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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
npdANAD-dependent deacetylase activates the enzyme acetyl-CoA synthetase by deacetylating its catalytic Lysine in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. It binds one zinc ion as a cofactor. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the sirtuin family. Class III subfamily. (230 aa)    
Predicted Functional Partners:
nadR
Nicotinamide-nucleotide adenylyltransferase / Ribosylnicotinamide kinase; Bifunctional enzyme involved in the nicotinate and nicotinamide metabolism possessing both NMN (nicotinamide mononucleotide) adenylytransferase (NMNAT) and Ribosylnicotinamide kinase (RNK) activities. NMNAT is an indispensable activity in the biosynthesis of NAD(+) and NADP(+) synthesizing NAD via the salvage pathway. RNK converts the N-ribosylnicotinamide to nicotinamide ribonucleotide; Localized in the cytoplasm. However, this bifunctional enzyme would loosely associate with the membrane through its interaction [...]
   
 
 0.989
nadD
Nicotinate-nucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
   
 0.928
nadE
NH(3)-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
    
 0.922
ppnK
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.
  
 
 0.919
punA
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.
    
 0.913
CAZ94118.1
Conserved hypothetical protein. Localized in the cytoplasm.
       0.713
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 0.706
gdhA1
Glutamate dehydrogenase catalyzes the NAD- and/or NADP-dependent reversible deamination of L-glutamate into alpha-ketoglutarate. It is involved with either ammonia assimilation or glutamate catabolism. Forms a homohexamer and binds one NAD(P) cofactor by subunit. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
   
 0.630
gdhA2
Glutamate dehydrogenase catalyzes the NAD- and/or NADP-dependent reversible deamination of L-glutamate into alpha-ketoglutarate. It is involved with either ammonia assimilation or glutamate catabolism. Forms a homohexamer and binds one NAD(P) cofactor by subunit. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
   
 0.630
CAZ94970.1
NAD(P)-dependent dehydrogenase distantly related to glutamate dehydrogenase; Localized in the cytoplasm; Specificity unclear; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
   
 0.630
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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