Lipoyltransferase 1, mitochondrial (EC 2.3.1.-) (Lipoate biosynthesis protein) (Lipoate-protein ligase) (Lipoyl ligase)
1_MLIPF 6_ SMKNC 11_ FQLLC 16_ NCQVP 21_ AAGFK 26_ KTVKN 31_ GLILQ 36_ SISND 41_ VYQNL 46_ AVEDW 51_ IHDHM 56_ NLEGK 61_ PILFF 66_ WQNSP 71_ SVVIG 76_ RHQNP 81_ WQECN 86_ LNLMR 91_ EEGIK 96_ LARRR 101_ SGGGT 106_ VYHDM 111_ GNINL 116_ TFFTT 121_ KKKYD 126_ RMENL 131_ KLIVR 136_ ALNAV 141_ QPQLD 146_ VQATK 151_ RFDLL 156_ LDGQF 161_ KISGT 166_ ASKIG 171_ RTTAY 176_ HHCTL 181_ LCSTD 186_ GTFLS 191_ SLLKS 196_ PYQGI 201_ RSNAT 206_ ASIPS 211_ LVKNL 216_ LEKDP 221_ TLTCE 226_ VLMNA 231_ VATEY 236_ AAYHQ 241_ IDNHI 246_ HLINP 251_ TDETL 256_ FPGIN 261_ SKAKE 266_ LQTWE 271_ WIYGK 276_ TPKFS 281_ INTSF 286_ HVLYE 291_ QSHLE 296_ IKVFI 301_ DIKNG 306_ RIEIC 311_ NIEAP 316_ DHWLP 321_ LEIRD 326_ KLNSS 331_ LIGSK 336_ FCPTE 341_ TTMLT 346_ NILLR 351_ TCPQD 356_ HKLNS 361_ KWNIL 366_CEKIK
1: Lipoyl amidotransferase that catalyzes the transfer of lipoyl moieties from lipoyl-protein H of the glycine cleavage system (lipoyl-GCSH) to E2 subunits of the pyruvate dehydrogenase complex (PDCE2) (PubMed:29987032). Unable to catalyze the transfer of octanoyl from octanoyl-GCSH to PDCE2 (PubMed:29987032). In vitro, it is also able to catalyze the transfer of the lipoyl group from lipoyl-AMP to the specific lysine residue of lipoyl domains of lipoate-dependent enzymes but this reaction may not be physiologically relevant (Probable)