ID A0A014KZJ8_9ACTN Unreviewed; 271 AA. AC A0A014KZJ8; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 22-FEB-2023, entry version 38. 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=Z951_41695 {ECO:0000313|EMBL:EXU62426.1}; OS Streptomyces sp. PRh5. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1158056 {ECO:0000313|EMBL:EXU62426.1, ECO:0000313|Proteomes:UP000019949}; RN [1] {ECO:0000313|EMBL:EXU62426.1, ECO:0000313|Proteomes:UP000019949} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PRh5 {ECO:0000313|EMBL:EXU62426.1, RC ECO:0000313|Proteomes:UP000019949}; RA Zhu D., Yang H., Wang Y., Zhang Z., Yan R.; RT "Whole-genome shotgun assembly and analysis of the genome of Streptomyces RT sp. PRh5, a strain for production of geldanamycin, nigericin and RT nocardamine."; RL Submitted (JAN-2014) 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: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|ARBA:ARBA00000953, ECO:0000256|HAMAP- CC Rule:MF_00013, 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:EXU62426.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JABQ01000105; EXU62426.1; -; Genomic_DNA. DR RefSeq; WP_051573945.1; NZ_JABQ01000105.1. DR AlphaFoldDB; A0A014KZJ8; -. DR EnsemblBacteria; EXU62426; EXU62426; Z951_41695. DR PATRIC; fig|1158056.3.peg.8354; -. DR OrthoDB; 9787061at2; -. DR UniPathway; UPA00538; UER00592. DR Proteomes; UP000019949; Unassembled WGS sequence. 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 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 PANTHER; PTHR10993:SF7; LIPOYLTRANSFERASE 2, MITOCHONDRIAL-RELATED; 1. DR PANTHER; PTHR10993; OCTANOYLTRANSFERASE; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00013}. FT DOMAIN 46..265 FT /note="BPL/LPL catalytic" FT /evidence="ECO:0000259|PROSITE:PS51733" FT ACT_SITE 226 FT /note="Acyl-thioester intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013, FT ECO:0000256|PIRSR:PIRSR016262-1" FT BINDING 84..91 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013, FT ECO:0000256|PIRSR:PIRSR016262-2" FT BINDING 195..197 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013, FT ECO:0000256|PIRSR:PIRSR016262-2" FT BINDING 208..210 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013, FT ECO:0000256|PIRSR:PIRSR016262-2" FT SITE 192 FT /note="Lowers pKa of active site Cys" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00013, FT ECO:0000256|PIRSR:PIRSR016262-3" SQ SEQUENCE 271 AA; 29676 MW; F70BDEF4BA58F157 CRC64; MTTSSPGSAP GSPALAYVHL GFGADAVDYE EAWQEQRRVH AARFADEIPD TCLLLEHPPV YTAGRRTADS ERPLDGTPVV DVDRGGKITW HGPGQLVGYP ILKLPRPVDV IAHVRRLEEA LLRTCAEFGL ETTRVEGRSG VWVLGDPVDQ RPALGGLKLD FDPRLEDEEF DARLNGPEYA PSNAGQRRED RKLAAIGVRI AKGVTMHGFS LNCNPDNTWF DRIVPCGIRD AGVTSLSEEL GRDVPISEVL PVVERHLREV LEASVPLPRA V //