STRINGSTRING
etfA etfA AHH16674.1 AHH16674.1 AHH16669.1 AHH16669.1 sdhC sdhC sdhB sdhB AHH15814.1 AHH15814.1 AHH15592.1 AHH15592.1 AHH15575.1 AHH15575.1 cydA cydA AHH15365.1 AHH15365.1 AHH15110.1 AHH15110.1 qcrB1 qcrB1 AHH18873.1 AHH18873.1 AHH18811.1 AHH18811.1 nuoN nuoN nuoM nuoM nuoL nuoL nuoJ nuoJ nuoG nuoG nuoF nuoF nuoD1 nuoD1 nuoB nuoB nuoA nuoA AHH18496.1 AHH18496.1 ctaD2 ctaD2 AHH18319.1 AHH18319.1 AHH17769.1 AHH17769.1 azoR azoR AHH19137.1 AHH19137.1 AHH19275.1 AHH19275.1 AHH19466.1 AHH19466.1 AHH19675.1 AHH19675.1 AHH19751.1 AHH19751.1 AHH19752.1 AHH19752.1 AHH19753.1 AHH19753.1 AHH19754.1 AHH19754.1 AHH19790.1 AHH19790.1 AHH19883.1 AHH19883.1 AHH20921.1 AHH20921.1 AHH21184.1 AHH21184.1 fdxA fdxA AHH21565.1 AHH21565.1 AHH21917.1 AHH21917.1 AHH22319.1 AHH22319.1 qcrB2 qcrB2 qcrC qcrC ctaE ctaE ctaF ctaF ctaC ctaC AHH16828.1 AHH16828.1 etfB etfB ctaD1 ctaD1 AHH18998.1 AHH18998.1 AHH18954.1 AHH18954.1 AHH18953.1 AHH18953.1 AHH18874.1 AHH18874.1
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
etfAElectron transfer flavoprotein subunit alpha. (319 aa)
AHH16674.1Putative membrane protein. (210 aa)
AHH16669.1Putative ferredoxin. (65 aa)
sdhCSuccinate dehydrogenase subunit C. (132 aa)
sdhBSuccinate dehydrogenase subunit B. (258 aa)
AHH15814.1Putative copper-binding protein. (142 aa)
AHH15592.1Putative membrane protein. (401 aa)
AHH15575.1Ferredoxin. (64 aa)
cydACytochrome D ubiquinol oxidase subunit I. (482 aa)
AHH15365.1Putative ferredoxin. (62 aa)
AHH15110.1Hypothetical protein. (197 aa)
qcrB1Ubiquinol-cytochrome c reductase cytochrome b subunit. (537 aa)
AHH18873.1Putative ferredoxin. (83 aa)
AHH18811.1Hypothetical protein. (294 aa)
nuoNNADH-quinone oxidoreductase 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. (541 aa)
nuoMNADH-quinone oxidoreductase subunit M. (548 aa)
nuoLNADH-quinone oxidoreductase subunit L. (634 aa)
nuoJNADH-quinone 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. (279 aa)
nuoGNADH-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. (822 aa)
nuoFNADH-quinone 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. (449 aa)
nuoD1NADH-quinone oxidoreductase 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. (259 aa)
nuoBNADH-quinone oxidoreductase 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)
nuoANADH-quinone 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 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. (126 aa)
AHH18496.1Hypothetical protein. (263 aa)
ctaD2Cytochrome c oxidase subunit 1; 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. (587 aa)
AHH18319.1Flavodoxin domain-containing protein. (170 aa)
AHH17769.1Putative ferredoxin. (63 aa)
azoRFMN-dependent NADH-azoreductase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity; Belongs to the azoreductase type 1 family. (211 aa)
AHH19137.1Hypothetical protein. (218 aa)
AHH19275.1Hypothetical protein. (239 aa)
AHH19466.1Putative cytochrome c oxidase subunit III. (200 aa)
AHH19675.1Putative flavodoxin. (184 aa)
AHH19751.1Putative NADH-ubiquinone/plastoquinone oxidoreductase. (681 aa)
AHH19752.1Putative NADH-ubiquinone oxidoreductase, 20kDa subunit. (261 aa)
AHH19753.1Putative NADH-ubiquinone oxidoreductase, chain 49kDa. (493 aa)
AHH19754.1Putative NADH-ubiquinone/plastoquinone oxidoreductase. (485 aa)
AHH19790.1Ferredoxin. (63 aa)
AHH19883.1Ferredoxin. (77 aa)
AHH20921.1Putative ferredoxin. (62 aa)
AHH21184.1Hypothetical protein. (163 aa)
fdxAFerredoxin; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (107 aa)
AHH21565.1Putative membrane protein. (557 aa)
AHH21917.1Monovalent cation/H+ antiporter subunit D. (538 aa)
AHH22319.1Putative succinate dehydrogenase/fumarate reductase iron-sulfur protein. (248 aa)
qcrB2Ubiquinol-cytochrome c reductase cytochrome b subunit. (542 aa)
qcrCUbiquinol-cytochrome c reductase cytochrome c subunit. (293 aa)
ctaEPutative cytochrome c oxidase subunit 3. (180 aa)
ctaFPutative cytochrome c oxidase polypeptide 4; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family. (138 aa)
ctaCPutative cytochrome c oxidase subunit 2. (364 aa)
AHH16828.1Putative ferredoxin. (65 aa)
etfBElectron transfer flavoprotein subunit beta. (261 aa)
ctaD1Cytochrome c oxidase subunit alpha; 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)
AHH18998.1Putative ferredoxin. (63 aa)
AHH18954.1Hypothetical protein. (76 aa)
AHH18953.1Putative NADH-ubiquinone oxidoreductase flavoprotein. (424 aa)
AHH18874.1NADH dehydrogenase. (370 aa)
Your Current Organism:
Nocardia nova
NCBI taxonomy Id: 1415166
Other names: N. nova SH22a, Nocardia nova SH22a
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