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
argJOrnithine acetyltransferase; 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. (408 aa)    
Predicted Functional Partners:
argA
N-acetylglutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the acetyltransferase family. ArgA subfamily.
 
 0.999
argB
Acetylglutamate kinase; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily.
 
 0.999
argD
Acetylornithine aminotransferase; DapATase; functions in arginine biosynthetic pathway; catalyzes the formation of N-acetyl-L-glutamate 5-semialdehyde from 2-oxoglutarate and N(2)-acetyl-L-ornithine; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
 
 
 0.998
argF
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.
 
 
 0.998
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
argH
Argininosuccinate lyase; Catalyzes the formation of arginine from (N-L-arginino)succinate; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.981
argG
Argininosuccinate synthase; Catalyzes the formation of arginosuccinate from citrulline and aspartate in arginine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the argininosuccinate synthase family. Type 2 subfamily.
  
  
 0.952
argE
Acetylornithine deacetylase; Catalyzes the formation of L-ornithine from N(2)-acetyl-L-ornithine; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.926
ALO37151.1
Converts 2-oxoglutarate to glutamate; in Escherichia coli this enzyme plays a role in glutamate synthesis when the cell is under energy restriction; uses NADPH; forms a homohexamer; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
     
 0.918
ALO38488.1
Glutamate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
     
 0.918
Your Current Organism:
Alcaligenes faecalis
NCBI taxonomy Id: 511
Other names: A. faecalis, ATCC 8750, Achromobacter sp. ATCC8750, Alcaligenes sp. BP11, CIP 55.84, CIP 60.80, DSM 30030, IAM 12369, IFO 13111, JCM 20522, JCM 20663, NBRC 13111, NCAIM B.01104, NCIMB 8156, NCTC 11953
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