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sdaAB protein (Bacillus cereus) - STRING interaction network
"sdaAB" - Sda_beta: L-serine dehydratase, iron-sulfur-dependent, beta subunit in Bacillus cereus
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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sdaABSda_beta- L-serine dehydratase, iron-sulfur-dependent, beta subunit (219 aa)    
Predicted Functional Partners:
sdaAA
Sda_alpha- L-serine dehydratase, iron-sulfur-dependent, alpha subunit (292 aa)
   
  0.999
trpB
Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine (397 aa)
     
 
  0.914
cysE
cysE- serine O-acetyltransferase (221 aa)
         
  0.913
dsdA
Probable D-serine dehydratase; D_Ser_am_lyase- D-serine ammonia-lyase; Belongs to the serine/threonine dehydratase family. DsdA subfamily (443 aa)
         
  0.909
trpA
Tryptophan synthase alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3- phosphate; Belongs to the TrpA family (258 aa)
         
  0.902
pcs
pssA- CDP-diacylglycerol-serine O-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family (233 aa)
     
 
    0.901
ilvA_1
L-threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short- lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA (420 aa)
   
  0.870
tdcB
L-threonine dehydratase catabolic TdcB; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short- lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA (333 aa)
   
  0.870
thrB
Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L- homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily (297 aa)
     
 
  0.823
mccB
annotation not available (377 aa)
         
  0.806
Your Current Organism:
Bacillus cereus
NCBI taxonomy Id: 1396
Other names: ATCC 14579, B. cereus, BCRC 10603, Bacillus cereus, Bacillus endorhythmos, Bacillus medusa, Bacillus sp. 2479, Bacillus sp. BS2(2013b), Bacillus sp. BV4, Bacillus sp. JKR50, Bacillus sp. JKR62, Bacillus sp. JP44SK22, Bacillus sp. JP44SK37, Bacillus sp. JP44SK43, Bacillus sp. JP44SK45, Bacillus sp. JSG1(2014), Bacillus sp. KER 17, Bacillus sp. MZ-01, Bacillus sp. PXDK-1, Bacillus sp. Pf-1, Bacillus sp. V3, Bacillus sp. mmm86, CCM 2010, CCRC 10603, CCUG 7414, CIP 66.24, DSM 31, IAM 12605, IFO 15305, JCM 2152, LMG 6923, NBRC 15305, NCCB 75008, NCIMB 9373, NCTC 2599, NRRL B-3711, VKM B-504
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