STRINGSTRING
nuoK nuoK nuoL nuoL nuoM nuoM nuoN nuoN kefF kefF ACD09684.1 ACD09684.1 kefG kefG hycE hycE ACD09103.1 ACD09103.1 ACD10019.1 ACD10019.1 nuoA nuoA nuoB nuoB nuoC nuoC nuoF nuoF nuoG nuoG nuoI nuoI nuoJ nuoJ
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
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:
nuoKNADH-quinone oxidoreductase, K 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; Belongs to the complex I subunit 4L family. (100 aa)
nuoLNADH-quinone oxidoreductase, L subunit; Identified by match to protein family HMM PF00361; match to protein family HMM PF00662; match to protein family HMM TIGR01974. (613 aa)
nuoMNADH-quinone oxidoreductase, M subunit; Identified by match to protein family HMM PF00361; match to protein family HMM TIGR01972. (509 aa)
nuoNNADH-quinone oxidoreductase, N 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; Belongs to the complex I subunit 2 family. (485 aa)
kefFGlutathione-regulated potassium-efflux system ancillary protein kefF; Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefC. Shows redox enzymatic activity, but this enzymatic activity is not required for activation of KefC; Belongs to the NAD(P)H dehydrogenase (quinone) family. KefF subfamily. (176 aa)
ACD09684.1NADPH-dependent FMN reductase; Identified by match to protein family HMM PF03358. (188 aa)
kefGGlutathione-regulated potassium-efflux system ancillary protein kefG; Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefB. (184 aa)
hycEFormate hydrogenlyase, subunit E; Identified by match to protein family HMM PF00329; match to protein family HMM PF00346. (569 aa)
ACD09103.1Hydrogenase-4, I subunit; Identified by match to protein family HMM PF01058. (252 aa)
ACD10019.1Hydrogenase-4, G subunit; Identified by match to protein family HMM PF00329; match to protein family HMM PF00346. (571 aa)
nuoANADH-quinone oxidoreductase, A 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; Belongs to the complex I subunit 3 family. (147 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. (220 aa)
nuoCNADH-quinone oxidoreductase, C/D 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; In the N-terminal section; belongs to the complex I 30 kDa subunit family. (600 aa)
nuoFNADH-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. (445 aa)
nuoGNADH-quinone oxidoreductase, G subunit; 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. (908 aa)
nuoINADH-quinone oxidoreductase, I 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. (180 aa)
nuoJNADH-quinone oxidoreductase, J subunit; 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. (184 aa)
Your Current Organism:
Shigella boydii
NCBI taxonomy Id: 344609
Other names: S. boydii CDC 3083-94, Shigella boydii BS512, Shigella boydii CDC 3083-94, Shigella boydii str. CDC 3083-94, Shigella boydii strain CDC 3083-94
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