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ppnKA protein (Bacillus subtilis) - STRING interaction network
"ppnKA" - NAD kinase 1 in Bacillus subtilis
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Predicted Interactions
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textmining
co-expression
protein homology
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ppnKANAD kinase 1; Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2’-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates (GTP, UTP) as well as inorganic polyphosphate (poly(P)) as a source of phosphorus (266 aa)    
Predicted Functional Partners:
nadE
NH(3)-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source (272 aa)
   
 
  0.974
nadD
Nicotinate-nucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD); Belongs to the NadD family (189 aa)
   
 
  0.947
relP
GTP pyrophosphokinase YjbM; Functions as a (p)ppGpp synthase; GDP can be used instead of GTP, resulting in an increase of (p)ppGpp synthesis. The enzyme binds ATP, then GDP or GTP and catalysis is highly cooperative. In eubacteria ppGpp (guanosine 3’-diphosphate 5-’ diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. Probably has a minor role in the stringent response; Belongs to the RelA/SpoT family (211 aa)
 
          0.900
yjbL
UPF0738 protein YjbL; Evidence 3- Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe- putative enzyme; Belongs to the UPF0738 family (122 aa)
 
          0.847
ppnKB
NAD kinase 2; Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2’-hydroxyl of the adenosine moiety of NAD to yield NADP (267 aa)
   
   
0.844
yjbO
Uncharacterized RNA pseudouridine synthase YjbO; Evidence 2b- Function of strongly homologous gene; Product type e- enzyme (283 aa)
              0.790
yjbK
Putative triphosphatase YjbK; Evidence 3- Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe- putative enzyme (190 aa)
 
          0.732
yhcT
Uncharacterized RNA pseudouridine synthase YhcT; Evidence 3- Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe - putative enzyme (302 aa)
         
  0.697
dusC
Probable tRNA-dihydrouridine synthase 2; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines (325 aa)
         
  0.664
nadC
Probable nicotinate-nucleotide pyrophosphorylase [carboxylating]; Involved in the catabolism of quinolinic acid (QA) (289 aa)
         
  0.638
Your Current Organism:
Bacillus subtilis
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis, Bacillus subtilis 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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