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DVU_0264 protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"DVU_0264" - Ferredoxin, 4Fe-4S, putative 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
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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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Score
DVU_0264Ferredoxin, 4Fe-4S, putative; Identified by similarity to SP-P33393; match to protein family HMM PF00037; match to protein family HMM PF02754 (439 aa)    
Predicted Functional Partners:
DVU_0266
Uncharacterized protein; Identified by Glimmer2; putative (408 aa)
 
 
 
  0.994
DVU_0265
annotation not available (219 aa)
 
     
  0.966
DVU_0263
Acidic cytochrome c3; Identified by similarity to SP-P94690 (126 aa)
 
     
  0.961
DVU_1772
Pyridine nucleotide-disulfide oxidoreductase; Identified by match to protein family HMM PF00070 (673 aa)
   
 
  0.941
DVU_2286
Hydrogenase, CooM subunit, putative; Identified by similarity to GP-1515466; match to protein family HMM PF00361 (1253 aa)
   
 
  0.931
DVU_0253
Oxidoreductase, FAD/iron-sulfur cluster-binding domain protein; Identified by match to protein family HMM PF00037; match to protein family HMM PF01565; match to protein family HMM PF02913 (941 aa)
   
 
  0.908
DVU_0261
Identified by match to protein family HMM PF00582; Belongs to the universal stress protein A family (308 aa)
 
          0.857
poR
Pyruvate synthase; Identified by similarity to GP-1770208; match to protein family HMM PF00037; match to protein family HMM PF01558; match to protein family HMM PF01855 (1215 aa)
   
   
  0.849
DVU_0267
Uncharacterized protein; Identified by Glimmer2; putative (51 aa)
              0.796
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)
 
     
  0.790
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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