Your Input: | |||||
Rcas_0566 | NADH dehydrogenase (quinone); PFAM: NADH/Ubiquinone/plastoquinone (complex I); KEGG: rrs:RoseRS_3854 NADH dehydrogenase (quinone). (526 aa) | ||||
atpC | ATP synthase F1, epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. (139 aa) | ||||
atpD | ATP synthase F1, beta subunit; 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. (471 aa) | ||||
atpG | ATP synthase F1, 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. (290 aa) | ||||
atpA | ATP synthase F1, alpha subunit; 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. (526 aa) | ||||
atpH | H+transporting two-sector ATPase delta (OSCP) 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; Belongs to the ATPase delta chain family. (158 aa) | ||||
atpF | ATP synthase F0, B 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. (163 aa) | ||||
atpE | ATP synthase F0, C 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. (77 aa) | ||||
atpB | ATP synthase F0, A subunit; 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. (331 aa) | ||||
Rcas_1320 | TIGRFAM: NADH-quinone oxidoreductase, E subunit; PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit; KEGG: rrs:RoseRS_3674 NADH-quinone oxidoreductase, E subunit. (174 aa) | ||||
nuoD1 | NADH dehydrogenase I, D 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; 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. (174 aa) | ||||
nuoB1 | 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. (167 aa) | ||||
nuoA | NADH-ubiquinone/plastoquinone oxidoreductase chain 3; 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) | ||||
Rcas_1364 | PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit; KEGG: rrs:RoseRS_3543 NADH dehydrogenase (ubiquinone), 24 kDa subunit. (173 aa) | ||||
Rcas_1365 | PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; KEGG: rrs:RoseRS_3542 NADH dehydrogenase (quinone). (532 aa) | ||||
Rcas_1366 | PFAM: ferredoxin; 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: rrs:RoseRS_3541 ferredoxin. (235 aa) | ||||
Rcas_1459 | PFAM: cytochrome oxidase assembly; KEGG: rrs:RoseRS_4134 cytochrome oxidase assembly. (337 aa) | ||||
Rcas_1574 | Cytochrome c oxidase subunit II; PFAM: blue (type 1) copper domain protein; cytochrome c oxidase subunit II; KEGG: rrs:RoseRS_0933 cytochrome c oxidase, subunit II. (168 aa) | ||||
Rcas_1575 | PFAM: cytochrome c oxidase subunit I; KEGG: rrs:RoseRS_0934 cytochrome c oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family. (561 aa) | ||||
nuoA-2 | NADH-ubiquinone/plastoquinone oxidoreductase chain 3; 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) | ||||
nuoB2 | 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. (268 aa) | ||||
Rcas_2090 | PFAM: NADH dehydrogenase (ubiquinone) 30 kDa subunit; KEGG: rrs:RoseRS_2991 NADH (or F420H2) dehydrogenase, subunit C. (189 aa) | ||||
nuoD2 | NADH dehydrogenase (quinone); 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. (374 aa) | ||||
Rcas_2092 | PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: rrs:RoseRS_2993 4Fe-4S ferredoxin, iron-sulfur binding domain protein. (449 aa) | ||||
nuoH | NADH dehydrogenase (quinone); 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. (452 aa) | ||||
Rcas_2094 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. (217 aa) | ||||
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. (108 aa) | ||||
Rcas_2096 | KEGG: rrs:RoseRS_2997 proton-translocating NADH-quinone oxidoreductase, chain L; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH-Ubiquinone oxidoreductase (complex I) chain 5/L domain protein; NADH/Ubiquinone/plastoquinone (complex I). (726 aa) | ||||
Rcas_2097 | KEGG: rrs:RoseRS_2998 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (566 aa) | ||||
Rcas_2098 | KEGG: rrs:RoseRS_2999 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (505 aa) | ||||
nuoN1 | Proton-translocating NADH-quinone oxidoreductase, 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. (540 aa) | ||||
Rcas_2276 | PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: gsu:GSU0493 pyridine nucleotide-disulphide oxidoreductase family protein. (416 aa) | ||||
Rcas_3079 | TIGRFAM: succinate dehydrogenase (or fumarate reductase) cytochrome b subunit, b558 family; KEGG: rrs:RoseRS_2400 succinate dehydrogenase (or fumarate reductase) cytochrome b subunit, b558 family. (226 aa) | ||||
Rcas_3080 | KEGG: rrs:RoseRS_2399 succinate dehydrogenase or fumarate reductase, flavoprotein subunit; TIGRFAM: succinate dehydrogenase or fumarate reductase, flavoprotein subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein; FAD dependent oxidoreductase. (656 aa) | ||||
Rcas_3081 | TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; PFAM: ferredoxin; 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: rrs:RoseRS_2398 succinate dehydrogenase and fumarate reductase iron-sulfur protein. (249 aa) | ||||
nuoN2 | Proton-translocating NADH-quinone oxidoreductase, 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. (498 aa) | ||||
Rcas_3383 | KEGG: rrs:RoseRS_2231 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (507 aa) | ||||
Rcas_3384 | KEGG: rrs:RoseRS_2232 proton-translocating NADH-quinone oxidoreductase, chain L; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH-Ubiquinone oxidoreductase (complex I) chain 5/L domain protein; NADH/Ubiquinone/plastoquinone (complex I). (654 aa) | ||||
nuoK-2 | 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. (100 aa) | ||||
Rcas_3386 | NADH-ubiquinone/plastoquinone oxidoreductase chain 6; 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. (170 aa) | ||||
nuoI | NADH-quinone 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. (165 aa) | ||||
nuoH-2 | NADH dehydrogenase (quinone); 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. (390 aa) | ||||
Rcas_3389 | NADH-quinone oxidoreductase, chain 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. (923 aa) | ||||
Rcas_3391 | NADH-quinone oxidoreductase, F subunit; 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. (451 aa) | ||||
ppk | Polyphosphate kinase; Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Belongs to the polyphosphate kinase 1 (PPK1) family. (708 aa) | ||||
Rcas_3555 | KEGG: rrs:RoseRS_2266 caa(3)-type oxidase, subunit IV. (113 aa) | ||||
Rcas_3556 | PFAM: cytochrome c oxidase subunit III; KEGG: rrs:RoseRS_2265 cytochrome c oxidase, subunit III. (203 aa) | ||||
Rcas_3557 | Cytochrome c oxidase subunit I type; 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. (641 aa) | ||||
Rcas_3558 | 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). (370 aa) | ||||
ppa | Inorganic diphosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (184 aa) | ||||
ctaB | 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. (535 aa) |