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D521_0029 D521_0029 D521_0033 D521_0033 D521_0081 D521_0081 D521_0084 D521_0084 D521_0121 D521_0121 D521_0122 D521_0122 D521_0123 D521_0123 D521_0241 D521_0241 D521_0304 D521_0304 D521_0361 D521_0361 msrQ msrQ D521_0590 D521_0590 D521_0675 D521_0675 D521_0678 D521_0678 D521_0707 D521_0707 D521_0708 D521_0708 D521_0709 D521_0709 nuoA nuoA nuoB nuoB nuoC nuoC nuoD nuoD D521_0750 D521_0750 D521_0751 D521_0751 D521_0752 D521_0752 D521_0755 D521_0755 nuoK nuoK D521_0757 D521_0757 D521_0758 D521_0758 nuoN nuoN D521_0825 D521_0825 D521_0830 D521_0830 D521_0903 D521_0903 D521_0904 D521_0904 D521_0976 D521_0976 D521_0980 D521_0980 D521_0981 D521_0981 D521_0984 D521_0984 D521_0989 D521_0989 D521_1009 D521_1009 D521_1010 D521_1010 D521_1012 D521_1012 D521_1124 D521_1124 D521_1161 D521_1161 D521_1163 D521_1163 D521_1186 D521_1186 D521_1189 D521_1189 D521_1339 D521_1339 frdB frdB D521_1346 D521_1346 D521_1356 D521_1356 D521_1444 D521_1444 D521_1463 D521_1463 D521_1508 D521_1508 D521_1509 D521_1509 D521_1525 D521_1525 D521_1527 D521_1527 D521_1528 D521_1528 D521_1580 D521_1580 D521_1581 D521_1581 D521_1601 D521_1601 D521_1602 D521_1602 D521_1660 D521_1660 D521_1763 D521_1763 D521_1933 D521_1933 D521_1937 D521_1937 D521_1938 D521_1938 D521_1990 D521_1990 D521_2066 D521_2066
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:
D521_0029Cytochrome c, class I. (61 aa)
D521_0033Cytochrome c, class I. (114 aa)
D521_0081Protein-disulfide reductase. (557 aa)
D521_0084Cytochrome c class I. (240 aa)
D521_0121Ubiquinol-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. (200 aa)
D521_0122Cytochrome b/b6 domain-containing protein; 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. (466 aa)
D521_0123Cytochrome c1. (257 aa)
D521_0241Rubredoxin-type Fe(Cys)4 protein. (50 aa)
D521_0304High 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. (102 aa)
D521_0361FMN-binding domain protein. (184 aa)
msrQFerric reductase domain-containing protein; 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 catalytic s [...] (195 aa)
D521_0590Hypothetical protein. (109 aa)
D521_0675Monoheme cytochrome SoxX (Sulfur oxidation). (144 aa)
D521_0678Diheme cytochrome SoxA (Sulfur oxidation). (261 aa)
D521_0707Hypothetical protein. (127 aa)
D521_0708Diheme cytochrome c. (129 aa)
D521_0709Cytochrome B561. (224 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. (119 aa)
nuoBNADH-quinone oxidoreductase, B subunit; 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. (160 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. (199 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. (417 aa)
D521_0750NADH-quinone oxidoreductase, E subunit. (168 aa)
D521_0751NADH-quinone oxidoreductase, F subunit; 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. (432 aa)
D521_0752NADH-quinone oxidoreductase, chain 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. (771 aa)
D521_0755NADH-ubiquinone/plastoquinone oxidoreductase, chain 6; 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. (215 aa)
nuoKNADH-ubiquinone oxidoreductase, chain 4L; 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)
D521_0757Proton-translocating NADH-quinone oxidoreductase, chain L. (686 aa)
D521_0758Proton-translocating NADH-quinone oxidoreductase, chain M. (488 aa)
nuoNNADH-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. (480 aa)
D521_0825Flavoprotein WrbA; Belongs to the WrbA family. (198 aa)
D521_0830Electron-transferring-flavoprotein dehydrogenase; Accepts electrons from ETF and reduces ubiquinone. (556 aa)
D521_0903Putative periplasmic cytochrome type-c oxidoreductase signal peptide protein. (124 aa)
D521_0904Cytochrome c class I. (114 aa)
D521_0976Hypothetical protein. (85 aa)
D521_0980Hypothetical protein. (212 aa)
D521_0981Hypothetical protein. (271 aa)
D521_0984Cytochrome c, class I. (359 aa)
D521_0989High 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. (102 aa)
D521_1009Succinate dehydrogenase and fumarate reductase iron-sulfur protein. (234 aa)
D521_1010Succinate dehydrogenase, flavoprotein subunit; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (592 aa)
D521_1012Succinate dehydrogenase, cytochrome b556 subunit. (139 aa)
D521_1124Putative cytochrome c5. (130 aa)
D521_1161Rubredoxin-type Fe(Cys)4 protein. (55 aa)
D521_1163Hypothetical protein. (197 aa)
D521_1186Formate dehydrogenase, gamma subunit. (351 aa)
D521_1189Molybdopterin oxidoreductase; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (994 aa)
D521_1339Putative fumarate reductase. (119 aa)
frdBSuccinate dehydrogenase and fumarate reductase iron-sulfur protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (243 aa)
D521_1346Ferredoxin, 2Fe-2S type, ISC system. (112 aa)
D521_1356Electron transport complex, RnfABCDGE type, B subunit; 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. (230 aa)
D521_14444Fe-4S ferredoxin iron-sulfur binding domain protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (116 aa)
D521_1463Electron transfer flavoprotein beta-subunit. (190 aa)
D521_1508Cytochrome c prime. (149 aa)
D521_1509Cytochrome B561. (227 aa)
D521_1525Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (307 aa)
D521_1527Cytochrome c oxidase, cbb3-type, subunit II. (216 aa)
D521_1528Cytochrome c oxidase, cbb3-type, subunit I; Belongs to the heme-copper respiratory oxidase family. (480 aa)
D521_1580Electron transfer flavoprotein, alpha subunit. (310 aa)
D521_1581Electron transfer flavoprotein beta-subunit. (249 aa)
D521_1601Electron transfer flavoprotein, alpha subunit; Belongs to the CoA-transferase III family. (478 aa)
D521_1602Electron transfer flavoprotein beta-subunit. (249 aa)
D521_1660Blue (Type 1) copper domain protein. (271 aa)
D521_1763D-lactate dehydrogenase (Cytochrome). (501 aa)
D521_1933Cytochrome c oxidase subunit III. (284 aa)
D521_1937Cytochrome 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. (539 aa)
D521_1938Cytochrome c oxidase, subunit II; 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). (385 aa)
D521_1990Putative flavodoxin. (185 aa)
D521_2066Hypothetical protein. (95 aa)
Your Current Organism:
beta proteobacterium CB
NCBI taxonomy Id: 543913
Other names: b. proteobacterium CB
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