Your Input: | |||||
nuoK | NADH-ubiquinone oxidoreductase, chain 4L; 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 4L family. (101 aa) | ||||
SEH60786.1 | Peptidase M16 domain-containing protein. (197 aa) | ||||
SEH60771.1 | Peptidase M16 domain-containing protein. (260 aa) | ||||
SEH60756.1 | Zinc protease; Belongs to the peptidase M16 family. (442 aa) | ||||
nuoI | NADH dehydrogenase subunit 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. (164 aa) | ||||
nuoH | Respiratory-chain NADH dehydrogenase subunit 1; 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. (354 aa) | ||||
SEH69940.1 | [similarity to] NADH dehydrogenase, G subunit_. (165 aa) | ||||
SEH69925.1 | NADH-quinone oxidoreductase subunit G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 75 kDa subunit family. (600 aa) | ||||
SEH69906.1 | NADH:ubiquinone oxidoreductase subunit F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. (423 aa) | ||||
SEH69890.1 | NADH-quinone oxidoreductase, E subunit. (157 aa) | ||||
nuoD | NADH dehydrogenase I subunit D; 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 49 kDa subunit family. (417 aa) | ||||
nuoC | NADH (or F420H2) dehydrogenase, subunit C; 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 30 kDa subunit family. (204 aa) | ||||
nuoN | Proton-translocating NADH-quinoneoxidoreductase, chain 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. (484 aa) | ||||
SEH70040.1 | Proton-translocating NADH-quinoneoxidoreductase subunit M. (501 aa) | ||||
SEH70025.1 | Proton-translocating NADH-quinoneoxidoreductase subunit l. (653 aa) | ||||
SEH69993.1 | NADH:ubiquinone oxidoreductase subunit J; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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. (204 aa) | ||||
nuoB | NADH-quinone oxidoreductase, B 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. (159 aa) | ||||
nuoA | NADH:ubiquinone oxidoreductase 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. (118 aa) | ||||
atpB | F0F1-type ATP synthase, subunit a; 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. (291 aa) | ||||
atpE | ATPase, F0 complex, subunit C, bacterial andchloroplast; 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. (79 aa) | ||||
SEH64084.1 | F0F1-type ATP synthase, subunit b; 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. (135 aa) | ||||
atpH | F0F1-type ATP synthase, delta subunit; 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. (183 aa) | ||||
atpA | F0F1 ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (513 aa) | ||||
atpG | F0F1-type ATP synthase, gamma subunit; 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. (264 aa) | ||||
atpD | F0F1 ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. (463 aa) | ||||
atpC | F0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane. (135 aa) | ||||
rbfA | Ribosome-binding factor A; One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA. (112 aa) | ||||
SEH75911.1 | Ferredoxin 2Fe-2S protein. (103 aa) | ||||
SEH71069.1 | 4Fe-4S ferredoxin iron-sulfur bindingdomain-containing protein. (77 aa) | ||||
SEH63044.1 | Polyphosphate kinase 2. (180 aa) | ||||
SEH91318.1 | Protein containing Zinc finger, CHCC-typedomain. (62 aa) | ||||
ppa | Inorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (176 aa) | ||||
SEH94181.1 | Ubiquinol-cytochrome c reductase cytochrome c1subunit. (288 aa) | ||||
SEH94163.1 | Cytochrome b/b6 domain-containing protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (408 aa) | ||||
SEH94150.1 | Ubiquinol-cytochrome c reductase iron-sulfursubunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (211 aa) | ||||
cyoE | Protoheme IX farnesyltransferase; 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. (294 aa) | ||||
SEH82723.1 | Cytochrome c oxidase assembly protein. (316 aa) | ||||
SEH82705.1 | Cytochrome c 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). (366 aa) | ||||
SEH82688.1 | Cytochrome c 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. (539 aa) | ||||
SEH82657.1 | Cytochrome c oxidase assembly proteinCtaG/Cox11. (173 aa) | ||||
SEH82643.1 | MFS transporter. (295 aa) | ||||
SEH82588.1 | Cytochrome oxidase maturation proteincbb3-type. (35 aa) | ||||
SEH82558.1 | Cbb3-type cytochrome c oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. (523 aa) | ||||
SEH82545.1 | Peptidase S41. (203 aa) | ||||
SEH82516.1 | Cytochrome c oxidase cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (299 aa) | ||||
SEH74460.1 | Adenylylsulfate reductase subunit alpha. (625 aa) | ||||
SEH64469.1 | Sulfide-quinone reductase. (230 aa) |