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nuoI2 nuoI2 nuoE1 nuoE1 nuoB1 nuoB1 nuoF1 nuoF1 nuoI1 nuoI1 nuoK1 nuoK1 STH2637 STH2637 STH2640 STH2640 nuoM2 nuoM2 nuoK2 nuoK2 nuoB2 nuoB2 STH2945 STH2945 STH3103 STH3103 STH3147 STH3147 STH3148 STH3148 STH3152 STH3152 STH3153 STH3153 STH3167 STH3167 STH3174 STH3174 STH3176 STH3176 STH3186 STH3186 STH3207 STH3207 STH3209 STH3209 STH3293 STH3293 STH934 STH934
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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:
nuoI2NADH dehydrogenase I 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. (240 aa)
nuoE1NADH dehydrogenase I subunit E. (274 aa)
nuoB1NADH dehydrogenase I 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 a menaquinone. 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. (153 aa)
nuoF1NADH dehydrogenase I 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. (425 aa)
nuoI1NADH dehydrogenase I 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)
nuoK1NADH dehydrogenase I 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 a menaquinone. 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)
STH2637Succinate dehydrogenase membrane subunit. (140 aa)
STH2640Succinate dehydrogenase iron-sulfur protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (243 aa)
nuoM2NADH dehydrogenase I subunit M. (508 aa)
nuoK2NADH dehydrogenase I 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 a menaquinone. 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. (107 aa)
nuoB2NADH dehydrogenase I 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 a menaquinone. 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. (182 aa)
STH2945Conserved hypothetical protein. (439 aa)
STH3103NADH dehydrogenase subunit. (394 aa)
STH3147Putative menaquinol-cytochrome C reductase. (253 aa)
STH3148Menaquinol-cytochrome C reductase. (258 aa)
STH3152Cytochrome C oxidase mono-heme subunit. (320 aa)
STH3153Cytochrome C oxidase heme b and copper-binding subunit. (467 aa)
STH3167Pyruvate flavodoxin dehydrogenase. (1183 aa)
STH3174Succinate dehydrogenase iron-sulfur protein. (251 aa)
STH3176Succinate dehydrogenase cytochrome b558 subunit. (211 aa)
STH31862-amino-4-hydroxy-6- hydroxymethyldihydropteridine pyrophosphokinase. (175 aa)
STH3207Putative iron hydrogenase small subunit gamma. (186 aa)
STH3209Iron hydrogenase. (596 aa)
STH3293Iron hydrogenase. (456 aa)
STH934Ferredoxin. (96 aa)
Your Current Organism:
Symbiobacterium thermophilum
NCBI taxonomy Id: 292459
Other names: S. thermophilum IAM 14863, Symbiobacterium thermophilum IAM 14863, Symbiobacterium thermophilum str. IAM 14863, Symbiobacterium thermophilum strain IAM 14863
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