lipA protein (Legionella waltersii) - STRING interaction network

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lipA

Lipoyl synthase; 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. (329 aa)

Predicted Functional Partners:

lipB

0.998

gcvH

0.910

rir1

0.686

PdhB_2

0.585

sucB

0.529

MerA

0.511

LpdA

0.495

Lwal_0197

0.479

trpE

0.478

guaA

0.477

Your Current Organism:

Legionella waltersii

NCBI taxonomy Id: 66969
Other names: ATCC 51914, CCUG 44924, CIP 104965, DSM 21908, L. waltersii, NCTC 13017, strain 2074-AUS-E

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
LpdA	PdhB_2	Lwal_3137	Lwal_2963	Dihydrolipoamide dehydrogenase.	2-oxoisovalerate dehydrogenase, E1 component, alpha and beta fusion.	0.999
LpdA	gcvH	Lwal_3137	Lwal_2348	Dihydrolipoamide dehydrogenase.	Glycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.	0.984
LpdA	lipA	Lwal_3137	Lwal_0196	Dihydrolipoamide dehydrogenase.	Lipoyl synthase; 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.	0.495
LpdA	lipB	Lwal_3137	Lwal_3127	Dihydrolipoamide dehydrogenase.	Lipoyltransferase; 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.	0.499
LpdA	sucB	Lwal_3137	Lwal_2612	Dihydrolipoamide dehydrogenase.	Dihydrolipoamide succinyltransferase, E2 subunit; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2).	0.999
Lwal_0197	lipA	Lwal_0197	Lwal_0196	Putative virulence protein.	Lipoyl synthase; 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.	0.479
MerA	PdhB_2	Lwal_3029	Lwal_2963	Oxydoreductase.	2-oxoisovalerate dehydrogenase, E1 component, alpha and beta fusion.	0.999
MerA	gcvH	Lwal_3029	Lwal_2348	Oxydoreductase.	Glycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.	0.865
MerA	lipA	Lwal_3029	Lwal_0196	Oxydoreductase.	Lipoyl synthase; 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.	0.511
MerA	sucB	Lwal_3029	Lwal_2612	Oxydoreductase.	Dihydrolipoamide succinyltransferase, E2 subunit; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2).	0.980
PdhB_2	LpdA	Lwal_2963	Lwal_3137	2-oxoisovalerate dehydrogenase, E1 component, alpha and beta fusion.	Dihydrolipoamide dehydrogenase.	0.999
PdhB_2	MerA	Lwal_2963	Lwal_3029	2-oxoisovalerate dehydrogenase, E1 component, alpha and beta fusion.	Oxydoreductase.	0.999
PdhB_2	gcvH	Lwal_2963	Lwal_2348	2-oxoisovalerate dehydrogenase, E1 component, alpha and beta fusion.	Glycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.	0.882
PdhB_2	lipA	Lwal_2963	Lwal_0196	2-oxoisovalerate dehydrogenase, E1 component, alpha and beta fusion.	Lipoyl synthase; 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.	0.585
PdhB_2	lipB	Lwal_2963	Lwal_3127	2-oxoisovalerate dehydrogenase, E1 component, alpha and beta fusion.	Lipoyltransferase; 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.	0.569
PdhB_2	sucB	Lwal_2963	Lwal_2612	2-oxoisovalerate dehydrogenase, E1 component, alpha and beta fusion.	Dihydrolipoamide succinyltransferase, E2 subunit; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2).	0.999
gcvH	LpdA	Lwal_2348	Lwal_3137	Glycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.	Dihydrolipoamide dehydrogenase.	0.984
gcvH	MerA	Lwal_2348	Lwal_3029	Glycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.	Oxydoreductase.	0.865
gcvH	PdhB_2	Lwal_2348	Lwal_2963	Glycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.	2-oxoisovalerate dehydrogenase, E1 component, alpha and beta fusion.	0.882
gcvH	lipA	Lwal_2348	Lwal_0196	Glycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.	Lipoyl synthase; 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.	0.910

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