ID E4X8T7_OIKDI Unreviewed; 222 AA.
AC E4X8T7;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase LIPT2, mitochondrial {ECO:0000256|PIRNR:PIRNR016262};
DE EC=2.3.1.181 {ECO:0000256|PIRNR:PIRNR016262};
GN ORFNames=GSOID_T00004570001 {ECO:0000313|EMBL:CBY19147.1},
GN GSOID_T00024250001 {ECO:0000313|EMBL:CBY34237.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY19147.1};
RN [1] {ECO:0000313|EMBL:CBY19147.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097902; DOI=10.1126/science.1194167;
RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA Roest Crollius H., Wincker P., Chourrout D.;
RT "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT pelagic tunicate.";
RL Science 330:1381-1385(2010).
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. Lipoyl-ACP can also act as a substrate although
CC octanoyl-ACP is likely to be the physiological substrate.
CC {ECO:0000256|PIRNR:PIRNR016262}.
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 Evidence={ECO:0000256|PIRNR:PIRNR016262};
CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC protein]: step 1/2. {ECO:0000256|ARBA:ARBA00004821,
CC ECO:0000256|PIRNR:PIRNR016262}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|PIRNR:PIRNR016262}.
CC -!- SIMILARITY: Belongs to the LipB family. {ECO:0000256|ARBA:ARBA00007907,
CC ECO:0000256|PIRNR:PIRNR016262}.
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DR EMBL; FN653030; CBY19147.1; -; Genomic_DNA.
DR EMBL; FN654488; CBY34237.1; -; Genomic_DNA.
DR AlphaFoldDB; E4X8T7; -.
DR InParanoid; E4X8T7; -.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000001307; Unassembled WGS sequence.
DR Proteomes; UP000011014; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd16444; LipB; 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 NCBIfam; TIGR00214; lipB; 1.
DR PANTHER; PTHR10993:SF7; LIPOYLTRANSFERASE 2, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR10993; OCTANOYLTRANSFERASE; 1.
DR PIRSF; PIRSF016262; LPLase; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR PROSITE; PS01313; LIPB; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR016262};
KW Mitochondrion {ECO:0000256|PIRNR:PIRNR016262};
KW Reference proteome {ECO:0000313|Proteomes:UP000001307};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR016262}.
FT DOMAIN 38..217
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT ACT_SITE 178
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-1"
FT BINDING 82..89
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT BINDING 147..149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT BINDING 160..162
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT SITE 144
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-3"
SQ SEQUENCE 222 AA; 24722 MW; A5A9EC8F72FB9AE8 CRC64;
MAAALTRPIR TKWLNRINYG EALKLQHNLV NQHLSKPDAT SNQLLLLEHP PTYTVGKRGA
IYDNTVEEYL REKGADFYRV NRGGLITFHG PGQLVAYPIL KLERRNAIRW YVDTLEVAII
DLLGEFGLNG ETSPHTGVWI GDNKICAMGI NAQKEVTSHG LAINCNTDMS WFGNIVPCGI
QDKGVTSLSK ELGREVTVQE VAPILIQKLS KHLKVPVEEL SI
//
