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dfrD protein (Bacillus cereus) - STRING interaction network
"dfrD" - Dihydrofolate reductase in Bacillus cereus
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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
dfrDDihydrofolate reductase; Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (162 aa)    
Predicted Functional Partners:
thyA
Thymidylate synthase; Catalyzes the reductive methylation of 2’-deoxyuridine- 5’-monophosphate (dUMP) to 2’-deoxythymidine-5’-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis (318 aa)
  0.999
folC
Folylpolyglutamate synthase; folC- bifunctional FolC family protein; Belongs to the folylpolyglutamate synthase family (433 aa)
   
  0.969
fhs
annotation not available (583 aa)
   
 
  0.964
folK
folK- 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase (171 aa)
 
   
  0.918
purN
Phosphoribosylglycinamide formyltransferase; Catalyzes the transfer of a formyl group from 10- formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate (195 aa)
   
 
  0.913
gcvT
Aminomethyltransferase; The glycine cleavage system catalyzes the degradation of glycine (366 aa)
   
 
  0.911
purH
Bifunctional purine biosynthesis protein PurH; purH- phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase (511 aa)
     
  0.910
phhA
annotation not available (584 aa)
         
  0.902
metH
metH- methionine synthase (1132 aa)
   
 
    0.900
folP
Dihydropteroate synthase; Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives (277 aa)
   
   
  0.887
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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