STRINGSTRING
AOM39252.1 AOM39252.1 nuoA nuoA nuoB nuoB nuoC nuoC AOM39439.1 AOM39439.1 AOM39440.1 AOM39440.1 AOM42767.1 AOM42767.1 nuoH nuoH nuoI nuoI AOM39443.1 AOM39443.1 nuoK nuoK AOM39445.1 AOM39445.1 AOM39446.1 AOM39446.1 nuoN nuoN AOM40478.1 AOM40478.1 AOM40655.1 AOM40655.1 AOM40736.1 AOM40736.1 AOM41961.1 AOM41961.1
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:
AOM39252.1Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology. (86 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 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. (143 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 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. (224 aa)
nuoCNADH-quinone oxidoreductase subunit C/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; In the C-terminal section; belongs to the complex I 49 kDa subunit family. (598 aa)
AOM39439.1NADH-quinone oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. (181 aa)
AOM39440.1NADH-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. (454 aa)
AOM42767.1NADH-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. (910 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 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. (325 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 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. (180 aa)
AOM39443.1NADH: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. (176 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 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)
AOM39445.1NADH-quinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (624 aa)
AOM39446.1NADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (506 aa)
nuoNNADH:ubiquinone 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 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. (485 aa)
AOM40478.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (208 aa)
AOM40655.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (370 aa)
AOM40736.1Fe-S-binding ATPase; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. (370 aa)
AOM41961.1Peptidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (491 aa)
Your Current Organism:
Xenorhabdus hominickii
NCBI taxonomy Id: 351679
Other names: CIP 109072, DSM 17903, X. hominickii, Xenorhabdus hominickii Taillez et al. 2006, Xenorhabdus sp. KE01, Xenorhabdus sp. KR01, Xenorhabdus sp. KR05, strain KE01
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