ID A0A0S8BCE8_9PROT Unreviewed; 212 AA.
AC A0A0S8BCE8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 ORFNames=AMJ64_00300 {ECO:0000313|EMBL:KPK09327.1};
OS Betaproteobacteria bacterium SG8_39.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703390 {ECO:0000313|EMBL:KPK09327.1, ECO:0000313|Proteomes:UP000051483};
RN [1] {ECO:0000313|EMBL:KPK09327.1, ECO:0000313|Proteomes:UP000051483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_39 {ECO:0000313|EMBL:KPK09327.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPK09327.1}.
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DR EMBL; LJTQ01000002; KPK09327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8BCE8; -.
DR STRING; 1703390.AMJ64_00300; -.
DR PATRIC; fig|1703390.3.peg.1607; -.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000051483; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Ligase {ECO:0000313|EMBL:KPK09327.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00013}.
FT DOMAIN 38..212
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT ACT_SITE 175
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT ECO:0000256|PIRSR:PIRSR016262-1"
FT BINDING 77..84
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT ECO:0000256|PIRSR:PIRSR016262-2"
FT BINDING 144..146
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT ECO:0000256|PIRSR:PIRSR016262-2"
FT BINDING 157..159
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT ECO:0000256|PIRSR:PIRSR016262-2"
FT SITE 141
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013,
FT ECO:0000256|PIRSR:PIRSR016262-3"
SQ SEQUENCE 212 AA; 22829 MW; BE6C659C2A1C851D CRC64;
MAAVLAPQHP GLVLKRLGCV EYLEALEAMR RFTRTRDAHT PDALWLLEHP PVYTLGQGAD
PKHGPRHGDI PVLRVERGGE VTYHGPGQVV LYTLVDLGRR AIRVRDFVCL LEQAVIDLLA
THGVRAERRP GAPGVYVDDA KVAALGIRVA RGRAFHGLAL NVDMDLAPFE AIDPCGYPGL
RVTQTRDLGI ALTPAQAGAA LAAQLEKGLA HA
//
