ID   LIPB_ALBFT              Reviewed;         230 AA.
AC   Q21RG9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013};
DE            EC=2.3.1.181 {ECO:0000255|HAMAP-Rule:MF_00013};
DE   AltName: Full=Lipoate-protein ligase B {ECO:0000255|HAMAP-Rule:MF_00013};
DE   AltName: Full=Lipoyl/octanoyl transferase {ECO:0000255|HAMAP-Rule:MF_00013};
DE   AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013};
GN   Name=lipB {ECO:0000255|HAMAP-Rule:MF_00013}; OrderedLocusNames=Rfer_3935;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) 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.
CC       {ECO:0000255|HAMAP-Rule:MF_00013}.
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_00013};
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:0000255|HAMAP-Rule:MF_00013}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00013}.
CC   -!- SIMILARITY: Belongs to the LipB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00013}.
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DR   EMBL; CP000267; ABD71634.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q21RG9; -.
DR   SMR; Q21RG9; -.
DR   STRING; 338969.Rfer_3935; -.
DR   EnsemblBacteria; ABD71634; ABD71634; Rfer_3935.
DR   KEGG; rfr:Rfer_3935; -.
DR   eggNOG; COG0321; Bacteria.
DR   HOGENOM; CLU_035168_3_1_4; -.
DR   OMA; GEVTYHC; -.
DR   UniPathway; UPA00538; UER00592.
DR   Proteomes; UP000008332; 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: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; IPR000544; Octanoyltransferase.
DR   InterPro; IPR020605; Octanoyltransferase_CS.
DR   PIRSF; PIRSF016262; LPLase; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00214; lipB; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR   PROSITE; PS01313; LIPB; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..230
FT                   /note="Octanoyltransferase"
FT                   /id="PRO_0000242755"
FT   DOMAIN          31..230
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   ACT_SITE        194
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT   BINDING         70..77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT   BINDING         163..165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT   BINDING         176..178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT   SITE            160
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
SQ   SEQUENCE   230 AA;  25077 MW;  E8A1DBF941F09FEE CRC64;
     MAMDLLRHRL GRIDYLPAYE AMQVFTAART PETPDELWIC EHPPVYTQGL AGKAEHVFNP
     GTIPVVQTNR GGQVTYHGPG QVVAYPLLDL KRAGYFIKEY VYRIEEAVIR TLVEFGVTGH
     RVAGAPGIYV RLDDPGSHAL LPQRPMKSGL ANPSFGGLGK IAALGLKVSR NCTYHGVALN
     VAMDLEPYTR INPCGYAGLQ TVDLSTIGVC AGWDEVAELL GDKLTRYLAP