STRINGSTRING
AOK51635.1 AOK51635.1 AOK51901.1 AOK51901.1 folK folK AOK52136.1 AOK52136.1 AOK53140.1 AOK53140.1 AOK53316.1 AOK53316.1 AOK53317.1 AOK53317.1 nuoI nuoI AOK53322.1 AOK53322.1 nuoF nuoF AOK53324.1 AOK53324.1 AOK53876.1 AOK53876.1 ctaD-2 ctaD-2 AOK54704.1 AOK54704.1 AOK55833.1 AOK55833.1 AOK55835.1 AOK55835.1 sdhB sdhB AOK56397.1 AOK56397.1
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.
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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:
AOK51635.1Cytochrome B; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (463 aa)
AOK51901.1Deoxyadenosine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. (228 aa)
folK2-amino-4-hydroxy-6- hydroxymethyldihydropteridine pyrophosphokinase; Derived by automated computational analysis using gene prediction method: Protein Homology. (181 aa)
AOK52136.1Formate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (525 aa)
AOK53140.1NADH:ubiquinone oxidoreductase subunit M; Catalyzes the transfer of electrons from NADH to quinone; Derived by automated computational analysis using gene prediction method: Protein Homology. (510 aa)
AOK53316.1NADH:ubiquinone oxidoreductase subunit M; Catalyzes the transfer of electrons from NADH to quinone; Derived by automated computational analysis using gene prediction method: Protein Homology. (496 aa)
AOK53317.1NADH:ubiquinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (684 aa)
nuoINADH dehydrogenase; 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. (162 aa)
AOK53322.1NADH dehydrogenase; 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. (776 aa)
nuoFNADH dehydrogenase; 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. (436 aa)
AOK53324.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (161 aa)
AOK53876.1Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (88 aa)
ctaD-2Cytochrome 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. (535 aa)
AOK54704.1Catalyzes the oxidation of tricarballylate to cis-aconitate; FAD-dependent; required for the utilization of tricarballylate as a carbon and energy source by S. enterica; Derived by automated computational analysis using gene prediction method: Protein Homology. (469 aa)
AOK55833.1Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (138 aa)
AOK55835.1Part of four member fumarate reductase enzyme complex FrdABCD which catalyzes the reduction of fumarate to succinate during anaerobic respiration; FrdAB are the catalytic subcomplex consisting of a flavoprotein subunit and an iron-sulfur subunit, respectively; FrdCD are the membrane components which interact with quinone and are involved in electron transfer; the catalytic subunits are similar to succinate dehydrogenase SdhAB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (591 aa)
sdhBPart of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; the catalytic subunits are similar to fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (233 aa)
AOK56397.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (483 aa)
Your Current Organism:
Burkholderia stagnalis
NCBI taxonomy Id: 1503054
Other names: B. stagnalis, Burkholderia sp. Bp6893, Burkholderia sp. Bp6916, Burkholderia sp. Bp7118, Burkholderia sp. Bp7119, Burkholderia sp. Bp7120, Burkholderia sp. Bp7137, Burkholderia sp. Bp7139, Burkholderia sp. Bp7142, Burkholderia sp. Bp7143, Burkholderia sp. Bp7145, Burkholderia sp. Bp7260, Burkholderia sp. Bp7266, Burkholderia sp. Bp7278, Burkholderia sp. Bp7280, Burkholderia sp. Bp7282, Burkholderia sp. Bp7288, Burkholderia sp. Bp7466, Burkholderia sp. Bp7469, Burkholderia sp. Bp7471, Burkholderia sp. Bp7483, Burkholderia sp. Bp7485, Burkholderia sp. Bp7491, Burkholderia sp. Bp7519, Burkholderia sp. Bp7520, Burkholderia sp. Bp7521, Burkholderia sp. Bp7554, Burkholderia sp. Bp7555, Burkholderia sp. Bp7571, Burkholderia sp. Bp7572, Burkholderia sp. Bp7635, Burkholderia sp. Bp7636, Burkholderia sp. Bp7639, Burkholderia sp. Bp7640, Burkholderia sp. Bp7641, Burkholderia sp. Bp7642, Burkholderia sp. Bp7643, Burkholderia sp. Bp7644, Burkholderia sp. Bp7645, Burkholderia sp. Bp7651, Burkholderia sp. Bp7656, Burkholderia sp. Bp7657, Burkholderia sp. Bp7658, Burkholderia sp. Bp7663, Burkholderia sp. Bp7665, Burkholderia sp. Bp7666, Burkholderia sp. Bp7667, Burkholderia sp. Bp7670, Burkholderia sp. Bp7671, Burkholderia sp. Bp7673, Burkholderia sp. Bp7681, Burkholderia sp. Bp7682, Burkholderia sp. Bp7684, Burkholderia sp. Bp7685, Burkholderia sp. Bp7686, Burkholderia sp. Bp7687, Burkholderia sp. Bp7690, Burkholderia sp. Bp7692, Burkholderia sp. Bp7693, Burkholderia sp. Bp7694, Burkholderia sp. Bp7697, Burkholderia sp. Bp7698, Burkholderia sp. Bp7699, Burkholderia sp. Bp7705, Burkholderia sp. Bp7707, Burkholderia sp. LMG 28156, Burkholderia sp. LMG 28157, Burkholderia sp. R-52095, Burkholderia sp. R-52096, Burkholderia sp. R-52235, Burkholderia sp. R-52237, Burkholderia sp. R-52238, Burkholderia sp. R-52240, Burkholderia stagnalis De Smet et al. 2015, CCUG 65686, LMG 28156, LMG:28156
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