ilvE-2 protein (Bordetella avium) - STRING interaction network

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ilvE-2

Putative branched-chain amino-acid aminotransferase. (279 aa)

Predicted Functional Partners:

leuA1

0.957

leuA2

0.957

ilvD

0.950

ilvE

0.900

gshA

0.900

ilvA

0.868

hom

0.861

tdcB-2

0.858

ldh

0.822

thrB

0.805

Your Current Organism:

Bordetella avium

NCBI taxonomy Id: 360910
Other names: B. avium 197N, Bordetella avium 197N, Bordetella avium str. 197N, Bordetella avium strain 197N

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
gshA	ilvE	BAV3188	BAV0746	Glutamate--cysteine ligase; Start codon not provided.	Branched-chain amino acid aminotransferase.	0.900
gshA	ilvE-2	BAV3188	BAV1085	Glutamate--cysteine ligase; Start codon not provided.	Putative branched-chain amino-acid aminotransferase.	0.900
hom	ilvE	BAV2163	BAV0746	Homoserine dehydrogenase.	Branched-chain amino acid aminotransferase.	0.861
hom	ilvE-2	BAV2163	BAV1085	Homoserine dehydrogenase.	Putative branched-chain amino-acid aminotransferase.	0.861
hom	thrB	BAV2163	BAV2281	Homoserine dehydrogenase.	Homoserine kinase; Belongs to the pseudomonas-type ThrB family.	0.930
ilvA	ilvD	BAV3102	BAV0317	Threonine dehydratase biosynthetic; 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; Belongs to the IlvD/Edd family.	0.520
ilvA	ilvE	BAV3102	BAV0746	Threonine dehydratase biosynthetic; 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.	Branched-chain amino acid aminotransferase.	0.874
ilvA	ilvE-2	BAV3102	BAV1085	Threonine dehydratase biosynthetic; 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 branched-chain amino-acid aminotransferase.	0.868
ilvA	ldh	BAV3102	BAV3171	Threonine dehydratase biosynthetic; 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.	L-lactate dehydrogenase; Belongs to the LDH2/MDH2 oxidoreductase family.	0.800
ilvA	tdcB-2	BAV3102	BAV2664	Threonine dehydratase biosynthetic; 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.	0.917
ilvD	ilvA	BAV0317	BAV3102	Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.	Threonine dehydratase biosynthetic; 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.	0.520
ilvD	ilvE	BAV0317	BAV0746	Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.	Branched-chain amino acid aminotransferase.	0.950
ilvD	ilvE-2	BAV0317	BAV1085	Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.	Putative branched-chain amino-acid aminotransferase.	0.950
ilvD	leuA1	BAV0317	BAV1174	Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.	2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily.	0.929
ilvD	leuA2	BAV0317	BAV3351	Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.	2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily.	0.929
ilvD	tdcB-2	BAV0317	BAV2664	Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.	Threonine dehydratase catabolic.	0.701
ilvE	gshA	BAV0746	BAV3188	Branched-chain amino acid aminotransferase.	Glutamate--cysteine ligase; Start codon not provided.	0.900
ilvE	hom	BAV0746	BAV2163	Branched-chain amino acid aminotransferase.	Homoserine dehydrogenase.	0.861
ilvE	ilvA	BAV0746	BAV3102	Branched-chain amino acid aminotransferase.	Threonine dehydratase biosynthetic; 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.	0.874
ilvE	ilvD	BAV0746	BAV0317	Branched-chain amino acid aminotransferase.	Dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family.	0.950