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
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[Homology]
Score
argJBifunctional ornithine acetyltransferase/N-acetylglutamate synthase; 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. (406 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.
 
 0.999
argA
Amino-acid N-acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the acetyltransferase family. ArgA subfamily.
 
 0.997
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.
 
 
 0.997
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.
 
 
 0.985
argD
Bifunctional succinylornithine transaminase/acetylornithine transaminase; DapATase; bifunctional enzyme that functions in arginine and lysine biosynthetic pathways; catalyzes the formation of N-acetyl-L-glutamate 5-semialdehyde from 2-oxoglutarate and N(2)-acetyl-L-ornithine or N-succinyl-2-L-amino-6-oxoheptanedioate from 2-oxoglutarate and N-succinyl-L-2,6-diaminoheptanedioate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
 
 
 0.972
argD-2
Bifunctional succinylornithine transaminase/acetylornithine transaminase; DapATase; bifunctional enzyme that functions in arginine and lysine biosynthetic pathways; catalyzes the formation of N-acetyl-L-glutamate 5-semialdehyde from 2-oxoglutarate and N(2)-acetyl-L-ornithine or N-succinyl-2-L-amino-6-oxoheptanedioate from 2-oxoglutarate and N-succinyl-L-2,6-diaminoheptanedioate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
 
 
 0.972
argH
Argininosuccinate lyase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.960
argE
Acetylornithine deacetylase (ArgE); Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.927
OEY97664.1
Glutamate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
     
 0.922
OEY97442.1
Glutamate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
     
 0.922
Your Current Organism:
Acinetobacter qingfengensis
NCBI taxonomy Id: 1262585
Other names: A. qingfengensis, Acinetobacter qingfengensis Li et al. 2014, Acinetobacter sp. 2BJ-1, Acinetobacter sp. 2C-3-1, Acinetobacter sp. HF5-2, CFCC 10890, KCTC 32225, strain 2BJ1
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