STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
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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Gene Fusion
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[Homology]
Score
srtNSirtuin NAD-dependent deacetylase; NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form; Belongs to the sirtuin family. Class U subfamily. (247 aa)    
Predicted Functional Partners:
acuC
Protein deacetylase; Role in growth and sporulation on acetoin or butanediol. Involved in the breakdown of these compounds used as a carbon source; Belongs to the histone deacetylase family.
    
 
 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.
   
 0.949
acsA
acetyl-CoA synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA (By similarity). Has a role in growth and sporulation on acetate.
    
 0.944
ytcI
Putative acyl-coenzyme A synthetase; 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 ATP-dependent AMP-binding enzyme family.
  
 0.940
ppnKA
Inorganic polyphosphate/ATP-NAD kinase; 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.
  
 
 0.930
deoD
Purine nucleoside phosphorylase; Cleavage of adenosine and its derivatives; Belongs to the PNP/UDP phosphorylase family.
    
 0.928
nadE
Ammonium-dependent NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
    
 0.927
ppnKB
Inorganic polyphosphate/ATP-NAD kinase; 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.
  
 
 0.927
acuA
Protein acetyltransferase; Part of the acuABC operon, which is possibly involved in the breakdown of acetoin and butanediol. Acts as an acetyltransferase inactivating acetyl-CoA synthetase AcsA via acetylation at a Lys residue.
     
 0.920
pupG
Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine, inosine, 2'-deoxyguanosine and 2'-deoxyinosine.
    
 0.915
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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