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:
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Gene Fusion
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[Homology]
Score
glnIIGlutamine synthetase (GS), also known as Glutamate-ammonia ligase, plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine. Belongs to the GS class II which is usually found in eukaryotes and in bacteria belonging to the Rhizobiaceae, Frankiaceae, and Streptomycetaceae families. GSII are octamer of identical subunits. Localized in the cytoplasm; High confidence in function and specificity. (338 aa)    
Predicted Functional Partners:
gltA-2
Glutamate synthase [NADPH] large chain; Glutamate synthase is a key enzyme in the early stages of the assimilation of ammonia. It is a complex iron-sulfur flavoprotein catalyzing the reductive transfer of the amido nitrogen from L-glutamine to 2-oxoglutarate to form two molecules of L-glutamate via intramolecular channelling of ammonia from the amidotransferase domain to the FMN-binding domain. Glutamate synthase forms an aggregate of 4 catalytic active heterodimers, consisting of a large and a small subunit (GltB). GltA binds as cofactors a 3Fe-4S cluster, a FAD and a FMN. Localized i [...]
  
 
 0.984
glnA
Glutamine synthetase (GS), also known as Glutamate-ammonia ligase, plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine. Belongs to the GS class III which includes GS from Bacteroides fragilis and Butyrivibrio fibrisolvens. GSIII enzymes are much larger (about 700 amino acids) than the GSI (450 to 470 amino acids) or GSII (350 to 420 amino acids) enzymes. It forms a hexamer. Localized in the cytoplasm; High confidence in function and specificity.
    
 0.958
glmS
Glucosamine--fructose-6-phosphate aminotransferase; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
  
 
 0.938
gltB
Glutamate synthase [NADPH] small chain; Glutamate synthase is a key enzyme in the early stages of the assimilation of ammonia. It is a complex iron-sulfur flavoprotein catalyzing the reductive transfer of the amido nitrogen from L-glutamine to 2-oxoglutarate to form two molecules of L-glutamate via intramolecular channelling of ammonia from the amidotransferase domain to the FMN-binding domain. Glutamate synthase forms an aggregate of 4 catalytic active heterodimers, consisting of a large (GltA) and a small subunit. GltB binds NADP(H) as a cofactor. Localized in the cytoplasm; High con [...]
  
 
 0.938
carA
Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the CarA family.
  
 
 0.930
purF
Amidophosphoribosyltransferase catalyzes the first step in purine biosynthesis: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O. PurF belongs to the Class-II glutamine amidotransferase family. It forms a homotetramer and binds one magnesium ion per subunit. Localized in the cytoplasm; High confidence in function and specificity.
    
 0.921
glsA
Glutaminase catalyzes the reaction: L-glutamine + H2O = L-glutamate + NH3. Localized in the cytoplasm; High confidence in function and specificity.
    
 0.920
CAZ97894.1
The ATP-grasp proteins catalyze the Magnesium- and ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule. They contribute predominantly to macromolecular synthesis. ATP-hydrolysis is used to activate a substrate; Binds 3 manganese ions; Localized in the cytoplasm; Function unclear.
  
 
 0.919
carB
Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. It is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. Binds three magnesium ion as cofactor. Localized in the cytoplasm; High confidence in function and specificity.
  
 
 0.919
nirB
Nitrite reductase, required for nitrite assimilation (reducing nitrite to ammonia), catalyzes the second step of nitrate assimilation (denitrification); Binds 1 siroheme and 1 2Fe-2S cluster, uses FAD as cofactor; It is an homodimer which associates with nirD; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family; Localized in the cytoplasm; High confidence in function and specificity.
    
 0.917
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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