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MARIT_1199 | Unannotated protein. (262 aa) | ||||
MARIT_1198 | Unannotated protein. (285 aa) | ||||
ccoNO | Unannotated protein; Belongs to the heme-copper respiratory oxidase family. (733 aa) | ||||
ccoP | Unannotated protein. (288 aa) | ||||
ctaA | Unannotated protein. (340 aa) | ||||
ctaC | Unannotated protein. (334 aa) | ||||
coxN | Unannotated protein; Belongs to the heme-copper respiratory oxidase family. (589 aa) | ||||
ppa | Unannotated protein; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (175 aa) | ||||
ndh | Unannotated protein. (434 aa) | ||||
atpB | Unannotated protein; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family. (372 aa) | ||||
atpE | Unannotated protein. (62 aa) | ||||
atpF | Unannotated protein; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family. (165 aa) | ||||
atpH | Unannotated protein; 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. (185 aa) | ||||
atpA | Unannotated protein; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (526 aa) | ||||
atpG | Unannotated protein; 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. (292 aa) | ||||
MARIT_2993 | Unannotated protein. (97 aa) | ||||
atpD | Unannotated protein; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. (503 aa) | ||||
sdhB | Unannotated protein. (248 aa) | ||||
sdhA | Unannotated protein. (671 aa) | ||||
sdhC | Unannotated protein. (224 aa) | ||||
ctaB | Unannotated protein; 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. (300 aa) | ||||
coxO | Unannotated protein. (194 aa) | ||||
coxP | Unannotated protein. (326 aa) | ||||
MARIT_0321 | Unannotated protein. (114 aa) |