ID A0A014KZJ8_9ACTN Unreviewed; 271 AA. AC A0A014KZJ8; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 24-JUN-2015, entry version 10. 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}; RN [1] {ECO:0000313|EMBL:EXU62426.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PRh5 {ECO:0000313|EMBL:EXU62426.1}; RA Zhu D., Yang H., Wang Y., Zhang Z., Yan R.; RT "Whole-genome shotgun assembly and analysis of the genome of RT Streptomyces sp. PRh5, a strain for production of geldanamycin, RT nigericin and nocardamine."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic CC acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of CC lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate CC although octanoyl-ACP is likely to be the physiological substrate. CC {ECO:0000256|HAMAP-Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262}. CC -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic CC acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of CC lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate CC although octanoyl-ACP is likely to be the physiological substrate CC (By similarity). {ECO:0000256|SAAS:SAAS00218458}. CC -!- CATALYTIC ACTIVITY: Octanoyl-[acyl-carrier-protein] + protein = CC protein N(6)-(octanoyl)lysine + [acyl-carrier-protein]. CC {ECO:0000256|HAMAP-Rule:MF_00013, ECO:0000256|PIRNR:PIRNR016262, CC ECO:0000256|SAAS:SAAS00218461}. 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|HAMAP-Rule:MF_00013, CC ECO:0000256|PIRNR:PIRNR016262, ECO:0000256|SAAS:SAAS00218466}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00013, CC ECO:0000256|SAAS:SAAS00218467}. CC -!- MISCELLANEOUS: In the reaction, the free carboxyl group of CC octanoic acid is attached via an amide linkage to the epsilon- CC amino group of a specific lysine residue of lipoyl domains of CC lipoate-dependent enzymes. {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 -!- SIMILARITY: Contains 1 BPL/LPL catalytic domain. CC {ECO:0000256|HAMAP-Rule:MF_00013}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblBacteria; EXU62426; EXU62426; Z951_41695. 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:0016415; F:octanoyltransferase activity; IEA:InterPro. DR GO; GO:0006464; P:cellular protein modification process; IEA:InterPro. DR GO; GO:0009107; P:lipoate biosynthetic process; IEA:InterPro. DR HAMAP; MF_00013; LipB; 1. 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 PROSITE; PS51733; BPL_LPL_CATALYTIC; 1. DR PROSITE; PS01313; LIPB; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00013, KW ECO:0000256|PIRNR:PIRNR016262}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00013, KW ECO:0000256|SAAS:SAAS00218469}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00013, KW ECO:0000256|PIRNR:PIRNR016262}. FT DOMAIN 46 265 BPL/LPL catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00013}. FT REGION 84 91 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00013, ECO:0000256|PIRSR: FT PIRSR016262-2}. FT REGION 195 197 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00013, ECO:0000256|PIRSR: FT PIRSR016262-2}. FT REGION 208 210 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00013, ECO:0000256|PIRSR: FT PIRSR016262-2}. FT ACT_SITE 226 226 Acyl-thioester intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00013, FT ECO:0000256|PIRSR:PIRSR016262-1}. FT SITE 192 192 Lowers pKa of active site Cys. FT {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 //