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| ndhF | Putative NADH dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the complex I subunit 5 family. (505 aa) | ||||
| ctaO | Minor protoheme IX farnesyltransferase 1 (heme O synthase); Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (329 aa) | ||||
| ndh | NADH dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the NADH dehydrogenase family. (392 aa) | ||||
| ctaA | heme-A synthase; Catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group. Also involved in the sporulation. (306 aa) | ||||
| ctaB | Protoheme IX farnesyltransferase 2; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. (305 aa) | ||||
| ctaC | Cytochrome caa3 oxidase (subunit II); Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (356 aa) | ||||
| ctaD | Cytochrome caa3 oxidase (subunit I); Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. (622 aa) | ||||
| ctaE | Cytochrome caa3 oxidase (subunit III); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the cytochrome c oxidase subunit 3 family. (207 aa) | ||||
| ctaF | Cytochrome caa3 oxidase (subunit IV); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the cytochrome c oxidase bacterial subunit 4 family. (110 aa) | ||||
| qcrC | Menaquinol:cytochrome c oxidoreductase (cytochrome cc subunit); Component of the menaquinol-cytochrome c reductase complex. (255 aa) | ||||
| qcrB | Menaquinol:cytochrome c oxidoreductase (cytochrome b subunit); Component of the menaquinol-cytochrome c reductase complex. (224 aa) | ||||
| qcrA | Menaquinol:cytochrome c oxidoreductase (iron-sulfur subunit); Component of the menaquinol-cytochrome c reductase complex. The Rieske protein is a high potential 2Fe-2S protein. (167 aa) | ||||
| sdhB | Succinate dehydrogenase (iron-sulfur protein); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (253 aa) | ||||
| sdhA | Succinate dehydrogenase (flavoprotein subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. (586 aa) | ||||
| sdhC | Succinate dehydrogenase (cytochrome b558 subunit); Di-heme cytochrome of the succinate dehydrogenase complex. (202 aa) | ||||
| ythA | Putative cytochrome bd menaquinol oxidase subunit I; May have a role in sporulation. Can compensate for the loss of cytochrome aa3; Belongs to the cytochrome ubiquinol oxidase subunit 1 family. (443 aa) | ||||
| ythB | Putative cytochrome bd menaquinol oxidase subunit II; May have a role in sporulation. Can compensate for the loss of cytochrome aa3; Belongs to the cytochrome ubiquinol oxidase subunit 2 family. (346 aa) | ||||
| yumB | Putative NAD-disulfide oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (406 aa) | ||||
| yutJ | Putative NADH dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (355 aa) | ||||
| ppaX | P-Ser-HPr phosphatase; Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool; Belongs to the HAD-like hydrolase superfamily. PpaX family. (216 aa) | ||||
| atpC | ATP synthase (subunit epsilon, F1 subunit); Produces ATP from ADP in the presence of a proton gradient across the membrane. (132 aa) | ||||
| atpD | ATP synthase (subunit beta, component F1); Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. (473 aa) | ||||
| atpG | ATP synthase (subunit gamma, component F1); Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. (287 aa) | ||||
| atpA | ATP synthase (subunit alpha, component F1); Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit; Belongs to the ATPase alpha/beta chains family. (502 aa) | ||||
| atpH | ATP synthase (subunit delta, component F1); F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. (181 aa) | ||||
| atpF | ATP synthase (subunit b, component F0); F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (170 aa) | ||||
| atpE | ATP synthase (subunit c, component F0); F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (70 aa) | ||||
| atpB | ATP synthase (subunit a, component F0); Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (244 aa) | ||||
| qoxD | Cytochrome aa3-600 quinol oxidase (subunit IV); Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Major component for energy conversion during vegetative growth (By similarity). (124 aa) | ||||
| qoxC | Cytochrome aa3-600 quinol oxidase (subunit III); Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Major component for energy conversion during vegetative growth (By similarity). (204 aa) | ||||
| qoxB | Cytochrome aa3-600 quinol oxidase (subunit I); Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Major component for energy conversion during vegetative growth (By similarity). (649 aa) | ||||
| qoxA | Cytochrome aa3-600 quinol oxidase (subunit II); Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Major component for energy conversion during vegetative growth. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I (By similarity). (321 aa) | ||||
| cydB | Cytochrome bb' ubiquinol oxidase (subunit II); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (338 aa) | ||||
| cydA | Cytochrome bb' ubiquinol oxidase (subunit I); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the cytochrome ubiquinol oxidase subunit 1 family. (468 aa) | ||||
| ppaC | Inorganic pyrophosphatase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (309 aa) | ||||