STRINGSTRING
SoxA SoxA SoxX SoxX SDW83969.1 SDW83969.1 SDW81667.1 SDW81667.1 SDW78210.1 SDW78210.1 CoxB-2 CoxB-2 SDX60052.1 SDX60052.1 nuoN-2 nuoN-2 SDX60504.1 SDX60504.1 SDX60534.1 SDX60534.1 nuoK-2 nuoK-2 SDX60607.1 SDX60607.1 SDX60717.1 SDX60717.1 SDX56934.1 SDX56934.1 SDX56174.1 SDX56174.1 SDX59288.1 SDX59288.1 SDX70306.1 SDX70306.1 SDW74238.1 SDW74238.1 SDW56326.1 SDW56326.1 SDW36926.1 SDW36926.1 SDW49663.1 SDW49663.1 SDX76284.1 SDX76284.1 SDX72721.1 SDX72721.1 SDW07306.1 SDW07306.1 CtaD CtaD SDW09499.1 SDW09499.1 SDW00765.1 SDW00765.1 SDW17480.1 SDW17480.1 SDW21288.1 SDW21288.1 CydB CydB SDW23409.1 SDW23409.1 nuoN nuoN SDW01916.1 SDW01916.1 NuoL NuoL nuoK nuoK SDW01996.1 SDW01996.1 nuoA nuoA nuoB nuoB nuoC nuoC nuoD nuoD NuoF NuoF SDX59956.1 SDX59956.1 SDX59926.1 SDX59926.1 SDX51919.1 SDX51919.1 azoR azoR SDX49460.1 SDX49460.1 SDX49432.1 SDX49432.1 SDX44878.1 SDX44878.1 SDX43914.1 SDX43914.1 SDX46993.1 SDX46993.1 SDW02140.1 SDW02140.1 CtaD-2 CtaD-2 SDX46759.1 SDX46759.1 CcoP CcoP CcoO CcoO CcoN CcoN SDX39637.1 SDX39637.1 SDX20777.1 SDX20777.1 SDX19531.1 SDX19531.1 SDX27802.1 SDX27802.1 SDX27440.1 SDX27440.1 FdhF FdhF msrQ msrQ CoxB CoxB SDW97900.1 SDW97900.1 SDX71845.1 SDX71845.1 SDX59989.1 SDX59989.1 PetA PetA SDX11284.1 SDX11284.1 SDX11251.1 SDX11251.1 SDX03109.1 SDX03109.1 SDW96133.1 SDW96133.1 SdhC SdhC SDX01557.1 SDX01557.1 SDX01433.1 SDX01433.1 TcuA TcuA SDW73282.1 SDW73282.1
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
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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:
SoxADiheme cytochrome SoxA (sulfur oxidation). (284 aa)
SoxXMonoheme cytochrome SoxX (sulfur oxidation). (158 aa)
SDW83969.1Cytochrome c. (143 aa)
SDW81667.1Cytochrome b561. (169 aa)
SDW78210.1Cytochrome b561. (180 aa)
CoxB-2Cytochrome c oxidase subunit 2. (328 aa)
SDX60052.1Cytochrome C oxidase, cbb3-type, subunit III. (164 aa)
nuoN-2NADH 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 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. (470 aa)
SDX60504.1NADH dehydrogenase subunit M. (495 aa)
SDX60534.1NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter, MnhA subunit. (636 aa)
nuoK-2NADH 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 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. (101 aa)
SDX60607.1NADH 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. (276 aa)
SDX60717.1NADH dehydrogenase subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (113 aa)
SDX56934.1Cytochrome C oxidase, cbb3-type, subunit III. (112 aa)
SDX56174.1Cytochrome c, mono-and diheme variants. (161 aa)
SDX59288.1Ubiquinol-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. (185 aa)
SDX70306.1Cytochrome c, mono-and diheme variants. (158 aa)
SDW74238.1Protein of unknown function. (407 aa)
SDW56326.1Cytochrome b561; Belongs to the UPF0312 family. (403 aa)
SDW36926.1Indolepyruvate ferredoxin oxidoreductase. (1138 aa)
SDW49663.1Multisubunit potassium/proton antiporter, PhaD subunit. (548 aa)
SDX76284.1Cytochrome c, mono-and diheme variants. (154 aa)
SDX72721.1Cytochrome b. (191 aa)
SDW07306.1Ferredoxin, 2Fe-2S. (107 aa)
CtaDCytochrome 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. (557 aa)
SDW09499.1Ferredoxin; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (112 aa)
SDW00765.1Indolepyruvate ferredoxin oxidoreductase. (1138 aa)
SDW17480.1Plastocyanin. (118 aa)
SDW21288.1Electron-transferring-flavoprotein dehydrogenase; Accepts electrons from ETF and reduces ubiquinone. (549 aa)
CydBCytochrome bd-I ubiquinol oxidase subunit 2 apoprotein. (335 aa)
SDW23409.1Cytochrome bd-I ubiquinol oxidase subunit 1 apoprotein. (471 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 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. (481 aa)
SDW01916.1NADH dehydrogenase subunit M. (518 aa)
NuoLNADH dehydrogenase subunit L. (703 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 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. (101 aa)
SDW01996.1NADH 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. (200 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 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. (117 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 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. (178 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 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. (201 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 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. (408 aa)
NuoFNADH 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. (431 aa)
SDX59956.1Cytochrome c556. (194 aa)
SDX59926.1Cytochrome c. (152 aa)
SDX51919.1Cytochrome c. (169 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)
SDX49460.1Electron transfer flavoprotein alpha subunit apoprotein. (308 aa)
SDX49432.1Electron transfer flavoprotein beta subunit. (252 aa)
SDX44878.1Cytochrome c. (146 aa)
SDX43914.1Fumarate reductase flavoprotein subunit. (455 aa)
SDX46993.1Cytochrome c553. (354 aa)
SDW02140.1NADH 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. (671 aa)
CtaD-2Cytochrome c oxidase subunit I+III; Belongs to the heme-copper respiratory oxidase family. (855 aa)
SDX46759.1Cytochrome c553. (248 aa)
CcoPCytochrome c oxidase cbb3-type subunit 3; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (301 aa)
CcoOCytochrome c oxidase cbb3-type subunit 2. (278 aa)
CcoNCytochrome c oxidase cbb3-type subunit 1; Belongs to the heme-copper respiratory oxidase family. (536 aa)
SDX39637.1Sulfite dehydrogenase (cytochrome) subunit SorB. (243 aa)
SDX20777.1Formate dehydrogenase gamma subunit. (400 aa)
SDX19531.1Uncharacterized membrane protein. (407 aa)
SDX27802.1Cytochrome c peroxidase. (449 aa)
SDX27440.1Cytochrome c. (160 aa)
FdhFFormate dehydrogenase major subunit; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (922 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 [...] (194 aa)
CoxBCytochrome 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). (298 aa)
SDW97900.1Cytochrome c oxidase subunit 3. (267 aa)
SDX71845.1Cytochrome c peroxidase. (626 aa)
SDX59989.1Cytochrome c, mono-and diheme variants. (296 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. (186 aa)
SDX11284.1Ubiquinol-cytochrome c reductase cytochrome b 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. (447 aa)
SDX11251.1Ubiquinol-cytochrome c reductase cytochrome c1 subunit. (280 aa)
SDX03109.1NADH dehydrogenase. (103 aa)
SDW96133.1Sulfoxide reductase heme-binding subunit YedZ. (200 aa)
SdhCSuccinate dehydrogenase subunit C. (127 aa)
SDX01557.1Succinate dehydrogenase subunit A; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (601 aa)
SDX01433.1Succinate dehydrogenase subunit B; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (259 aa)
TcuATricarballylate dehydrogenase. (461 aa)
SDW73282.1Sulfur dehydrogenase subunit SoxD. (341 aa)
Your Current Organism:
Sulfitobacter pontiacus
NCBI taxonomy Id: 60137
Other names: DSM 10014, JCM 21789, S. pontiacus, VKM B-2022, strain ChLG 10
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