ilvA protein (Shewanella oneidensis) - STRING interaction network

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ilvA

Threonine dehydratase IlvA; 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. (545 aa)

Predicted Functional Partners:

ilvM

0.994

ilvD

0.991

ilvG

0.980

ilvH

0.977

thrC

0.963

ilvI

0.961

leuB

0.958

agxT

0.957

trpB

0.955

SO_3262

0.955

Your Current Organism:

Shewanella oneidensis

NCBI taxonomy Id: 211586
Other names: S. oneidensis MR-1, Shewanella oneidensis ATCC 700550, Shewanella oneidensis MR-1, Shewanella oneidensis str. MR-1, Shewanella oneidensis strain MR-1, Shewanella sp. MR-1

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
SO_3262	ilvA	SO_3262	SO_4344	TPP-dependent enzyme involved in flagella modificaiton.	Threonine dehydratase IlvA; 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.	0.955
SO_3262	ilvD	SO_3262	SO_4345	TPP-dependent enzyme involved in flagella modificaiton.	Dihydroxy-acid dehydratase IlvD; Belongs to the IlvD/Edd family.	0.836
SO_3262	ilvG	SO_3262	SO_4347	TPP-dependent enzyme involved in flagella modificaiton.	Acetolactate synthase II large subunit IlvG.	0.916
SO_3262	ilvH	SO_3262	SO_2278	TPP-dependent enzyme involved in flagella modificaiton.	Acetolactate synthase III small subunit IlvH.	0.998
SO_3262	ilvI	SO_3262	SO_2279	TPP-dependent enzyme involved in flagella modificaiton.	Acetolactate synthase III large subunit IlvI.	0.921
SO_3262	ilvM	SO_3262	SO_4346	TPP-dependent enzyme involved in flagella modificaiton.	Acetolactate synthase II small subunit IlvM.	0.913
SO_3262	leuB	SO_3262	SO_4235	TPP-dependent enzyme involved in flagella modificaiton.	3-isopropylmalate dehydrogenase LeuB; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate; Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.	0.977
agxT	ilvA	SO_4343	SO_4344	Serine-pyruvate aminotransferase AgxT.	Threonine dehydratase IlvA; 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.	0.957
agxT	ilvD	SO_4343	SO_4345	Serine-pyruvate aminotransferase AgxT.	Dihydroxy-acid dehydratase IlvD; Belongs to the IlvD/Edd family.	0.499
agxT	ilvG	SO_4343	SO_4347	Serine-pyruvate aminotransferase AgxT.	Acetolactate synthase II large subunit IlvG.	0.549
agxT	ilvI	SO_4343	SO_2279	Serine-pyruvate aminotransferase AgxT.	Acetolactate synthase III large subunit IlvI.	0.402
agxT	trpB	SO_4343	SO_3023	Serine-pyruvate aminotransferase AgxT.	Tryptophan synthase beta subunit TrpB; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.	0.914
ilvA	SO_3262	SO_4344	SO_3262	Threonine dehydratase IlvA; 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.	TPP-dependent enzyme involved in flagella modificaiton.	0.955
ilvA	agxT	SO_4344	SO_4343	Threonine dehydratase IlvA; 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.	Serine-pyruvate aminotransferase AgxT.	0.957
ilvA	ilvD	SO_4344	SO_4345	Threonine dehydratase IlvA; 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.	Dihydroxy-acid dehydratase IlvD; Belongs to the IlvD/Edd family.	0.991
ilvA	ilvG	SO_4344	SO_4347	Threonine dehydratase IlvA; 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 II large subunit IlvG.	0.980
ilvA	ilvH	SO_4344	SO_2278	Threonine dehydratase IlvA; 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 III small subunit IlvH.	0.977
ilvA	ilvI	SO_4344	SO_2279	Threonine dehydratase IlvA; 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 III large subunit IlvI.	0.961
ilvA	ilvM	SO_4344	SO_4346	Threonine dehydratase IlvA; 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 II small subunit IlvM.	0.994
ilvA	leuB	SO_4344	SO_4235	Threonine dehydratase IlvA; 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 LeuB; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate; Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.	0.958

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