ID A0A160F6R0_9BACI Unreviewed; 278 AA.
AC A0A160F6R0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=GFC30_2613 {ECO:0000313|EMBL:ANB61832.1};
OS Anoxybacillus amylolyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=294699 {ECO:0000313|EMBL:ANB61832.1, ECO:0000313|Proteomes:UP000076865};
RN [1] {ECO:0000313|EMBL:ANB61832.1, ECO:0000313|Proteomes:UP000076865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15939 {ECO:0000313|EMBL:ANB61832.1,
RC ECO:0000313|Proteomes:UP000076865};
RX PubMed=16682297; DOI=10.1016/j.syapm.2005.10.003;
RA Poli A., Esposito E., Lama L., Orlando P., Nicolaus G., de Appolonia F.,
RA Gambacorta A., Nicolaus B.;
RT "Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing
RT bacterium isolated from Mount Rittmann (Antarctica).";
RL Syst. Appl. Microbiol. 29:300-307(2006).
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}.
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DR EMBL; CP015438; ANB61832.1; -; Genomic_DNA.
DR RefSeq; WP_066326178.1; NZ_CP015438.1.
DR AlphaFoldDB; A0A160F6R0; -.
DR KEGG; aamy:GFC30_2613; -.
DR PATRIC; fig|294699.3.peg.2693; -.
DR OrthoDB; 9774653at2; -.
DR Proteomes; UP000076865; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Ligase {ECO:0000313|EMBL:ANB61832.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076865};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02118}.
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; 31963 MW; 79DD08AB591B2812 CRC64;
MEKERWRFID SGDCSPAFNM ALDEALLEWH SEGKIPPTIR FYGWNPPTLS IGYFQKVEKE
IDMEAVKKYS LGFVRRPTGG RGVLHDQELT YSVIVSESHP AMPQTVTEAY RVISQGILEG
FRFLGLDAYF AVPKTEEEKA DLKNPRSAVC FDAPSWYELV VEGRKVAGSA QTRQKGVILQ
HGSILLDLDE EMLFSLFKYP NERVKERLRQ NFKHKAVAIN ELTERKITLS EAKEAFFKGF
EKGLEIVLEP YTLSAEEMAY VNELAEKKYA SDEWNFKR
//
