7 items (Psychrobacter sp. AntiMn1) - STRING interaction network

Nodes:

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Your Input:
	AOT82_1482	Homoserine dehydrogenase. (452 aa)
	AOT82_1833	Threonine synthase. (473 aa)
	thrB	Hypothetical protein; Belongs to the pseudomonas-type ThrB family. (388 aa)
	asd	Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family. (377 aa)
	AOT82_2778	Aspartokinase; Belongs to the aspartokinase family. (428 aa)
	AOT82_523	Threonine synthase. (86 aa)
	ilvA	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. (517 aa)

Your Current Organism:

Psychrobacter sp. AntiMn1

NCBI taxonomy Id: 1720344
Other names: P. sp. AntiMn-1, Psychrobacter sp. AntiMn-1

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
AOT82_1482	AOT82_1833	AOT82_1482	AOT82_1833	Homoserine dehydrogenase.	Threonine synthase.	0.879
AOT82_1482	AOT82_2778	AOT82_1482	AOT82_2778	Homoserine dehydrogenase.	Aspartokinase; Belongs to the aspartokinase family.	0.848
AOT82_1482	AOT82_523	AOT82_1482	AOT82_523	Homoserine dehydrogenase.	Threonine synthase.	0.789
AOT82_1482	asd	AOT82_1482	AOT82_2710	Homoserine dehydrogenase.	Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family.	0.968
AOT82_1482	ilvA	AOT82_1482	AOT82_537	Homoserine dehydrogenase.	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.	0.513
AOT82_1482	thrB	AOT82_1482	AOT82_1930	Homoserine dehydrogenase.	Hypothetical protein; Belongs to the pseudomonas-type ThrB family.	0.925
AOT82_1833	AOT82_1482	AOT82_1833	AOT82_1482	Threonine synthase.	Homoserine dehydrogenase.	0.879
AOT82_1833	AOT82_2778	AOT82_1833	AOT82_2778	Threonine synthase.	Aspartokinase; Belongs to the aspartokinase family.	0.689
AOT82_1833	asd	AOT82_1833	AOT82_2710	Threonine synthase.	Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family.	0.602
AOT82_1833	ilvA	AOT82_1833	AOT82_537	Threonine synthase.	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.	0.952
AOT82_1833	thrB	AOT82_1833	AOT82_1930	Threonine synthase.	Hypothetical protein; Belongs to the pseudomonas-type ThrB family.	0.912
AOT82_2778	AOT82_1482	AOT82_2778	AOT82_1482	Aspartokinase; Belongs to the aspartokinase family.	Homoserine dehydrogenase.	0.848
AOT82_2778	AOT82_1833	AOT82_2778	AOT82_1833	Aspartokinase; Belongs to the aspartokinase family.	Threonine synthase.	0.689
AOT82_2778	AOT82_523	AOT82_2778	AOT82_523	Aspartokinase; Belongs to the aspartokinase family.	Threonine synthase.	0.667
AOT82_2778	asd	AOT82_2778	AOT82_2710	Aspartokinase; Belongs to the aspartokinase family.	Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family.	0.982
AOT82_2778	ilvA	AOT82_2778	AOT82_537	Aspartokinase; Belongs to the aspartokinase family.	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.	0.459
AOT82_523	AOT82_1482	AOT82_523	AOT82_1482	Threonine synthase.	Homoserine dehydrogenase.	0.789
AOT82_523	AOT82_2778	AOT82_523	AOT82_2778	Threonine synthase.	Aspartokinase; Belongs to the aspartokinase family.	0.667
AOT82_523	asd	AOT82_523	AOT82_2710	Threonine synthase.	Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family.	0.429
AOT82_523	ilvA	AOT82_523	AOT82_537	Threonine synthase.	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.	0.436