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ndhN ndhN ppk ppk ndhE ndhE ndhG ndhG ndhI ndhI ndhA ndhA sdhA sdhA ndhC ndhC ndhJ ndhJ ndhH ndhH atpG-2 atpG-2 cydA cydA cydB cydB sdhB sdhB ndhD2 ndhD2 ppa ppa ctaB ctaB ctaA1 ctaA1 ctaE ctaE ctaD ctaD ctaC ctaC atpB atpB atpE atpE atpG atpG atpF atpF atpH atpH atpA atpA ndhM ndhM ndhF4 ndhF4 ndhD4 ndhD4 ndhB ndhB ndhK ndhK ndhL ndhL ndhD1 ndhD1 ndhF1 ndhF1 ndhF3 ndhF3 ndhD3 ndhD3 hdrB hdrB atpD atpD atpC atpC
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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ndhNProton-translocating NADH-quinone dehydrogenase subunit N NdhN; 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. (150 aa)
ppkPolyphosphate kinase Ppk; 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. (745 aa)
ndhEProton-translocating NADH-quinone dehydrogenase K subunit NdhE; 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)
ndhGProton-translocating NADH-quinone dehydrogenase subunit 6 NdhG; 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. (200 aa)
ndhIProton-translocating NADH-quinone dehydrogenase subunit NdhI; 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. (196 aa)
ndhAProton-translocating NADH-quinone dehydrogenase subunit NdhA; 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)
sdhASuccinate dehydrogenase flavoprotein subunit SdhA. (576 aa)
ndhCProton-translocating NADH-quinone dehydrogenase subunit 3 NdhC; 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. (132 aa)
ndhJProton-translocating NADH-quinone dehydrogenase subunit J NdhJ; 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. (168 aa)
ndhHProton-translocating NADH-quinone dehydrogenase subunit H NdhH; 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)
atpG-2F1 ATP synthase complex gamma subunit AtpG; 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)
cydACytochrome d ubiquinol oxidase subunit I CydA. (483 aa)
cydBCytochrome d ubiquinol oxidase subunit II CydB. (321 aa)
sdhBSuccinate dehydrogenase iron-sulfur subunit SdhB; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (335 aa)
ndhD2Proton-translocating NADH-quinone dehydrogenase subunit D2 NdhD2; 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. (533 aa)
ppaInorganic pyrophosphatase Ppa; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (172 aa)
ctaBHeme O synthase protoheme IX farnesyltransferase CtaB; 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)
ctaA1Heme A synthase cytochrome oxidase biogenesis protein CtaA1. (307 aa)
ctaEHeme-copper quinol oxidase small subunit (subunit III) CtaE. (201 aa)
ctaDHeme-copper quinol oxidase large subunit (subunit I) CtaD; 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)
ctaCHeme-copper quinol oxidase subunit II CtaC; 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). (337 aa)
atpBF0 ATP synthase complex subunit A AtpB; 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. (252 aa)
atpEF0 ATP synthase complex subunit C AtpE; 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. (82 aa)
atpGF0 ATP synthase complex B' subunit AtpG; 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. (138 aa)
atpFF0 ATP synthase complex B subunit AtpF; 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. (176 aa)
atpHF1 ATP synthase complex delta subunit AtpH; 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)
atpAF1 ATP synthase complex alpha subunit AtpA; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (503 aa)
ndhMProton-translocating NADH-quinone dehydrogenase subunit M NdhM; 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. (111 aa)
ndhF4Proton-translocating NADH-quinone dehydrogenase subunit F NdhF4. (609 aa)
ndhD4Proton-translocating NADH-quinone dehydrogenase subunit D4 NdhD4. (493 aa)
ndhBProton-translocating NADH-quinone dehydrogenase subunit B NdhB; 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. (515 aa)
ndhKProton-translocating NADH-quinone dehydrogenase subunit B NadhK; 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. (237 aa)
ndhLProton-translocating NADH-quinone dehydrogenase subunit NdhL. (82 aa)
ndhD1Proton-translocating NADH-quinone dehydrogenase subunit D1 NdhD1; 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. (533 aa)
ndhF1Proton-translocating NADH-quinone dehydrogenase subunit F1 NdhF1. (659 aa)
ndhF3Proton-translocating NADH-quinone dehydrogenase subunit 5 NdhF. (611 aa)
ndhD3Proton-translocating NADH-quinone dehydrogenase subunit D3 NdhD3. (492 aa)
hdrBHeterodisulfide reductase subunit B HdrB. (299 aa)
atpDF1 ATP synthase complex beta subunit AtpD; 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)
atpCF1 ATP synthase complex epsilon subunit AtpC; Produces ATP from ADP in the presence of a proton gradient across the membrane. (138 aa)
Your Current Organism:
Thermosynechococcus sp. NK55a
NCBI taxonomy Id: 1394889
Other names: T. sp. NK55a
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