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glnE protein (Alcaligenes faecalis) - STRING interaction network
"glnE" - Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme in Alcaligenes faecalis
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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glnEBifunctional 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 [...] (918 aa)    
Predicted Functional Partners:
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 (859 aa)
   
   
  0.859
glnA
Forms 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 (470 aa)
 
     
  0.846
JT27_17500
Uncharacterized protein; Derived by automated computational analysis using gene prediction method- Protein Homology (1201 aa)
 
          0.774
JT27_09125
Alkyl hydroperoxide reductase; Derived by automated computational analysis using gene prediction method- Protein Homology (155 aa)
            0.705
queH
Epoxyqueuosine reductase QueH; Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr) (232 aa)
              0.665
JT27_13705
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)
 
 
  0.584
AFA_12530
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)
 
 
  0.584
JT27_16905
Ammonium transporter; Derived by automated computational analysis using gene prediction method- Protein Homology (413 aa)
         
  0.542
JT27_02830
Thiol-disulfide interchange protein; Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process (243 aa)
   
        0.496
JT27_09000
ATP-dependent helicase; Derived by automated computational analysis using gene prediction method- Protein Homology (1263 aa)
   
   
  0.496
Your Current Organism:
Alcaligenes faecalis
NCBI taxonomy Id: 511
Other names: A. faecalis, ATCC 8750, Alcaligenes faecalis, 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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