AFE_0724 protein (Acidithiobacillus ferrooxidans)

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AFE_0724

Hydrolase, alpha/beta hydrolase fold family; Identified by match to protein family HMM PF00561. (321 aa)

Predicted Functional Partners:

ilvA

0.805

AFE_0723

0.805

AFE_0725

0.805

AFE_0727

0.433

Your Current Organism:

Acidithiobacillus ferrooxidans

NCBI taxonomy Id: 243159
Other names: A. ferrooxidans ATCC 23270, Acidithiobacillus ferrooxidans ATCC 23270, Acidithiobacillus ferrooxidans str. ATCC 23270

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
AFE_0723	AFE_0724	AFE_0723	AFE_0724	Helix-turn-helix domain protein; Identified by match to protein family HMM PF00126.	Hydrolase, alpha/beta hydrolase fold family; Identified by match to protein family HMM PF00561.	0.805
AFE_0723	AFE_0725	AFE_0723	AFE_0725	Helix-turn-helix domain protein; Identified by match to protein family HMM PF00126.	Conserved hypothetical protein.	0.805
AFE_0723	ilvA	AFE_0723	AFE_0722	Helix-turn-helix domain protein; Identified by match to protein family HMM PF00126.	Threonine ammonia-lyase, 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.	0.805
AFE_0724	AFE_0723	AFE_0724	AFE_0723	Hydrolase, alpha/beta hydrolase fold family; Identified by match to protein family HMM PF00561.	Helix-turn-helix domain protein; Identified by match to protein family HMM PF00126.	0.805
AFE_0724	AFE_0725	AFE_0724	AFE_0725	Hydrolase, alpha/beta hydrolase fold family; Identified by match to protein family HMM PF00561.	Conserved hypothetical protein.	0.805
AFE_0724	AFE_0727	AFE_0724	AFE_0727	Hydrolase, alpha/beta hydrolase fold family; Identified by match to protein family HMM PF00561.	1-acyl-sn-glycerol-3-phosphate acyltransferase; Identified by similarity to SP:Q59601; match to protein family HMM PF01553; match to protein family HMM TIGR00530.	0.433
AFE_0724	ilvA	AFE_0724	AFE_0722	Hydrolase, alpha/beta hydrolase fold family; Identified by match to protein family HMM PF00561.	Threonine ammonia-lyase, 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.	0.805
AFE_0725	AFE_0723	AFE_0725	AFE_0723	Conserved hypothetical protein.	Helix-turn-helix domain protein; Identified by match to protein family HMM PF00126.	0.805
AFE_0725	AFE_0724	AFE_0725	AFE_0724	Conserved hypothetical protein.	Hydrolase, alpha/beta hydrolase fold family; Identified by match to protein family HMM PF00561.	0.805
AFE_0725	ilvA	AFE_0725	AFE_0722	Conserved hypothetical protein.	Threonine ammonia-lyase, 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.	0.805
AFE_0727	AFE_0724	AFE_0727	AFE_0724	1-acyl-sn-glycerol-3-phosphate acyltransferase; Identified by similarity to SP:Q59601; match to protein family HMM PF01553; match to protein family HMM TIGR00530.	Hydrolase, alpha/beta hydrolase fold family; Identified by match to protein family HMM PF00561.	0.433
ilvA	AFE_0723	AFE_0722	AFE_0723	Threonine ammonia-lyase, 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.	Helix-turn-helix domain protein; Identified by match to protein family HMM PF00126.	0.805
ilvA	AFE_0724	AFE_0722	AFE_0724	Threonine ammonia-lyase, 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.	Hydrolase, alpha/beta hydrolase fold family; Identified by match to protein family HMM PF00561.	0.805
ilvA	AFE_0725	AFE_0722	AFE_0725	Threonine ammonia-lyase, 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.	Conserved hypothetical protein.	0.805

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