STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
dxs1-deoxyxylulose-5-phosphate synthase; Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D- xylulose-5-phosphate (DXP); Belongs to the transketolase family. DXPS subfamily. (633 aa)    
Predicted Functional Partners:
dxr
1-deoxy-D-xylulose-5-phosphate reductoisomerase; Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- phosphate (MEP); Belongs to the DXR family.
 
 
 0.999
ispH
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase; Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. Belongs to the IspH family.
  
 0.996
ispD
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, nonmevalonate isoprenoid pathway; Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
 
  
 0.995
ispF
2-C-methyl-D-erythritol-2,4-cyclodiphosphate synthase; Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2- C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP); Belongs to the IspF family.
 
  
 0.995
ispA
Geranyltranstransferase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme.
  
 0.990
ispG
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin); Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family.
 
  
 0.989
ispE
4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase; Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
 
  
 0.974
thiG
Hydroxyethylthiazole phosphate synthetase (thiamine biosynthesis); 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.
     
 0.963
yqxC
Putative methyltransferase with RNA binding domain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the TlyA family.
 
  
 0.935
fni
Isopentenyl diphosphate isomerase; Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
  
  
 0.932
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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