ID   LIPM_CARHZ              Reviewed;         269 AA.
AC   Q3AET1;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=CHY_0495;
OS   Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS   Z-2901).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Carboxydothermus.
OX   NCBI_TaxID=246194;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX   PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA   Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA   Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA   Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT   "Life in hot carbon monoxide: the complete genome sequence of
RT   Carboxydothermus hydrogenoformans Z-2901.";
RL   PLoS Genet. 1:563-574(2005).
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; CP000141; ABB13955.1; -; Genomic_DNA.
DR   RefSeq; WP_011343429.1; NC_007503.1.
DR   AlphaFoldDB; Q3AET1; -.
DR   SMR; Q3AET1; -.
DR   STRING; 246194.CHY_0495; -.
DR   EnsemblBacteria; ABB13955; ABB13955; CHY_0495.
DR   KEGG; chy:CHY_0495; -.
DR   eggNOG; COG0095; Bacteria.
DR   HOGENOM; CLU_022986_5_0_9; -.
DR   OMA; YAYLDDW; -.
DR   OrthoDB; 871298at2; -.
DR   Proteomes; UP000002706; Chromosome.
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; Reference proteome; Transferase.
FT   CHAIN           1..269
FT                   /note="Octanoyltransferase LipM"
FT                   /id="PRO_0000410854"
FT   DOMAIN          31..239
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   ACT_SITE        141
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02118"
FT   SITE            156
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02118"
SQ   SEQUENCE   269 AA;  30792 MW;  F0FDF64C1EFEABB0 CRC64;
     METWRFIDHC SFSGAENMAI DEALLQEAIN NHGAPVLRFY TWTRPTLSLG YFQKAQEEVD
     FSECEKLGVE VVRRPTGGRA VLHEFELTYS IVGSIQHPKL SGTVLESYLK ISKGLLLGLK
     NLGIEGEIAE GKKTSDLSAI CFEAPSWYEL TVMGRKVIGS AQVRRGDYLL QHGAIVIKMD
     VDKLFRVLKF KSLEQKERIR ASFHRKAGAI HDFSSREFSL AEIKEAFLAG FSEGFEVNFI
     RSELSLKERE LSRQLLREKY NTREWLFRF