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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
AEB85801.1PFAM: Amidase; KEGG: ajs:Ajs_2586 amidase; Belongs to the amidase family. (448 aa)    
Predicted Functional Partners:
gatB
glutamyl-tRNA(Gln) amidotransferase, B subunit; 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
glutamyl-tRNA(Gln) amidotransferase, C subunit; 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.
 
 0.992
glnS
TIGRFAM: Glutaminyl-tRNA synthetase, class Ic; KEGG: ajs:Ajs_1608 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain.
  
 0.952
gatA
Glutamyl-tRNA(Gln) 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).
 
  
 
0.931
AEB82672.1
PFAM: Amidase; KEGG: reh:H16_A1882 Asp-tRNA Asn / Glu-tRNA Gln amidotransferase A subunit or related amidase.
  
  
 
0.928
AEB83347.1
PFAM: Amidase; KEGG: dia:Dtpsy_0815 amidase.
  
  
 
0.928
AEB85526.1
Urea amidolyase related protein; SMART: Allophanate hydrolase subunit 2; Allophanate hydrolase subunit 1; TIGRFAM: Allophanate hydrolase subunit 2; Conserved hypothetical protein CHP00370; KEGG: reu:Reut_A2450 allophanate hydrolase subunit 2; PFAM: Allophanate hydrolase subunit 2; Allophanate hydrolase subunit 1.
    
 0.772
aspS
aspartyl-tRNA synthetase; 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.
 
 
 0.656
AEB85802.1
KEGG: ajs:Ajs_2587 D-amino-acid dehydrogenase; PFAM: FAD dependent oxidoreductase.
  
  
 0.637
AEB86943.1
Biotin carboxylase; PFAM: Carbamoyl-phosphate synthetase, large subunit, ATP-binding; Biotin carboxylase, C-terminal; Carbamoyl-phosphate synthase, large subunit, N-terminal; KEGG: dac:Daci_1096 carbamoyl-phosphate synthase subunit L; SMART: Biotin carboxylase, C-terminal.
    
 0.595
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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