STRINGSTRING
nuoB nuoB NuoE NuoE NuoF NuoF NuoG NuoG nuoH nuoH nuoI nuoI nuoK nuoK NuoL NuoL NuoM NuoM nuoN nuoN
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:
nuoBHypothetical 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. (223 aa)
NuoENADH-quinone oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. (169 aa)
NuoFNADH oxidoreductase (quinone) subunit F; Derived by automated computational analysis using gene prediction method: Protein Homology. (478 aa)
NuoGNADH-quinone oxidoreductase subunit G; Catalyzes the transfer of electrons from NADH to quinone; Derived by automated computational analysis using gene prediction method: Protein Homology. (1022 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. (345 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. (182 aa)
nuoKNADH-quinone oxidoreductase subunit J; 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. (110 aa)
NuoLNADH-quinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology. (623 aa)
NuoMNADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology. (534 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 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. (491 aa)
Your Current Organism:
Moraxella cuniculi
NCBI taxonomy Id: 34061
Other names: ATCC 14688, CCUG 2154, DSM 21768, LMG 8382, LMG:8382, M. cuniculi, NCTC 10297, Neisseria cuniculi, strain K 19
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.