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
KNB70259.1LOG family protein YvdD; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the LOG family. (193 aa)    
Predicted Functional Partners:
KNB73875.1
5'-nucleotidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the 5'-nucleotidase family.
   
  0.780
sdhB
Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; the catalytic subunits are similar to fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.667
KNB71846.1
NADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
  0.658
nuoA
NADH:ubiquinone 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.
    
  0.654
nuoK
NADH 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; Belongs to the complex I subunit 4L family.
  
 
  0.648
KNB71842.1
NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
  0.645
KNB71845.1
NADH:ubiquinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.632
KNB69338.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
    0.623
KNB70332.1
Ribonucleotide-diphosphate reductase; Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides; Belongs to the ribonucleoside diphosphate reductase small chain family.
  
    0.560
KNB69267.1
Pyridine nucleotide-disulfide oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
  0.551
Your Current Organism:
Brevibacillus reuszeri
NCBI taxonomy Id: 54915
Other names: ATCC 51665, B. reuszeri, Bacillus reuszeri, CIP 104543, DSM 9887, IFO 15719, JCM 9170, LMG 16012, LMG:16012, NBRC 15719, strain H.W. Reuszer Army strain 39
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