STRINGSTRING
CEW89_07510 CEW89_07510 nuoN nuoN CEW89_07440 CEW89_07440 CEW89_07445 CEW89_07445 CEW89_07460 CEW89_07460 CEW89_07485 CEW89_07485 nuoC nuoC nuoB nuoB nuoA nuoA ctaD ctaD CEW89_17215 CEW89_17215 CEW89_17210 CEW89_17210 CEW89_15985 CEW89_15985 coxB coxB CEW89_17685 CEW89_17685 CEW89_00840 CEW89_00840 CEW89_00830 CEW89_00830 CEW89_00825 CEW89_00825 cyoA cyoA cyoB cyoB cyoC cyoC cyoD cyoD GCA_001550095_03577 GCA_001550095_03577 ccoN ccoN petA petA CEW89_12405 CEW89_12405
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:
CEW89_07510Unannotated protein; 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. (432 aa)
nuoNUnannotated 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; Belongs to the complex I subunit 2 family. (478 aa)
CEW89_07440Unannotated protein. (510 aa)
CEW89_07445Unannotated protein. (697 aa)
CEW89_07460Unannotated protein; 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. (204 aa)
CEW89_07485Unannotated protein; 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. (672 aa)
nuoCUnannotated 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; Belongs to the complex I 30 kDa subunit family. (200 aa)
nuoBUnannotated 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. (177 aa)
nuoAUnannotated 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; Belongs to the complex I subunit 3 family. (121 aa)
ctaDUnannotated protein; 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)
CEW89_17215Unannotated protein. (974 aa)
CEW89_17210Unannotated protein. (508 aa)
CEW89_15985Unannotated protein; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. (878 aa)
coxBUnannotated protein; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (291 aa)
CEW89_17685Unannotated protein. (267 aa)
CEW89_00840Unannotated protein. (1041 aa)
CEW89_00830Unannotated protein; Belongs to the complex I 20 kDa subunit family. (229 aa)
CEW89_00825Unannotated protein. (185 aa)
cyoAUnannotated protein. (365 aa)
cyoBUnannotated protein; Belongs to the heme-copper respiratory oxidase family. (665 aa)
cyoCUnannotated protein. (201 aa)
cyoDUnannotated protein. (138 aa)
GCA_001550095_03577Unannotated protein. (563 aa)
ccoNUnannotated protein; Belongs to the heme-copper respiratory oxidase family. (531 aa)
petAUnannotated protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (187 aa)
CEW89_12405Unannotated protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (468 aa)
Your Current Organism:
Celeribacter ethanolicus
NCBI taxonomy Id: 1758178
Other names: C. ethanolicus, CGMCC 1.15406, Celeribacter ethanolicus Jian et al. 2016, Celeribacter sp. NH195, JCM 31095, strain NH195
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