ID F7XUB3_MIDMI Unreviewed; 224 AA.
AC F7XUB3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Octanoyltransferase {ECO:0000256|HAMAP-Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262};
DE EC=2.3.1.181 {ECO:0000256|HAMAP-Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262};
DE AltName: Full=Lipoate-protein ligase B {ECO:0000256|HAMAP-Rule:MF_00013};
DE AltName: Full=Lipoyl/octanoyl transferase {ECO:0000256|HAMAP-Rule:MF_00013};
DE AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000256|HAMAP-Rule:MF_00013};
GN Name=lipB {ECO:0000256|HAMAP-Rule:MF_00013,
GN ECO:0000313|EMBL:AEI89472.1};
GN OrderedLocusNames=midi_01196 {ECO:0000313|EMBL:AEI89472.1};
OS Midichloria mitochondrii (strain IricVA).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Candidatus Midichloriaceae; Midichloria.
OX NCBI_TaxID=696127 {ECO:0000313|EMBL:AEI89472.1, ECO:0000313|Proteomes:UP000006639};
RN [1] {ECO:0000313|EMBL:AEI89472.1, ECO:0000313|Proteomes:UP000006639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IricVA {ECO:0000313|EMBL:AEI89472.1,
RC ECO:0000313|Proteomes:UP000006639};
RX PubMed=21690562; DOI=10.1093/molbev/msr159;
RA Sassera D., Lo N., Epis S., D'Auria G., Montagna M., Comandatore F.,
RA Horner D., Pereto J., Luciano A.M., Franciosi F., Ferri E., Crotti E.,
RA Bazzocchi C., Daffonchio D., Sacchi L., Moya A., Latorre A., Bandi C.;
RT "Phylogenomic evidence for the presence of a flagellum and cbb3 oxidase in
RT the free-living mitochondrial ancestor.";
RL Mol. Biol. Evol. 28:3285-3296(2011).
CC -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid
CC from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-
CC dependent enzymes. Lipoyl-ACP can also act as a substrate although
CC octanoyl-ACP is likely to be the physiological substrate.
CC {ECO:0000256|ARBA:ARBA00024732, ECO:0000256|HAMAP-Rule:MF_00013,
CC ECO:0000256|PIRNR:PIRNR016262}.
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_00013,
CC ECO:0000256|PIRNR:PIRNR016262};
CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC protein]: step 1/2. {ECO:0000256|ARBA:ARBA00004821, ECO:0000256|HAMAP-
CC Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00013}.
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 {ECO:0000256|HAMAP-Rule:MF_00013}.
CC -!- SIMILARITY: Belongs to the LipB family. {ECO:0000256|HAMAP-
CC Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002130; AEI89472.1; -; Genomic_DNA.
DR AlphaFoldDB; F7XUB3; -.
DR STRING; 696127.midi_01196; -.
DR KEGG; mmn:midi_01196; -.
DR HOGENOM; CLU_035168_3_0_5; -.
DR OrthoDB; 9787061at2; -.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000006639; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd16444; LipB; 1.
DR HAMAP; MF_00013; LipB; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR000544; Octanoyltransferase.
DR InterPro; IPR020605; Octanoyltransferase_CS.
DR NCBIfam; TIGR00214; lipB; 1.
DR PANTHER; PTHR10993:SF7; LIPOYLTRANSFERASE 2, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR10993; OCTANOYLTRANSFERASE; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR PIRSF; PIRSF016262; LPLase; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR PROSITE; PS01313; LIPB; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_00013}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00013};
KW Reference proteome {ECO:0000313|Proteomes:UP000006639};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00013}.
FT DOMAIN 41..224
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT ACT_SITE 186
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT ECO:0000256|PIRSR:PIRSR016262-1"
FT BINDING 80..87
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT ECO:0000256|PIRSR:PIRSR016262-2"
FT BINDING 155..157
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT ECO:0000256|PIRSR:PIRSR016262-2"
FT BINDING 168..170
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT ECO:0000256|PIRSR:PIRSR016262-2"
FT SITE 152
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT ECO:0000256|PIRSR:PIRSR016262-3"
SQ SEQUENCE 224 AA; 25134 MW; 0FB9A835C7EC8B32 CRC64;
MERSECLFSN SFLSCFSSFN LVPYAAAISS MASVVDQILN RHHNSVLWFL EHDHLYTAGA
SANSSDLIAN PQAPIFTTDR GGKYTYHGPG QLIVYMMLDL KALYHNQPDI KKFVSDMCEW
LIASLKEVGA HCITDEENIG IWCFDETQNK KKIASIGLKL KKWVTYHGVA INISPDLSKF
NFIKPCGLSS HSISSLEALG HNIDISKLRS ILIKNFLIMF NIND
//
