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cooF protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"cooF" - Iron-sulfur protein CooF in Desulfovibrio vulgaris Hildenborough
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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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[Homology]
Score
cooFIron-sulfur protein CooF; Identified by similarity to SP-P31894; match to protein family HMM PF00037 (173 aa)    
Predicted Functional Partners:
DVU_2291
Carbon monoxide-induced hydrogenase CooH, putative; Identified by similarity to SP-P31895; match to protein family HMM PF00346 (366 aa)
   
 
  0.967
DVU_2288
Hydrogenase, CooL subunit, putative; Identified by similarity to GP-1515468; match to protein family HMM PF01058 (144 aa)
   
 
  0.965
DVU_2289
Hydrogenase, CooX subunit, putative; Identified by match to protein family HMM PF00037 (211 aa)
   
 
  0.959
DVU_1772
Pyridine nucleotide-disulfide oxidoreductase; Identified by match to protein family HMM PF00070 (673 aa)
     
  0.936
DVU_2290
Hydrogenase, CooU subunit, putative; Identified by similarity to GP-1515470; match to protein family HMM PF00329 (178 aa)
         
  0.929
DVU_2286
Hydrogenase, CooM subunit, putative; Identified by similarity to GP-1515466; match to protein family HMM PF00361 (1253 aa)
   
 
  0.921
cooS
Carbon monoxide dehydrogenase; Identified by similarity to SP-P31896 (629 aa)
       
  0.916
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)
       
  0.907
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)
       
  0.907
fdnG-3
Formate dehydrogenase 2 subunit alpha (cytochrome c-553); Alpha chain of the formate dehydrogenase (FDH) that catalyzes the reversible two-electron oxidation of formate to carbon dioxide. The alpha subunit of formate dehydrogenase forms the active site (1012 aa)
 
  0.898
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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