ID A0A1B0AL12_9MUSC Unreviewed; 227 AA.
AC A0A1B0AL12;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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};
OS Glossina palpalis gambiensis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=67801 {ECO:0000313|EnsemblMetazoa:GPPI000500-PA, ECO:0000313|Proteomes:UP000092460};
RN [1] {ECO:0000313|Proteomes:UP000092460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000092460};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GPPI000500-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPPI000500-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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; JXJN01029586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A1B0AL12; -.
DR STRING; 67801.A0A1B0AL12; -.
DR EnsemblMetazoa; GPPI000500-RA; GPPI000500-PA; GPPI000500.
DR VEuPathDB; VectorBase:GPPI000500; -.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000092460; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR016262}.
FT DOMAIN 39..220
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT ACT_SITE 181
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-1"
FT BINDING 83..90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT BINDING 150..152
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT BINDING 163..165
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-2"
FT SITE 147
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-3"
SQ SEQUENCE 227 AA; 26267 MW; DEDB0B94A4A020F7 CRC64;
MTLKSRPLVS VLRIGLINYN TGLQLQKMLS NQSIDHHRWD FHNYLILQEH KPVYTIGIRR
QDYIEEDEKR LRKLGAEFYR TNRGGLITFH GPGQLVAYPI IHLQQFTPSM RWYVSALEEL
IIRTCRELGI AEATRTEHTG IWVKDRKICA IGVHGSRYIT THGIGLNCCT NLKWFEHIVP
CGIEGKGVTS LSEQLDRRVT VEESIEVLLK MFAEVFQCQL CEENNNT
//