Ajs_3205 protein (Acidovorax sp. JS42) - STRING interaction network

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Ajs_3205

KEGG: rfr:Rfer_1913 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit. (476 aa)

Predicted Functional Partners:

Ajs_3206

0.984

Ajs_0080

0.956

serC

0.947

ilvA

0.941

Ajs_3847

0.941

thrB

0.920

Ajs_4155

0.919

Ajs_0787

0.904

Ajs_1628

0.881

leuD

0.840

Your Current Organism:

Acidovorax sp. JS42

NCBI taxonomy Id: 232721
Other names: A. sp. JS42

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
Ajs_0080	Ajs_1628	Ajs_0080	Ajs_1628	L-threonine ammonia-lyase; 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.	KEGG: pol:Bpro_2860 aspartate kinase; TIGRFAM: aspartate kinase; aspartate kinase, monofunctional class; PFAM: aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; Belongs to the aspartokinase family.	0.407
Ajs_0080	Ajs_3205	Ajs_0080	Ajs_3205	L-threonine ammonia-lyase; 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.	KEGG: rfr:Rfer_1913 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit.	0.956
Ajs_0080	Ajs_3847	Ajs_0080	Ajs_3847	L-threonine ammonia-lyase; 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.	PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: pol:Bpro_4245 pyridoxal-5'-phosphate-dependent enzyme, beta subunit.	0.923
Ajs_0080	ilvA	Ajs_0080	Ajs_0679	L-threonine ammonia-lyase; 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-threonine ammonia-lyase; 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.	0.917
Ajs_0080	leuD	Ajs_0080	Ajs_3232	L-threonine ammonia-lyase; 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.	0.472
Ajs_0787	Ajs_3205	Ajs_0787	Ajs_3205	KEGG: rfr:Rfer_2962 4-hydroxythreonine-4-phosphate dehydrogenase; TIGRFAM: 4-hydroxythreonine-4-phosphate dehydrogenase; PFAM: Pyridoxal phosphate biosynthetic protein PdxA; Belongs to the PdxA family.	KEGG: rfr:Rfer_1913 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit.	0.904
Ajs_0787	serC	Ajs_0787	Ajs_2465	KEGG: rfr:Rfer_2962 4-hydroxythreonine-4-phosphate dehydrogenase; TIGRFAM: 4-hydroxythreonine-4-phosphate dehydrogenase; PFAM: Pyridoxal phosphate biosynthetic protein PdxA; Belongs to the PdxA family.	Phosphoserine aminotransferase apoenzyme; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.	0.922
Ajs_1628	Ajs_0080	Ajs_1628	Ajs_0080	KEGG: pol:Bpro_2860 aspartate kinase; TIGRFAM: aspartate kinase; aspartate kinase, monofunctional class; PFAM: aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; Belongs to the aspartokinase family.	L-threonine ammonia-lyase; 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.	0.407
Ajs_1628	Ajs_3205	Ajs_1628	Ajs_3205	KEGG: pol:Bpro_2860 aspartate kinase; TIGRFAM: aspartate kinase; aspartate kinase, monofunctional class; PFAM: aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; Belongs to the aspartokinase family.	KEGG: rfr:Rfer_1913 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit.	0.881
Ajs_1628	Ajs_3206	Ajs_1628	Ajs_3206	KEGG: pol:Bpro_2860 aspartate kinase; TIGRFAM: aspartate kinase; aspartate kinase, monofunctional class; PFAM: aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; Belongs to the aspartokinase family.	PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase, NAD-binding; KEGG: pol:Bpro_2190 homoserine dehydrogenase.	0.932
Ajs_1628	Ajs_4155	Ajs_1628	Ajs_4155	KEGG: pol:Bpro_2860 aspartate kinase; TIGRFAM: aspartate kinase; aspartate kinase, monofunctional class; PFAM: aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; Belongs to the aspartokinase family.	PFAM: oxidoreductase domain protein; homoserine dehydrogenase; homoserine dehydrogenase, NAD-binding; KEGG: dar:Daro_2386 homoserine dehydrogenase:amino acid-binding ACT:homoserine dehydrogenase, NAD-binding.	0.931
Ajs_1628	ilvA	Ajs_1628	Ajs_0679	KEGG: pol:Bpro_2860 aspartate kinase; TIGRFAM: aspartate kinase; aspartate kinase, monofunctional class; PFAM: aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; Belongs to the aspartokinase family.	L-threonine ammonia-lyase; 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.	0.405
Ajs_1628	serC	Ajs_1628	Ajs_2465	KEGG: pol:Bpro_2860 aspartate kinase; TIGRFAM: aspartate kinase; aspartate kinase, monofunctional class; PFAM: aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; Belongs to the aspartokinase family.	Phosphoserine aminotransferase apoenzyme; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.	0.446
Ajs_3205	Ajs_0080	Ajs_3205	Ajs_0080	KEGG: rfr:Rfer_1913 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit.	L-threonine ammonia-lyase; 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.	0.956
Ajs_3205	Ajs_0787	Ajs_3205	Ajs_0787	KEGG: rfr:Rfer_1913 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit.	KEGG: rfr:Rfer_2962 4-hydroxythreonine-4-phosphate dehydrogenase; TIGRFAM: 4-hydroxythreonine-4-phosphate dehydrogenase; PFAM: Pyridoxal phosphate biosynthetic protein PdxA; Belongs to the PdxA family.	0.904
Ajs_3205	Ajs_1628	Ajs_3205	Ajs_1628	KEGG: rfr:Rfer_1913 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit.	KEGG: pol:Bpro_2860 aspartate kinase; TIGRFAM: aspartate kinase; aspartate kinase, monofunctional class; PFAM: aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; Belongs to the aspartokinase family.	0.881
Ajs_3205	Ajs_3206	Ajs_3205	Ajs_3206	KEGG: rfr:Rfer_1913 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit.	PFAM: homoserine dehydrogenase; amino acid-binding ACT domain protein; homoserine dehydrogenase, NAD-binding; KEGG: pol:Bpro_2190 homoserine dehydrogenase.	0.984
Ajs_3205	Ajs_3847	Ajs_3205	Ajs_3847	KEGG: rfr:Rfer_1913 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit.	PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit; KEGG: pol:Bpro_4245 pyridoxal-5'-phosphate-dependent enzyme, beta subunit.	0.941
Ajs_3205	Ajs_4155	Ajs_3205	Ajs_4155	KEGG: rfr:Rfer_1913 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit.	PFAM: oxidoreductase domain protein; homoserine dehydrogenase; homoserine dehydrogenase, NAD-binding; KEGG: dar:Daro_2386 homoserine dehydrogenase:amino acid-binding ACT:homoserine dehydrogenase, NAD-binding.	0.919
Ajs_3205	ilvA	Ajs_3205	Ajs_0679	KEGG: rfr:Rfer_1913 threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent enzyme, beta subunit.	L-threonine ammonia-lyase; 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.	0.941