ID   LIPT2_XENTR             Reviewed;         239 AA.
AC   Q0VFH3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Putative lipoyltransferase 2, mitochondrial;
DE            EC=2.3.1.181;
DE   AltName: Full=Lipoate-protein ligase B;
DE   AltName: Full=Lipoyl/octanoyl transferase;
DE   AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase;
DE   Flags: Precursor;
GN   Name=lipt2;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid
CC       from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-
CC       dependent enzymes, which catalyze essential redox reactions (By
CC       similarity). Lipoyl-ACP can also act as a substrate although octanoyl-
CC       ACP is likely to be the physiological substrate (By similarity).
CC       {ECO:0000250, ECO:0000250|UniProtKB:A6NK58}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-
CC         octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA-
CC         COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181;
CC   -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC       pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC       protein]: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:A6NK58}.
CC   -!- MISCELLANEOUS: In the reaction, the free carboxyl group of octanoic
CC       acid is attached via an amide linkage to the epsilon-amino group of a
CC       specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LipB family. {ECO:0000305}.
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DR   EMBL; BC118829; AAI18830.1; -; mRNA.
DR   RefSeq; NP_001072237.1; NM_001078769.1.
DR   AlphaFoldDB; Q0VFH3; -.
DR   SMR; Q0VFH3; -.
DR   DNASU; 779684; -.
DR   GeneID; 779684; -.
DR   KEGG; xtr:779684; -.
DR   CTD; 387787; -.
DR   Xenbase; XB-GENE-6458907; lipt2.
DR   InParanoid; Q0VFH3; -.
DR   UniPathway; UPA00538; UER00592.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:2000376; P:positive regulation of oxygen metabolic process; ISS:UniProtKB.
DR   GO; GO:0009249; P:protein lipoylation; ISS:UniProtKB.
DR   CDD; cd16444; LipB; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00013; LipB; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR000544; Octanoyltransferase.
DR   InterPro; IPR020605; Octanoyltransferase_CS.
DR   PIRSF; PIRSF016262; LPLase; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00214; lipB; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR   PROSITE; PS01313; LIPB; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Ligase; Mitochondrion; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..18
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..239
FT                   /note="Putative lipoyltransferase 2, mitochondrial"
FT                   /id="PRO_0000332308"
FT   DOMAIN          37..217
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   REGION          220..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        178
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         81..88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         147..149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         160..162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            144
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   239 AA;  25864 MW;  F73206DB0689A279 CRC64;
     MSVPVLRVRR LGLVGYAEAL GVQGRYVREL KAGGEAGSPG GALLLCEHPA VYTVGVRRGR
     YPGEEEARLR GLGADFQRTD RGGLITFHGP GQLVCYPVLH LGALRRSLRS YVCGLESAVI
     RLCRGLGLPG ERQPDTGVWV RGNKICAIGV HCARHITSHG LALNCNTDLG WFGHIVPCGI
     VGKGVTSLTQ ELGRQVTIDD IIAPFLEAFE EEFQCQLVPE QNPEQNPVQN RPDRDAGPL