KEGG   ORTHOLOGY: K23763
Entry
K23763                      KO                                     
Symbol
lipL2, lplA2
Name
lipoyl-AMP:Nepsilon-lysine lipoyltransferase / lipoyl(octanoyl) transferase [EC:2.3.1.181]
Pathway
map00785  Lipoic acid metabolism
map01100  Metabolic pathways
map01240  Biosynthesis of cofactors
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09108 Metabolism of cofactors and vitamins
   00785 Lipoic acid metabolism
    K23763  lipL2, lplA2; lipoyl-AMP:Nepsilon-lysine lipoyltransferase / lipoyl(octanoyl) transferase
Enzymes [BR:ko01000]
 2. Transferases
  2.3  Acyltransferases
   2.3.1  Transferring groups other than aminoacyl groups
    2.3.1.181  lipoyl(octanoyl) transferase
     K23763  lipL2, lplA2; lipoyl-AMP:Nepsilon-lysine lipoyltransferase / lipoyl(octanoyl) transferase
Other DBs
RN: R12427 R12435
GO: 0033819
Genes
PFA: PF3D7_0923600
PFD: PFDG_03787
PFH: PFHG_01365
PREI: PRSY57_0921600
PGAB: PGSY75_0923600
PYO: PY17X_0827800
PCB: PCHAS_082480(PC000179.03.0)
PBE: PBANKA_0824500
PVV: PVVCY_0802200
PKN: PKNH_0721600
TAN: TA03985
TPV: TP03_0090
BBO: BBOV_I002370(19.m02131)
 » show all
Reference
  Authors
Allary M, Lu JZ, Zhu L, Prigge ST
  Title
Scavenging of the cofactor lipoate is essential for the survival of the malaria parasite Plasmodium falciparum.
  Journal
Mol Microbiol 63:1331-44 (2007)
DOI:10.1111/j.1365-2958.2007.05592.x
  Sequence
Reference
  Authors
Afanador GA, Guerra AJ, Swift RP, Rodriguez RE, Bartee D, Matthews KA, Schon A, Freire E, Freel Meyers CL, Prigge ST
  Title
A novel lipoate attachment enzyme is shared by Plasmodium and Chlamydia species.
  Journal
Mol Microbiol 106:439-451 (2017)
DOI:10.1111/mmi.13776

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