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sodA protein (Yersinia pseudotuberculosis) - STRING interaction network
"sodA" - Superoxide dismutase in Yersinia pseudotuberculosis
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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sodASuperoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems (207 aa)    
Predicted Functional Partners:
nifJ
Pyruvate-flavodoxin oxidoreductase; Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin (1177 aa)
   
   
  0.902
sodC
annotation not available (201 aa)
     
 
  0.799
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (97 aa)
   
 
  0.750
ahpC
Putative alkyl hydroperoxide reductase subunit c; C-terminal domain of 1-Cys peroxiredoxin family protein (200 aa)
   
   
  0.721
nifU
Iron-sulfur cluster assembly scaffold protein IscU; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters (128 aa)
   
 
  0.699
rplQ
L17- ribosomal protein L17 (129 aa)
     
 
  0.680
DJ40_2304
annotation not available (243 aa)
     
 
  0.679
rpmA
L27- ribosomal protein L27; Belongs to the bacterial ribosomal protein bL27 family (85 aa)
     
      0.679
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (932 aa)
     
 
  0.664
atpH
ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (177 aa)
     
   
  0.636
Your Current Organism:
Yersinia pseudotuberculosis
NCBI taxonomy Id: 633
Other names: ATCC 29833, Bacillus pseudotuberkulosis, Bacterium pseudotuberculosis, CCUG 5855, CIP 55.85, DSM 8992, NCTC 10275, Pasteurella pseudotuberculosis, Shigella pseudotuberculosis, Y. pseudotuberculosis, Yersinia pseudotuberculosis
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