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glnD protein (Alcaligenes faecalis) - STRING interaction network
"glnD" - Bifunctional uridylyltransferase/uridylyl-removing enzyme in Alcaligenes faecalis
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Predicted Interactions
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textmining
co-expression
protein homology
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glnDBifunctional 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)    
Predicted Functional Partners:
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)
 
  0.948
JT27_13420
Methionine aminopeptidase; Derived by automated computational analysis using gene prediction method- Protein Homology (267 aa)
 
        0.903
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 [...] (918 aa)
   
   
  0.859
JT27_13430
UPF0056 membrane protein; Derived by automated computational analysis using gene prediction method- Protein Homology (237 aa)
              0.852
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)
 
 
  0.755
JT27_13435
Disulfide bond formation protein DsbB; Derived by automated computational analysis using gene prediction method- Protein Homology (153 aa)
         
  0.732
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)
 
   
  0.724
JT27_16905
Ammonium transporter; Derived by automated computational analysis using gene prediction method- Protein Homology (413 aa)
 
   
  0.691
JT27_13325
Phosphoenolpyruvate synthase; Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate; Belongs to the PEP-utilizing enzyme family (788 aa)
     
   
  0.621
argA
Amino-acid acetyltransferase; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the acetyltransferase family. ArgA subfamily (451 aa)
   
   
  0.587
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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