ID A0A0U3MYX9_9LACT Unreviewed; 290 AA.
AC A0A0U3MYX9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=NY10_1994 {ECO:0000313|EMBL:ALV22583.1};
OS Carnobacterium sp. CP1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1564681 {ECO:0000313|EMBL:ALV22583.1, ECO:0000313|Proteomes:UP000064734};
RN [1] {ECO:0000313|EMBL:ALV22583.1, ECO:0000313|Proteomes:UP000064734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CP1 {ECO:0000313|EMBL:ALV22583.1,
RC ECO:0000313|Proteomes:UP000064734};
RA Chen J., Yang J., Zhu S., Zhang D., Xiong S.;
RT "Whole genome Sequence of Carnobacterium sp. strain CP1 Isolated from
RT Amanda bay, East Antarctic.";
RL Submitted (FEB-2015) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP010796; ALV22583.1; -; Genomic_DNA.
DR RefSeq; WP_058919778.1; NZ_CP010796.1.
DR AlphaFoldDB; A0A0U3MYX9; -.
DR STRING; 1564681.NY10_1994; -.
DR KEGG; carc:NY10_1994; -.
DR PATRIC; fig|1564681.3.peg.2004; -.
DR OrthoDB; 2080934at2; -.
DR Proteomes; UP000064734; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Ligase {ECO:0000313|EMBL:ALV22583.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000064734};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02119}.
FT DOMAIN 46..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 290 AA; 32651 MW; 9FDC9A89E3805A57 CRC64;
MPEIEKTDFL TNHSYLLFDA ATMPFNNQPV AHFALADSLM TYIGKNQQQA ALHFWPTSDL
VILGMMDTKL PYFRDALASL KANDQHYIVR NSGGLAVVGD EGVLNFSLIF PEDPENKISI
DEGYEFMLRL IREAFGAYAK TIEAYEIPDS YCPGDFDLSI DGKKFAGIAQ RRLKNGVAVM
IYLSVNGNQQ KRAQMLHDFY AAGLKGETVK WHFPTIDPAV MGTLEELLGV SLTVADVEEK
ILQALQKNHC TIQNGNYTPD ILASYEEAKQ KMIRRNVQML QDDLEKELLD
//
