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
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
nadENH(3)-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. (300 aa)    
Predicted Functional Partners:
nadD
Nicotinate-nucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
 
 
 0.942
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 [...]
    
 0.937
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.
    
 0.930
npdA
NAD-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.
    
 0.922
gldC
Gliding motility protein; GldC is not absolutely required for gliding motility but enhances colony spreading; Localized in the cytoplasm; Function unclear.
       0.667
gldB
Lipoprotein involved in the gliding motility; It is possible that GldB interacts with, or is involved in production of polysaccharides or glycoproteins; Signal peptide cleaved between the residues 16 and 17; Putatively localized in the cytoplasmic membrane; Function unclear.
       0.667
serA2
D-3-phosphoglycerate dehydrogenase; SerA catalyzes the conversion of 3-phosphoglycerate to 3-phosphonooxypyruvate, which is the first step of the serine biosynthesis pathway. SerA2 is composed of a substrate-binding domain (D-isomer specific 2-hydroxyacid dehydrogenase family) and a NAD-binding domain (Rossman fold). Localized in the cytoplasm; High confidence in function and specificity.
 
   
 0.574
CAZ95405.1
Conserved hypothetical protein; Protein that displays similarity with the C-terminal region of the transcriptional regulator nadR; Localized in the cytoplasm.
     
 0.555
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP.
     
 0.529
cinA
Conserved protein belonging to the CinA family. Contains a N-terminal molybdopterin binding domain and a C-terminal Competence-damaged domain. CinA is the first gene in the competence-inducible (cin) operon, and is thought to be specifically required at some stage in the process of transformation. Localized in the cytoplasm; Function unclear.
     
 0.517
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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