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nuoG nuoG scyA scyA frdC frdC frdC-2 frdC-2 frdA frdA frdB frdB petB petB petC petC napG napG folK folK nuoM nuoM nuoL nuoL nuoK nuoK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoF nuoF nuoE nuoE nuoB nuoB nuoA nuoA SO_1248 SO_1248 SO_1251 SO_1251 SO_1292 SO_1292 sdhC sdhC sdhA sdhA sdhB sdhB ccoP ccoP ccoO ccoO ccoN ccoN SO_2930 SO_2930 SO_2931 SO_2931 SO_3301 SO_3301 SO_4142 SO_4142 shp shp coxB coxB coxA coxA urdA urdA
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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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
protein homology
Your Input:
nuoGNADH-ubiquinone oxidoreductase subunit G NuoG; 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 (By similarity). (909 aa)
scyAPeriplasmic monoheme cytochrome c5 ScyA. (99 aa)
frdCQuinol:fumarate reductase menaquinol-oxidizing subunit FrdC. (241 aa)
frdC-2Quinol:fumarate reductase menaquinol-oxidizing subunit FrdC. (223 aa)
frdAQuinol:fumarate reductase FAD-binding subunit FrdA. (668 aa)
frdBQuinol:fumarate reductase FeS subunit FrdB. (243 aa)
petBUbiquinol-cytochrome c reductase cytochrome b subunit PetB; 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. (404 aa)
petCUbiquinol-cytochrome c reductase cytochrome c1 subunit PetC. (231 aa)
napGPeriplasmic nitrate reductase ferredoxin component NapG. (244 aa)
folK2-amino-4-hydroxy-6- hydroxymethyldihydropteridine pyrophosphokinase FolK. (162 aa)
nuoMNADH-ubiquinone oxidoreductase subunit M NuoM. (514 aa)
nuoLNADH-ubiquinone oxidoreductase subunit L NuoL. (615 aa)
nuoKNADH-ubiquinone oxidoreductase subunit K NuoK; 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; Belongs to the complex I subunit 4L family. (102 aa)
nuoJNADH-ubiquinone oxidoreductase subunit J NuoJ; 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. (183 aa)
nuoINADH-ubiquinone oxidoreductase subunit I NuoI; 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. (180 aa)
nuoHNADH-ubiquinone oxidoreductase subunit H NuoH; 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. This subunit may bind ubiquinone. (322 aa)
nuoFNADH-ubiquinone oxidoreductase subunit F NuoF; 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. (461 aa)
nuoENADH-ubiquinone oxidoreductase subunit E NuoE. (180 aa)
nuoBNADH-ubiquinone oxidoreductase subunit B NuoB; 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. (224 aa)
nuoANADH-ubiquinone oxidoreductase subunit A NuoA; 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; Belongs to the complex I subunit 3 family. (134 aa)
SO_1248Peptidase U32 family YhbV. (289 aa)
SO_1251Ferredoxin 4Fe-4S. (83 aa)
SO_12922-amino-4-hydroxy-6- hydroxymethyldihydropteridine pyrophosphokinase FolK-like protein. (167 aa)
sdhCSuccinate dehydrogenase cytochrome b556 subunit SdhC. (131 aa)
sdhASuccinate dehydrogenase flavoprotein subunit SdhA; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (588 aa)
sdhBSuccinate dehydrogenase iron-sulfur protein SdhB; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (235 aa)
ccoPCbb3-type cytochrome c oxidase subunit III CcoP; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (322 aa)
ccoOCbb3-type cytochrome c oxidase subunit II CcoO. (208 aa)
ccoNCbb3-type cytochrome c oxidase subunit I CcoN; Belongs to the heme-copper respiratory oxidase family. (478 aa)
SO_2930Bifunctional pectinolytic enzyme/cytochrome c. (907 aa)
SO_2931Cytochrome c lipoprotein. (390 aa)
SO_3301Flavocytochrome c flavin subunit; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (499 aa)
SO_4142Periplasmic monoheme cytochrome c. (109 aa)
shpMonoheme cytochrome c Shp. (144 aa)
coxBAa3-type cytochrome c oxidase subunit II CoxB; 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). (513 aa)
coxAAa3 type cytochrome c oxidase subunit I CoxA; 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. (530 aa)
urdAFAD-dependent oxidoreductase; Catalyzes the two-electron reduction of urocanate to dihydrourocanate (also named imidazole propionate or deamino- histidine). The physiological electron donor is unknown; it might be the membrane-bound tetraheme cytochrome c (CymA). Enables anaerobic growth with urocanate as a sole terminal electron acceptor, and thus can provide the cells with a niche where no other bacteria can compete and survive. Is unable to reduce cinnamate and other unsaturated organic acids such as acrylic, crotonic, fumaric and orotic acids. Has no fumarate reductase or succinate [...] (582 aa)
Your Current Organism:
Shewanella oneidensis
NCBI taxonomy Id: 211586
Other names: S. oneidensis MR-1, Shewanella oneidensis ATCC 700550, Shewanella oneidensis MR-1, Shewanella oneidensis str. MR-1, Shewanella oneidensis strain MR-1, Shewanella sp. MR-1
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