ACWI_25950 protein (Acetobacterium wieringae)

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ACWI_25950

YheO-like PAS domain protein. (214 aa)

Predicted Functional Partners:

tdcF

0.632

sdhB

0.576

sdhA

0.545

ygeX

0.492

ispG

0.419

tdcB

0.416

Your Current Organism:

Acetobacterium wieringae

NCBI taxonomy Id: 52694
Other names: A. wieringae, ATCC 43740, JCM 2380, LMG 7579, LMG:7579, strain C

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
ACWI_25950	ispG	ACWI_25950	ACWI_25990	YheO-like PAS domain protein.	4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family.	0.419
ACWI_25950	sdhA	ACWI_25950	ACWI_02580	YheO-like PAS domain protein.	L-serine dehydratase, alpha chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	0.545
ACWI_25950	sdhB	ACWI_25950	ACWI_02590	YheO-like PAS domain protein.	L-serine dehydratase, beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	0.576
ACWI_25950	tdcB	ACWI_25950	ACWI_26770	YheO-like PAS domain protein.	L-threonine dehydratase catabolic TdcB; 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.	0.416
ACWI_25950	tdcF	ACWI_25950	ACWI_25940	YheO-like PAS domain protein.	Putative reactive intermediate deaminase TdcF.	0.632
ACWI_25950	ygeX	ACWI_25950	ACWI_09520	YheO-like PAS domain protein.	Diaminopropionate ammonia-lyase.	0.492
ispG	ACWI_25950	ACWI_25990	ACWI_25950	4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family.	YheO-like PAS domain protein.	0.419
sdhA	ACWI_25950	ACWI_02580	ACWI_25950	L-serine dehydratase, alpha chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	YheO-like PAS domain protein.	0.545
sdhA	sdhB	ACWI_02580	ACWI_02590	L-serine dehydratase, alpha chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	L-serine dehydratase, beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	0.999
sdhA	tdcB	ACWI_02580	ACWI_26770	L-serine dehydratase, alpha chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	L-threonine dehydratase catabolic TdcB; 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.	0.933
sdhB	ACWI_25950	ACWI_02590	ACWI_25950	L-serine dehydratase, beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	YheO-like PAS domain protein.	0.576
sdhB	sdhA	ACWI_02590	ACWI_02580	L-serine dehydratase, beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	L-serine dehydratase, alpha chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	0.999
sdhB	tdcB	ACWI_02590	ACWI_26770	L-serine dehydratase, beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	L-threonine dehydratase catabolic TdcB; 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.	0.934
sdhB	ygeX	ACWI_02590	ACWI_09520	L-serine dehydratase, beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	Diaminopropionate ammonia-lyase.	0.417
tdcB	ACWI_25950	ACWI_26770	ACWI_25950	L-threonine dehydratase catabolic TdcB; 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.	YheO-like PAS domain protein.	0.416
tdcB	sdhA	ACWI_26770	ACWI_02580	L-threonine dehydratase catabolic TdcB; 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-serine dehydratase, alpha chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	0.933
tdcB	sdhB	ACWI_26770	ACWI_02590	L-threonine dehydratase catabolic TdcB; 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-serine dehydratase, beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	0.934
tdcB	tdcF	ACWI_26770	ACWI_25940	L-threonine dehydratase catabolic TdcB; 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 reactive intermediate deaminase TdcF.	0.732
tdcF	ACWI_25950	ACWI_25940	ACWI_25950	Putative reactive intermediate deaminase TdcF.	YheO-like PAS domain protein.	0.632
tdcF	tdcB	ACWI_25940	ACWI_26770	Putative reactive intermediate deaminase TdcF.	L-threonine dehydratase catabolic TdcB; 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.	0.732