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glnD glnD VS_2333 VS_2333 VS_2520 VS_2520 VS_2275 VS_2275 glnE glnE VS_0119 VS_0119 map map cca cca gltB gltB VS_0472 VS_0472 VS_0474 VS_0474
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query proteins and first shell of interactors
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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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experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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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 assimilation and metabolism. (873 aa)    
Predicted Functional Partners:
VS_2333
Nitrogen regulatory protein P-II; Belongs to the P(II) protein family.
 
 
 0.942
VS_2520
Nitrogen regulatory protein P-II; Belongs to the P(II) protein family.
 
 
 0.918
VS_2275
Putative nitrogen regulatory protein P-II family protein.
   
 0.855
glnE
Glutamine synthetase 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 transducti [...]
 
   
 0.777
VS_0119
Nitrogen regulation protein ntrB.
  
 
 
 0.648
map
Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
  
    0.581
cca
Multifunctional CCA protein; Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic phosphodiesterase activities. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases.
    
  0.563
gltB
Glutamate synthase, large subunit.
     
 0.538
VS_0472
Putative glutamate synthase precursor; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
     
 0.538
VS_0474
Glutamate synthase [NADPH] large chain.
     
 0.538
Your Current Organism:
Vibrio tasmaniensis
NCBI taxonomy Id: 575788
Other names: V. tasmaniensis LGP32, Vibrio lentus MEL32, Vibrio splendidus LGP32, Vibrio tasmaniensis LGP32
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