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
dsdATIGRFAM: D-serine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: bur:Bcep18194_B1364 D-serine dehydratase; Belongs to the serine/threonine dehydratase family. DsdA subfamily. (379 aa)    
Predicted Functional Partners:
Aave_0302
KEGG: pol:Bpro_4369 L-serine dehydratase 1; TIGRFAM: L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.
     
 0.913
Aave_0142
L-threonine ammonia-lyase; TIGRFAM: threonine dehydratase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; amino acid-binding ACT domain protein; KEGG: pol:Bpro_0165 threonine dehydratase.
     
 0.903
ilvA
L-threonine ammonia-lyase; 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.
     
 0.903
Aave_3768
L-threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: pol:Bpro_0952 pyridoxal-5'-phosphate-dependent enzyme, beta subunit.
     
 0.903
Aave_4441
Threonine ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: pol:Bpro_4245 pyridoxal-5'-phosphate-dependent enzyme, beta subunit.
     
 0.903
Aave_2182
PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; KEGG: bcn:Bcen_6449 D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding.
     
  0.800
Aave_2516
KEGG: eba:ebA3749 lactoylglutathione lyase.
     
  0.800
Aave_2791
Lactoylglutathione lyase; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione.
     
  0.800
Aave_3305
PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, catalytic region; D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; KEGG: pol:Bpro_3078 D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding.
     
  0.800
Aave_3758
PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; KEGG: bxe:Bxe_B1490 D-isomer specific 2-hydroxyacid dehydrogenase.
     
  0.800
Your Current Organism:
Acidovorax citrulli
NCBI taxonomy Id: 397945
Other names: A. citrulli AAC00-1, Acidovorax avenae subsp. citrulli AAC00-1, Acidovorax citrulli AAC00-1, Acidovorax citrulli str. AAC00-1, Acidovorax citrulli strain AAC00-1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.