close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
argFOrnithine carbamoyltransferase; Catalyzes the transfer of the carbamoyl group from carbamoyl phosphate to the delta-amino group of N(2)-acetyl-L-ornithine to produce N(2)-acetyl-L-citrulline. This is a step in an alternative arginine biosynthesis pathway. The enzyme has no activity with ornithine. (339 aa)    
Predicted Functional Partners:
argG
Argininosuccinate synthase; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the argininosuccinate synthase family. Type 1 subfamily.
 
 
 0.998
argH
Argininosuccinate lyase; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.
 
  
 0.997
argC
N-acetyl-gamma-glutamyl-phosphate reductase; Catalyzes the NADPH-dependent reduction of N-acetyl-5- glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.
 
  
 0.997
argB
Acetylglutamate kinase; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.
 
  
 0.997
argD
Acetylornithine aminotransferase; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
 
 0.992
argE
Acetylornithine deacetylase; Catalyzes the deacetylation of N-acetyl-L-citrulline to produce L-citrulline. This is a step in an alternative arginine biosynthesis pathway. Is also able to catalyze the deacetylation of N-acetylornithine in vitro, with almost equal velocity. However, this reaction may be not relevant in vivo since Xanthomonas does not possess the canonical argF gene and cannot convert ornithine to citrulline via ArgF'.
 
 
 0.986
carB
Carbamoyl-phosphate synthase large chain; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark.
 
 
 0.932
carA
Carbamoyl-phosphate synthase small chain; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the CarA family.
  
 
 0.910
pyrB
Aspartate carbamoyltransferase; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
    
0.852
XCC2381
L-lysine 6-aminotransferase; Identified by sequence similarity; putative; ORF located using Blastx/Glimmer/Genemark; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
 
  
 0.831
Your Current Organism:
Xanthomonas campestris
NCBI taxonomy Id: 190485
Other names: X. campestris pv. campestris str. ATCC 33913, Xanthomonas campestris pv. campestris str. ATCC 33913
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.