STRINGSTRING
gatC gatC gatA gatA gatB gatB Dde_0518 Dde_0518 asnS asnS glnS glnS aspS aspS dapA dapA rpsZ rpsZ Dde_3237 Dde_3237 guaA guaA
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Score
gatCglutamyl-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. (94 aa)    
Predicted Functional Partners:
gatA
glutamyl-tRNA(Gln) amidotransferase, A subunit; 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).
 
 0.999
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.
 
 0.999
Dde_0518
PFAM: Amidase; KEGG: mxa:MXAN_2852 amidase family protein; Belongs to the amidase family.
 
 
 0.982
asnS
TIGRFAM: Asparaginyl-tRNA synthetase, class IIb; KEGG: dvu:DVU0007 asparaginyl-tRNA synthetase; PFAM: Aminoacyl-tRNA synthetase, class II (D/K/N); Nucleic acid binding, OB-fold, tRNA/helicase-type.
   
 0.976
glnS
TIGRFAM: Glutaminyl-tRNA synthetase, class Ic; KEGG: dvm:DvMF_1485 glutaminyl-tRNA synthetase; PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain.
  
 
 0.924
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.
  
 
 0.901
dapA
Dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
  
  
 0.790
rpsZ
Ribosomal protein S14; Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
   
    0.786
Dde_3237
SMART: Pyruvate-flavodoxin oxidoreductase, EKR domain; TIGRFAM: Pyruvate-flavodoxin oxidoreductase; KEGG: dvl:Dvul_0348 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal; Pyruvate-flavodoxin oxidoreductase, EKR domain; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; Thiamine pyrophosphate enzyme, C-terminal TPP-binding; Pyruvate/ketoisovalerate oxidoreductase; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family.
   
 
 0.762
guaA
GMP synthase, large subunit; Catalyzes the synthesis of GMP from XMP.
  
 
 0.718
Your Current Organism:
Desulfovibrio alaskensis
NCBI taxonomy Id: 207559
Other names: D. alaskensis G20, Desulfovibrio alaskensis G20, Desulfovibrio alaskensis str. G20, Desulfovibrio alaskensis strain G20, Desulfovibrio desulfuricans subsp. desulfuricans str. G20
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