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
AOG28729.1Geranylgeranyl pyrophosphate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the FPP/GGPP synthase family. (324 aa)    
Predicted Functional Partners:
AOG27715.1
Geranylgeranyl pyrophosphate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the FPP/GGPP synthase family.
  
  
0.924
uppS
Isoprenyl transferase; Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
 
  
 0.767
AOG29214.1
Isoprenyl transferase; Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
 
  
 0.727
nuoN
NADH-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 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 2 family.
 
     0.699
nuoK
NADH-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 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.
  
    0.692
AOG28727.1
NADH-quinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.678
AOG28730.1
precorrin-6A synthase (deacetylating); Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.676
idi
Isopentenyl-diphosphate delta-isomerase; Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
  
  
 0.662
nuoB
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.
  
    0.657
AOG28726.1
NADH-quinone oxidoreductase subunit L; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.654
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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