STRINGSTRING
SACE_0290 SACE_0290 SACE_0950 SACE_0950 SACE_1089 SACE_1089 SACE_1090 SACE_1090 acpM acpM SACE_1682 SACE_1682 SACE_1770 SACE_1770 SACE_2093 SACE_2093 SACE_2404 SACE_2404 SACE_2433 SACE_2433 SACE_2470 SACE_2470 SACE_2766 SACE_2766 SACE_2774 SACE_2774 SACE_2775 SACE_2775 SACE_3083 SACE_3083 acpP acpP SACE_4170 SACE_4170 acpP-2 acpP-2 pepR pepR nuoN nuoN nuoM nuoM nuoL nuoL nuoK nuoK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF nuoE nuoE nuoD nuoD nuoC nuoC nuoB nuoB nuoA nuoA SACE_6903 SACE_6903
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:
SACE_0290Alpha/beta hydrolase fold-3. (358 aa)
SACE_0950Lipase. (314 aa)
SACE_1089Peptidase M16-like. (440 aa)
SACE_1090Peptidase M16-like. (455 aa)
acpMAcyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis. (79 aa)
SACE_1682Putative two-component system response regulator. (136 aa)
SACE_1770Membrane protein. (99 aa)
SACE_2093Putative lysophospholipase. (299 aa)
SACE_2404Phosphopantetheine-binding. (84 aa)
SACE_2433NADH-quinone oxidoreductase chain F. (559 aa)
SACE_2470Iron sulphur binding protein. (142 aa)
SACE_2766NAD-dependent epimerase/dehydratase. (293 aa)
SACE_2774Alpha/beta hydrolase domain protein. (127 aa)
SACE_2775Alpha/beta hydrolase domain protein. (165 aa)
SACE_3083NmrA family protein. (272 aa)
acpPAcyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family. (95 aa)
SACE_4170Iron-sulfur binding oxidoreductase. (500 aa)
acpP-2Probable acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family. (79 aa)
pepRPutative zinc protease; Belongs to the peptidase M16 family. (449 aa)
nuoNNADH dehydrogenase I chain 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 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 2 family. (515 aa)
nuoMNADH dehydrogenase I chain M. (525 aa)
nuoLNADH dehydrogenase I chain L. (668 aa)
nuoKNADH dehydrogenase I chain 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. (99 aa)
nuoJNADH dehydrogenase I chain 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. (329 aa)
nuoINADH dehydrogenase (quinone); 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. (188 aa)
nuoHNADH dehydrogenase I chain 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. (441 aa)
nuoGNADH dehydrogenase I chain G; 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. (837 aa)
nuoFNADH dehydrogenase I chain 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. (431 aa)
nuoEPutative NADH dehydrogenase chain E. (241 aa)
nuoDNADH dehydrogenase I chain 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 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 49 kDa subunit family. (449 aa)
nuoCPutative NADH dehydrogenase chain C; 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 30 kDa subunit family. (249 aa)
nuoBNADH dehydrogenase I chain 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. (220 aa)
nuoANADH dehydrogenase I chain A; 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 3 family. (126 aa)
SACE_6903Electron transfer oxidoreductase. (432 aa)
Your Current Organism:
Saccharopolyspora erythraea
NCBI taxonomy Id: 405948
Other names: S. erythraea NRRL 2338, Saccharopolyspora erythraea ATCC 11635, Saccharopolyspora erythraea DSM 40517, Saccharopolyspora erythraea JCM 4748, Saccharopolyspora erythraea NRRL 2338, Saccharopolyspora erythraea str. NRRL 2338, Saccharopolyspora erythraea strain NRRL 2338
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