LIPM_EXISA
ID LIPM_EXISA Reviewed; 276 AA.
AC C4KZ18;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
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=EAT1b_1404;
OS Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC Bacteria; Firmicutes; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium;
OC unclassified Exiguobacterium.
OX NCBI_TaxID=360911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1283 / AT1b;
RX PubMed=21460088; DOI=10.1128/jb.00303-11;
RA Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina del Rio T.,
RA Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA Hendrix C., Richardson P., Tiedje J.M.;
RT "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT AT1b.";
RL J. Bacteriol. 193:2880-2881(2011).
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; CP001615; ACQ70331.1; -; Genomic_DNA.
DR RefSeq; WP_012727450.1; NC_012673.1.
DR AlphaFoldDB; C4KZ18; -.
DR SMR; C4KZ18; -.
DR STRING; 360911.EAT1b_1404; -.
DR PRIDE; C4KZ18; -.
DR EnsemblBacteria; ACQ70331; ACQ70331; EAT1b_1404.
DR KEGG; eat:EAT1b_1404; -.
DR eggNOG; COG0095; Bacteria.
DR HOGENOM; CLU_022986_5_0_9; -.
DR OMA; YAYLDDW; -.
DR OrthoDB; 871298at2; -.
DR Proteomes; UP000000716; 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..276
FT /note="Octanoyltransferase LipM"
FT /id="PRO_0000410857"
FT DOMAIN 33..247
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT ACT_SITE 150
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02118"
FT SITE 165
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02118"
SQ SEQUENCE 276 AA; 31019 MW; 9B4B2366B9B5BC80 CRC64;
MTGTTWHLLR TESTSPAENM AIDEAIANWV AKGELKPTLR FYSWAPHAIS VGRFQRATRD
LDRDALEANN IPVVRRLTGG RAVLHADELT YSVILPESTP ALPTNIIESY RLLTEGVRRG
YRELGVPAEF SVPLTEEDRE ALRKPKSAVC FDAASYYELA VDGKKIAGSA QVRHQGAVLQ
HGSIPLSVDD EVLFDCFAMD ETEKQEAKTR FSEKAVALND TLKRFVSFDE VAAAFETGFK
DAFSLTFEPL VFTKEQQAEI DLLVKKYESD EWVWKR
