ID   LIPM_MOOTA              Reviewed;         273 AA.
AC   Q2RH52;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Octanoyltransferase LipM {ECO:0000255|HAMAP-Rule:MF_02118};
DE            EC=2.3.1.181 {ECO:0000255|HAMAP-Rule:MF_02118};
DE   AltName: Full=Octanoyl-[acyl-carrier-protein]:[GcvH] N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_02118};
GN   Name=lipM {ECO:0000255|HAMAP-Rule:MF_02118}; OrderedLocusNames=Moth_1939;
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39073 / JCM 9320;
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT   thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(2008).
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_02118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|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:0000255|HAMAP-Rule:MF_02118}.
CC   -!- SIMILARITY: Belongs to the octanoyltransferase LipM family.
CC       {ECO:0000255|HAMAP-Rule:MF_02118}.
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DR   EMBL; CP000232; ABC20237.1; -; Genomic_DNA.
DR   RefSeq; WP_011393437.1; NC_007644.1.
DR   RefSeq; YP_430780.1; NC_007644.1.
DR   AlphaFoldDB; Q2RH52; -.
DR   SMR; Q2RH52; -.
DR   STRING; 264732.Moth_1939; -.
DR   EnsemblBacteria; ABC20237; ABC20237; Moth_1939.
DR   GeneID; 61290704; -.
DR   KEGG; mta:Moth_1939; -.
DR   PATRIC; fig|264732.11.peg.2102; -.
DR   eggNOG; COG0095; Bacteria.
DR   HOGENOM; CLU_022986_5_0_9; -.
DR   OMA; YAYLDDW; -.
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:0009249; P:protein lipoylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 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   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Transferase.
FT   CHAIN           1..273
FT                   /note="Octanoyltransferase LipM"
FT                   /id="PRO_0000410861"
FT   DOMAIN          33..244
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   ACT_SITE        146
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02118"
FT   SITE            161
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02118"
SQ   SEQUENCE   273 AA;  30196 MW;  DDD550CBBB53A653 CRC64;
     MPAETWRLLD TGVSDPYTNM AIDEAILLEH REGKTPPTLR FYAWSPPTIS LGYFQQLEKE
     IDLEAVKERG LGLVRRLTGG RAVLHDDEVT YSVVAREDHP LMIGGIRPSY LRLAKALAAG
     LRELGAPVEI ASGRKGGREE HTTAACFDAP SWYEITCGGR KLVGSAQTRK GGVVLQHGSI
     VLTLNGDDLF AVLKMPSEAV RQRLLAKFYH QACGLEEVLG RRVEAGVIKE NIVRAFTRLY
     AVEFVPGGLT EGEKGRLKEL RAKYAAADWL KRR