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nagA_1 protein (Bacillus cereus) - STRING interaction network
"nagA_1" - nagA: N-acetylglucosamine-6-phosphate deacetylase in Bacillus cereus
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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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nagA_1nagA- N-acetylglucosamine-6-phosphate deacetylase; Belongs to the metallo-dependent hydrolases superfamily. NagA family (380 aa)    
Predicted Functional Partners:
nagB
Glucosamine-6-phosphate deaminase; Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion (262 aa)
  0.999
murQ
N-acetylmuramic acid 6-phosphate etherase; Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6- phosphate and D-lactate (294 aa)
   
  0.987
yvoA
annotation not available (225 aa)
 
     
  0.975
glmS
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source (600 aa)
       
  0.954
ptsG
annotation not available (687 aa)
   
  0.830
fruA
annotation not available (619 aa)
         
  0.777
nagE
PTS-II-BC-nag- PTS system, N-acetylglucosamine-specific IIBC component (500 aa)
     
  0.777
glmM
Phosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate; Belongs to the phosphohexose mutase family (448 aa)
     
   
  0.718
nfo
Probable endonuclease 4; Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5’-ends that are base-free deoxyribose 5-phosphate residues. It preferentially attacks modified AP sites created by bleomycin and neocarzinostatin (298 aa)
         
  0.676
murR
annotation not available (287 aa)
 
     
  0.646
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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