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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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GlnBNitrogen regulatory protein P-II. (92 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.
 
 
 0.998
Amt
Ammonium transporter integral membrane protein.
 
 
 0.998
argB
Acetylglutamate kinase; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily.
  
 
 
 0.915
GltB
Glutamate synthase large subunit.
  
  
 0.848
GlnA1
Glutamine synthetase; Overlaps another CDS with the same product name.
 
 
 0.810
RN09_2730
Glutamine synthetase; Overlaps another CDS with the same product name.
 
 
 0.771
GlnA2
Glutamine synthetase.
  
 
 0.753
GlnA4
Glutamine synthetase.
  
 
 0.739
RN09_2732
Glutamate-ammonia-ligase adenylyltransferase; 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 region of GlnE binds the signal transd [...]
 
 
 
 0.697
nadE
Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
  
  
 0.689
Your Current Organism:
Mycobacterium tuberculosis variant africanum
NCBI taxonomy Id: 33894
Other names: ATCC 25420, CIP 105147, M. tuberculosis variant africanum, Mycobacterium africanum
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