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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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glnDUridylyltransferase; 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. (872 aa)    
Predicted Functional Partners:
glnB
Regulatory protein (P-II) for nitrogen assimilation by glutamine synthetase (ATase); Function of homologous gene experimentally demonstrated in an other organism; regulator; Belongs to the P(II) protein family.
 
 
 0.977
dapD-2
2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase; Function of strongly homologous gene; enzyme; Belongs to the transferase hexapeptide repeat family.
     
 0.871
glnE
Adenylyl transferase for glutamine synthetase; 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 trans [...]
 
   
 0.822
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.
  
    0.801
gltB
Glutamate synthase, large subunit, GOGAT; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
     
 0.784
glnK
Nitrogen regulatory protein P-II; Function of homologous gene experimentally demonstrated in an other organism; regulator; Belongs to the P(II) protein family.
 
 
 
 0.779
rpsB
30S ribosomal subunit protein S2; Function of homologous gene experimentally demonstrated in an other organism; structural protein; Belongs to the universal ribosomal protein uS2 family.
     
 0.662
ecfK
Putative outer membrane protein assembly factor; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
 
    0.655
glnL
Two-component system, NtrC family, nitrogen regulation sensor histidine kinase GlnL; Function of homologous gene experimentally demonstrated in an other organism; regulator.
  
 
 
 0.644
glnA
Glutamine synthetase; Function of homologous gene experimentally demonstrated in an other organism; enzyme.
 
   
 0.634
Your Current Organism:
Pseudoalteromonas haloplanktis
NCBI taxonomy Id: 326442
Other names: P. haloplanktis TAC125, Pseudoalteromonas haloplanktis TAC125, Pseudoalteromonas haloplanktis str. TAC125, Pseudoalteromonas haloplanktis strain TAC125
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