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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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glnEHypothetical protein; 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 transduction protein PII (GlnB [...] (1063 aa)    
Predicted Functional Partners:
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.
 
   
 0.844
glnD
protein-PII uridylyltransferase; 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.
 
   
 0.840
KKB63066.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
     0.675
KKB62644.1
ATP-dependent helicase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
   
 0.595
KKB65285.1
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.
 
 
 
 0.540
KKB61380.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the P(II) protein family.
 
 
 
 0.530
tldD
Protease TldD; Responsible for the proteolytic maturation of the E. coli pMccB17 plasmid-encoded microcin B17, an exported protein that targets the essential topoisomerase II DNA gyrase; degrades the E. coli plasmid F-encoded CcdA; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.521
nadE
NAD synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
     
 0.499
guaA
GMP synthase; Catalyzes the synthesis of GMP from XMP.
     
 0.499
nadE-2
NAD synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
     
 0.499
Your Current Organism:
Robbsia andropogonis
NCBI taxonomy Id: 28092
Other names: ATCC 19311 [[Pseudomonas woodsii]], ATCC 23061, Aplanobacter stizolobii, Bacterium andropogoni, Bacterium woodsii, Burkholderia andropogonis, CCUG 32772, CFBP 2421, CIP 105771, DSM 9511, DSM 9884 [[Pseudomonas woodsii]], IBSBF 199, ICMP 2807, ICMP 3967 [[Pseudomonas woodsii]], JCM 10487, LMG 2129, LMG 2362 [[Pseudomonas woodsii]], LMG:2129, LMG:2362 [[Pseudomonas woodsii]], NCPPB 934, NCPPB 968 [[Pseudomonas woodsii]], NRRL B-14296, Paraburkholderia andropogonis, Pseudomonas andropogonis, Pseudomonas stizolobii, Pseudomonas woodsii, R. andropogonis, strain PW 102 [[Pseudomonas woodsii]]
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