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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
Databases
Textmining
[Homology]
Score
glnDUTP-GlnB uridylyltransferase, GlnD; 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. (874 aa)    
Predicted Functional Partners:
AEB85480.1
KEGG: dia:Dtpsy_1960 nitrogen regulatory protein P-II; PFAM: Nitrogen regulatory protein PII; SMART: Nitrogen regulatory protein PII; Belongs to the P(II) protein family.
 
 
 0.978
AEB85732.1
KEGG: dia:Dtpsy_2211 nitrogen regulatory protein P-II; PFAM: Nitrogen regulatory protein PII; SMART: Nitrogen regulatory protein PII.
 
 
 0.973
AEB82649.1
KEGG: aav:Aave_0233 nitrogen regulatory protein P-II; PFAM: Nitrogen regulatory protein PII; SMART: Nitrogen regulatory protein PII; Belongs to the P(II) protein family.
 
 
 
 0.801
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.
  
    0.769
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 tra [...]
 
   
 0.744
purL
Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.
     
 0.633
AEB83225.1
KEGG: ajs:Ajs_0741 glutamate synthase (NADH) large subunit; PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, central-N; Glutamate synthase, alpha subunit, C-terminal.
     
 0.630
AEB83830.1
TIGRFAM: Glutamine synthetase type I; KEGG: aav:Aave_1442 L-glutamine synthetase; PFAM: Glutamine synthetase, catalytic domain; Glutamine synthetase, beta-Grasp.
 
   
 0.629
bamA
Outer membrane protein assembly complex, YaeT protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
 
    0.617
AEB83832.1
Manually curated; PFAM: ATPase-like, ATP-binding domain; Signal transduction histidine kinase, subgroup 1, dimerisation/phosphoacceptor domain; KEGG: dia:Dtpsy_1111 signal transduction histidine kinase, nitrogen specific, NtrB; SMART: ATPase-like, ATP-binding domain; Signal transduction histidine kinase, subgroup 1, dimerisation/phosphoacceptor domain.
  
 
 
 0.555
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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