leuB protein (Saccharopolyspora erythraea) - STRING interaction network

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Score

leuB

3-isopropylmalate dehydrogenase. (407 aa)

Predicted Functional Partners:

leuD

0.996

leuC

0.993

ilvN

0.989

ilvB

0.988

ilvB-2

0.987

ilvA-2

0.977

ilvA

0.976

ilvB1

0.962

ilvB1-2

0.962

ilvB4

0.949

Your Current Organism:

Saccharopolyspora erythraea

NCBI taxonomy Id: 405948
Other names: S. erythraea NRRL 2338, Saccharopolyspora erythraea ATCC 11635, Saccharopolyspora erythraea DSM 40517, Saccharopolyspora erythraea JCM 4748, Saccharopolyspora erythraea NRRL 2338, Saccharopolyspora erythraea str. NRRL 2338, Saccharopolyspora erythraea strain NRRL 2338

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
ilvA	ilvA-2	SACE_0904	SACE_4356	Putative threonine dehydratase.	Threonine dehydratase; 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.	0.920
ilvA	ilvB	SACE_0904	SACE_0604	Putative threonine dehydratase.	Acetolactate synthase large subunit; Belongs to the TPP enzyme family.	0.974
ilvA	ilvB-2	SACE_0904	SACE_6159	Putative threonine dehydratase.	Putative acetolactate synthase large subunit.	0.974
ilvA	ilvB1	SACE_0904	SACE_3465	Putative threonine dehydratase.	Acetolactate synthase; Belongs to the TPP enzyme family.	0.941
ilvA	ilvB1-2	SACE_0904	SACE_4565	Putative threonine dehydratase.	Acetolactate synthase; Belongs to the TPP enzyme family.	0.939
ilvA	ilvB4	SACE_0904	SACE_5632	Putative threonine dehydratase.	Putative acetolactate synthase; Belongs to the TPP enzyme family.	0.931
ilvA	ilvN	SACE_0904	SACE_6158	Putative threonine dehydratase.	Acetolactate synthase small subunit.	0.989
ilvA	leuB	SACE_0904	SACE_3196	Putative threonine dehydratase.	3-isopropylmalate dehydrogenase.	0.976
ilvA	leuC	SACE_0904	SACE_6144	Putative threonine dehydratase.	3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.	0.509
ilvA	leuD	SACE_0904	SACE_6143	Putative threonine dehydratase.	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.	0.797
ilvA-2	ilvA	SACE_4356	SACE_0904	Threonine dehydratase; 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.	Putative threonine dehydratase.	0.920
ilvA-2	ilvB	SACE_4356	SACE_0604	Threonine dehydratase; 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 large subunit; Belongs to the TPP enzyme family.	0.977
ilvA-2	ilvB-2	SACE_4356	SACE_6159	Threonine dehydratase; 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.	Putative acetolactate synthase large subunit.	0.978
ilvA-2	ilvB1	SACE_4356	SACE_3465	Threonine dehydratase; 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; Belongs to the TPP enzyme family.	0.938
ilvA-2	ilvB1-2	SACE_4356	SACE_4565	Threonine dehydratase; 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; Belongs to the TPP enzyme family.	0.938
ilvA-2	ilvB4	SACE_4356	SACE_5632	Threonine dehydratase; 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.	Putative acetolactate synthase; Belongs to the TPP enzyme family.	0.937
ilvA-2	ilvN	SACE_4356	SACE_6158	Threonine dehydratase; 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 small subunit.	0.986
ilvA-2	leuB	SACE_4356	SACE_3196	Threonine dehydratase; 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.	0.977
ilvA-2	leuC	SACE_4356	SACE_6144	Threonine dehydratase; 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 dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.	0.583
ilvA-2	leuD	SACE_4356	SACE_6143	Threonine dehydratase; 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 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.	0.850

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