STRINGSTRING
SU9_15392 SU9_15392 sdhB sdhB SU9_01405 SU9_01405 nuoI-2 nuoI-2 SU9_32253 SU9_32253 SU9_08644 SU9_08644 nuoI nuoI
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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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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
SU9_15392Hypothetical protein; COG0247 Fe-S oxidoreductase. (755 aa)
sdhBCOG0479 Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (257 aa)
SU9_01405Iron-sulfur protein; COG1139 Uncharacterized conserved protein containing a ferredoxin-like domain. (496 aa)
nuoI-2NADH dehydrogenase subunit NuoI2; 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. (196 aa)
SU9_32253COG1146 Ferredoxin. (75 aa)
SU9_08644Ferredoxin; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (106 aa)
nuoINADH dehydrogenase 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. (194 aa)
Your Current Organism:
Streptomyces auratus
NCBI taxonomy Id: 1160718
Other names: S. auratus AGR0001, Streptomyces auratus AGR0001, Streptomyces auratus str. AGR0001, Streptomyces auratus strain AGR0001
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