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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
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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 fixation and metabolism. (877 aa)    
Predicted Functional Partners:
MCA0977
Putative nitrogen regulatory protein P-II; Identified by match to protein family HMM PF00543.
 
 
 0.977
MCA0283
Putative nitrogen regulatory protein P-II; Identified by match to protein family HMM PF00543.
 
 
 0.972
MCA2044
Nitrogen regulatory protein P-II; Identified by similarity to SP:P05826; match to protein family HMM PF00543; Belongs to the P(II) protein family.
 
 
 0.964
MCA1299
Putative nitrogen regulatory protein P-II; Identified by match to protein family HMM PF00543.
 
 
 0.957
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 [...]
 
   
 0.941
glnA
Glutamine synthetase, type I; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase family.
 
   
 0.852
map
Methionine aminopeptidase, type I; 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.
  
    0.834
gltB
Glutamate synthase, large subunit; Identified by similarity to SP:P39812; match to protein family HMM PF01493; match to protein family HMM PF01645; match to protein family HMM PF04897; match to protein family HMM PF04898.
     
 0.766
mviN
Membrane protein MviN; Involved in peptidoglycan biosynthesis. Transports lipid- linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
     
 0.736
MCA1005
Identified by match to protein family HMM PF01384.
      
 0.696
Your Current Organism:
Methylococcus capsulatus
NCBI taxonomy Id: 243233
Other names: M. capsulatus str. Bath, Methylococcus capsulatus ATCC 33009, Methylococcus capsulatus Bath, Methylococcus capsulatus MC, Methylococcus capsulatus NCIB 11132, Methylococcus capsulatus str. Bath
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