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thiH protein (Desulfovibrio vulgaris Hildenborough) - STRING interaction network
"thiH" - ThiH protein in Desulfovibrio vulgaris Hildenborough
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second shell of interactors
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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
thiHThiH protein; Identified by similarity to SP-P30140; match to protein family HMM PF04055 (444 aa)    
Predicted Functional Partners:
thiG
Thiazole synthase; Catalyzes the rearrangement of 1-deoxy-D-xylulose 5- phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S (265 aa)
  0.999
thiC
Thiamine biosynthesis protein ThiC; Identified by match to protein family HMM PF01964; match to protein family HMM TIGR00190 (429 aa)
 
 
  0.963
DVU_2092
Identified by match to protein family HMM PF00899 (213 aa)
 
   
  0.952
thiE-1
Thiamine-phosphate synthase; Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP) (226 aa)
 
   
  0.913
thiS
Thiamine biosynthesis protein ThiS; Identified by match to protein family HMM PF02597; match to protein family HMM TIGR01683 (66 aa)
 
        0.908
DVU_1765
ThiH protein, putative; Identified by similarity to SP-P30140; match to protein family HMM PF04055 (464 aa)
   
   
 
0.845
thiE-2
Thiamine-phosphate synthase; Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP); Belongs to the thiamine-phosphate synthase family (219 aa)
   
   
  0.779
birA
Bifunctional ligase/repressor BirA; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor (330 aa)
   
   
  0.659
bioD
ATP-dependent dethiobiotin synthetase BioD; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA) to form an ureido ring (246 aa)
   
   
  0.632
nnrD
Multifunctional fusion protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration; Belongs to the NnrD/CARKD family (574 aa)
   
        0.624
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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