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
EAR12429.1COG1832 Predicted CoA-binding protein. (120 aa)    
Predicted Functional Partners:
EAR13429.1
Hypothetical protein.
  
     0.668
thrA
Bifunctional aspartokinase I/homoserine dehydrogenase I; COG2021 Homoserine acetyltransferase.
    
  0.637
EAR12428.1
Hypothetical protein.
       0.592
EAR12427.1
Ribonuclease Z.
       0.535
EAR12875.1
COG0735 Fe2+/Zn2+ uptake regulation proteins; Belongs to the Fur family.
  
    0.481
EAR12960.1
Hypothetical protein; COG0735 Fe2+/Zn2+ uptake regulation proteins; Belongs to the Fur family.
  
    0.481
EAR12966.1
Hypothetical protein; COG0735 Fe2+/Zn2+ uptake regulation proteins.
  
    0.481
EAR13428.1
OmpA family protein; COG2885 Outer membrane protein and related peptidoglycan-associated (lipo)proteins.
  
     0.460
EAR13249.1
COG2873 O-acetylhomoserine sulfhydrylase.
    
  0.424
ilvA
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.
    
  0.424
Your Current Organism:
Polaribacter irgensii
NCBI taxonomy Id: 313594
Other names: P. irgensii 23-P, Polaribacter irgensii 23-P
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