrophilic quinones in parallel with acting as triggers for the KefC efflux system. Belongs to the NAD(P)H dehydrogenase (quinone) family. KefF subfamily. (176 aa) |
| | cyoD | Cytochrome o ubiquinol oxidase subunit IV; Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. (109 aa) |
| | cyoC | Cytochrome o ubiquinol oxidase subunit III; Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. (204 aa) |
| | cyoB | Cytochrome o ubiquinol oxidase subunit I; Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. Protons are probably pumped via D- and K- channels found in this subunit. (663 aa) |
| | cyoA | Cytochrome o ubiquinol oxidase subunit II; Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. (315 aa) |
| | fldA | Flavodoxin 1; Low-potential electron donor to a number of redox enzymes (Potential). Involved in the reactivation of inactive cob(II)alamin in methionine synthase. (176 aa) |
| | sdhC | Succinate dehydrogenase, membrane subunit, binds cytochrome b556; Membrane-anchoring subunit of succinate dehydrogenase (SDH); Belongs to the cytochrome b560 family. (129 aa) |
| | sdhD | Succinate dehydrogenase, membrane subunit, binds cytochrome b556; Membrane-anchoring subunit of succinate dehydrogenase (SDH). (115 aa) |
| | sdhA | Succinate dehydrogenase, flavoprotein subunit; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. (588 aa) |
| | sdhB | Succinate dehydrogenase, FeS subunit; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. (238 aa) |
| | cydA | Cytochrome d terminal oxidase, subunit I; A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. Belongs to the cytochrome ubiquinol oxidase subunit 1 family. (522 aa) |
| | cydB | Cytochrome d terminal oxidase, subunit II; A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. (379 aa) |
| | grxA | Glutaredoxin 1, redox coenzyme for ribonucleotide reductase (RNR1a); The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase; Belongs to the glutaredoxin family. (85 aa) |
| | dmsA | Dimethyl sulfoxide reductase, anaerobic, subunit A; Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant. (814 aa) |
| | dmsB | Dimethyl sulfoxide reductase, anaerobic, subunit B; Electron transfer subunit of the terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. (205 aa) |
| | dmsC | Dimethyl sulfoxide reductase, anaerobic, subunit C; Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. DmsC anchors the DmsAB dimer to the membrane and stabilizes it. (287 aa) |
| | hyaA | Hydrogenase 1, small subunit; This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth; Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit family. (372 aa) |
| | hyaB | Hydrogenase 1, large subunit; This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth; Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family. (597 aa) |
| | hyaC | Hydrogenase 1, b-type cytochrome subunit; Probable b-type cytochrome; Belongs to the HupC/HyaC/HydC family. (235 aa) |
| | cbdA | Cytochrome bd-II oxidase, subunit I; A terminal oxidase that catalyzes quinol-dependent, Na(+)- independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. (514 aa) |
| | cbdB | Cytochrome bd-II oxidase, subunit II; A terminal oxidase that catalyzes quinol-dependent, Na(+)- independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. (378 aa) |
| | torC | Trimethylamine N-oxide (TMAO) reductase I, cytochrome c-type subunit; Part of the anaerobic respiratory chain of trimethylamine-N- oxide reductase TorA. Acts by transferring electrons from the membranous menaquinones to TorA. This transfer probably involves an electron transfer pathway from menaquinones to the N-terminal domain of TorC, then from the N-terminus to the C-terminus, and finally to TorA. TorC apocytochrome negatively autoregulates the torCAD operon probably by inhibiting the TorS kinase activity. (390 aa) |
| | torA | Trimethylamine N-oxide (TMAO) reductase I, catalytic subunit; Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions. (848 aa) |
| | yceJ | Putative cytochrome b561; Protein involved in cytochrome complex assembly; Belongs to the cytochrome b561 family. (188 aa) |
| | ndh | Respiratory NADH dehydrogenase 2/cupric reductase; Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Does not couple the redox reaction to proton translocation. (434 aa) |
| | icd | Isocitrate dehydrogenase, specific for NADP+; Protein involved in tricarboxylic acid cycle and anaerobic respiration; Belongs to the isocitrate and isopropylmalate dehydrogenases family. (416 aa) |
| | dsbB | Oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I; Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. (176 aa) |
| | narG | 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. (1247 aa) |
| | narH | Nitrate reductase 1, beta (Fe-S) subunit; The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four 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. (512 aa) |
| | narI | Nitrate reductase 1, gamma (cytochrome b(NR)) subunit; The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit. (225 aa) |
| | pfo | Pyruvate-flavodoxin oxidoreductase; Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin. (1174 aa) |
| | azoR | 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. (201 aa) |
| | cybB | Cytochrome b561; B-type di-heme cytochrome with a major alpha-absorption peak at 561 nm and a minor peak at 555 nm. (176 aa) |
| | narV | Nitrate reductase 2 (NRZ), gamma subunit; This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit. (226 aa) |
| | narY | Nitrate reductase 2 (NRZ), beta subunit; This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four 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. (514 aa) |
| | narZ | Nitrate reductase 2 (NRZ), alpha subunit; This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and allows E.coli to use nitrate as an electron acceptor during anaerobic growth; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (1246 aa) |
| | fdnG | 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). (1015 aa) |
| | fdnH | 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 [...] (294 aa) |
| | fdnI | 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). (217 aa) |
| | ynfE | Putative selenate reductase, periplasmic; Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (808 aa) |
| | ynfF | S- and N-oxide reductase, A subunit, periplasmic; Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. (807 aa) |
| | ynfH | Oxidoreductase, membrane subunit; Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. The C subunit anchors the other two subunits to the membrane and stabilize the catalytic subunits (By similarity); Belongs to the DmsC family. (284 aa) |
| | rsxA | SoxR iron-sulfur cluster reduction factor component; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required to maintain the reduced state of SoxR. Probably transfers electron from NAD(P)H to SoxR. (193 aa) |
| | rsxB | SoxR iron-sulfur cluster reduction factor component; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required to maintain the reduced state of SoxR. Probably transfers electron from NAD(P)H to SoxR. Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily. (192 aa) |
| | rsxC | SoxR iron-sulfur cluster reduction factor component; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required to maintain the reduced state of SoxR. Probably transfers electron from NAD(P)H to SoxR. Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC subfamily. (740 aa) |
| | rsxD | SoxR iron-sulfur cluster reduction factor component; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required to maintain the reduced state of SoxR. Probably transfers electron from NAD(P)H to SoxR. Belongs to the NqrB/RnfD family. (352 aa) |
| | rsxG | SoxR iron-sulfur cluster reduction factor component; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required to maintain the reduced state of SoxR. Probably transfers electron from NAD(P)H to SoxR. Belongs to the RnfG family. (206 aa) |
| | rsxE | SoxR iron-sulfur cluster reduction factor component; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required to maintain the reduced state of SoxR. Probably transfers electron from NAD(P)H to SoxR. (231 aa) |
| | ydhU | Putative cytochrome b subunit of YdhYVWXUT oxidoreductase complex. (261 aa) |
| | ydhV | Putative oxidoreductase subunit. (700 aa) |
| | ydiQ | Putative electron transfer flavoprotein subunit; May play a role in a redox process; Belongs to the ETF beta-subunit/FixA family. (254 aa) |
| | ydiR | Putative electron transfer flavoprotein, FAD-binding subunit; May play a role in a redox process; Belongs to the ETF alpha-subunit/FixB family. (312 aa) |
| | torZ | Trimethylamine N-oxide reductase system III, catalytic subunit; Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions. Can also reduce other N- and S-oxide compounds such as 4-methylmorpholine-N- oxide and biotin sulfoxide (BSO), but with a lower catalytic efficiency; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (809 aa) |
| | torY | TMAO reductase III (TorYZ), cytochrome c-type subunit; Part of the anaerobic respiratory chain of trimethylamine-N- oxide reductase TorZ. Required for electron transfer to the TorZ terminal enzyme. (366 aa) |
| | yedZ | Inner membrane heme subunit for periplasmic YedYZ reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides el [...] (211 aa) |
| | yodB | Cytochrome b561 homolog 1; Protein involved in cytochrome complex assembly. (176 aa) |
| | dld | D-lactate dehydrogenase, FAD-binding, NADH independent; Catalyzes the oxidation of D-lactate to pyruvate. Electrons derived from D-lactate oxidation are transferred to the ubiquinone/cytochrome electron transfer chain, where they may be used to provide energy for the active transport of a variety of amino acids and sugars across the membrane. (571 aa) |
| | napC | Quinol dehydrogenase, electron source for NapAB; Mediates electron flow from quinones to the NapAB complex. (200 aa) |
| | napA | Nitrate reductase, periplasmic, large subunit; Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. (828 aa) |
| | yfaE | Uncharacterized ferredoxin-like protein YfaE; Ferredoxin involved with ribonucleotide reductase diferric-tyrosyl radical (Y*) cofactor maintenance. (84 aa) |
| | glpC | Anaerobic sn-glycerol-3-phosphate dehydrogenase, C subunit, 4Fe-4S iron-sulfur cluster; Electron transfer protein; may also function as the membrane anchor for the GlpAB dimer. (396 aa) |
| | nuoN | NADH:ubiquinone oxidoreductase, membrane subunit N; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 2 family. (485 aa) |
| | nuoM | NADH:ubiquinone oxidoreductase, membrane subunit M; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 4 family. (509 aa) |
| | nuoL | NADH:ubiquinone oxidoreductase, membrane subunit L; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 5 family. (613 aa) |
| | nuoK | NADH:ubiquinone oxidoreductase, membrane subunit K; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (100 aa) |
| | nuoJ | NADH:ubiquinone oxidoreductase, membrane subunit J; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 6 family. (184 aa) |
| | nuoI | NADH:ubiquinone oxidoreductase, chain I; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (180 aa) |
| | nuoH | NADH:ubiquinone oxidoreductase, membrane subunit H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. (325 aa) |
| | nuoG | NADH:ubiquinone oxidoreductase, chain G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (908 aa) |
| | nuoF | NADH:ubiquinone oxidoreductase, chain F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (445 aa) |
| | nuoE | NADH:ubiquinone oxidoreductase, chain E; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (166 aa) |
| | nuoC | NADH:ubiquinone oxidoreductase, fused CD subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the C-terminal section; belongs to the complex I 49 kDa subunit family. (596 aa) |
| | nuoB | NADH:ubiquinone oxidoreductase, chain B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (220 aa) |
| | nuoA | NADH:ubiquinone oxidoreductase, membrane subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family. (147 aa) |
| | hyfB | Hydrogenase 4, membrane subunit; Possible component of hydrogenase 4. (672 aa) |
| | hyfC | Hydrogenase 4, membrane subunit; Possible component of hydrogenase 4. Belongs to the complex I subunit 1 family. (315 aa) |
| | hyfD | Hydrogenase 4, membrane subunit; Possible component of hydrogenase 4. Belongs to the complex I subunit 5 family. (479 aa) |
| | hyfE | Hydrogenase 4, membrane subunit; Possible component of hydrogenase 4. (216 aa) |
| | hyfF | Hydrogenase 4, membrane subunit; Possible component of hydrogenase 4. Belongs to the complex I subunit 5 family. (526 aa) |
| | hyfG | Hydrogenase 4, subunit; Possible component of hydrogenase 4. (555 aa) |
| | hyfI | Hydrogenase 4, Fe-S subunit; Possible component of hydrogenase 4. Belongs to the complex I 20 kDa subunit family. (252 aa) |
| | fdx | [2Fe-2S] ferredoxin; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Although the function of this ferredoxin is unknown it is probable that it has a role as a cellular electron transfer protein. Involved in the in vivo assembly of the Fe-S clusters in a wide variety of iron-sulfur proteins. (111 aa) |
| | nrdH | Hydrogen donor for NrdEF electron transport system; Electron transport system for the ribonucleotide reductase system NrdEF; Belongs to the glutaredoxin family. (81 aa) |
| | norV | 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. (479 aa) |
| | hydN | Formate dehydrogenase-H, [4Fe-4S] ferredoxin subunit; Electron transport from formate to hydrogen. (175 aa) |
| | hycG | Hydrogenase 3 and formate hydrogenase complex, HycG subunit; Hydrogenase activity; Protein involved in fermentation and anaerobic respiration. (255 aa) |
| | hycF | Formate hydrogenlyase complex iron-sulfur protein; Probable electron transfer protein for hydrogenase 3. (180 aa) |
| | hycE | Large subunit of hydrogenase 3 (part of FHL complex); Protein involved in fermentation and anaerobic respiration; Belongs to the complex I 49 kDa subunit family. (569 aa) |
| | hycD | Membrane-spanning protein of hydrogenase 3 (part of FHL complex); Protein involved in fermentation; Belongs to the complex I subunit 1 family. (307 aa) |
| | hycC | Membrane-spanning protein of hydrogenase 3 (part of FHL complex); Protein involved in fermentation; Belongs to the complex I subunit 4 family. (608 aa) |
| | hycB | Hydrogenase 3, Fe-S subunit; Probable electron transfer protein for hydrogenase 3. (203 aa) |
| | ygcQ | Putative flavoprotein; May play a role in a redox process; Belongs to the ETF alpha-subunit/FixB family. (286 aa) |
| | ygcR | Putative flavoprotein; May play a role in a redox process. (259 aa) |
| | fldB | Flavodoxin 2; Low-potential electron donor to a number of redox enzymes. Belongs to the flavodoxin family. (173 aa) |
| | hybC | Hydrogenase 2, large subunit; This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake; Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family. (567 aa) |
| | hybB | Putative hydrogenase 2 cytochrome b type component; Probable b-type cytochrome; Belongs to the NrfD family. (392 aa) |
| | hybA | Hydrogenase 2 4Fe-4S ferredoxin-type component; Participates in the periplasmic electron-transferring activity of hydrogenase 2 during its catalytic turnover. (328 aa) |
| | kefG | Potassium-efflux system ancillary protein for KefB, glutathione-regulated; Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefB. (184 aa) |
| | glpD | Sn-glycerol-3-phosphate dehydrogenase, aerobic, FAD/NAD(P)-binding; Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses molecular oxygen or nitrate as electron acceptor. (501 aa) |
| | yhjA | Protein involved in cytochrome complex assembly. (465 aa) |
| | bisC | Biotin sulfoxide reductase; This enzyme may serve as a scavenger, allowing the cell to utilize biotin sulfoxide as a biotin source. It reduces a spontaneous oxidation product of biotin, D-biotin D-sulfoxide (BSO or BDS), back to biotin. Also exhibits methionine-(S)-sulfoxide (Met-S-SO) reductase activity, acting specifically on the (S) enantiomer in the free, but not the protein-bound form. It thus plays a role in assimilation of oxidized methionines. (777 aa) |
| | ysaA | Putative hydrogenase, 4Fe-4S ferredoxin-type component. (157 aa) |
| | hemG | Protoporphyrin oxidase, flavoprotein; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX using menaquinone as electron acceptor. (181 aa) |
| | fdoI | 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. (211 aa) |
| | fdoH | 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). (300 aa) |
| | fdoG | 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. (1016 aa) |
| | nrfA | 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). (478 aa) |
| | nrfB | Nitrite reductase, formate-dependent, penta-heme cytochrome c; Plays a role in nitrite reduction. (188 aa) |
| | fdhF | Formate dehydrogenase-H, selenopolypeptide subunit; Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. (715 aa) |
| | dsbD | Thiol:disulfide interchange protein and activator of DsbC; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps; Belongs to the thioredoxin family. DsbD subfamily. (565 aa) |
| | frdB | Fumarate reductase (anaerobic), Fe-S subunit; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. (244 aa) |
