Meso_1420 protein (Chelativorans sp. BNC1) - STRING interaction network

Nodes:

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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.

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query proteins and first shell of interactors

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second shell of interactors

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proteins of unknown 3D structure

filled nodes:
a 3D structure is known or predicted

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Assay-based Predictions

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co-expression

Genomic Predictions

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Your Current Organism:

Chelativorans sp. BNC1

NCBI taxonomy Id: 266779
Other names: C. sp. BNC1, Mesorhizobium sp. BNC1

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
Meso_1420	Meso_1422	Meso_1420	Meso_1422	Hypothetical protein.	PFAM: protein of unknown function DUF1697; KEGG: mlo:mlr0163 hypothetical protein.	0.642
Meso_1420	ilvA	Meso_1420	Meso_1421	Hypothetical protein.	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.	0.642
Meso_1422	Meso_1420	Meso_1422	Meso_1420	PFAM: protein of unknown function DUF1697; KEGG: mlo:mlr0163 hypothetical protein.	Hypothetical protein.	0.642
Meso_1422	ilvA	Meso_1422	Meso_1421	PFAM: protein of unknown function DUF1697; KEGG: mlo:mlr0163 hypothetical protein.	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.	0.787
ilvA	Meso_1420	Meso_1421	Meso_1420	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.	Hypothetical protein.	0.642
ilvA	Meso_1422	Meso_1421	Meso_1422	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: protein of unknown function DUF1697; KEGG: mlo:mlr0163 hypothetical protein.	0.787