STRINGSTRING
SU9_07785 SU9_07785 SU9_08809 SU9_08809 SU9_10249 SU9_10249 SU9_12372 SU9_12372 nuoB nuoB SU9_16367 SU9_16367 SU9_16372 SU9_16372 SU9_16377 SU9_16377 nuoI nuoI SU9_16407 SU9_16407 nuoB-2 nuoB-2 nuoI-2 nuoI-2 SU9_19280 SU9_19280 SU9_21925 SU9_21925 SU9_21930 SU9_21930 SU9_21940 SU9_21940 SU9_22845 SU9_22845 SU9_22850 SU9_22850 SU9_22855 SU9_22855 SU9_22885 SU9_22885 SU9_22890 SU9_22890 SU9_25024 SU9_25024 SU9_25814 SU9_25814 SU9_31266 SU9_31266 SU9_32228 SU9_32228 SU9_32948 SU9_32948
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:
SU9_07785Hypothetical protein. (88 aa)
SU9_08809COG0479 Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit. (265 aa)
SU9_10249COG2009 Succinate dehydrogenase/fumarate reductase, cytochrome b subunit. (126 aa)
SU9_123722-amino-4-hydroxy-6- hydroxymethyldihydropteridine pyrophosphokinase; COG0801 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase. (207 aa)
nuoBNADH dehydrogenase 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. (184 aa)
SU9_16367COG1905 NADH:ubiquinone oxidoreductase 24 kD subunit. (294 aa)
SU9_16372NADH-quinone oxidoreductase 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. (460 aa)
SU9_16377NADH dehydrogenase subunit 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. (853 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)
SU9_16407COG1008 NADH:ubiquinone oxidoreductase subunit 4 (chain M). (552 aa)
nuoB-2NADH 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. (214 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_19280Oxidoreductase; COG1894 NADH:ubiquinone oxidoreductase, NADH-binding (51 kD) subunit. (515 aa)
SU9_21925COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. (66 aa)
SU9_21930COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1; Belongs to the heme-copper respiratory oxidase family. (226 aa)
SU9_21940Hypothetical protein. (117 aa)
SU9_22845COG1622 Heme/copper-type cytochrome/quinol oxidases, subunit 2. (277 aa)
SU9_22850COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. (271 aa)
SU9_22855COG0843 Heme/copper-type cytochrome/quinol oxidases, subunit 1. (273 aa)
SU9_22885Ubiquinol-cytochrome C reductase iron-sulfur subunit; COG0201 Preprotein translocase subunit SecY. (328 aa)
SU9_22890COG1290 Cytochrome b subunit of the bc complex. (545 aa)
SU9_25024Secreted protein. (364 aa)
SU9_25814Hypothetical protein; COG0446 Uncharacterized NAD(FAD)-dependent dehydrogenases. (93 aa)
SU9_31266Cytochrome c oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (559 aa)
SU9_32228Respiratory-chain NADH dehydrogenase domain 51 kDa subunit; COG1894 NADH:ubiquinone oxidoreductase, NADH-binding (51 kD) subunit. (428 aa)
SU9_32948Hypothetical protein; COG0446 Uncharacterized NAD(FAD)-dependent dehydrogenases. (104 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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