LIPB_PSEMY
ID LIPB_PSEMY Reviewed; 205 AA.
AC A4XYX4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Pmen_3792;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) 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; CP000680; ABP86540.1; -; Genomic_DNA.
DR RefSeq; WP_012019715.1; NC_009439.1.
DR AlphaFoldDB; A4XYX4; -.
DR SMR; A4XYX4; -.
DR STRING; 399739.Pmen_3792; -.
DR EnsemblBacteria; ABP86540; ABP86540; Pmen_3792.
DR KEGG; pmy:Pmen_3792; -.
DR PATRIC; fig|399739.8.peg.3845; -.
DR eggNOG; COG0321; Bacteria.
DR HOGENOM; CLU_035168_3_1_6; -.
DR OMA; GEVTYHC; -.
DR OrthoDB; 1806796at2; -.
DR UniPathway; UPA00538; UER00592.
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 Pfam; PF03099; BPL_LplA_LipB; 1.
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; Transferase.
FT CHAIN 1..205
FT /note="Octanoyltransferase"
FT /id="PRO_0000321660"
FT DOMAIN 30..205
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT ACT_SITE 167
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 69..76
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 136..138
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 149..151
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT SITE 133
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
SQ SEQUENCE 205 AA; 22631 MW; 41D4E4198E2E3AB0 CRC64;
MPELVVRHLG LVEYQPTLES MRQLTRERDE RTADEIWLLQ HPKVFTQGQA GKAEHLLAPG
DIPVVQVERG GQVTYHGPGQ LVAYLMLDLR RLDLGVRELV TAMEQSLVDL LASYGIEAAP
KADAPGVYVA GDKIASLGLR VSRGCSFHGL ALNVDMDMTP FLRINPCGYA GLKMVQMRDL
LPSPPAFDEV SQRLEQALRA RLGYA
