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
EGW23155.1PFAM: Asparaginase/glutaminase; KEGG: pjd:Pjdr2_5900 asparaginase/glutaminase. (338 aa)    
Predicted Functional Partners:
EGW21964.1
KEGG: mca:MCA2039 glutamate synthase, large subunit; PFAM: Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, central-C; Glutamate synthase, alpha subunit, C-terminal.
    
 0.934
EGW20594.1
Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; In the C-terminal section; belongs to the aldehyde dehydrogenase family.
   
 
 0.897
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).
    
 0.886
gatB
Aspartyl/glutamyl-tRNA(Asn/Gln) 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.
    
 0.870
glnS
PFAM: Glutamyl/glutaminyl-tRNA synthetase, class Ic, catalytic domain; Glutamyl/glutaminyl-tRNA synthetase, class Ic, anti-codon binding domain; TIGRFAM: Glutaminyl-tRNA synthetase, class Ic; HAMAP: Glutaminyl-tRNA synthetase; KEGG: gpb:HDN1F_33480 glutaminyl-tRNA synthetase.
  
 
 0.849
gatC
Aspartyl/glutamyl-tRNA(Asn/Gln) 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.
    
  0.840
gcvP
Glycine dehydrogenase (decarboxylating); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.
     
 0.838
EGW21526.1
L-aspartate oxidase; Catalyzes the oxidation of L-aspartate to iminoaspartate.
   
 
 0.814
EGW22674.1
KEGG: mca:MCA2202 aspartate aminotransferase; PFAM: Aminotransferase, class I/II.
    
 0.798
argG
PFAM: Argininosuccinate synthase; TIGRFAM: Argininosuccinate synthase; HAMAP: Argininosuccinate synthase; KEGG: mca:MCA1099 argininosuccinate synthase; Belongs to the argininosuccinate synthase family. Type 1 subfamily.
   
 
 0.794
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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