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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
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dsdAD-serine ammonia-lyase; Belongs to the serine/threonine dehydratase family. DsdA subfamily. (408 aa)    
Predicted Functional Partners:
sdaA
L-serine ammonia-lyase; Belongs to the iron-sulfur dependent L-serine dehydratase family.
    
 0.918
ilvA1
Threonine dehydratase biosynthetic 1; 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.
  
  
 0.916
ADP13372.1
Pyridoxal-phosphate dependent enzyme family protein 1.
     
0.905
ADP14052.1
Pyridoxal-phosphate dependent enzyme family protein 2.
     
 0.905
tdcB
Threonine dehydratase catabolic.
     
 0.905
ilvA2
Threonine dehydratase biosynthetic 2; 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.
     
 0.905
gloA
Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
     
 0.801
ADP17318.1
Glyoxalase/bleomycin resistance protein/dioxygenase superfamily protein 18.
     
 0.801
ADP13433.1
Metal-activated pyridoxal enzyme.
     
  0.800
ADP14110.1
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain protein 2.
     
  0.800
Your Current Organism:
Achromobacter xylosoxidans
NCBI taxonomy Id: 762376
Other names: A. xylosoxidans A8, Achromobacter xylosoxidans A8, Achromobacter xylosoxidans str. A8, Achromobacter xylosoxidans strain A8
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