J056_000145 protein (Wallemia ichthyophaga) - STRING interaction network

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Score

J056_000145

Lipoyl-binding domain-containing protein. (363 aa)

Predicted Functional Partners:

J056_004185

0.999

J056_004270

0.999

J056_001853

0.998

J056_001099

0.992

J056_000107

0.983

J056_002443

0.982

J056_001378

0.973

J056_001487

0.970

J056_000896

0.957

J056_002114

0.863

Your Current Organism:

Wallemia ichthyophaga

NCBI taxonomy Id: 1299270
Other names: W. ichthyophaga EXF-994, Wallemia ichthyophaga EXF-994

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
J056_000107	J056_000145	R9ARD8	R9AXJ5	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	Lipoyl-binding domain-containing protein.	0.983
J056_000107	J056_000896	R9ARD8	R9ADW3	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	Lipoate-protein ligase A.	0.862
J056_000107	J056_001487	R9ARD8	R9AHW2	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis.	0.977
J056_000107	J056_002443	R9ARD8	R9AAH0	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.999
J056_000107	J056_004185	R9ARD8	R9AGP2	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	Glycine cleavage system P protein; The glycine cleavage system catalyzes the degradation of glycine.	0.601
J056_000145	J056_000107	R9AXJ5	R9ARD8	Lipoyl-binding domain-containing protein.	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	0.983
J056_000145	J056_000896	R9AXJ5	R9ADW3	Lipoyl-binding domain-containing protein.	Lipoate-protein ligase A.	0.957
J056_000145	J056_001099	R9AXJ5	R9ADH6	Lipoyl-binding domain-containing protein.	Serine hydroxymethyltransferase; Interconversion of serine and glycine. Belongs to the SHMT family.	0.992
J056_000145	J056_001378	R9AXJ5	R9ACE3	Lipoyl-binding domain-containing protein.	DASH complex subunit dad4.	0.973
J056_000145	J056_001487	R9AXJ5	R9AHW2	Lipoyl-binding domain-containing protein.	Acyl carrier protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis.	0.970
J056_000145	J056_001853	R9AXJ5	R9AB14	Lipoyl-binding domain-containing protein.	Dihydrolipoyl dehydrogenase.	0.998
J056_000145	J056_002114	R9AXJ5	R9AVA8	Lipoyl-binding domain-containing protein.	Glutamine synthetase.	0.863
J056_000145	J056_002443	R9AXJ5	R9AAH0	Lipoyl-binding domain-containing protein.	Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.982
J056_000145	J056_004185	R9AXJ5	R9AGP2	Lipoyl-binding domain-containing protein.	Glycine cleavage system P protein; The glycine cleavage system catalyzes the degradation of glycine.	0.999
J056_000145	J056_004270	R9AXJ5	R9AGX8	Lipoyl-binding domain-containing protein.	Uncharacterized protein.	0.999
J056_000896	J056_000107	R9ADW3	R9ARD8	Lipoate-protein ligase A.	Octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.	0.862
J056_000896	J056_000145	R9ADW3	R9AXJ5	Lipoate-protein ligase A.	Lipoyl-binding domain-containing protein.	0.957
J056_000896	J056_001853	R9ADW3	R9AB14	Lipoate-protein ligase A.	Dihydrolipoyl dehydrogenase.	0.857
J056_000896	J056_002443	R9ADW3	R9AAH0	Lipoate-protein ligase A.	Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.	0.998
J056_001099	J056_000145	R9ADH6	R9AXJ5	Serine hydroxymethyltransferase; Interconversion of serine and glycine. Belongs to the SHMT family.	Lipoyl-binding domain-containing protein.	0.992