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AQA01128.1 AQA01128.1 AQA01281.1 AQA01281.1 nuoA nuoA nuoB nuoB nuoC nuoC nuoD nuoD AQA01286.1 AQA01286.1 AQA01287.1 AQA01287.1 AQA01288.1 AQA01288.1 nuoH nuoH nuoI nuoI AQA01291.1 AQA01291.1 nuoK nuoK AQA01293.1 AQA01293.1 AQA01294.1 AQA01294.1 nuoN nuoN AQA01342.1 AQA01342.1 AQA02320.1 AQA02320.1 AQA06266.1 AQA06266.1 AQA06288.1 AQA06288.1 AQA03381.1 AQA03381.1 AQA06454.1 AQA06454.1 AQA03792.1 AQA03792.1 AQA04028.1 AQA04028.1 AQA04584.1 AQA04584.1 AQA04589.1 AQA04589.1 BVC93_23105 BVC93_23105 AQA04827.1 AQA04827.1 AQA04830.1 AQA04830.1 AQA06637.1 AQA06637.1 AQA06636.1 AQA06636.1 AQA04831.1 AQA04831.1 nuoA-2 nuoA-2 AQA05257.1 AQA05257.1 nuoD-2 nuoD-2 AQA05259.1 AQA05259.1 AQA05260.1 AQA05260.1 nuoH-2 nuoH-2 BVC93_25930 BVC93_25930 nuoK-2 nuoK-2 BVC93_25945 BVC93_25945 AQA05266.1 AQA05266.1 ctaB ctaB BVC93_29945 BVC93_29945 AQA05941.1 AQA05941.1
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:
AQA01128.1Cytochrome 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. (581 aa)
AQA01281.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (135 aa)
nuoANADH-quinone oxidoreductase subunit 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 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 3 family. (119 aa)
nuoBNADH 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)
nuoCNADH-quinone oxidoreductase subunit 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 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 30 kDa subunit family. (225 aa)
nuoDNADH dehydrogenase subunit 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 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 49 kDa subunit family. (456 aa)
AQA01286.1NADH-quinone oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. (288 aa)
AQA01287.1NADH-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. (439 aa)
AQA01288.1NADH-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. (791 aa)
nuoHNADH-quinone oxidoreductase subunit 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 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. (408 aa)
nuoINADH-quinone oxidoreductase 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 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. (167 aa)
AQA01291.1NADH:ubiquinone oxidoreductase subunit 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. (242 aa)
nuoKNADH-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. (99 aa)
AQA01293.1NADH-quinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (625 aa)
AQA01294.1NADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (520 aa)
nuoNNADH-quinone oxidoreductase 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. (521 aa)
AQA01342.1Cytochrome 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)
AQA02320.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (62 aa)
AQA06266.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (181 aa)
AQA06288.1Proline dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (81 aa)
AQA03381.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (240 aa)
AQA06454.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (280 aa)
AQA03792.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (240 aa)
AQA04028.1NAD-dependent epimerase; Derived by automated computational analysis using gene prediction method: Protein Homology. (384 aa)
AQA04584.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (677 aa)
AQA04589.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (246 aa)
BVC93_23105Asparagine synthase (glutamine-hydrolyzing); Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. (352 aa)
AQA04827.1Cytochrome C oxidase subunit IV; Part of cytochrome c oxidase, its function is unknown. Belongs to the cytochrome c oxidase bacterial subunit CtaF family. (139 aa)
AQA04830.1Derived by automated computational analysis using gene prediction method: Protein Homology. (552 aa)
AQA06637.1Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (383 aa)
AQA06636.1Derived by automated computational analysis using gene prediction method: Protein Homology. (272 aa)
AQA04831.1Derived by automated computational analysis using gene prediction method: Protein Homology. (203 aa)
nuoA-2NADH-quinone oxidoreductase subunit 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 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 3 family. (119 aa)
AQA05257.1NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (184 aa)
nuoD-2NADH-quinone oxidoreductase subunit 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 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 49 kDa subunit family. (456 aa)
AQA05259.1NADH-quinone oxidoreductase subunit F; Derived by automated computational analysis using gene prediction method: Protein Homology. (646 aa)
AQA05260.1NADH-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. (778 aa)
nuoH-2NADH-quinone oxidoreductase subunit 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 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. (382 aa)
BVC93_25930NADH-quinone oxidoreductase subunit I; 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. (243 aa)
nuoK-2NADH-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. (99 aa)
BVC93_25945NADH-quinone oxidoreductase subunit L; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. (502 aa)
AQA05266.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (136 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. (314 aa)
BVC93_29945Class A beta-lactamase; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the peptidase M16 family. (442 aa)
AQA05941.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (84 aa)
Your Current Organism:
Mycobacterium sp. MS1601
NCBI taxonomy Id: 1936029
Other names: M. sp. MS1601
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