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glnD protein (Methylobacter tundripaludum) - STRING interaction network
"glnD" - Bifunctional uridylyltransferase/uridylyl-removing enzyme in Methylobacter tundripaludum
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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glnDBifunctional uridylyltransferase/uridylyl-removing enzyme; 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 metabolism (881 aa)    
Predicted Functional Partners:
Mettu_3262
PFAM- Nitrogen regulatory protein PII; KEGG- maq-Maqu_0523 nitrogen regulatory protein P-II; Belongs to the P(II) protein family (112 aa)
 
  0.959
Mettu_3260
PFAM- Nitrogen regulatory protein PII; KEGG- gpb-HDN1F_28000 P2-like signal transmitter protein; Belongs to the P(II) protein family (112 aa)
 
  0.959
map
TIGRFAM- Peptidase M24A, methionine aminopeptidase, subfamily 1; KEGG- pha-PSHAa2037 methionine aminopeptidase; contains a divalent metal, usually cobalt; PFAM- Peptidase M24, structural domain (254 aa)
 
        0.890
Mettu_0758
KEGG- mca-MCA2039 glutamate synthase, large subunit; PFAM- Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, central-C; Glutamate synthase, alpha subunit, C-terminal (1539 aa)
       
  0.886
Mettu_3264
KEGG- mca-MCA1677 glutamine synthetase, type I; TIGRFAM- Glutamine synthetase type I; PFAM- Glutamine synthetase, catalytic region; Glutamine synthetase, beta-Grasp (469 aa)
 
 
  0.826
glnE
Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme; 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 regi [...] (992 aa)
   
   
  0.811
Mettu_3480
Pyruvate-flavodoxin oxidoreductase; Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin (1212 aa)
         
  0.794
Mettu_1570
KEGG- putative nitrogen regulatory protein P-II; Belongs to the P(II) protein family (116 aa)
   
  0.777
Mettu_0443
Phosphoenolpyruvate synthase; Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate; Belongs to the PEP-utilizing enzyme family (803 aa)
     
   
  0.732
metZ
O-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O- succinyl-L-homoserine (OSHS) and hydrogen sulfide (393 aa)
 
 
    0.678
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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