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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.
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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[Homology]
Score
AEB83582.1TIGRFAM: Threonine synthase; KEGG: dia:Dtpsy_2558 threonine synthase; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit. (476 aa)    
Predicted Functional Partners:
AEB83579.1
KEGG: ajs:Ajs_3206 homoserine dehydrogenase; PFAM: Homoserine dehydrogenase, catalytic; Aspartate/homoserine dehydrogenase, NAD-binding; Amino acid-binding ACT.
 
 
 0.970
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.
   
 0.956
AEB82543.1
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.
  
 
 0.943
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.
  
 
 0.943
AEB86557.1
Threonine ammonia-lyase; KEGG: dia:Dtpsy_3120 hypothetical protein; PFAM: Pyridoxal phosphate-dependent enzyme, beta subunit.
  
 
 0.943
thrB
TIGRFAM: Homoserine kinase ThrB; KEGG: ajs:Ajs_3320 homoserine kinase; PFAM: Aminoglycoside phosphotransferase; Belongs to the pseudomonas-type ThrB family.
    
 0.921
AEB83270.1
4-hydroxythreonine-4-phosphate dehydrogenase; TIGRFAM: Pyridoxal phosphate (active vitamin B6) biosynthesis PdxA; KEGG: ajs:Ajs_0787 4-hydroxythreonine-4-phosphate dehydrogenase; PFAM: Pyridoxal phosphate (active vitamin B6) biosynthesis PdxA; Belongs to the PdxA family.
    
 0.904
AEB82460.1
PFAM: Homoserine dehydrogenase, catalytic; Aspartate/homoserine dehydrogenase, NAD-binding; KEGG: ajs:Ajs_4155 homoserine dehydrogenase.
 
 
 0.898
AEB84682.1
KEGG: aav:Aave_2324 aspartate kinase; TIGRFAM: Aspartate kinase domain; Aspartate kinase, monofunctional class; PFAM: Aspartate/glutamate/uridylate kinase; Amino acid-binding ACT; Belongs to the aspartokinase family.
  
 
 0.892
AEB82761.1
Aconitate hydratase domain-containing protein; PFAM: Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha; Aconitase A/isopropylmalate dehydratase small subunit, swivel; KEGG: cti:RALTA_B0856 putative hydrolyase.
  
  
 0.877
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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