STRINGSTRING
ANS66439.1 ANS66439.1 ANS63049.1 ANS63049.1 ANS64138.1 ANS64138.1 ANS64229.1 ANS64229.1 ANS64576.1 ANS64576.1 ANS64703.1 ANS64703.1 ANS64706.1 ANS64706.1 ANS64710.1 ANS64710.1 ANS64711.1 ANS64711.1 ANS65550.1 ANS65550.1 ANS66440.1 ANS66440.1 ANS67171.1 ANS67171.1 nuoK nuoK ANS67176.1 ANS67176.1 ANS67177.1 ANS67177.1 nuoN nuoN nuoK-2 nuoK-2 ANS67219.1 ANS67219.1 ANS67220.1 ANS67220.1 nuoN-2 nuoN-2 ANS69321.1 ANS69321.1 nuoK-3 nuoK-3 ANS69528.1 ANS69528.1 ANS69529.1 ANS69529.1 nuoN-3 nuoN-3
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:
ANS66439.1Cytochrome oxidase subunit II. (335 aa)
ANS63049.1Oxidoreductase. (458 aa)
ANS64138.1Hypothetical protein. (206 aa)
ANS64229.1Cytochrome 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. (564 aa)
ANS64576.1Cytochrome b subunit. (548 aa)
ANS64703.1Cytochrome B subunit. (546 aa)
ANS64706.1Cytochrome c oxidase subunit III. (206 aa)
ANS64710.1Cytochrome 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. (580 aa)
ANS64711.1Cytochrome c oxidase subunit II. (298 aa)
ANS65550.1Oxidoreductase. (468 aa)
ANS66440.1Cytochrome bd-I oxidase subunit I. (504 aa)
ANS67171.1NADH 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. (834 aa)
nuoKNADH dehydrogenase 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. (99 aa)
ANS67176.1NADH-quinone oxidoreductase subunit L. (639 aa)
ANS67177.1NADH dehydrogenase subunit M. (523 aa)
nuoNNADH dehydrogenase subunit 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. (549 aa)
nuoK-2NADH dehydrogenase subunit NuoK2; 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. (135 aa)
ANS67219.1NADH dehydrogenase I subunit L. (664 aa)
ANS67220.1NADH dehydrogenase I subunit M. (524 aa)
nuoN-2NADH dehydrogenase I subunit 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. (510 aa)
ANS69321.1Hypothetical protein. (100 aa)
nuoK-3NADH dehydrogenase 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. (101 aa)
ANS69528.1NADH:ubiquinone oxidoreductase subunit 5 (chain L)/multisubunit Na+/H+ antiporter, MnhA subunit. (610 aa)
ANS69529.1Proton-translocating NADH-quinone oxidoreductase, chain M. (502 aa)
nuoN-3Putative NADH dehydrogenase 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. (476 aa)
Your Current Organism:
Streptomyces lincolnensis
NCBI taxonomy Id: 1915
Other names: ATCC 25466, BCRC 11173, CBS 630.70, CBS 699.69, CCRC 11173, CCRC:11173, DSM 2013, DSM 40355, IFO 13054, ISP 5355, JCM 4287, JCM 4488, KCTC 9088, KCTC 9089, NBRC 13054, NCIMB 9413, NRRL 2936, NRRL-ISP 5355, S. lincolnensis, VKM Ac-727
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