STRINGSTRING
nuoF nuoF nuoE nuoE nuoB nuoB folK folK CBG73053.1 CBG73053.1 nuoG nuoG nuoI nuoI nuoM nuoM nuoB2 nuoB2 nuoI2 nuoI2 CBG70618.1 CBG70618.1 CBG70261.1 CBG70261.1 CBG68821.1 CBG68821.1 CBG68314.1 CBG68314.1
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:
nuoFNuoF, NADH dehydrogenase 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. (452 aa)
nuoENuoE, NADH dehydrogenase subunit. (287 aa)
nuoBNuoB, NADH dehydrogenase 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 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. (184 aa)
folKPutative2-amino-4-hydroxy-6-hydroxymethyldihydr op teridinediphosphokinase. (203 aa)
CBG73053.1Putative oxidoreductase. (537 aa)
nuoGNuoG, NADH dehydrogenase 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. (834 aa)
nuoINuoI, NADH dehydrogenase 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. (213 aa)
nuoMNuoM, NADH dehydrogenase subunit. (523 aa)
nuoB2NADH dehydrogenase subunit NuoB2; 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. (226 aa)
nuoI2NADH 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. (192 aa)
CBG70618.1Putative succinate dehydrogenase membrane subunit. (110 aa)
CBG70261.1Putative succinate dehydrogenase iron-sulfur subunit. (258 aa)
CBG68821.1Putative respiratory chain oxidoreductase; TTA-Leu codon(s) 59 may indicate regulation by BldA. (610 aa)
CBG68314.1Putative reductase iron-sulfur protein. (249 aa)
Your Current Organism:
Streptomyces scabiei
NCBI taxonomy Id: 680198
Other names: S. scabiei 87.22, Streptomyces scabiei 87.22, Streptomyces scabiei str. 87.22, Streptomyces scabiei strain 87.22
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