STRINGSTRING
SEQ79543.1 SEQ79543.1 SEP92641.1 SEP92641.1 SEP92666.1 SEP92666.1 SEP92732.1 SEP92732.1 SEP93887.1 SEP93887.1 SEQ13049.1 SEQ13049.1 SEQ14396.1 SEQ14396.1 SEQ14429.1 SEQ14429.1 SEQ14857.1 SEQ14857.1 SEQ30101.1 SEQ30101.1 SEQ48333.1 SEQ48333.1 SEQ48370.1 SEQ48370.1 SEQ54315.1 SEQ54315.1 SEQ63517.1 SEQ63517.1 SEQ65767.1 SEQ65767.1 SEQ65830.1 SEQ65830.1 SEQ65889.1 SEQ65889.1 SEQ67262.1 SEQ67262.1 SEQ67287.1 SEQ67287.1 SEQ67411.1 SEQ67411.1 SEQ67426.1 SEQ67426.1 SEQ67456.1 SEQ67456.1 SEQ67481.1 SEQ67481.1 SEQ69030.1 SEQ69030.1 SEQ69055.1 SEQ69055.1 SEQ62683.1 SEQ62683.1 SEP86031.1 SEP86031.1 SEQ77557.1 SEQ77557.1 SEQ89579.1 SEQ89579.1 SER05983.1 SER05983.1 SER15689.1 SER15689.1 SER32264.1 SER32264.1 SER41269.1 SER41269.1 SER51962.1 SER51962.1 SER51986.1 SER51986.1 SER62668.1 SER62668.1 SER59945.1 SER59945.1 SER60497.1 SER60497.1 SER72125.1 SER72125.1 SER68121.1 SER68121.1 SER70328.1 SER70328.1 SER75984.1 SER75984.1 SER96537.1 SER96537.1 SER95087.1 SER95087.1 SES01462.1 SES01462.1 SES11938.1 SES11938.1 azoR azoR SES23136.1 SES23136.1 SES23197.1 SES23197.1 SES31574.1 SES31574.1 SES34026.1 SES34026.1 SEP75666.1 SEP75666.1 SEP64823.1 SEP64823.1 SEP64853.1 SEP64853.1 nuoA nuoA nuoB nuoB nuoC nuoC nuoD nuoD SEP85318.1 SEP85318.1 SEP85345.1 SEP85345.1 SEP85371.1 SEP85371.1 SEP85458.1 SEP85458.1 nuoK nuoK SEP85522.1 SEP85522.1 SEP85555.1 SEP85555.1 nuoN nuoN SEP85991.1 SEP85991.1
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:
SEQ79543.1Ferredoxin. (64 aa)
SEP92641.1Succinate dehydrogenase subunit B. (260 aa)
SEP92666.1Succinate dehydrogenase subunit A. (584 aa)
SEP92732.1Succinate dehydrogenase subunit C. (140 aa)
SEP93887.1NADPH-dependent FMN reductase. (150 aa)
SEQ13049.1Hypothetical protein. (174 aa)
SEQ14396.1Cytochrome d ubiquinol oxidase subunit I. (386 aa)
SEQ14429.1Cytochrome bd terminal oxidase subunit II. (207 aa)
SEQ14857.1NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (108 aa)
SEQ30101.1NADH dehydrogenase subunit D; Belongs to the complex I 49 kDa subunit family. (361 aa)
SEQ48333.1Reductase C-terminal. (415 aa)
SEQ48370.1Ferredoxin. (63 aa)
SEQ54315.1TIGR03085 family protein. (203 aa)
SEQ63517.1Ferredoxin. (63 aa)
SEQ65767.1Ferredoxin, 2Fe-2S. (107 aa)
SEQ65830.13-phenylpropionate/trans-cinnamate dioxygenase ferredoxin reductase subunit. (405 aa)
SEQ65889.1NAD(P)H dehydrogenase (quinone). (195 aa)
SEQ67262.1Cytochrome c oxidase subunit 2; 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). (310 aa)
SEQ67287.1Cytochrome c oxidase subunit IV; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family. (138 aa)
SEQ67411.1Cytochrome c oxidase subunit 3. (202 aa)
SEQ67426.1Menaquinol-cytochrome c reductase cytochrome c1 subunit precursor. (270 aa)
SEQ67456.1Menaquinol-cytochrome c reductase iron-sulfur subunit precursor. (375 aa)
SEQ67481.1Ubiquinol-cytochrome c reductase cytochrome b subunit. (554 aa)
SEQ69030.1Succinate dehydrogenase / fumarate reductase flavoprotein subunit. (622 aa)
SEQ69055.1Succinate dehydrogenase subunit B. (249 aa)
SEQ62683.1Hypothetical protein. (104 aa)
SEP86031.1NADH-quinone oxidoreductase subunit C. (176 aa)
SEQ77557.1Ferredoxin. (64 aa)
SEQ89579.1Ferredoxin-NADP reductase. (351 aa)
SER05983.1Hypothetical protein. (169 aa)
SER15689.1NAD-dependent formate dehydrogenase flavoprotein subunit. (589 aa)
SER32264.1Reductase C-terminal. (367 aa)
SER41269.1Anaerobic selenocysteine-containing dehydrogenase; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (722 aa)
SER51962.1Electron transfer flavoprotein beta subunit. (260 aa)
SER51986.1Electron transfer flavoprotein alpha subunit apoprotein. (317 aa)
SER62668.1Sulfoxide reductase heme-binding subunit YedZ. (275 aa)
SER59945.1Conserved domain-containing protein. (251 aa)
SER60497.1Glycine/D-amino acid oxidase. (492 aa)
SER72125.1Cytochrome 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. (584 aa)
SER68121.1Cytochrome 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. (588 aa)
SER70328.12Fe-2S iron-sulfur cluster binding domain-containing protein. (60 aa)
SER75984.1Divergent 4Fe-4S mono-cluster. (77 aa)
SER96537.1Oxidoreductase alpha (molybdopterin) subunit; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (762 aa)
SER95087.1Hypothetical protein. (151 aa)
SES01462.1Uncharacterized membrane protein YeiB. (309 aa)
SES11938.1Cytochrome 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. (596 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. (193 aa)
SES23136.1YMGG-like Gly-zipper. (152 aa)
SES23197.1Hypothetical protein. (139 aa)
SES31574.1Flavodoxin domain-containing protein. (137 aa)
SES34026.1Ferredoxin. (63 aa)
SEP75666.1Glycolate oxidase. (467 aa)
SEP64823.1Cytochrome bd-I ubiquinol oxidase subunit 2 apoprotein. (323 aa)
SEP64853.1Cytochrome bd-I ubiquinol oxidase subunit 1 apoprotein. (484 aa)
nuoANADH 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. (121 aa)
nuoBNADH 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. (183 aa)
nuoCNADH 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. (250 aa)
nuoDNADH 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. (465 aa)
SEP85318.1NADH dehydrogenase subunit E. (239 aa)
SEP85345.1NADH 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. (432 aa)
SEP85371.1NADH 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. (821 aa)
SEP85458.1NADH 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. (282 aa)
nuoKNADH 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)
SEP85522.1NADH dehydrogenase subunit L. (644 aa)
SEP85555.1NADH dehydrogenase subunit M. (522 aa)
nuoNNADH 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. (523 aa)
SEP85991.1NADH-quinone oxidoreductase subunit B. (175 aa)
Your Current Organism:
Lechevalieria xinjiangensis
NCBI taxonomy Id: 402600
Other names: CGMCC 4.3525, DSM 45081, JCM 15473, L. xinjiangensis, Lechevalieria xinjiangensis Wang et al. 2007, strain R24
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