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
DFW101_0232Major facilitator superfamily MFS_1. (398 aa)    
Predicted Functional Partners:
DFW101_2279
Prephenate dehydratase.
  
 
 0.733
DFW101_0176
Flagellar basal-body rod protein FlgF; Belongs to the flagella basal body rod proteins family.
   
 
 0.716
DFW101_0234
Phosphoglycerate mutase; Belongs to the phosphoglycerate mutase family.
     
 0.700
DFW101_0233
Flagellar protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family.
       0.697
DFW101_1617
SNARE associated golgi family protein.
   
 
 0.686
DFW101_1221
Methionine synthase.
   
 
  0.667
DFW101_2186
Nitrate reductase gamma subunit.
     
 0.578
DFW101_1117
Nitrogen fixation protein NifU; May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins.
  
 
 0.570
DFW101_1463
4-aminobutyrate aminotransferase; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
  
  
 0.557
DFW101_1614
L-threonine dehydratase catabolic TdcB; 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.
    
 0.553
Your Current Organism:
Desulfovibrio carbinoliphilus
NCBI taxonomy Id: 694327
Other names: D. carbinoliphilus subsp. oakridgensis, Desulfovibrio carbinoliphilus subsp. oakridgensis, Desulfovibrio sp. FW-101-2B, personal::FW-101-2B
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