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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
AQS73307.1Amidase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the amidase family. (495 aa)    
Predicted Functional Partners:
gatB
aspartyl/glutamyl-tRNA amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily.
 
 0.997
gatC
asparaginyl/glutamyl-tRNA amidotransferase subunit C; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family.
 
 0.990
gatA
aspartyl/glutamyl-tRNA amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln).
  
  
 
0.951
AQS73477.1
glutaminyl-tRNA synthase (glutamine-hydrolyzing) subunit A; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the amidase family.
  
  
 
0.927
speB
Agmatinase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the arginase family.
     
  0.499
AQS74699.1
Amidase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 
0.454
aspS
aspartate--tRNA ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
 
 0.442
AQS73308.1
Proton-motive-force-driven choline transporter; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the BCCT transporter (TC 2.A.15) family.
       0.435
pfkB
1-phosphofructokinase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the carbohydrate kinase PfkB family.
   
    0.424
AQS74695.1
tRNA glutamyl-Q synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
 0.419
Your Current Organism:
Corynebacterium ammoniagenes
NCBI taxonomy Id: 1697
Other names: ATCC 6871, Bacterium ammoniagenes, Brevibacterium ammoniagenes, Brevibacterium sp. NCIM 2268, C. ammoniagenes, CCUG 38796, CIP 101283, Corynebacterium ammoniigenes, DSM 20306, IFO 12612, NBRC 12612, NCCB 60030, NCIB 8143, NCIB:8143, NCIMB 8143, VKM B-672
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