STRINGSTRING
STRING protein interaction network
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
amb0594Uncharacterized conserved protein. (357 aa)    
Predicted Functional Partners:
amb0593
Uncharacterized conserved protein; Belongs to the multicopper oxidase YfiH/RL5 family.
      0.880
nuoD
NADH:ubiquinone oxidoreductase 49 kD subunit 7; 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.
 
 
 0.839
amb0592
Hypothetical protein.
       0.828
amb3931
NADH-ubiquinone oxidoreductase 40 kDa subunit.
  
  
 0.823
nuoB
NADH:ubiquinone oxidoreductase 20 kD subunit and related Fe-S oxidoreductase; 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 (By similarity).
 
 
 0.811
nuoC
NADH:ubiquinone oxidoreductase 27 kD subunit; 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.
 
 
 0.808
nuoI
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit; 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.
  
  
 0.800
amb2508
Phytoene/squalene synthetase.
  
  
 0.752
amb1605
SAM-dependent methyltransferase.
  
    0.750
lgt
Prolipoprotein diacylglyceryltransferase; Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins; Belongs to the Lgt family.
 
     0.721
Your Current Organism:
Magnetospirillum magneticum
NCBI taxonomy Id: 342108
Other names: M. magneticum AMB-1, Magnetospirillum magneticum AMB-1, Magnetospirillum magneticum str. AMB-1, Magnetospirillum magneticum strain AMB-1, Magnetospirillum sp. (strain AMB-1), Magnetospirillum sp. AMB-1
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.