close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING newly available directed regulatory networks a new typed view showing functional, physical, and regulatory edges in one network new clustering options and cluster-based layouts … and much more!
Explore STRING v12.5 →
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
glnDBifunctional uridylyltransferase/uridylyl-removing protein; 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. (874 aa)    
Predicted Functional Partners:
glnB
Transcriptional regulator; Indirectly regulates nitrogen metabolism; at high nitrogen levels P-II prevents the phosphorylation of NR-I, the transcriptional activator of the glutamine synthetase gene (glnA); at low nitrogen levels P-II is uridylylated to form PII-UMP and interacts with an adenylyltransferase (GlnE) that activates GlnA; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.989
AMF97404.1
Transcriptional regulator; Indirectly regulates nitrogen metabolism; at high nitrogen levels P-II prevents the phosphorylation of NR-I, the transcriptional activator of the glutamine synthetase gene (glnA); at low nitrogen levels P-II is uridylylated to form PII-UMP and interacts with an adenylyltransferase (GlnE) that activates GlnA; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 
 0.885
glnE
Bifunctional glutamine synthetase adenylyltransferase/deadenyltransferase; 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 [...]
 
   
 0.802
glnA
Forms a homododecamer; forms glutamine from ammonia and glutamate with the conversion of ATP to ADP and phosphate; also functions in the assimilation of ammonia; highly regulated protein controlled by the addition/removal of adenylyl groups by adenylyltransferase from specific tyrosine residues; addition of adenylyl groups results in inactivation of the enzyme; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.732
trmE
tRNA uridine(34) 5-carboxymethylaminomethyl synthesis GTPase MnmE; Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.
     
 0.731
gidA
tRNA uridine(34) 5-carboxymethylaminomethyl synthesis enzyme MnmG; NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34; Belongs to the MnmG family.
      
 0.726
AMF98664.1
Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.637
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.
  
    0.628
glnL
Sensory histidine kinase in two-component regulatory system with GlnG; acts as a signal transducer which responds to the nitrogen level of cell and modulates the activity of ntrC by phosphorylation/dephosphorylation; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 
 0.615
glpK
Glycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate; Belongs to the FGGY kinase family.
      
 0.583
Your Current Organism:
Vibrio harveyi
NCBI taxonomy Id: 669
Other names: ATCC 14126, Achromobacter harveyi, Beneckea harveyi, Beneckea neptuna, CAIM 513, CCUG 28584, CECT 525, CIP 103192, DSM 19623, IFO 15634, LMG 4044, LMG:4044, Lucibacterium harveyi, NBRC 15634, NCCB 80033, NCTC 12970, Photobacterium harveyi, Pseudomonas harveyi, V. harveyi, Vibrio carchariae, Vibrio sp. HENC-01, Vibrio sp. HENC-02, Vibrio sp. PG 001, Vibrio sp. PG 002, Vibrio sp. PG 006, Vibrio sp. PG 007, Vibrio trachuri
Server load: low (38%) [HD]