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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
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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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glnDprotein-P-II 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. (881 aa)    
Predicted Functional Partners:
VC_2239
Nitrogen regulatory protein P-II; Similar to SP:P11671 PID:43806; identified by sequence similarity; putative; Belongs to the P(II) protein family.
 
 
 0.988
VC_0606
Nitrogen regulatory protein P-II; Similar to GB:U00096 PID:1788904 PID:1799977; identified by sequence similarity; putative; Belongs to the P(II) protein family.
 
 
 
 0.874
glnE
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 [...]
 
   
 0.874
VC_2748
Nitrogen regulation protein; Similar to SP:P19906 PID:155172; identified by sequence similarity; putative.
  
 
 
 0.799
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.
  
    0.782
VC_2373
Glutamate synthase, large subunit; Similar to GB:X80485 PID:515938 SP:P55037 PID:1652093; identified by sequence similarity; putative.
     
 0.694
VC_2376
Glutamate synthase, large subunit; Similar to PID:606151 GB:U00096 PID:1789605; identified by sequence similarity; putative.
     
 0.694
rpsB
Ribosomal protein S2; Similar to GB:D26562 SP:P02351 GB:V00343 PID:42842 PID:473824; identified by sequence similarity; putative; Belongs to the universal ribosomal protein uS2 family.
     
 0.675
glnAv
Glutamate--ammonia ligase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase family.
 
   
 0.651
bamA
Surface antigen; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
 
    0.644
Your Current Organism:
Vibrio cholerae
NCBI taxonomy Id: 243277
Other names: V. cholerae O1 biovar El Tor str. N16961, Vibrio cholerae El Tor N16961, Vibrio cholerae O1 biovar El Tor str. N16961, Vibrio cholerae O1 biovar eltor str. N16961, Vibrio cholerae serotype O1 biotype El Tor strain N16961, Vibrio cholerae serotype O1 biotype ElTor strain N16961
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