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glnA protein (Agrobacterium rhizogenes) - STRING interaction network
"glnA" - Forms a homododecamer in Agrobacterium rhizogenes
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textmining
co-expression
protein homology
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glnAForms a homododecamer; forms glutamine from ammonia and glutamate with the conversion of ATP to ADP and phosphate; also functions in the assimilation of ammonia; highly regulated protein controlled by the addition/removal of adenylyl groups by adenylyltransferase from specific tyrosine residues; addition of adenylyl groups results in inactivation of the enzyme; Derived by automated computational analysis using gene prediction method- Protein Homology (469 aa)    
Predicted Functional Partners:
CN09_01825
Glutamate synthase; Derived by automated computational analysis using gene prediction method- Protein Homology (1574 aa)
   
   
  0.999
CN09_07490
Nitrogen regulatory protein P-II 1; Indirectly regulates nitrogen metabolism; at high nitrogen levels P-II prevents the phosphorylation of NR-I, the transcriptional activator of the glutamine synthetase gene (glnA); at low nitrogen levels P-II is uridylylated to form PII-UMP and interacts with an adenylyltransferase (GlnE) that activates GlnA; Derived by automated computational analysis using gene prediction method- Protein Homology (112 aa)
 
 
  0.987
gltD
Glutamate synthase is composed of subunits alpha and beta; beta subunit is a flavin adenine dinucleotide-NADPH dependent oxidoreductase; provides electrons to the alpha subunit, which binds L-glutamine and 2-oxoglutarate and forms L-glutamate; Derived by automated computational analysis using gene prediction method- Protein Homology (484 aa)
   
 
  0.986
carB
Carbamoyl-phosphate synthase large chain; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the CarB family (1161 aa)
 
 
  0.946
CN09_07755
ATPase; Derived by automated computational analysis using gene prediction method- Protein Homology (385 aa)
   
   
  0.911
CN09_28470
Nitrogen regulatory protein P-II 1; Indirectly regulates nitrogen metabolism; at high nitrogen levels P-II prevents the phosphorylation of NR-I, the transcriptional activator of the glutamine synthetase gene (glnA); at low nitrogen levels P-II is uridylylated to form PII-UMP and interacts with an adenylyltransferase (GlnE) that activates GlnA; Derived by automated computational analysis using gene prediction method- Protein Homology (116 aa)
 
 
  0.900
glnE
Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory regi [...] (986 aa)
 
     
  0.899
glnD
Bifunctional uridylyltransferase/uridylyl-removing enzyme; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism (971 aa)
 
     
  0.893
CN09_28465
Ammonium transporter; Derived by automated computational analysis using gene prediction method- Protein Homology (453 aa)
   
   
  0.883
gltA
Citrate synthase; Type II enzyme; in Escherichia coli this enzyme forms a trimer of dimers which is allosterically inhibited by NADH and competitively inhibited by alpha-ketoglutarate; allosteric inhibition is lost when Cys206 is chemically modified which also affects hexamer formation; forms oxaloacetate and acetyl-CoA and water from citrate and coenzyme A; functions in TCA cycle, glyoxylate cycle and respiration; enzyme from Helicobacter pylori is not inhibited by NADH; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the citrate [...] (429 aa)
 
   
  0.867
Your Current Organism:
Agrobacterium rhizogenes
NCBI taxonomy Id: 359
Other names: A. rhizogenes, ATCC 11325, Agrobacterium biovar 2, Agrobacterium genomic group 10, Agrobacterium genomic species 10, Agrobacterium genomosp. 10, Agrobacterium rhizogenes, Agrobacterium rhizogenes (RI plasmid PRI1724), Agrobacterium rhizogenes (RI plasmid PRI8196), Agrobacterium rhizogenes (RI plasmid PRIA4B), CFBP 5520, CIP 104328, DSM 30148, ICMP 5794, IFO 13257, JCM 20919, LMG 150, NBRC 13257, NCPPB 2991, Rhizobium rhizogenes, Rhizobium sp. LMG 9509
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