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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
BFS79_09640Isochorismate synthase; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. (428 aa)    
Predicted Functional Partners:
AOG27818.1
Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.875
AOG27820.1
Electron transfer flavoprotein subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.870
BFS79_03925
Oxidoreductase; FAD/NAD(P)-binding domain; possibly part of an electron transfer system required for anaerobic carnitine reduction; frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.770
AOG28715.1
NADH-quinone oxidoreductase subunit A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
     
 0.653
AOG28721.1
NADH-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.
 
   
 0.582
AOG28243.1
Cobaltochelatase subunit CobN; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.549
AOG28720.1
NADH oxidoreductase (quinone) 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.
     
 0.540
nuoC
NADH-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.
 
     0.533
nuoI
NADH-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.
  
  
 0.530
AOG28729.1
Geranylgeranyl pyrophosphate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the FPP/GGPP synthase family.
  
 
 0.525
Your Current Organism:
Cutibacterium avidum
NCBI taxonomy Id: 33010
Other names: ATCC 25577, Bacteroides avidus, C. avidum, CCUG 36754, CIP 103261, Corynebacterium avidum, DSM 4901, IFO 15671, Mycobacterium avidum, NBRC 15671, NCTC 11864, Propionibacterium avidum, Propionicibacterium avidum
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