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nadA protein (Bacillus cereus) - STRING interaction network
"nadA" - Quinolinate synthase A 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
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textmining
co-expression
protein homology
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Score
nadAQuinolinate synthase A; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate (368 aa)    
Predicted Functional Partners:
nadB
L-aspartate oxidase; Catalyzes the oxidation of L-aspartate to iminoaspartate (509 aa)
 
  0.999
nadC
Putative nicotinate-nucleotide pyrophosphorylase [carboxylating]; nadC- nicotinate-nucleotide diphosphorylase; Belongs to the NadC/ModD family (277 aa)
 
 
  0.998
nadR
annotation not available (180 aa)
 
     
  0.897
birA
Bifunctional ligase/repressor BirA; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor (326 aa)
         
  0.790
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity (877 aa)
         
  0.772
nifS_1
annotation not available (380 aa)
 
   
  0.713
cinA
cinA_cterm- competence/damage-inducible CinA C-terminal domain protein; Belongs to the CinA family (412 aa)
         
  0.689
rfbC
dTDP-4-dehydrorhamnose 3,5-epimerase; Catalyzes the epimerization of the C3’ and C5’positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4- hexulose; Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family (181 aa)
         
  0.675
nadD
Probable nicotinate-nucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD) (189 aa)
         
  0.671
lipA
Lipoyl synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (298 aa)
           
  0.664
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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