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
KIU17707.1Pyridoxal-5'-phosphate-dependent protein subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology. (392 aa)    
Predicted Functional Partners:
thrB
Serine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily.
 
 
 0.969
KIU15016.1
Homoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.939
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.
 
 
 0.917
serC
Phosphoserine 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.
   
 0.891
KIU15473.1
Aspartate kinase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aspartokinase family.
  
 0.868
KIU15015.1
Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine.
  
  
 
0.846
KIU17477.1
Threonine aldolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.839
KIU15442.1
Aminoglycoside phosphotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.773
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.
  
  
 0.755
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.
 
  
 0.713
Your Current Organism:
Mycolicibacterium llatzerense
NCBI taxonomy Id: 280871
Other names: CCUG 54744, CECT 7273, DSM 45343, JCM 16229, M. llatzerense, Mycobacterium llatzerense, Mycobacterium llatzerense Gomila et al. 2008, Mycobacterium sp. 13-009-09768, Mycobacterium sp. MG12, Mycobacterium sp. MG13, Mycobacterium sp. MG14, Mycobacterium sp. MG15, Mycobacterium sp. MG16, Mycobacterium sp. MG18, Mycolicibacterium llatzerense (Gomila et al. 2008) Gupta et al. 2018, strain MG13
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