ID   LIPB_MYXXA              Reviewed;         357 AA.
AC   Q9X6X4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Octanoyltransferase;
DE            EC=2.3.1.181;
DE   AltName: Full=Lipoate-protein ligase B;
DE   AltName: Full=Lipoyl/octanoyl transferase;
DE   AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase;
GN   Name=lipB;
OS   Myxococcus xanthus.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=34;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Downard J.S., Kupfer D.M., Davis A.J., Roe B.A.;
RT   "Sequence analysis of SR171 mutant of the branched-chain keto acid
RT   dehydrogenase complex in Myxococcus xanthus.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       similarity). {ECO:0000250}.
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   -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC       pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC       protein]: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the LipB family.
CC       {ECO:0000305}.
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DR   EMBL; AF153678; AAD34635.1; -; Genomic_DNA.
DR   RefSeq; WP_011554218.1; NZ_JABFNQ010000025.1.
DR   AlphaFoldDB; Q9X6X4; -.
DR   SMR; Q9X6X4; -.
DR   GeneID; 41361532; -.
DR   OMA; RWLTTHG; -.
DR   UniPathway; UPA00538; UER00592.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009249; P:protein lipoylation; IEA:InterPro.
DR   CDD; cd16444; LipB; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00013; LipB; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR020476; Nudix_hydrolase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR000544; Octanoyltransferase.
DR   InterPro; IPR020605; Octanoyltransferase_CS.
DR   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   TIGRFAMs; TIGR00214; lipB; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR   PROSITE; PS01313; LIPB; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Hydrolase; Multifunctional enzyme; Transferase.
FT   CHAIN           1..357
FT                   /note="Octanoyltransferase"
FT                   /id="PRO_0000062852"
FT   DOMAIN          31..219
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   DOMAIN          224..356
FT                   /note="Nudix hydrolase"
FT   REGION          1..222
FT                   /note="LipB domain"
FT   MOTIF           261..282
FT                   /note="Nudix box"
FT   ACT_SITE        180
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         76..83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         149..151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         162..164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            146
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   357 AA;  39373 MW;  7FA08E117B4A77D3 CRC64;
     MNTITVYRLG RVEYEDGLAL MHLFSESRRQ GLSGDVLLLL EHPPILTLGR AAKRENIVAS
     DAQLAKEGAE VFETNRGGDV TYHGPGQLVG YPIFLLPEDR RDVRRYVRDV ERSVMQVLAQ
     WGITAGPIPK WPGVWIGAEG APDARKIAAI GVHLSRWLTT HGFALNVNTN LDHFQLIVPC
     GIREAGVTSM QRELGRALPM AEVEEAIANS FCTVFDSERV DAPPPMRTVS IAVVKGRGPE
     ARVLLVRRRP ERGGFWQVLT GRLEAGESPA QAAARELEEE TGLRVPLVDL DYRHAFALGE
     ALPPQLVEEN GFAVHVPPDA DVRLGAEHDA FEWVDVPTAL ERLPFQGLRE TVKRATA