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
ridAReactive intermediate/imine deaminase; Derived by automated computational analysis using gene prediction method: Protein Homology. (126 aa)    
Predicted Functional Partners:
fusA
Translation elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...]
    
  0.827
ilvA
PLP-dependent threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
 
 0.728
OBX61217.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.584
pheA
Chorismate mutase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.578
ilvH
Acetolactate synthase small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.546
ilvI
Acetolactate synthase, large subunit, biosynthetic type; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.546
rph
Ribonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
  
   0.525
gabD
Succinate-semialdehyde dehydrogenase (NADP(+)); Catalyzes the formation of succinate from succinate semialdehyde; NADP dependent; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.470
acoD
Catalyzes the oxidation of acetaldehyde, benzaldehyde, propionaldehyde and other aldehydes; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.470
betB
Betaine-aldehyde dehydrogenase; Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the reversible oxidation of betaine aldehyde to the corresponding acid.
    
  0.470
Your Current Organism:
Moraxella lacunata
NCBI taxonomy Id: 477
Other names: ATCC 17967, Bacillus lacunatus, CCUG 4441, CIP A182, DSM 18052, Diplobacille de la conjonctivite subaigue, Diplobacillus moraxenfeld, JCM 20914, LMG 5301, LMG:5301, M. lacunata, NBRC 102154, NCTC 11011, strain Morax 260
Server load: medium (44%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.