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
argCN-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 2 subfamily. (304 aa)    
Predicted Functional Partners:
argB
Acetylglutamate kinase; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily.
 0.998
argD
TIGRFAM: acetylornithine and succinylornithine aminotransferase; PFAM: aminotransferase class-III; KEGG: bid:Bind_0150 acetylornithine and succinylornithine aminotransferase; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
 
 
 0.977
argJ
Arginine biosynthesis bifunctional protein ArgJ; Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. Belongs to the ArgJ family.
 
  
 0.976
argH
TIGRFAM: argininosuccinate lyase; PFAM: fumarate lyase; KEGG: met:M446_5988 argininosuccinate lyase.
 
  
 0.967
arcB
Ornithine carbamoyltransferase; Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline; Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.
 
  
 0.961
argG
PFAM: argininosuccinate synthase; KEGG: bid:Bind_1273 argininosuccinate synthase; Belongs to the argininosuccinate synthase family. Type 1 subfamily.
  
  
 0.956
glgC
Glucose-1-phosphate adenylyltransferase; Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc; Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family.
  
  
 0.876
carB
TIGRFAM: carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain ATP-binding; Carbamoyl-phosphate synthetase large chain oligomerisation; Carbamoyl-phosphate synthetase large chain domain protein; MGS domain protein; KEGG: bid:Bind_0869 carbamoyl-phosphate synthase, large subunit; Belongs to the CarB family.
  
  
 0.737
Msil_1014
TIGRFAM: acetylornithine deacetylase (ArgE); PFAM: peptidase M20; peptidase dimerisation domain protein; KEGG: bid:Bind_1040 acetylornithine deacetylase (ArgE).
  
 
 0.729
Msil_1660
TIGRFAM: ornithine aminotransferase; PFAM: aminotransferase class-III; KEGG: bid:Bind_2814 ornithine aminotransferase; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
  
  
 0.701
Your Current Organism:
Methylocella silvestris
NCBI taxonomy Id: 395965
Other names: M. silvestris BL2, Methylocella silvestris BL2, Methylocella silvestris str. BL2, Methylocella silvestris strain BL2, Methylocella sp. BL2
Server load: low (36%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.