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ndhC ndhC nuoB nuoB nqo5 nqo5 nuoD nuoD nqo2 nqo2 nqo1 nqo1 nqo3 nqo3 nuoH nuoH nuoI nuoI nuoJ nuoJ nuoK nuoK nuoL nuoL nuoM_2 nuoM_2 nuoN nuoN petA_1 petA_1 BVIR_2028 BVIR_2028 petC petC petB petB petA petA BVIR_2691 BVIR_2691 BVIR_2692 BVIR_2692 ptrA ptrA hoxF hoxF rmlD rmlD cycA cycA
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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:
ndhCNAD(P)H-quinone oxidoreductase subunit 3; 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)
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. (192 aa)
nqo5NADH-quinone oxidoreductase subunit C 1; 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. (212 aa)
nuoDNADH-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. (397 aa)
nqo2NADH-quinone oxidoreductase chain 2. (258 aa)
nqo1NADH-quinone oxidoreductase chain 1; 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. (435 aa)
nqo3NADH-quinone oxidoreductase chain 3; 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)
nuoHNADH-quinone oxidoreductase subunit H; 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. (348 aa)
nuoINADH-quinone oxidoreductase subunit I; 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. (162 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. (203 aa)
nuoKNADH-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. (659 aa)
nuoM_2NADH-quinone oxidoreductase subunit M. (503 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. (484 aa)
petA_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. (183 aa)
BVIR_2028Hydrogen cyanide synthase subunit HcnA. (98 aa)
petCCytochrome b/c1; 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. c1 functions as an electron donor to cytochrome c. (282 aa)
petBCytochrome b/c1; 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. (419 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; Belongs to the Rieske iron-sulfur protein family. (179 aa)
BVIR_2691Peptidase M16 inactive domain protein. (451 aa)
BVIR_2692Peptidase M16 inactive domain protein; Belongs to the peptidase M16 family. (448 aa)
ptrAProtease 3 precursor; Belongs to the peptidase M16 family. (423 aa)
hoxFNAD-reducing hydrogenase HoxS subunit alpha. (566 aa)
rmlDdTDP-4-dehydrorhamnose reductase. (317 aa)
cycACytochrome c2 precursor; Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria. (127 aa)
Your Current Organism:
Blastochloris viridis
NCBI taxonomy Id: 1079
Other names: ATCC 19567, B. viridis, CCUG 30818, CCUG 7830, DSM 133, LMG 4321, LMG:4321, NBRC 102659, Rhodopseudomonas viridis, strain G. Drews F
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