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
aatBAspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity. (415 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 [...]
  
 
 0.941
mdh
Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate.
  
 0.922
argG
Argininosuccinate synthase (AS) is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate; Belongs to the argininosuccinate synthase family, type 1 subfamily; Localized in the cytoplasm; High confidence in function and specificity.
  
 0.921
icdA
Isocitrate dehydrogenase NADP-dependent, monomeric type; NADP(+)-dependent isocitrate dehydrogenase (ICD) is an important enzyme of the intermediary metabolism, as it controls the carbon flux within the citric acid cycle and supplies the cell to 2-oxoglutarate and NADPH for biosynthetic purposes; The activity of this enzyme, which is controlled by phosphorylation, helps regulate carbon flux between the Krebs cycle and the glyoxylate bypass, which is an alternate route that accumulates carbon for biosynthesis when acetate is the sole carbon source for growth; Localized in the cytoplasm; [...]
 
 
 
  0.920
pruA
1-pyrroline-5-carboxylate dehydrogenase is involved in L-proline degradation. It catalyzes the reaction: 1-pyrroline-5-carboxylate + NAD+ + H2O = L-glutamate + NADH. Belongs to the aldehyde dehydrogenase family and uses NAD as cofactor. Localized in the cytoplasm; High confidence in function and specificity.
   
 0.917
metB
The Cystathionine gamma-synthase is found in the Selenoamino acid metabolism pathway and involved in the second step of the methionine biosynthesis; Uses a pyridoxal phosphate group as cofactor, attached to a lysine residue located in the central section of the enzyme; Localized in the cytoplasm; High confidence in function and specificity.
  
 
 0.916
metC
Cystathionine beta-lyase (CBL) is found in the Selenoamino acids metabolism pathway and in methionine and cysteine biosynthesis pathways. It converts (seleno)cystathionine to (seleno)homocysteine but is also able to catalyze an alpha, gamma elimination; Uses a pyridoxal phosphate group as cofactor, attached to a lysine residue located in the central section of the enzyme; Localized in the cytoplasm; High confidence in function and specificity.
  
 
 0.916
aatA-2
Aspartate aminotransferase or Transaminase A or Glutamic-aspartic transaminase or Glutamic-oxaloacetic transaminase converts the L-aspartic acid and the 2-oxoglutarate into L-glutamate and oxaloacetate using the Pyridoxal phosphate as cofactor bound by covalent linkage to a lysine residue; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family; Localized in the cytoplasm; High confidence in function and specificity.
  
  
 
0.916
purA
Adenylosuccinate synthase; Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP; Belongs to the adenylosuccinate synthetase family.
  
 0.915
tyrA
Prephenate dehydrogenase is involved in tyrosine biosynthesis. It catalyzes the reaction: prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH. It uses NAD as a cofactor. Localized in the cytoplam; High confidence in function and specificity.
  
 
 0.915
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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