LIPM_ANOFW
ID LIPM_ANOFW Reviewed; 278 AA.
AC B7GHD6;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=Aflv_0919;
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1;
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(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; CP000922; ACJ33297.1; -; Genomic_DNA.
DR RefSeq; WP_012574579.1; NC_011567.1.
DR AlphaFoldDB; B7GHD6; -.
DR SMR; B7GHD6; -.
DR STRING; 491915.Aflv_0919; -.
DR EnsemblBacteria; ACJ33297; ACJ33297; Aflv_0919.
DR KEGG; afl:Aflv_0919; -.
DR PATRIC; fig|491915.6.peg.939; -.
DR eggNOG; COG0095; Bacteria.
DR HOGENOM; CLU_022986_5_0_9; -.
DR OMA; YAYLDDW; -.
DR OrthoDB; 871298at2; -.
DR Proteomes; UP000000742; 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..278
FT /note="Octanoyltransferase LipM"
FT /id="PRO_0000410847"
FT DOMAIN 33..248
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 278 AA; 32173 MW; 4CFE78BAC60EC580 CRC64;
MEKEVWRFID SGNCSPAFNM ALDEALLEWH SEGKIPPTIR FYGWNPPTLS IGYFQKVEKE
IDMEAVKKYG LGFVRRPTGG RGVLHDQELT YSVIVSELHP AMPQTVTEAY RVISQGILEG
FRFLGLDAYF AVPKTEEEKA DLKNPRSAVC FDAPSWYELV VEGRKVAGSA QTRQKGVILQ
HGSILLHLDE DMLFSLFKYP NERVKERLRQ NFKNKAVAIN ELTDRNITIN EAKEAFFRGF
EKGLNVQLER YELTDDELFY VQQLAKNKYE TDEWNFKR
