ID A0A0M0GNP1_9BACI Unreviewed; 278 AA.
AC A0A0M0GNP1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Octanoyltransferase LipM {ECO:0000256|HAMAP-Rule:MF_02118};
DE EC=2.3.1.181 {ECO:0000256|HAMAP-Rule:MF_02118};
DE AltName: Full=Octanoyl-[acyl-carrier-protein]:[GcvH] N-octanoyltransferase {ECO:0000256|HAMAP-Rule:MF_02118};
GN Name=lipM {ECO:0000256|HAMAP-Rule:MF_02118};
GN ORFNames=AF331_02450 {ECO:0000313|EMBL:KON91403.1};
OS Rossellomorea marisflavi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=189381 {ECO:0000313|EMBL:KON91403.1, ECO:0000313|Proteomes:UP000037405};
RN [1] {ECO:0000313|Proteomes:UP000037405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 11544 {ECO:0000313|Proteomes:UP000037405};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-14235 jcm11544.";
RL Submitted (JUL-2015) 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 domain of GcvH, an
CC intermediate carrier during protein lipoylation. {ECO:0000256|HAMAP-
CC Rule:MF_02118}.
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|HAMAP-Rule:MF_02118};
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_02118}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02118}.
CC -!- MISCELLANEOUS: In the reaction, the free carboxyl group of octanoic
CC acid is attached via an amide linkage to the epsilon-amino group of a
CC specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
CC The reaction proceeds via an octanoyl-thioester enzyme intermediate.
CC {ECO:0000256|HAMAP-Rule:MF_02118}.
CC -!- SIMILARITY: Belongs to the octanoyltransferase LipM family.
CC {ECO:0000256|HAMAP-Rule:MF_02118}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KON91403.1}.
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DR EMBL; LGUE01000001; KON91403.1; -; Genomic_DNA.
DR RefSeq; WP_053426606.1; NZ_LGUE01000001.1.
DR AlphaFoldDB; A0A0M0GNP1; -.
DR STRING; 189381.GCA_900166615_03813; -.
DR GeneID; 42290788; -.
DR PATRIC; fig|189381.12.peg.577; -.
DR OrthoDB; 9774653at2; -.
DR Proteomes; UP000037405; Unassembled WGS sequence.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
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_02118; LipM; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR024898; LipM.
DR PANTHER; PTHR43679:SF2; OCTANOYLTRANSFERASE LIPM; 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_02118};
KW Reference proteome {ECO:0000313|Proteomes:UP000037405};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02118, ECO:0000313|EMBL:KON91403.1}.
FT DOMAIN 33..248
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT ACT_SITE 150
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02118"
FT SITE 165
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02118"
SQ SEQUENCE 278 AA; 31832 MW; 7100B6DADCE20E87 CRC64;
MEKEIWRFID SGHCSPSFNM ALDEALLDWH SEGKIPPTIR FYGWDPATLS IGYFQKVEKE
INMENVKKHN LGFVRRPTGG RGVLHEHELT YSVIVSEDHP DMPKTVTEAY RVISEGILQG
FRALGLEAYF AVPKTAEERE GLKNPRSAVC FDAPSWYELV VEGRKVAGSA QTRQKGVILQ
HGSILLDLDE DKLFSLFNYP NDRVKERMQR AFKSKAVAMN EISAEPITME MAKDAFKKGF
EDGLGIGLEP YELSPEETQY VEKLAKERYE SDEWNYKR
//
