leuB2 protein (Achromobacter xylosoxidans) - STRING interaction network

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Score

leuB2

3-isopropylmalate dehydrogenase 2. (362 aa)

Predicted Functional Partners:

leuC2

0.992

leuC3

0.989

leuD2

0.988

leuD3

0.984

leuC1

0.983

leuD1

0.977

ADP13372.1

0.928

ADP14052.1

0.928

tdcB

0.928

ilvA1

0.928

Your Current Organism:

Achromobacter xylosoxidans

NCBI taxonomy Id: 762376
Other names: A. xylosoxidans A8, Achromobacter xylosoxidans A8, Achromobacter xylosoxidans str. A8, Achromobacter xylosoxidans strain A8

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
ADP13372.1	ADP14052.1	AXYL_00010	AXYL_00695	Pyridoxal-phosphate dependent enzyme family protein 1.	Pyridoxal-phosphate dependent enzyme family protein 2.	0.856
ADP13372.1	ilvA1	AXYL_00010	AXYL_03080	Pyridoxal-phosphate dependent enzyme family protein 1.	Threonine dehydratase biosynthetic 1; 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.	0.698
ADP13372.1	leuB2	AXYL_00010	AXYL_03894	Pyridoxal-phosphate dependent enzyme family protein 1.	3-isopropylmalate dehydrogenase 2.	0.928
ADP13372.1	tdcB	AXYL_00010	AXYL_01246	Pyridoxal-phosphate dependent enzyme family protein 1.	Threonine dehydratase catabolic.	0.673
ADP14052.1	ADP13372.1	AXYL_00695	AXYL_00010	Pyridoxal-phosphate dependent enzyme family protein 2.	Pyridoxal-phosphate dependent enzyme family protein 1.	0.856
ADP14052.1	ilvA1	AXYL_00695	AXYL_03080	Pyridoxal-phosphate dependent enzyme family protein 2.	Threonine dehydratase biosynthetic 1; 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.	0.850
ADP14052.1	leuB2	AXYL_00695	AXYL_03894	Pyridoxal-phosphate dependent enzyme family protein 2.	3-isopropylmalate dehydrogenase 2.	0.928
ADP14052.1	tdcB	AXYL_00695	AXYL_01246	Pyridoxal-phosphate dependent enzyme family protein 2.	Threonine dehydratase catabolic.	0.853
ilvA1	ADP13372.1	AXYL_03080	AXYL_00010	Threonine dehydratase biosynthetic 1; 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.	Pyridoxal-phosphate dependent enzyme family protein 1.	0.698
ilvA1	ADP14052.1	AXYL_03080	AXYL_00695	Threonine dehydratase biosynthetic 1; 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.	Pyridoxal-phosphate dependent enzyme family protein 2.	0.850
ilvA1	leuB2	AXYL_03080	AXYL_03894	Threonine dehydratase biosynthetic 1; 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.	3-isopropylmalate dehydrogenase 2.	0.928
ilvA1	tdcB	AXYL_03080	AXYL_01246	Threonine dehydratase biosynthetic 1; 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.	Threonine dehydratase catabolic.	0.688
leuB2	ADP13372.1	AXYL_03894	AXYL_00010	3-isopropylmalate dehydrogenase 2.	Pyridoxal-phosphate dependent enzyme family protein 1.	0.928
leuB2	ADP14052.1	AXYL_03894	AXYL_00695	3-isopropylmalate dehydrogenase 2.	Pyridoxal-phosphate dependent enzyme family protein 2.	0.928
leuB2	ilvA1	AXYL_03894	AXYL_03080	3-isopropylmalate dehydrogenase 2.	Threonine dehydratase biosynthetic 1; 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.	0.928
leuB2	leuC1	AXYL_03894	AXYL_02234	3-isopropylmalate dehydrogenase 2.	3-isopropylmalate dehydratase large subunit 1; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.	0.983
leuB2	leuC2	AXYL_03894	AXYL_02693	3-isopropylmalate dehydrogenase 2.	3-isopropylmalate dehydratase large subunit 2.	0.992
leuB2	leuC3	AXYL_03894	AXYL_06237	3-isopropylmalate dehydrogenase 2.	3-isopropylmalate dehydratase large subunit 3; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.	0.989
leuB2	leuD1	AXYL_03894	AXYL_02235	3-isopropylmalate dehydrogenase 2.	3-isopropylmalate dehydratase small subunit 1; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.	0.977
leuB2	leuD2	AXYL_03894	AXYL_02694	3-isopropylmalate dehydrogenase 2.	3-isopropylmalate dehydratase small subunit 2; Belongs to the LeuD family.	0.988

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