ID A0A1I1XMD1_9BACI Unreviewed; 283 AA.
AC A0A1I1XMD1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Octanoyl-[GcvH]:protein N-octanoyltransferase {ECO:0000256|HAMAP-Rule:MF_02119};
DE EC=2.3.1.204 {ECO:0000256|HAMAP-Rule:MF_02119};
DE AltName: Full=Octanoyl-[GcvH]:E2 amidotransferase {ECO:0000256|HAMAP-Rule:MF_02119};
GN Name=lipL {ECO:0000256|HAMAP-Rule:MF_02119};
GN ORFNames=SAMN05216238_10840 {ECO:0000313|EMBL:SFE08525.1};
OS Lentibacillus persicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX NCBI_TaxID=640948 {ECO:0000313|EMBL:SFE08525.1, ECO:0000313|Proteomes:UP000199474};
RN [1] {ECO:0000313|EMBL:SFE08525.1, ECO:0000313|Proteomes:UP000199474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22530 {ECO:0000313|EMBL:SFE08525.1,
RC ECO:0000313|Proteomes:UP000199474};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the amidotransfer (transamidation) of the octanoyl
CC moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of
CC lipoate-dependent enzymes. {ECO:0000256|HAMAP-Rule:MF_02119}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[lipoyl-carrier protein] + N(6)-octanoyl-L-lysyl-
CC [glycine-cleavage complex H protein] = L-lysyl-[glycine-cleavage
CC complex H protein] + N(6)-octanoyl-L-lysyl-[lipoyl-carrier protein];
CC Xref=Rhea:RHEA:20213, Rhea:RHEA-COMP:10500, Rhea:RHEA-COMP:10501,
CC Rhea:RHEA-COMP:10503, Rhea:RHEA-COMP:10504, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:78809; EC=2.3.1.204; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02119};
CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC protein]. {ECO:0000256|HAMAP-Rule:MF_02119}.
CC -!- MISCELLANEOUS: The reaction proceeds via a thioester-linked acyl-enzyme
CC intermediate. {ECO:0000256|HAMAP-Rule:MF_02119}.
CC -!- SIMILARITY: Belongs to the octanoyltransferase LipL family.
CC {ECO:0000256|HAMAP-Rule:MF_02119}.
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DR EMBL; FOMR01000008; SFE08525.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1XMD1; -.
DR STRING; 640948.SAMN05216238_10840; -.
DR OrthoDB; 2080934at2; -.
DR Proteomes; UP000199474; Unassembled WGS sequence.
DR GO; GO:0016415; F:octanoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009107; P:lipoate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd16443; LplA; 1.
DR HAMAP; MF_02119; LipL; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR024897; LipL.
DR PANTHER; PTHR43679:SF3; OCTANOYL-[GCVH]:PROTEIN N-OCTANOYLTRANSFERASE; 1.
DR PANTHER; PTHR43679; OCTANOYLTRANSFERASE LIPM-RELATED; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_02119};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02119, ECO:0000313|EMBL:SFE08525.1}.
FT DOMAIN 48..232
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT ACT_SITE 152
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02119"
FT SITE 164
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02119"
SQ SEQUENCE 283 AA; 32419 MW; 0AAF424F6B4BA568 CRC64;
MKNWRDMVAY KRFRWLDHTG KKYFHGKSYT ALTSFAVDDV LSLFVRGGEA TPAIRLWTHP
ETVVLGIPDS RLPYLKEGVR MLSENGYYTI VRNSGGLAVA LDDGVLNMSL VLPDMKRISI
YDCYEAMVSF VRFVLRDLTD DIEAYEIVGS YCPGDYDLSI RGRKFAGISQ RRVRDGAAIQ
IYLDVEGKGR ERAELIRDFY EVAKKDAETK FTYPVVNPAV MASLSELLGM DLTVSDMKKR
VQNALEHLTD EIVTEDFSIG ELEQFEKRYN QMVKRNEEIA EMQ
//
