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
AMD88430.1Threonine synthase; Catalyzes the formation of L-threonine from O-phospho-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology. (476 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
AMD86452.1
Homoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.967
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.
 
 
 0.951
AMD88314.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.945
serC
3-phosphoserine/phosphohydroxythreonine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
   
 0.938
tdh
L-threonine 3-dehydrogenase; Converts threonine and NAD to 1,2-amino-3-oxobutanoate and NADH; functions in threonine catabolism; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.901
AMD87120.1
Aspartate kinase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aspartokinase family.
  
 
 0.739
AMD88030.1
Glutamate synthase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.720
leuD
Isopropylmalate isomerase; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.
  
  
 0.707
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.
  
  
 0.594
Your Current Organism:
Actinomyces radicidentis
NCBI taxonomy Id: 111015
Other names: A. radicidentis, Actinomyces radicidentis Collins et al. 2001 emend. Nouioui et al. 2018, Actinomyces sp. CCUG 36733, Actinomyces sp. CCUG 36733T, CCUG 36733, CIP 106352, DSM 15433
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