STRINGSTRING
STRING protein interaction network
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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
glnEGlutamate-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 [...] (948 aa)    
Predicted Functional Partners:
glnD
protein-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.
 
   
 0.893
glnA
Glutamine synthetase, type I; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase family.
 
  
 0.865
ilvE
Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
       0.683
MCA0977
Putative nitrogen regulatory protein P-II; Identified by match to protein family HMM PF00543.
 
 
 
 0.677
MCA1482
ATP-dependent helicase HrpA; Identified by similarity to SP:P43329; match to protein family HMM PF00270; match to protein family HMM PF00271; match to protein family HMM PF04408; match to protein family HMM PF07717; match to protein family HMM TIGR01967.
  
     0.633
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.
     
 0.550
MCA1224
Identified by match to protein family HMM PF03061; match to protein family HMM TIGR00051.
 
    0.528
rplQ
Ribosomal protein L17; Identified by similarity to SP:P02416; match to protein family HMM PF01196; match to protein family HMM TIGR00059.
       0.492
MCA0664
Antioxidant, AhpC/Tsa family; Identified by similarity to GP:17428331; match to protein family HMM PF00578.
      0.484
MCA1238
Polyketide synthase; Identified by similarity to GP:24575128; match to protein family HMM PF00109; match to protein family HMM PF00698; match to protein family HMM PF01590; match to protein family HMM PF02801.
 
   
 0.480
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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