ID A8FF37_BACP2 Unreviewed; 278 AA.
AC A8FF37;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
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 OrderedLocusNames=BPUM_2185 {ECO:0000313|EMBL:ABV62854.1};
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV62854.1, ECO:0000313|Proteomes:UP000001355};
RN [1] {ECO:0000313|EMBL:ABV62854.1, ECO:0000313|Proteomes:UP000001355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV62854.1,
RC ECO:0000313|Proteomes:UP000001355};
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(2007).
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; CP000813; ABV62854.1; -; Genomic_DNA.
DR RefSeq; WP_003216009.1; NZ_VEIS01000005.1.
DR AlphaFoldDB; A8FF37; -.
DR STRING; 315750.BPUM_2185; -.
DR KEGG; bpu:BPUM_2185; -.
DR eggNOG; COG0095; Bacteria.
DR HOGENOM; CLU_022986_5_0_9; -.
DR OrthoDB; 9774653at2; -.
DR Proteomes; UP000001355; 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: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 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; 32081 MW; E6A5D06E4B483C2C CRC64;
MQKEKWCFID TGNQDPAFNM AMDEALLYWH SEKLIPPVIR FYGWNPATLS VGYFQHVEKE
INMEAVERYG LGFVRRPTGG RGVLHDQELT YSVIVSEEHP EMPATVTEAY RVISEGILEG
FKELGLDAYF AIPRTDKEKE SLKNPRSSVC FDAPSWYELV VEGRKVAGSA QTRQKGVILQ
HGSILIDLDE DKLFDLFLYP NDRVRERMQR SFKNKAVAIN EISDRTCTID DARVAFKRGF
EKGLNIELVP YELTDEELAF VHHLAKTKYA SDEWNYKR
//
