(4 nodes) Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain network (Fusarium venenatum)

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Your Input:
	A0A2L2T6H2	BPL/LPL catalytic domain-containing protein. (399 aa)
	A0A2L2T6Z7	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. (328 aa)
	A0A2L2TBZ6	BPL/LPL catalytic domain-containing protein. (669 aa)
	A0A2L2U0K7	BPL/LPL catalytic domain-containing protein. (326 aa)

Your Current Organism:

Fusarium venenatum

NCBI taxonomy Id: 56646
Other names: CBS 458.93, F. venenatum, Fusarium venetum

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Browse interactions in tabular form:

node1	node2	node1 annotation	node2 annotation	score
A0A2L2T6H2	A0A2L2T6Z7	BPL/LPL catalytic 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.	0.836
A0A2L2T6H2	A0A2L2TBZ6	BPL/LPL catalytic domain-containing protein.	BPL/LPL catalytic domain-containing protein.	0.426
A0A2L2T6Z7	A0A2L2T6H2	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.	BPL/LPL catalytic domain-containing protein.	0.836
A0A2L2TBZ6	A0A2L2T6H2	BPL/LPL catalytic domain-containing protein.	BPL/LPL catalytic domain-containing protein.	0.426