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cooS protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"cooS" - Carbon monoxide dehydrogenase in Desulfovibrio vulgaris Hildenborough
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query proteins and first shell of interactors
white nodes:
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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[Homology]
Score
cooSCarbon monoxide dehydrogenase; Identified by similarity to SP-P31896 (629 aa)    
Predicted Functional Partners:
DVU_2099
Carbon monoxide dehydrogenase accessory protein CooC, putative; Identified by similarity to SP-P31897; match to protein family HMM PF00991 (293 aa)
 
     
  0.969
DVU_1772
Pyridine nucleotide-disulfide oxidoreductase; Identified by match to protein family HMM PF00070 (673 aa)
   
  0.941
DVU_2288
Hydrogenase, CooL subunit, putative; Identified by similarity to GP-1515468; match to protein family HMM PF01058 (144 aa)
       
  0.927
DVU_2291
Carbon monoxide-induced hydrogenase CooH, putative; Identified by similarity to SP-P31895; match to protein family HMM PF00346 (366 aa)
       
  0.926
DVU_2289
Hydrogenase, CooX subunit, putative; Identified by match to protein family HMM PF00037 (211 aa)
       
  0.924
DVU_2290
Hydrogenase, CooU subunit, putative; Identified by similarity to GP-1515470; match to protein family HMM PF00329 (178 aa)
       
  0.923
dvsB
Sulfite reductase, dissimilatory-type subunit beta; Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration, a process catalyzed by the sulfate-reducing bacteria (381 aa)
   
   
  0.918
dsvA
Sulfite reductase, dissimilatory-type subunit alpha; Part of the complex that catalyzes the reduction of sulfite to sulfide. The alpha and beta subunits may have arisen by gene duplication. They both bind 2 iron-sulfur clusters, but the alpha subunit seems to be catalytically inactive, due to substitutions along the putative substrate access channel, and because it binds sirohydrochlorin (the dematallated form of siroheme) instead of siroheme (437 aa)
   
   
  0.917
DVU_2399
Hydrogenase, putative; Identified by similarity to GP-21327886; match to protein family HMM PF00175; match to protein family HMM PF00970 (283 aa)
   
  0.916
cooF
Iron-sulfur protein CooF; Identified by similarity to SP-P31894; match to protein family HMM PF00037 (173 aa)
       
  0.916
Your Current Organism:
Desulfovibrio vulgaris Hildenborough
NCBI taxonomy Id: 882
Other names: D. vulgaris str. Hildenborough, Desulfovibrio vulgaris (STRAIN HILDENBOROUGH), Desulfovibrio vulgaris ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris str. Hildenborough, Desulfovibrio vulgaris subsp. vulgaris (strain Hildenborough), Desulfovibrio vulgaris subsp. vulgaris ATCC 29579, Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
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