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

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	glnD	Uridylyl transferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen metabolism. (918 aa)
	AOT82_1334	D-3-phosphoglycerate dehydrogenase; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. (408 aa)
	AOT82_1368	GDP/GTP pyrophosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. (845 aa)
	AOT82_1482	Homoserine dehydrogenase. (452 aa)
	purU	Formyltetrahydrofolate deformylase; Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4). (309 aa)
	AOT82_2488	Acetolactate synthase isozyme III small subunit. (165 aa)
	AOT82_2778	Aspartokinase; Belongs to the aspartokinase family. (428 aa)
	AOT82_299	Bifunctional chorismate mutase/prephenate dehydratase. (390 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_1334	AOT82_1482	AOT82_1334	AOT82_1482	D-3-phosphoglycerate dehydrogenase; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.	Homoserine dehydrogenase.	0.406
AOT82_1482	AOT82_1334	AOT82_1482	AOT82_1334	Homoserine dehydrogenase.	D-3-phosphoglycerate dehydrogenase; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.	0.406
AOT82_1482	AOT82_2488	AOT82_1482	AOT82_2488	Homoserine dehydrogenase.	Acetolactate synthase isozyme III small subunit.	0.800
AOT82_1482	AOT82_2778	AOT82_1482	AOT82_2778	Homoserine dehydrogenase.	Aspartokinase; Belongs to the aspartokinase family.	0.848
AOT82_1482	AOT82_299	AOT82_1482	AOT82_299	Homoserine dehydrogenase.	Bifunctional chorismate mutase/prephenate dehydratase.	0.631
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_2488	AOT82_1482	AOT82_2488	AOT82_1482	Acetolactate synthase isozyme III small subunit.	Homoserine dehydrogenase.	0.800
AOT82_2488	AOT82_299	AOT82_2488	AOT82_299	Acetolactate synthase isozyme III small subunit.	Bifunctional chorismate mutase/prephenate dehydratase.	0.687
AOT82_2488	ilvA	AOT82_2488	AOT82_537	Acetolactate synthase isozyme III small subunit.	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.	0.976
AOT82_2778	AOT82_1482	AOT82_2778	AOT82_1482	Aspartokinase; Belongs to the aspartokinase family.	Homoserine dehydrogenase.	0.848
AOT82_2778	AOT82_299	AOT82_2778	AOT82_299	Aspartokinase; Belongs to the aspartokinase family.	Bifunctional chorismate mutase/prephenate dehydratase.	0.681
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_299	AOT82_1482	AOT82_299	AOT82_1482	Bifunctional chorismate mutase/prephenate dehydratase.	Homoserine dehydrogenase.	0.631
AOT82_299	AOT82_2488	AOT82_299	AOT82_2488	Bifunctional chorismate mutase/prephenate dehydratase.	Acetolactate synthase isozyme III small subunit.	0.687
AOT82_299	AOT82_2778	AOT82_299	AOT82_2778	Bifunctional chorismate mutase/prephenate dehydratase.	Aspartokinase; Belongs to the aspartokinase family.	0.681
AOT82_299	ilvA	AOT82_299	AOT82_537	Bifunctional chorismate mutase/prephenate dehydratase.	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.	0.543
ilvA	AOT82_1482	AOT82_537	AOT82_1482	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.	Homoserine dehydrogenase.	0.513
ilvA	AOT82_2488	AOT82_537	AOT82_2488	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.	Acetolactate synthase isozyme III small subunit.	0.976
ilvA	AOT82_2778	AOT82_537	AOT82_2778	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.	Aspartokinase; Belongs to the aspartokinase family.	0.459
ilvA	AOT82_299	AOT82_537	AOT82_299	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.	Bifunctional chorismate mutase/prephenate dehydratase.	0.543