STRINGSTRING
ctaD2 ctaD2 cydB cydB cydA cydA AFL49012.1 AFL49012.1 AFL49013.1 AFL49013.1 ctaC1 ctaC1 ctaD1 ctaD1 ctaE ctaE AFL49299.1 AFL49299.1 cycG cycG mrpD1 mrpD1 AFL49359.1 AFL49359.1 yoaE1 yoaE1 AFL49577.1 AFL49577.1 AFL49895.1 AFL49895.1 cyoA cyoA cyoB cyoB cyoC cyoC cyoD cyoD AFL50202.1 AFL50202.1 AFL50346.1 AFL50346.1 etfA1 etfA1 AFL50567.1 AFL50567.1 AFL50571.1 AFL50571.1 AFL50837.1 AFL50837.1 bcp1 bcp1 azoR9 azoR9 AFL51168.1 AFL51168.1 pazS pazS etfB1 etfB1 etfA2 etfA2 fdxB1 fdxB1 AFL51277.1 AFL51277.1 petA1 petA1 cycA cycA cycB1 cycB1 AFL51671.1 AFL51671.1 nuoD1 nuoD1 nuoE1 nuoE1 nuoF1 nuoF1 nuoG1 nuoG1 nuoJ nuoJ nuoK1 nuoK1 nuoL nuoL nuoM1 nuoM1 nuoN1 nuoN1 azoR azoR yedZ yedZ AFL52007.1 AFL52007.1 AFL52032.1 AFL52032.1 AFL52184.1 AFL52184.1 AFL52189.1 AFL52189.1 norE norE norC norC norB norB AFL52395.1 AFL52395.1 bcp3 bcp3 napA napA fixN1 fixN1 fixO2 fixO2 fixP fixP nosZ nosZ AFL52481.1 AFL52481.1 fdxB2 fdxB2 fbcH fbcH petB petB petA2 petA2 AFL52726.1 AFL52726.1 AFL52791.1 AFL52791.1 AFL52850.1 AFL52850.1 AFL52929.1 AFL52929.1 nuoG2 nuoG2 nuoF2 nuoF2 nuoE2 nuoE2 nuoD2 nuoD2 nuoC nuoC nuoB nuoB nuoA nuoA nuoN2 nuoN2 nuoM2 nuoM2 mrpD2 mrpD2 nuoN3 nuoN3 nuoK2 nuoK2 AFL53147.1 AFL53147.1 AFL53287.1 AFL53287.1 mauG mauG AFL53510.1 AFL53510.1 coxM coxM coxN coxN coxO coxO coxP coxP etfB2 etfB2 etfA3 etfA3 AFL53671.1 AFL53671.1 cyc cyc ctaC2 ctaC2 AFL53684.1 AFL53684.1 phaD phaD cycB2 cycB2 AFL54005.1 AFL54005.1 yrhE yrhE nuoF3 nuoF3 fdsG fdsG sdhB sdhB sdhA sdhA AFL54102.1 AFL54102.1 AFL54171.1 AFL54171.1 fixN2 fixN2 AFL54177.1 AFL54177.1 AFL54179.1 AFL54179.1 AFL54183.1 AFL54183.1 fdxA fdxA cycM cycM AFL54622.1 AFL54622.1
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:
ctaD2Cytochrome c oxidase subunit 1; Belongs to the heme-copper respiratory oxidase family. (838 aa)
cydBCytochrome d ubiquinol oxidase subunit 2. (334 aa)
cydACytochrome d ubiquinol oxidase subunit 1. (471 aa)
AFL49012.1Hypothetical protein. (177 aa)
AFL49013.1Hypothetical protein. (79 aa)
ctaC1Cytochrome 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). (294 aa)
ctaD1Cytochrome 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. (562 aa)
ctaECytochrome c oxidase subunit 3. (292 aa)
AFL49299.1Cytochrome c-556. (148 aa)
cycGDiheme cytochrome c-type. (304 aa)
mrpD1Na(+)/H(+) antiporter subunit D. (645 aa)
AFL49359.1Electron transfer flavoprotein-ubiquinone oxidoreductase; Accepts electrons from ETF and reduces ubiquinone. (554 aa)
yoaE1Putative oxidoreductase YoaE; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (711 aa)
AFL49577.1Hypothetical protein. (412 aa)
AFL49895.1Nutrient deprivation-induced protein. (322 aa)
cyoAUbiquinol oxidase subunit 2. (388 aa)
cyoBUbiquinol oxidase subunit 1; Belongs to the heme-copper respiratory oxidase family. (670 aa)
cyoCCytochrome o ubiquinol oxidase subunit 3. (209 aa)
cyoDCytochrome o ubiquinol oxidase protein CyoD. (133 aa)
AFL50202.1Putative amicyanin protein. (105 aa)
AFL50346.1Electron transfer flavoprotein-ubiquinone oxidoreductase; Accepts electrons from ETF and reduces ubiquinone. (554 aa)
etfA1Electron transfer flavoprotein subunit alpha. (217 aa)
AFL50567.1Hypothetical protein. (201 aa)
AFL50571.1Hypothetical protein. (77 aa)
AFL50837.1Hypothetical protein. (347 aa)
bcp1Pseudoazurin. (165 aa)
azoR9FMN-dependent NADH-azoreductase 9; 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)
AFL51168.1Cytochrome c550. (228 aa)
pazSPseudoazurin. (144 aa)
etfB1Electron transfer flavoprotein subunit beta. (249 aa)
etfA2Electron transfer flavoprotein subunit alpha. (313 aa)
fdxB12Fe-2S ferredoxin. (106 aa)
AFL51277.1Cytochrome c, class I. (157 aa)
petA1Ubiquinol-cytochrome c reductase iron-sulfur subunit PetA; 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. (187 aa)
cycACytochrome c2. (137 aa)
cycB1Cytochrome c-553I. (178 aa)
AFL51671.1Hypothetical protein. (147 aa)
nuoD1NADH-quinone oxidoreductase 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 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 49 kDa subunit family. (396 aa)
nuoE1NADH-quinone oxidoreductase subunit E. (281 aa)
nuoF1NADH-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. (434 aa)
nuoG1NADH-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. (692 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. (239 aa)
nuoK1NADH-quinone oxidoreductase 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 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)
nuoLNADH-quinone oxidoreductase subunit L. (664 aa)
nuoM1NADH-quinone oxidoreductase subunit M. (503 aa)
nuoN1NADH-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 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 2 family. (482 aa)
azoRFMN-dependent NADH-azoreductase AzoR; 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. (206 aa)
yedZSulfoxide 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 [...] (220 aa)
AFL52007.1Transglutaminase-like cysteine peptidase, BTLCP. (201 aa)
AFL52032.1Cytochrome b561. (206 aa)
AFL52184.1Putative copper oxidase, possibly exported. (159 aa)
AFL52189.1Hypothetical protein. (188 aa)
norECytochrome c oxidase subunit III-like protein NorE. (183 aa)
norCNitric oxide reductase subunit C. (150 aa)
norBNitric oxide reductase subunit B; Belongs to the heme-copper respiratory oxidase family. (448 aa)
AFL52395.1Hypothetical protein. (452 aa)
bcp3Pseudoazurin. (147 aa)
napAPeriplasmic nitrate reductase NapA; Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite. (834 aa)
fixN1Cytochrome c oxidase subunit 1; Belongs to the heme-copper respiratory oxidase family. (539 aa)
fixO2Cytochrome-c oxidase FixO2. (243 aa)
fixPCbb3-type cytochrome c oxidase subunit FixP; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (287 aa)
nosZNitrous-oxide reductase NosZ; Nitrous-oxide reductase is part of a bacterial respiratory system which is activated under anaerobic conditions in the presence of nitrate or nitrous oxide; In the C-terminal section; belongs to the cytochrome c oxidase subunit 2 family. (639 aa)
AFL52481.1Hypothetical protein. (107 aa)
fdxB22Fe-2S ferredoxin. (106 aa)
fbcHCytochrome b/c1. (292 aa)
petBCytochrome 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. (426 aa)
petA2Ubiquinol-cytochrome c reductase iron-sulfur subunit PetA; 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. (192 aa)
AFL52726.1Hypothetical protein. (236 aa)
AFL52791.1Hypothetical protein. (233 aa)
AFL52850.1Hypothetical protein. (163 aa)
AFL52929.1Transglutaminase-like cysteine peptidase, BTLCP. (187 aa)
nuoG2NADH-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. (858 aa)
nuoF2NADH-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. (421 aa)
nuoE2NADH-quinone oxidoreductase subunit E. (170 aa)
nuoD2NADH-quinone oxidoreductase 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 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 49 kDa subunit family. (404 aa)
nuoCNADH-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 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 30 kDa subunit family. (187 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 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. (167 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 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. (121 aa)
nuoN2NADH-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 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 2 family. (479 aa)
nuoM2NADH-quinone oxidoreductase subunit M. (491 aa)
mrpD2Na(+)/H(+) antiporter subunit D. (587 aa)
nuoN3NADH-quinone oxidoreductase subunit N. (326 aa)
nuoK2NADH-quinone oxidoreductase 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 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. (100 aa)
AFL53147.1Putative NADH-ubiquinone oxidoreductase protein, chain 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. (166 aa)
AFL53287.1Hypothetical protein. (410 aa)
mauGPutative methylamine utilization protein MauG. (365 aa)
AFL53510.1Cytochrome c2. (128 aa)
coxMAlternative cytochrome c oxidase subunit 2. (280 aa)
coxNAlternative cytochrome 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. (593 aa)
coxOCytochrome c oxidase, subunit III. (232 aa)
coxPCytochrome c oxidase, subunit III. (240 aa)
etfB2Electron transfer flavoprotein subunit beta. (249 aa)
etfA3Electron transfer flavoprotein subunit alpha. (313 aa)
AFL53671.1Hypothetical protein. (175 aa)
cycCytochrome c-552. (375 aa)
ctaC2Cytochrome c oxidase subunit 2. (328 aa)
AFL53684.1Gluconate 2-dehydrogenase cytochrome c subunit. (462 aa)
phaDPutative K(+)/H(+) antiporter subunit D. (539 aa)
cycB2Cytochrome c-553I. (173 aa)
AFL54005.1Hypothetical protein. (201 aa)
yrhEPutative formate dehydrogenase YrhE. (959 aa)
nuoF3NADH-quinone oxidoreductase subunit F. (518 aa)
fdsGPutative NAD-dependent formate dehydrogenase gamma subunit FdsG. (159 aa)
sdhBSuccinate dehydrogenase iron-sulfur subunit SdhB; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (259 aa)
sdhASuccinate dehydrogenase flavoprotein subunit SdhA; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (613 aa)
AFL54102.1Putative succinate dehydrogenase membrane anchor subunit. (130 aa)
AFL54171.1Cytochrome C oxidase mono-heme subunit/FixO. (554 aa)
fixN2Cytochrome c oxidase subunit 1. (485 aa)
AFL54177.1Putative lipoprotein. (249 aa)
AFL54179.1Hypothetical protein. (156 aa)
AFL54183.1Cytochrome c553. (123 aa)
fdxAFerredoxin-2; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (112 aa)
cycMCytochrome c. (213 aa)
AFL54622.1Putative transglutaminase family protein cysteine peptidase, BTLCP. (172 aa)
Your Current Organism:
Sinorhizobium fredii USDA257
NCBI taxonomy Id: 1185652
Other names: S. fredii USDA 257, Sinorhizobium fredii USDA 257, Sinorhizobium fredii str. USDA 257, Sinorhizobium fredii strain USDA 257
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