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Acel_0266 | TIGRFAM: geranylgeranyl reductase; PFAM: monooxygenase, FAD-binding; FAD dependent oxidoreductase; tryptophan halogenase; Lycopene beta and epsilon cyclase; KEGG: fra:Francci3_0537 geranylgeranyl reductase. (445 aa) | ||||
nuoA | NADH dehydrogenase 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 a menaquinone. 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. (119 aa) | ||||
nuoB | NADH dehydrogenase subunit 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 believed to be a menaquinone. 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. (184 aa) | ||||
nuoC | NADH 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 a menaquinone. 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. (192 aa) | ||||
nuoD | NADH dehydrogenase 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 a menaquinone. 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. (440 aa) | ||||
Acel_0271 | TIGRFAM: NADH-quinone oxidoreductase, E subunit; PFAM: NADH dehydrogenase (ubiquinone), 24 kDa subunit; KEGG: sco:SCO4566 NADH dehydrogenase I chain E. (269 aa) | ||||
Acel_0272 | NADH dehydrogenase 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. (434 aa) | ||||
Acel_0273 | NADH dehydrogenase 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. (830 aa) | ||||
nuoH | NADH dehydrogenase 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. (451 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. (199 aa) | ||||
Acel_0276 | NADH dehydrogenase 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. (275 aa) | ||||
nuoK | NADH dehydrogenase 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 a menaquinone. 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. (99 aa) | ||||
Acel_0278 | KEGG: sma:SAV4848 putative NADH dehydrogenase 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). (634 aa) | ||||
Acel_0279 | NADH dehydrogenase subunit M; KEGG: tfu:Tfu_2683 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (507 aa) | ||||
nuoN | NADH dehydrogenase 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 a menaquinone. 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. (519 aa) | ||||
Acel_0490 | Cytochrome-c oxidase; 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. (589 aa) | ||||
Acel_0724 | PFAM: major facilitator superfamily MFS_1; KEGG: gme:Gmet_0906 major facilitator superfamily MFS_1. (404 aa) | ||||
Acel_0725 | PFAM: glycosyl transferase, family 2; KEGG: efa:EF2180 glycosyl transferase, group 2 family protein. (734 aa) | ||||
Acel_0726 | PFAM: NADH/Ubiquinone/plastoquinone (complex I); KEGG: rfr:Rfer_3292 NADH dehydrogenase (quinone). (684 aa) | ||||
Acel_0727 | PFAM: NADH ubiquinone oxidoreductase, 20 kDa subunit; KEGG: ade:Adeh_3660 NADH ubiquinone oxidoreductase, 20 kDa subunit. (269 aa) | ||||
Acel_0728 | PFAM: NADH-ubiquinone oxidoreductase, chain 49kDa; NADH dehydrogenase (ubiquinone), 30 kDa subunit; KEGG: dsy:DSY3115 formate hydrogenlyase subunit 5 precursor. (499 aa) | ||||
Acel_0729 | NADH dehydrogenase (quinone); PFAM: NADH/Ubiquinone/plastoquinone (complex I); KEGG: eca:ECA1242 NADH dehydrogenase subunit N. (512 aa) | ||||
Acel_0730 | KEGG: mca:MCA1140 hydrogenase subunit. (224 aa) | ||||
Acel_0731 | PFAM: respiratory-chain NADH dehydrogenase, subunit 1; KEGG: sso:SSO1026 formate hydrogenlyase subunit 4 (HycD). (320 aa) | ||||
Acel_0732 | Hypothetical protein. (160 aa) | ||||
Acel_0956 | 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). (280 aa) | ||||
Acel_0957 | Cytochrome-c oxidase; 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. (570 aa) | ||||
Acel_0958 | Putative integral membrane protein; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family. (132 aa) | ||||
Acel_0961 | PFAM: Cytochrome b/b6, N-terminal domain; KEGG: tfu:Tfu_1019 ubiquinol-cytochrome c reductase, cytochrome b subunit. (568 aa) | ||||
Acel_0962 | Menaquinol-cytochrome c reductase iron-sulfur subunit precursor; PFAM: Rieske [2Fe-2S] domain protein; KEGG: sco:SCO2149 Rieske iron-sulfur protein. (330 aa) | ||||
Acel_0963 | Menaquinol-cytochrome c reductase cytochrome c1 subunit precursor; PFAM: cytochrome c, class I; KEGG: sco:SCO2150 cytochrome C heme-binding subunit. (268 aa) | ||||
Acel_0964 | PFAM: cytochrome c oxidase, subunit III; KEGG: fra:Francci3_3108 heme/copper-type cytochrome/quinol oxidase subunit 3-like. (223 aa) | ||||
Acel_0965 | KEGG: tfu:Tfu_1023 putative response regulator. (135 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. (307 aa) | ||||
Acel_1133 | PFAM: cytochrome oxidase assembly; KEGG: sma:SAV6320 putative integral membrane transport protein. (370 aa) | ||||
Acel_1507 | PFAM: peptidase M16 domain protein; KEGG: sco:SCO5738 putative protease; Belongs to the peptidase M16 family. (451 aa) | ||||
Acel_1781 | Hypothetical protein; KEGG: gsu:GSU1649 cytochrome b/b6. (611 aa) | ||||
Acel_1986 | PFAM: electron transport protein SCO1/SenC; KEGG: bbr:BB4821 SCO1/SenC family protein. (271 aa) | ||||
Acel_1987 | KEGG: fra:Francci3_2497 putative copper resistance protein D. (354 aa) |