STRINGSTRING
GAU_0129 GAU_0129 GAU_0130 GAU_0130 ctaC ctaC ctaD ctaD ctaE ctaE GAU_0507 GAU_0507 ctaG ctaG GAU_0509 GAU_0509 GAU_0696 GAU_0696 GAU_0697 GAU_0697 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 GAU_1763 GAU_1763 GAU_2032 GAU_2032 GAU_2033 GAU_2033 GAU_2034 GAU_2034 GAU_2035 GAU_2035 GAU_2036 GAU_2036 GAU_2037 GAU_2037 GAU_2058 GAU_2058 GAU_2071 GAU_2071 GAU_2216 GAU_2216 GAU_2217 GAU_2217 nuoN-2 nuoN-2 nuoM-2 nuoM-2 nuoL-2 nuoL-2 nuoK-2 nuoK-2 nuoJ-2 nuoJ-2 nuoI-2 nuoI-2 nuoH-2 nuoH-2 nuoG-2 nuoG-2 nuoF-2 nuoF-2 nuoE-2 nuoE-2 nuoD-2 nuoD-2 nuoC-2 nuoC-2 nuoB-2 nuoB-2 nuoA-2 nuoA-2 GAU_2580 GAU_2580 ctaB ctaB GAU_2709 GAU_2709 GAU_2936 GAU_2936 GAU_3316 GAU_3316 GAU_3317 GAU_3317 GAU_3683 GAU_3683 GAU_3776 GAU_3776
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:
GAU_0129Hypothetical protein. (499 aa)
GAU_0130Hypothetical protein. (465 aa)
ctaCCytochrome c oxidase subunit II; 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). (429 aa)
ctaDCytochrome 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. (626 aa)
ctaECytochrome c oxidase subunit III. (230 aa)
GAU_0507Hypothetical membrane protein. (114 aa)
ctaGPutative CtaG protein. (307 aa)
GAU_0509Hypothetical protein. (209 aa)
GAU_0696Putative menaquinol-cytochrome c reductase cytochrome b/c subunit. (611 aa)
GAU_0697Rieske iron-sulfur protein. (178 aa)
nuoNNADH-quinone oxidoreductase 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 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. (520 aa)
nuoMNADH-quinone oxidoreductase chain M. (521 aa)
nuoLNADH-quinone oxidoreductase chain L. (674 aa)
nuoKNADH-quinone oxidoreductase 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 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 4L family. (97 aa)
nuoJNADH-quinone oxidoreductase 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. (168 aa)
nuoINADH-quinone oxidoreductase chain 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. (151 aa)
nuoHNADH-quinone oxidoreductase 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. (418 aa)
nuoGPutative NADH-quinone oxidoreductase chain G. (521 aa)
nuoFNADH-quinone oxidoreductase 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. (442 aa)
nuoENADH-quinone oxidoreductase chain E. (155 aa)
nuoDNADH-quinone oxidoreductase 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 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 49 kDa subunit family. (394 aa)
nuoCNADH-quinone oxidoreductase 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 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. (213 aa)
nuoBNADH-quinone oxidoreductase 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 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. (212 aa)
nuoANADH-quinone oxidoreductase 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 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. (134 aa)
GAU_1763Putative S16B family peptidase. (429 aa)
GAU_2032Hypothetical membrane protein. (443 aa)
GAU_2033Hypothetical protein. (266 aa)
GAU_2034Hypothetical membrane protein. (166 aa)
GAU_2035Hypothetical protein. (475 aa)
GAU_2036Putative oxidoreductase; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (1028 aa)
GAU_2037Cytochrome c3. (205 aa)
GAU_2058Hypothetical protein. (299 aa)
GAU_2071Hypothetical protein. (169 aa)
GAU_2216Putative M16B family peptidase. (470 aa)
GAU_2217Putative M16B family peptidase. (496 aa)
nuoN-2NADH-quinone oxidoreductase 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 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. (463 aa)
nuoM-2NADH-quinone oxidoreductase chain M. (512 aa)
nuoL-2NADH-quinone oxidoreductase chain L. (631 aa)
nuoK-2NADH-quinone oxidoreductase 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 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 4L family. (100 aa)
nuoJ-2NADH-quinone oxidoreductase 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. (169 aa)
nuoI-2NADH-quinone oxidoreductase chain 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. (185 aa)
nuoH-2NADH-quinone oxidoreductase 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. (384 aa)
nuoG-2Putative NADH-quinone oxidoreductase chain G. (500 aa)
nuoF-2NADH-quinone oxidoreductase chain F. (439 aa)
nuoE-2NADH-quinone oxidoreductase chain E. (158 aa)
nuoD-2NADH-quinone oxidoreductase 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 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 49 kDa subunit family. (412 aa)
nuoC-2NADH-quinone oxidoreductase chain C. (174 aa)
nuoB-2NADH-quinone oxidoreductase 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 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. (171 aa)
nuoA-2NADH-quinone oxidoreductase chain A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (122 aa)
GAU_2580Cytochrome oxidase assembly family protein. (326 aa)
ctaBProtoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (307 aa)
GAU_2709Hypothetical membrane protein. (241 aa)
GAU_2936Putative cytochrome c. (161 aa)
GAU_3316Hypothetical protein. (275 aa)
GAU_3317Hypothetical protein. (262 aa)
GAU_3683Hypothetical protein. (250 aa)
GAU_3776Putative cbb3 oxidase subunit IV. (65 aa)
Your Current Organism:
Gemmatimonas aurantiaca
NCBI taxonomy Id: 379066
Other names: G. aurantiaca T-27, Gemmatimonas aurantiaca DSM 14586, Gemmatimonas aurantiaca JCM 11422, Gemmatimonas aurantiaca NBRC 100505, Gemmatimonas aurantiaca T-27, Gemmatimonas aurantiaca str. T-27, Gemmatimonas aurantiaca strain T-27
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