Protein: Lipoate--protein ligase 1 (EC 6.3.1.20) (Q8IEG9)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. In the mitochondrion, functions as a redox switch between two lipoylation routes. Senses the oxidation state of lipoate and determines which downstream enzymes will be lipoylated. In low reducing conditions, uses lipoate in its oxidized ring form to lipoylate glycine cleavage system H-protein GCVH. In high reducing conditions and together with LipL2, uses reduced lipoate (dihydrolipoate) to lipoylate the E2 component of the branched chain alpha-ketoacid dehydrogenase complex BCKDH-E2/BCDH and the E2 component of the alpha-ketoglutarate dehydrogenase complex KDH. LipL1 is responsible for catalysing the activation of lipoate, forming lipoyl-AMP while LipL2 is required but is not capable of catalyzing this reaction.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:15225307}.
InterPro domains:
- IPR004562: Lipoyltransferase/lipoate-protein ligase (family) [13-405]
- IPR019491: Lipoate protein ligase, C-terminal (domain) [322-393]
- IPR004143: Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL), catalytic domain (domain) [33-242]
- IPR045864: Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL) (homologous_superfamily) [11-323]
Sequence:
MKRIFRLVRRCHYSTEKRTNGPLVLVSNNQNIHFNLSLENFLLNNYNDLLKYLNINTIEKFNEPILFLWRNNRSIIIGKNQNIWSECNLKNIKEDGVLVARRFTGGGAVYHDLGNVCFTFLNNNINTSSNFLIILNTLKNHFNIEAKTQGRNDITVNDQKCSGSAFKKIKDVFLHHGTILINLEKNILNKYLTPDKIKYIKHGVSSVNARTINLSEINNNITCENLCIALIKEFTKFYEQNYKENINNIKNLENNINNSNFQNKEQININNTNENNLINNTNIIPNDITVHYIDQNNNITKNPEFLKYYNLLKDWDWCYGKTPKFQNHIWKQFTFGKLELFFNVSNGFIKDGNIFSDCLDINLIDHLKSIFNNDIKYSKEDISIFFKKLNVENKNYLDEVRSWILQEL
Predicted GO terms:
Molecular Function (MF): GO:0003674 (molecular function), GO:0003824 (catalytic activity), GO:0016874 (ligase activity), GO:0016740 (transferase activity), GO:0140096 (catalytic activity, acting on a protein), GO:0016879 (ligase activity, forming carbon-nitrogen bonds), GO:0016772 (transferase activity, transferring phosphorus-containing groups), GO:0016779 (nucleotidyltransferase activity)
Biological Process (BP): GO:0008150 (biological process), GO:0008152 (metabolic process), GO:0044238 (primary metabolic process), GO:0006807 (nitrogen compound metabolic process), GO:0071704 (organic substance metabolic process), GO:0043170 (macromolecule metabolic process), GO:1901564 (organonitrogen compound metabolic process), GO:0019538 (protein metabolic process), GO:0036211 (protein modification process), GO:0051604 (protein maturation), GO:0010467 (gene expression), GO:0043412 (macromolecule modification), GO:0009249 (protein lipoylation), GO:0018193 (peptidyl-amino acid modification), GO:0018205 (peptidyl-lysine modification)
Cellular Component (CC): GO:0005575 (cellular component), GO:0110165 (cellular anatomical entity), GO:0005622 (intracellular anatomical structure), GO:0043226 (organelle), GO:0005737 (cytoplasm), GO:0043229 (intracellular organelle), GO:0005739 (mitochondrion), GO:0043227 (membrane-bounded organelle), GO:0043231 (intracellular membrane-bounded organelle)