STRINGSTRING
QcrC QcrC KUN52266.1 KUN52266.1 NuoM2 NuoM2 nuoK1 nuoK1 NuoI2 NuoI2 nuoB2 nuoB2 NuoM1 NuoM1 nuoI1 nuoI1 NuoG1 NuoG1 nuoF nuoF NuoE NuoE nuoB1 nuoB1 ctaD1_2 ctaD1_2 ctaC ctaC ctaD1_1 ctaD1_1 qcrA qcrA qcrB qcrB NuoF2 NuoF2 SdhC1 SdhC1
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:
QcrCCystathionine beta-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology. (269 aa)
KUN52266.1Oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (536 aa)
NuoM2NADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (527 aa)
nuoK1NADH-quinone oxidoreductase 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. (129 aa)
NuoI2NADH-quinone oxidoreductase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (216 aa)
nuoB2Hydroxyacid dehydrogenase; 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. (203 aa)
NuoM1NADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (532 aa)
nuoI1Hypothetical protein; 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. (200 aa)
NuoG1NADH-quinone oxidoreductase 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. (834 aa)
nuoFNADH dehydrogenase; 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. (448 aa)
NuoENADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (287 aa)
nuoB1NADH dehydrogenase; 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)
ctaD1_2Cytochrome ubiquinol 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. (563 aa)
ctaCCytochrome C oxidase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (319 aa)
ctaD1_1Cytochrome ubiquinol 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. (579 aa)
qcrAUbiquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (357 aa)
qcrBUbiquinol-cytochrome c reductase cytochrome b subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (548 aa)
NuoF2NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (607 aa)
SdhC1Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (114 aa)
Your Current Organism:
Streptomyces avermitilis
NCBI taxonomy Id: 33903
Other names: ATCC 31267, DSM 46492, JCM 5070, NBRC 14893, NCIMB 12804, NRRL 8165, S. avermitilis, Streptomyces avermectinius, Streptomyces avermectinius Takahashi et al. 2002, strain MA-4680
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