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
ADV66207.1Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (345 aa)    
Predicted Functional Partners:
thrB
Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily.
 
 
 0.999
ADV67109.1
COGs: COG0460 Homoserine dehydrogenase; InterPro IPR005106: IPR001342; KEGG: dge:Dgeo_0610 homoserine dehydrogenase; PFAM: Homoserine dehydrogenase, catalytic; Aspartate/homoserine dehydrogenase, NAD-binding; PRIAM: Homoserine dehydrogenase; SPTR: Homoserine dehydrogenase; PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain.
 
 
 0.969
ilvA
Threonine dehydratase, biosynthetic; 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.
  
 
0.962
ADV68307.1
COGs: COG2008 Threonine aldolase; InterPro IPR001597; KEGG: ddr:Deide_09290 putative threonine aldolase; PFAM: Aromatic amino acid beta-eliminating lyase/threonine aldolase; PRIAM: Threonine aldolase; SPTR: Putative Threonine aldolase; PFAM: Beta-eliminating lyase.
  
 0.926
tdh
L-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family.
     
 0.900
ADV67470.1
COGs: COG0527 Aspartokinase; InterPro IPR001048: IPR002912: IPR005260: IPR001341; KEGG: dge:Dgeo_1127 aspartate kinase; PFAM: Aspartate/glutamate/uridylate kinase; Amino acid-binding ACT; SPTR: Aspartokinase; TIGRFAM: Aspartate kinase domain; Aspartate kinase, monofunctional class; PFAM: ACT domain; Amino acid kinase family; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase; Belongs to the aspartokinase family.
 
 
 0.858
ADV67604.1
COGs: COG0069 Glutamate synthase domain 2; InterPro IPR000583: IPR002932: IPR002489; KEGG: mrb:Mrub_1802 glutamate synthase (ferredoxin); PFAM: Glutamate synthase, central-C; Glutamine amidotransferase, class-II; Glutamate synthase, alpha subunit, C-terminal; PRIAM: Glutamate synthase (ferredoxin); SPTR: Glutamate synthase (Ferredoxin); PFAM: Conserved region in glutamate synthase; GXGXG motif; Glutamate synthase central domain; Glutamine amidotransferases class-II.
  
  
 0.735
ilvC
Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
 
  
 0.725
asd
Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family.
 
 
 0.660
ADV67003.1
COGs: COG0066 3-isopropylmalate dehydratase small subunit; InterPro IPR011827: IPR000573; KEGG: dge:Dgeo_1154 3-isopropylmalate dehydratase small subunit; PFAM: Aconitase A/isopropylmalate dehydratase small subunit, swivel; SPTR: Lysine biosynthesis protein, homoaconitate hydratase; TIGRFAM: 3-isopropylmalate dehydratase, small subunit, subgroup; PFAM: Aconitase C-terminal domain; TIGRFAM: 3-isopropylmalate dehydratase, small subunit; Belongs to the LeuD family.
  
  
 0.653
Your Current Organism:
Deinococcus maricopensis
NCBI taxonomy Id: 709986
Other names: D. maricopensis DSM 21211, Deinococcus maricopensis DSM 21211, Deinococcus maricopensis LB-34, Deinococcus maricopensis str. DSM 21211, Deinococcus maricopensis strain DSM 21211
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.