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ADU48959.1L-threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (364 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
ADU48960.1
COGs: COG0460 Homoserine dehydrogenase; InterProIPR016204: IPR019811: IPR005106: IPR001342: IPR 002912; KEGG: kra:Krad_1252 homoserine dehydrogenase; PFAM: homoserine dehydrogenase; homoserine dehydrogenase NAD-binding; amino acid-binding ACT domain protein; SPTR: Homoserine dehydrogenase; PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain.
 
 
 0.990
ADU49680.1
L-threonine ammonia-lyase; COGs: COG1171 Threonine dehydratase; InterPro IPR005789: IPR001926: IPR002912; KEGG: sma:SAV_3302 threonine dehydratase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; amino acid-binding ACT domain protein; SPTR: Putative threonine dehydratase; TIGRFAM: threonine dehydratase; PFAM: ACT domain; Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine dehydratase, medium form.
 
 
0.947
serC
Phosphoserine aminotransferase apoenzyme; 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.
   
 0.944
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.
  
 
0.944
ADU48476.1
COGs: COG2008 Threonine aldolase; InterPro IPR001597; KEGG: nca:Noca_3094 L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase; PRIAM: Threonine aldolase; SPTR: L-allo-threonine aldolase; PFAM: Beta-eliminating lyase.
   
 0.926
ADU49850.1
L-threonine 3-dehydrogenase; COGs: COG1063 Threonine dehydrogenase and related Zn-dependent dehydrogenase; InterPro IPR002328: IPR013154: IPR013149; KEGG: nca:Noca_3757 L-threonine 3-dehydrogenase; PFAM: Alcohol dehydrogenase GroES domain protein; Alcohol dehydrogenase zinc-binding domain protein; SPTR: L-threonine 3-dehydrogenase; PFAM: Alcohol dehydrogenase GroES-like domain; Zinc-binding dehydrogenase; TIGRFAM: L-threonine 3-dehydrogenase; 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase.
   
 
 0.903
ADU46982.1
COGs: COG0527 Aspartokinase; InterProIPR001048: IPR002912: IPR018042: IPR005260: IPR 001341; KEGG: tcu:Tcur_4886 aspartate kinase; PFAM: aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; SPTR: Aspartokinase; TIGRFAM: aspartate kinase; aspartate kinase, monofunctional class; PFAM: Amino acid kinase family; ACT domain; TIGRFAM: aspartate kinase, monofunctional class; aspartate kinase; Belongs to the aspartokinase family.
  
 
 0.867
leuD
3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.
  
  
 0.821
lysA
Diaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine.
 
   
 0.774
Your Current Organism:
Intrasporangium calvum
NCBI taxonomy Id: 710696
Other names: I. calvum DSM 43043, Intrasporangium calvum DSM 43043, Intrasporangium calvum IFO 12989, Intrasporangium calvum NBRC 12989, Intrasporangium calvum str. DSM 43043, Intrasporangium calvum strain DSM 43043
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