ID A0A0N4VH30_ENTVE Unreviewed; 228 AA.
AC A0A0N4VH30;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=EVEC_LOCUS9476 {ECO:0000313|EMBL:VDD94725.1};
OS Enterobius vermicularis (Human pinworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0001013101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EVEC_0001013101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDD94725.1, ECO:0000313|Proteomes:UP000274131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (OCT-2018) 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. 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; UXUI01010074; VDD94725.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4VH30; -.
DR STRING; 51028.A0A0N4VH30; -.
DR WBParaSite; EVEC_0001013101-mRNA-1; EVEC_0001013101-mRNA-1; EVEC_0001013101.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000038041; Unplaced.
DR Proteomes; UP000274131; 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 InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR000544; Octanoyltransferase.
DR InterPro; IPR020605; Octanoyltransferase_CS.
DR PANTHER; PTHR10993:SF7; LIPOYLTRANSFERASE 2, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR10993; OCTANOYLTRANSFERASE; 1.
DR PIRSF; PIRSF016262; LPLase; 2.
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:UP000274131};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR016262}.
FT DOMAIN 44..228
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT ACT_SITE 173
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR016262-1"
SQ SEQUENCE 228 AA; 25492 MW; D95C4FEC6A26BB8A CRC64;
MHVSRCLKSS VLEAVHFGRI SYSSGLEVQK QFFERIKKAK AYGRVRRNYL LLLEHDPVYT
VGLRSHVYSS AEEARLKKLG ASFYRTNRGG LITFHGPGQL VAYPIFDLNS LAVRSEAESS
VKVGVRRFVF LVEEAIIQTL HKFGLTEAAR SEATGTALNC NTDLRWFHEI IPCGLVGKEV
TSLTKEFGRE VCVSDLLRPL SETFAAVFQC TLEFHDNCLS SSNLLSIG
//
