(8 nodes) L-threonine ammonia-lyase activity, and Threonine synthase activity network (Pseudomonas putida KT2440)

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	ltaE	Low specificity L-threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. (346 aa)
	PP_0662	Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. (462 aa)
	thrC	Threonine synthase. (469 aa)
	PP_2930	Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. (305 aa)
	PP_3191	Putative threonine ammonia-lyase / dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Energymetabolism : Amino acids and amines. (350 aa)
	ilvA-I	Threonine deaminase; 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. (530 aa)
	PP_4430	Putative threonine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. (330 aa)
	ilvA-II	Threonine deaminase; 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. (504 aa)

Your Current Organism:

Pseudomonas putida KT2440

NCBI taxonomy Id: 160488
Other names: P. putida KT2440, Pseudomonas putida (strain KT2440), Pseudomonas putida str. KT2440

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
PP_0662	PP_2930	PP_0662	PP_2930	Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	0.949
PP_0662	PP_3191	PP_0662	PP_3191	Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Putative threonine ammonia-lyase / dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Energymetabolism : Amino acids and amines.	0.938
PP_0662	PP_4430	PP_0662	PP_4430	Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Putative threonine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	0.938
PP_0662	ilvA-I	PP_0662	PP_3446	Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Threonine deaminase; 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.	0.938
PP_0662	ilvA-II	PP_0662	PP_5149	Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Threonine deaminase; 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.	0.938
PP_0662	ltaE	PP_0662	PP_0321	Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Low specificity L-threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde.	0.926
PP_0662	thrC	PP_0662	PP_1471	Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Threonine synthase.	0.907
PP_2930	PP_0662	PP_2930	PP_0662	Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	0.949
PP_2930	PP_3191	PP_2930	PP_3191	Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Putative threonine ammonia-lyase / dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Energymetabolism : Amino acids and amines.	0.928
PP_2930	PP_4430	PP_2930	PP_4430	Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Putative threonine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	0.927
PP_2930	ilvA-I	PP_2930	PP_3446	Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Threonine deaminase; 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.	0.924
PP_2930	ilvA-II	PP_2930	PP_5149	Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Threonine deaminase; 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.	0.923
PP_2930	ltaE	PP_2930	PP_0321	Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Low specificity L-threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde.	0.912
PP_2930	thrC	PP_2930	PP_1471	Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	Threonine synthase.	0.948
PP_3191	PP_0662	PP_3191	PP_0662	Putative threonine ammonia-lyase / dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Energymetabolism : Amino acids and amines.	Putative Threonine synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	0.938
PP_3191	PP_2930	PP_3191	PP_2930	Putative threonine ammonia-lyase / dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Energymetabolism : Amino acids and amines.	Putative L-serine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	0.928
PP_3191	PP_4430	PP_3191	PP_4430	Putative threonine ammonia-lyase / dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Energymetabolism : Amino acids and amines.	Putative threonine dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	0.917
PP_3191	ilvA-I	PP_3191	PP_3446	Putative threonine ammonia-lyase / dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Energymetabolism : Amino acids and amines.	Threonine deaminase; 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.	0.919
PP_3191	ilvA-II	PP_3191	PP_5149	Putative threonine ammonia-lyase / dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Energymetabolism : Amino acids and amines.	Threonine deaminase; 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.	0.918
PP_3191	ltaE	PP_3191	PP_0321	Putative threonine ammonia-lyase / dehydratase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Energymetabolism : Amino acids and amines.	Low specificity L-threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde.	0.912