STRINGSTRING
ctaD-2 ctaD-2 AOK53912.1 AOK53912.1 grxC grxC AOK54087.1 AOK54087.1 AOK54551.1 AOK54551.1 AOK54849.1 AOK54849.1 dsbB-2 dsbB-2 AOK55117.1 AOK55117.1 AOK55835.1 AOK55835.1 AOK57606.1 AOK57606.1 AOK57249.1 AOK57249.1 ctaD ctaD msrQ msrQ petA petA AOK51635.1 AOK51635.1 AOK51994.1 AOK51994.1 dsbB dsbB AOK52219.1 AOK52219.1 AOK52811.1 AOK52811.1 AOK53138.1 AOK53138.1 AOK53139.1 AOK53139.1 AOK53404.1 AOK53404.1 AOK53437.1 AOK53437.1 AOK53500.1 AOK53500.1 cyoB cyoB AOK53792.1 AOK53792.1 AOK53885.1 AOK53885.1
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:
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)
AOK53912.1Cytochrome-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). (526 aa)
grxCGlutaredoxin; Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. (86 aa)
AOK54087.1High potential iron-sulfur protein; Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria; Belongs to the high-potential iron-sulfur protein (HiPIP) family. (105 aa)
AOK54551.1Electron transfer flavoprotein-ubiquinone oxidoreductase; Accepts electrons from ETF and reduces ubiquinone. (557 aa)
AOK54849.1Ferredoxin; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (107 aa)
dsbB-2Disulfide bond formation protein B; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. (167 aa)
AOK55117.1Ferredoxin; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (111 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)
AOK57606.1Amine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aromatic amine dehydrogenase light chain family. (176 aa)
AOK57249.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (470 aa)
ctaDCytochrome 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. (584 aa)
msrQSulfoxide reductase heme-binding subunit YedZ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalyti [...] (224 aa)
petAUbiquinol-cytochrome c reductase iron-sulfur subunit; 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. (206 aa)
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)
AOK51994.1Rubredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (56 aa)
dsbBDisulfide bond formation protein B; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. (170 aa)
AOK52219.1Ferredoxin; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (107 aa)
AOK52811.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (466 aa)
AOK53138.1Cytochrome ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. (668 aa)
AOK53139.1Cytochrome ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (295 aa)
AOK53404.1Ferredoxin; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily. (317 aa)
AOK53437.1Rubredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (60 aa)
AOK53500.1Rubredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (61 aa)
cyoBCytochrome ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. (670 aa)
AOK53792.1Cytochrome ubiquinol oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (296 aa)
AOK53885.1Cytochrome d terminal oxidase subunit 1; Part of the aerobic respiratory chain; catalyzes the ubiquinol to ubiquinone; Derived by automated computational analysis using gene prediction method: Protein Homology. (526 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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