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ctaB ctaB EKF04221.1 EKF04221.1 EKF04500.1 EKF04500.1 EKF04499.1 EKF04499.1 EKF04498.1 EKF04498.1 EKF05463.1 EKF05463.1 EKF05462.1 EKF05462.1 EKF05343.1 EKF05343.1 EKF05274.1 EKF05274.1 EKF05194.1 EKF05194.1 ppk ppk EKF05859.1 EKF05859.1 EKF05858.1 EKF05858.1 EKF05806.1 EKF05806.1 EKF05805.1 EKF05805.1 EKF05754.1 EKF05754.1 EKF05692.1 EKF05692.1 EKF05553.1 EKF05553.1 ndhH ndhH EKF05888.1 EKF05888.1 EKF05885.1 EKF05885.1 EKE96950.1 EKE96950.1 EKE96611.1 EKE96611.1 EKF02558.1 EKF02558.1 ndhN ndhN atpG atpG atpA atpA atpH atpH atpF atpF atpG-2 atpG-2 atpE atpE atpB atpB EKF02047.1 EKF02047.1 EKF02048.1 EKF02048.1 EKF02050.1 EKF02050.1 EKF02096.1 EKF02096.1 ppk-2 ppk-2 EKF01669.1 EKF01669.1 EKF01437.1 EKF01437.1 EKF01467.1 EKF01467.1 EKF01264.1 EKF01264.1 EKF01265.1 EKF01265.1 EKF01015.1 EKF01015.1 EKF00858.1 EKF00858.1 EKF00667.1 EKF00667.1 EKF00680.1 EKF00680.1 EKF00710.1 EKF00710.1 ndhD-3 ndhD-3 ppa ppa EKF00356.1 EKF00356.1 EKF00357.1 EKF00357.1 ndhB ndhB atpC atpC atpD atpD ndhE ndhE EKE99675.1 EKE99675.1 ndhI ndhI ndhA ndhA EKE99495.1 EKE99495.1 EKE99498.1 EKE99498.1 ndhM ndhM rbfA rbfA EKE99357.1 EKE99357.1 EKF04222.1 EKF04222.1 EKF02676.1 EKF02676.1 EKF02953.1 EKF02953.1 EKF02864.1 EKF02864.1 EKF02863.1 EKF02863.1 EKF02803.1 EKF02803.1 EKF02802.1 EKF02802.1 EKF02801.1 EKF02801.1 EKF02791.1 EKF02791.1 EKF02738.1 EKF02738.1 EKE97154.1 EKE97154.1 EKE97557.1 EKE97557.1 EKE97470.1 EKE97470.1 EKE97464.1 EKE97464.1 EKE97463.1 EKE97463.1 EKE97833.1 EKE97833.1 EKE97831.1 EKE97831.1 EKE97830.1 EKE97830.1 EKE98194.1 EKE98194.1 EKE98781.1 EKE98781.1 EKE98780.1 EKE98780.1 EKE98779.1 EKE98779.1 EKE98778.1 EKE98778.1 EKE98873.1 EKE98873.1 EKE98669.1 EKE98669.1 EKE98668.1 EKE98668.1 EKE98666.1 EKE98666.1 ndhJ ndhJ ndhK ndhK ndhC ndhC EKE99083.1 EKE99083.1 EKF04012.1 EKF04012.1 EKF03358.1 EKF03358.1 ndhD-2 ndhD-2 ndhD ndhD EKF03728.1 EKF03728.1 EKF03810.1 EKF03810.1
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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ctaBProtoheme 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. (317 aa)
EKF04221.1KEGG: ava:Ava_4047 1.1e-161 cytochrome bd ubiquinol oxidase, subunit II; K00426 cytochrome bd-I oxidase subunit II; Psort location: CytoplasmicMembrane, score: 10.00. (337 aa)
EKF04500.1KEGG: ava:Ava_B0177 7.4e-108 cytochrome c oxidase subunit III K02276; Psort location: CytoplasmicMembrane, score: 10.00. (239 aa)
EKF04499.1Cytochrome 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. (558 aa)
EKF04498.1Cytochrome c oxidase subunit; 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). (298 aa)
EKF05463.1Cation transporting ATPase; KEGG: ava:Ava_3565 1.4e-90 ATPase, E1-E2 type K01537; Psort location: CytoplasmicMembrane, score: 10.00. (200 aa)
EKF05462.1Cation transporter/ATPase; KEGG: ava:Ava_3565 3.7e-32 ATPase, E1-E2 type K01537; Psort location: CytoplasmicMembrane, score: 10.00. (105 aa)
EKF05343.1Peptidase M16 inactive domain protein; KEGG: ana:alr5125 1.5e-180 processing protease; K01412 mitochondrial processing peptidase; Belongs to the peptidase M16 family. (427 aa)
EKF05274.1Putative pyridine; KEGG: amt:Amet_3000 0.00015 succinate dehydrogenase. (588 aa)
EKF05194.1Hypothetical protein; KEGG: det:DET0729 5.0e-07 [Fe] hydrogenase, HymB subunit, putative; K00335 NADH dehydrogenase I subunit F. (216 aa)
ppkPolyphosphate kinase 1; 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. (787 aa)
EKF05859.1KEGG: npu:Npun_R3535 1.7e-92 cytochrome c oxidase, subunit III K02276; Psort location: CytoplasmicMembrane, score: 10.00. (200 aa)
EKF05858.1KEGG: ana:alr2732 6.5e-235 coxA; cytochrome c oxidase subunit I; K02274 cytochrome c oxidase subunit I; Psort location: CytoplasmicMembrane, score: 10.00; Belongs to the heme-copper respiratory oxidase family. (457 aa)
EKF05806.1KEGG: ana:alr2732 4.7e-42 coxA; cytochrome c oxidase subunit I; K02274 cytochrome c oxidase subunit I; Psort location: CytoplasmicMembrane, score: 9.82. (105 aa)
EKF05805.1Cytochrome c oxidase; 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). (308 aa)
EKF05754.1Putative calcium-translocating P-type ATPase, PMCA-type; KEGG: ava:Ava_3557 3.0e-294 ATPase, E1-E2 type K01537; Psort location: CytoplasmicMembrane, score: 10.00. (912 aa)
EKF05692.1Pyridine nucleotide-disulfide oxidoreductase family protein; KEGG: npu:Npun_R4765 1.5e-148 FAD-dependent pyridine nucleotide-disulphide oxidoreductase; Psort location: Cytoplasmic, score: 8.96. (391 aa)
EKF05553.1KEGG: npu:Npun_F5153 0. peptidase M16 domain-containing protein K07263. (921 aa)
ndhHNAD(P)H-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (394 aa)
EKF05888.1KEGG: ava:Ava_0749 4.7e-296 NAD(P)H-quinone oxidoreductase subunit F K05577; Psort location: CytoplasmicMembrane, score: 10.00. (619 aa)
EKF05885.1NAD(P)H-quinone oxidoreductase subunit M; KEGG: npu:Npun_F3688 1.8e-230 proton-translocating NADH-quinone oxidoreductase, chain M K05575; Psort location: CytoplasmicMembrane, score: 10.00. (499 aa)
EKE96950.1FAD binding domain protein; KEGG: npu:Npun_R2389 2.8e-273 fumarate reductase/succinate dehydrogenase flavoprotein domain-containing protein; Psort location: CytoplasmicMembrane, score: 7.88. (570 aa)
EKE96611.1Hypothetical protein; KEGG: cpb:Cphamn1_0926 0.049 amine oxidase; K00231 protoporphyrinogen oxidase. (677 aa)
EKF02558.1Pyridine nucleotide-disulfide oxidoreductase; KEGG: npu:Npun_R1785 2.2e-204 FAD-dependent pyridine nucleotide-disulphide oxidoreductase K03885. (455 aa)
ndhNHypothetical protein; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (158 aa)
atpGH(+)-transporting two-sector ATPase 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. (315 aa)
atpAATP 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. (506 aa)
atpHATP synthase F1, 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. (184 aa)
atpFATP synthase F0, B subunit; 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. (185 aa)
atpG-2F0F1 ATP synthase subunit B; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria. Belongs to the ATPase B chain family. (143 aa)
atpEATP 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. (81 aa)
atpBATP 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. (254 aa)
EKF02047.1Cytochrome c oxidase subunit; 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). (281 aa)
EKF02048.1Cytochrome 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. (552 aa)
EKF02050.1KEGG: cyn:Cyan7425_3956 3.9e-86 cytochrome c oxidase subunit III; K02276 cytochrome c oxidase subunit III; Psort location: CytoplasmicMembrane, score: 10.00. (203 aa)
EKF02096.1KEGG: ana:alr0762 1.0e-117 hoxU; bidirectional hydrogenase complex protein HoxU; K05588 diaphorase subunit of the bidirectional hydrogenase; Psort location: Cytoplasmic, score: 9.97. (238 aa)
ppk-2Polyphosphate kinase 1; 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. (733 aa)
EKF01669.1Hypothetical protein; KEGG: hma:rrnAC3011 5.1e-10 cbiK; colbalt chelase thioredoxin K01773. (109 aa)
EKF01437.1Eight transmembrane protein EpsH; KEGG: nca:Noca_2718 0.25 CDP-diacylglycerol-phosphatidylglycerol phosphatidyltransferase K00995; Psort location: CytoplasmicMembrane, score: 10.00. (299 aa)
EKF01467.1Putative thioredoxin; KEGG: pth:PTH_2011 6.8e-07 nuoF; NADH:ubiquinone oxidoreductase, NADH-binding 51 kD subunit; K00335 NADH dehydrogenase I subunit F; Psort location: Cytoplasmic, score: 8.96. (178 aa)
EKF01264.1KEGG: npu:Npun_R2847 1.7e-229 peptidase M16 domain-containing protein; Psort location: Cytoplasmic, score: 8.96. (509 aa)
EKF01265.1KEGG: npu:Npun_R2846 1.4e-216 peptidase M16 domain-containing protein. (509 aa)
EKF01015.1Hypothetical protein; KEGG: pdi:BDI_1043 7.5e-11 NADH:ubiquinone oxidoreductase subunit; K00335 NADH dehydrogenase I subunit F; Psort location: Cytoplasmic, score: 8.96. (290 aa)
EKF00858.1FAD binding domain protein; KEGG: ava:Ava_5007 3.0e-262 fumarate reductase/succinate dehydrogenase flavoprotein-like K00278. (546 aa)
EKF00667.1KEGG: ava:Ava_4994 9.5e-195 FAD-dependent pyridine nucleotide-disulphide oxidoreductase K03885. (467 aa)
EKF00680.1KEGG: ava:Ava_4690 7.2e-197 FAD-dependent pyridine nucleotide-disulphide oxidoreductase K03885. (453 aa)
EKF00710.1Hypothetical protein; KEGG: ava:Ava_2796 1.5e-61 NAD(P)H-quinone oxidoreductase subunit 4 K05575. (146 aa)
ndhD-3Proton-translocating NADH-quinone oxidoreductase, chain M; NDH-1 shuttles electrons from NAD(P)H, 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 plastoquinone. 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 4 family. (537 aa)
ppaInorganic diphosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (170 aa)
EKF00356.1NAD(P)H-quinone oxidoreductase subunit F; KEGG: npu:Npun_R4290 2.9e-287 NdhF3 family NAD(P)H dehydrogenase K05577; Psort location: CytoplasmicMembrane, score: 10.00. (618 aa)
EKF00357.1NAD(P)H-quinone oxidoreductase subunit D4; KEGG: npu:Npun_R4289 6.0e-225 proton-translocating NADH-quinone oxidoreductase, chain M K05575; Psort location: CytoplasmicMembrane, score: 10.00. (499 aa)
ndhBProton-translocating NADH-quinone oxidoreductase, chain; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (520 aa)
atpCH(+)-transporting ATPase F; Produces ATP from ADP in the presence of a proton gradient across the membrane. (151 aa)
atpDH(+)-transporting ATPase F(1) 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. (482 aa)
ndhENADH dehydrogenase subunit K; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (101 aa)
EKE99675.1NADH-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. Belongs to the complex I subunit 6 family. (216 aa)
ndhINADH-plastoquinone oxidoreductase, I subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient; Belongs to the complex I 23 kDa subunit family. (194 aa)
ndhANADH dehydrogenase; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. (372 aa)
EKE99495.1KEGG: npu:Npun_R4070 6.5e-180 peptidase M16 domain-containing protein; Psort location: Cytoplasmic, score: 8.96. (413 aa)
EKE99498.1KEGG: npu:Npun_R4069 1.8e-168 peptidase M16 domain-containing protein. (406 aa)
ndhMNADH dehydrogenase I subunit M; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (164 aa)
rbfARibosome-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. (140 aa)
EKE99357.1KEGG: npu:Npun_R2767 1.3e-286 succinate dehydrogenase or fumarate reductase, flavoprotein subunit K00239; Psort location: CytoplasmicMembrane, score: 7.88. (575 aa)
EKF04222.1KEGG: ava:Ava_4048 2.7e-222 cytochrome bd ubiquinol oxidase, subunit I; K00425 cytochrome bd-I oxidase subunit I; Psort location: CytoplasmicMembrane, score: 10.00. (468 aa)
EKF02676.1KEGG: npu:Npun_R4998 0. peptidase M16 domain-containing protein K07263. (927 aa)
EKF02953.1KEGG: dar:Daro_3585 1.4e-111 polyphosphate:AMP phosphotransferase K00947. (502 aa)
EKF02864.1KEGG: ava:Ava_4787 2.1e-220 putative monovalent cation/H+ antiporter subunit D K05568:K05575; Psort location: CytoplasmicMembrane, score: 10.00. (461 aa)
EKF02863.1CPA3 family monovalent cation:proton; KEGG: tko:TK1221 8.4e-13 putative monovalent cation/H+ antiporter subunit C; K00340 NADH dehydrogenase I subunit K; Psort location: CytoplasmicMembrane, score: 9.82. (114 aa)
EKF02803.1KEGG: cyn:Cyan7425_3998 2.1e-149 cytochrome d ubiquinol oxidase, subunit II; K00426 cytochrome bd-I oxidase subunit II; Psort location: CytoplasmicMembrane, score: 10.00. (337 aa)
EKF02802.1KEGG: ava:Ava_B0175 1.1e-159 cytochrome bd ubiquinol oxidase, subunit I; K00425 cytochrome bd-I oxidase subunit I; Psort location: CytoplasmicMembrane, score: 10.00. (374 aa)
EKF02801.1Hypothetical protein; KEGG: ana:all4024 2.2e-35 cytochrome d ubiquinol oxidase chain I; K00425 cytochrome bd-I oxidase subunit I; Psort location: CytoplasmicMembrane, score: 10.00. (78 aa)
EKF02791.1Cysteine-rich domain protein; KEGG: ana:all3341 2.1e-149 heterodisulfide reductase, subunit B; K03389 heterodisulfide reductase subunit B; Psort location: Cytoplasmic, score: 8.96. (301 aa)
EKF02738.1ABC transporter, permease family protein; KEGG: ago:AGOS_AER152W 0.14 AER152Wp; K00021 3-hydroxy-3-methylglutaryl-CoA reductase; Psort location: CytoplasmicMembrane, score: 10.00. (351 aa)
EKE97154.1KEGG: npu:Npun_F5945 1.9e-157 succinate dehydrogenase and fumarate reductase iron-sulfur protein K00240; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (335 aa)
EKE97557.1FAD-dependent pyridine; KEGG: ana:alr5211 7.0e-199 hypothetical protein; K03885 NADH dehydrogenase; Psort location: CytoplasmicMembrane, score: 9.82. (485 aa)
EKE97470.1Putative calcium-translocating P-type ATPase, PMCA-type; KEGG: ava:Ava_4083 0. ATPase, E1-E2 type K01537; Psort location: CytoplasmicMembrane, score: 10.00. (967 aa)
EKE97464.1H(+)-transporting two-sector protein; KEGG: ava:Ava_4653 1.4e-65 bidirectional hydrogenase complex protein HoxE K05586; Psort location: Cytoplasmic, score: 9.26. (181 aa)
EKE97463.1Protein HymB; KEGG: ava:Ava_4654 4.7e-232 respiratory-chain NADH dehydrogenase domain-containing protein K05587; Psort location: Cytoplasmic, score: 9.12. (548 aa)
EKE97833.1KEGG: ava:Ava_3575 4.7e-106 cytochrome c oxidase subunit III K02276; Psort location: CytoplasmicMembrane, score: 10.00. (222 aa)
EKE97831.1Cytochrome 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. (561 aa)
EKE97830.1Cytochrome 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). (306 aa)
EKE98194.1KEGG: sat:SYN_01114 0.00085 nucleotidyltransferase K00992. (119 aa)
EKE98781.1KEGG: ava:Ava_0530 7.3e-101 cytochrome c oxidase subunit III K02276; Psort location: CytoplasmicMembrane, score: 10.00. (208 aa)
EKE98780.1Cytochrome 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. (578 aa)
EKE98779.1Cytochrome c oxidase subunit; 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). (365 aa)
EKE98778.1Cytochrome oxidase assembly protein; KEGG: tro:trd_A0395 4.9e-21 protoheme IX farnesyltransferase (heme O synthase) (HemeB farnesyltransferase) K02301; Psort location: CytoplasmicMembrane, score: 10.00. (340 aa)
EKE98873.1WbqC-like family protein; KEGG: lsp:Bsph_1469 0.999 orotate phosphoribosyltransferase K00762; Psort location: Cytoplasmic, score: 8.96. (234 aa)
EKE98669.1Cytochrome 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). (325 aa)
EKE98668.1Cytochrome 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. (560 aa)
EKE98666.1KEGG: ava:Ava_0448 1.7e-85 cytochrome c oxidase subunit III K02276; Psort location: CytoplasmicMembrane, score: 10.00. (195 aa)
ndhJNADH dehydrogenase, subunit C; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (174 aa)
ndhKNADH dehydrogenase subunit B; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration; Belongs to the complex I 20 kDa subunit family. (245 aa)
ndhCNADH dehydrogenase subunit A; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. (120 aa)
EKE99083.1Polyphosphate:nucleotide phosphotransferase, PPK2 family; KEGG: ava:Ava_3133 2.4e-127 polyphosphate:AMP phosphotransferase K00947; Psort location: Cytoplasmic, score: 8.96. (289 aa)
EKF04012.1Putative potassium/sodium efflux P-type ATPase, fungal-type; KEGG: ava:Ava_3392 0. ATPase, E1-E2 type K01537; Psort location: CytoplasmicMembrane, score: 10.00. (953 aa)
EKF03358.1KEGG: npu:Npun_R5878 5.0e-228 fumarate reductase/succinate dehydrogenase flavoprotein domain-containing protein; Psort location: Cytoplasmic, score: 9.26. (544 aa)
ndhD-2Proton-translocating NADH-quinone oxidoreductase, chain M; NDH-1 shuttles electrons from NAD(P)H, 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 plastoquinone. 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 4 family. (562 aa)
ndhDProton-translocating NADH-quinone oxidoreductase, chain M; NDH-1 shuttles electrons from NAD(P)H, 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 plastoquinone. 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 4 family. (524 aa)
EKF03728.1NAD(P)H-quinone oxidoreductase subunit F; KEGG: npu:Npun_R6185 0. proton-translocating NADH-quinone oxidoreductase, chain L K05577; Psort location: CytoplasmicMembrane, score: 10.00. (699 aa)
EKF03810.1Hypothetical protein; KEGG: tel:tsr0706 1.1e-10 ndhL; NADH dehydrogenase subunit; K05583 NADH dehydrogenase I subunit L. (39 aa)
Your Current Organism:
Tolypothrix sp. PCC7601
NCBI taxonomy Id: 1188
Other names: Calothrix sp. PCC 7601, Fremyella diplosiphon ACMM 396, Fremyella diplosiphon IAM M-100, Fremyella diplosiphon UTEX B 481, Microchaete diplosiphon UTEX B 481, T. sp. PCC 7601, Tolypothrix (Calothrix) sp. PCC 7601, Tolypothrix sp. PCC 7601, Tolypothrix sp. PCC 7601 = UTEX B 481
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