ID G0L2I5_ZOBGA Unreviewed; 239 AA.
AC G0L2I5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
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:CAZ95008.1};
GN OrderedLocusNames=zobellia_950 {ECO:0000313|EMBL:CAZ95008.1};
OS Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
OS NCIMB 13871 / Dsij).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zobellia.
OX NCBI_TaxID=63186 {ECO:0000313|EMBL:CAZ95008.1, ECO:0000313|Proteomes:UP000008898};
RN [1] {ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RG Genoscope - CEA;
RT "Complete genome sequence of Zobellia galactanivorans Dsij.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAZ95008.1, ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RX PubMed=22513138; DOI=10.1111/j.1462-2920.2012.02751.x;
RA Thomas F., Barbeyron T., Tonon T., Genicot S., Czjzek M., Michel G.;
RT "Characterization of the first alginolytic operons in a marine bacterium:
RT from their emergence in marine Flavobacteriia to their independent
RT transfers to marine Proteobacteria and human gut Bacteroides.";
RL Environ. Microbiol. 14:2379-2394(2012).
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}.
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DR EMBL; FP476056; CAZ95008.1; -; Genomic_DNA.
DR RefSeq; WP_013992320.1; NZ_JAUOSS010000018.1.
DR AlphaFoldDB; G0L2I5; -.
DR STRING; 63186.ZOBELLIA_950; -.
DR KEGG; zga:ZOBELLIA_950; -.
DR PATRIC; fig|63186.3.peg.933; -.
DR HOGENOM; CLU_035168_1_3_10; -.
DR OrthoDB; 9787061at2; -.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000008898; 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; OCTANOYLTRANSFERASE; 1.
DR PANTHER; PTHR10993:SF12; OCTANOYLTRANSFERASE LIP2P, CHLOROPLASTIC-RELATED; 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:UP000008898};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00013}.
FT DOMAIN 43..231
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT ACT_SITE 191
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT ECO:0000256|PIRSR:PIRSR016262-1"
FT BINDING 88..95
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT ECO:0000256|PIRSR:PIRSR016262-2"
FT BINDING 160..162
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT ECO:0000256|PIRSR:PIRSR016262-2"
FT BINDING 173..175
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT ECO:0000256|PIRSR:PIRSR016262-2"
FT SITE 157
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT ECO:0000256|PIRSR:PIRSR016262-3"
SQ SEQUENCE 239 AA; 27232 MW; 11B6F5F3DA9E7ED6 CRC64;
MNKKVLFQDL GQKDYKETWD YQELLFKQTV DLKIKNRREE ADEPTPNHFL FVEHPHVYTL
GKSGDLANLL VGEEELAAKK AKFYKINRGG DITYHGPGQI VGYPILDLDN FFTDIHKYLR
FLEEMVILTL AEYGVKAERS EGETGVWLDV GTPFARKICA MGVRASRWVT MHGFALNVNA
DLGYFDLMIP CGIKDKAVTS LNVELGKKEV DLNEVKGKLL KHFEALFEAE IIEQEKTSA
//