LIPT_BOVIN
ID LIPT_BOVIN Reviewed; 373 AA.
AC O46419;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Lipoyltransferase 1, mitochondrial;
DE EC=2.3.1.-;
DE AltName: Full=Lipoate biosynthesis protein;
DE AltName: Full=Lipoate-protein ligase;
DE AltName: Full=Lipoyl ligase;
DE Flags: Precursor;
GN Name=LIPT1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=9405389; DOI=10.1074/jbc.272.51.31974;
RA Fujiwara K., Okamura-Ikeda K., Motokawa Y.;
RT "Cloning and expression of a cDNA encoding bovine lipoyltransferase.";
RL J. Biol. Chem. 272:31974-31978(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 27-373 IN COMPLEX WITH LIPOYL-AMP,
RP AND FUNCTION.
RX PubMed=17570395; DOI=10.1016/j.jmb.2007.05.059;
RA Fujiwara K., Hosaka H., Matsuda M., Okamura-Ikeda K., Motokawa Y.,
RA Suzuki M., Nakagawa A., Taniguchi H.;
RT "Crystal structure of bovine lipoyltransferase in complex with lipoyl-
RT AMP.";
RL J. Mol. Biol. 371:222-234(2007).
CC -!- FUNCTION: Catalyzes the transfer of the lipoyl group from lipoyl-AMP to
CC the specific lysine residue of lipoyl domains of lipoate-dependent
CC enzymes. {ECO:0000269|PubMed:17570395}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lipoyl-5'-AMP + L-lysyl-[lipoyl-carrier protein] = (R)-
CC N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + 2 H(+);
CC Xref=Rhea:RHEA:20473, Rhea:RHEA-COMP:10500, Rhea:RHEA-COMP:10502,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:83091,
CC ChEBI:CHEBI:83099, ChEBI:CHEBI:456215;
CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the LplA family. {ECO:0000305}.
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DR EMBL; AB006441; BAA24354.1; -; mRNA.
DR RefSeq; NP_777220.1; NM_174795.2.
DR PDB; 2E5A; X-ray; 2.10 A; A=27-373.
DR PDB; 3A7U; X-ray; 3.44 A; A=27-373.
DR PDBsum; 2E5A; -.
DR PDBsum; 3A7U; -.
DR AlphaFoldDB; O46419; -.
DR SMR; O46419; -.
DR STRING; 9913.ENSBTAP00000005171; -.
DR PaxDb; O46419; -.
DR Ensembl; ENSBTAT00000005171; ENSBTAP00000005171; ENSBTAG00000003965.
DR GeneID; 286864; -.
DR KEGG; bta:286864; -.
DR CTD; 51601; -.
DR VEuPathDB; HostDB:ENSBTAG00000003965; -.
DR VGNC; VGNC:30910; LIPT1.
DR eggNOG; KOG3159; Eukaryota.
DR GeneTree; ENSGT00390000008846; -.
DR HOGENOM; CLU_022986_4_1_1; -.
DR InParanoid; O46419; -.
DR OMA; RTCPEDD; -.
DR OrthoDB; 1090038at2759; -.
DR TreeFam; TF314085; -.
DR BRENDA; 2.3.1.181; 908.
DR Reactome; R-BTA-389661; Glyoxylate metabolism and glycine degradation.
DR UniPathway; UPA00537; UER00595.
DR EvolutionaryTrace; O46419; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000003965; Expressed in oocyte and 105 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0017118; F:lipoyltransferase activity; IBA:GO_Central.
DR GO; GO:0009249; P:protein lipoylation; IBA:GO_Central.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR PANTHER; PTHR12561; PTHR12561; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00545; lipoyltrans; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Direct protein sequencing; Mitochondrion;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT CHAIN 26..373
FT /note="Lipoyltransferase 1, mitochondrial"
FT /id="PRO_0000017855"
FT DOMAIN 57..243
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT BINDING 107
FT /ligand="substrate"
FT BINDING 151
FT /ligand="substrate"
FT BINDING 161
FT /ligand="substrate"
FT BINDING 179
FT /ligand="substrate"
FT BINDING 208
FT /ligand="substrate"
FT BINDING 210
FT /ligand="substrate"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2E5A"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:2E5A"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2E5A"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:2E5A"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:2E5A"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:2E5A"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2E5A"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2E5A"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2E5A"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:2E5A"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2E5A"
FT HELIX 126..140
FT /evidence="ECO:0007829|PDB:2E5A"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3A7U"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2E5A"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3A7U"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2E5A"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2E5A"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:2E5A"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:2E5A"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:2E5A"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:2E5A"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:2E5A"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:2E5A"
FT HELIX 224..239
FT /evidence="ECO:0007829|PDB:2E5A"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:2E5A"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:2E5A"
FT HELIX 259..267
FT /evidence="ECO:0007829|PDB:2E5A"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:2E5A"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:2E5A"
FT STRAND 279..288
FT /evidence="ECO:0007829|PDB:2E5A"
FT STRAND 293..303
FT /evidence="ECO:0007829|PDB:2E5A"
FT STRAND 306..313
FT /evidence="ECO:0007829|PDB:2E5A"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:2E5A"
FT HELIX 321..331
FT /evidence="ECO:0007829|PDB:2E5A"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:2E5A"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:3A7U"
FT HELIX 357..370
FT /evidence="ECO:0007829|PDB:2E5A"
SQ SEQUENCE 373 AA; 42072 MW; 101ECE836B9D11E0 CRC64;
MLIPFSMKNC FQLLCNLKVP AAGFKNTVKS GLILQSISND VYHNLAVEDW IHDHMNLEGK
PVLFLWRNSP TVVIGRHQNP WQECNLNLMR EEGVKLARRR SGGGTVYHDM GNINLTFFTT
KKKYDRMENL KLVVRALKAV HPHLDVQATK RFDLLLDGQF KISGTASKIG RNAAYHHCTL
LCGTDGTFLS SLLKSPYQGI RSNATASTPA LVKNLMEKDP TLTCEVVINA VATEYATSHQ
IDNHIHLINP TDETVFPGIN SKAIELQTWE WIYGKTPKFS VDTSFTVLHE QSHVEIKVFI
DVKNGRIEVC NIEAPDHWLP LEICDQLNSS LIGSKFSPIE TTVLTSILHR TYPGDDELHS
KWNILCEKIK GIM
