ID A0A2E9CYH6_9ACTN Unreviewed; 542 AA. AC A0A2E9CYH6; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 18-JUL-2018, entry version 7. DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00013, ECO:0000256|HAMAP-Rule:MF_00206}; DE Includes: DE RecName: Full=Octanoyltransferase {ECO:0000256|HAMAP-Rule:MF_00013}; DE EC=2.3.1.181 {ECO:0000256|HAMAP-Rule:MF_00013}; 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}; DE Includes: DE RecName: Full=Lipoyl synthase {ECO:0000256|HAMAP-Rule:MF_00206}; DE EC=2.8.1.8 {ECO:0000256|HAMAP-Rule:MF_00206}; DE AltName: Full=Lip-syn {ECO:0000256|HAMAP-Rule:MF_00206}; DE AltName: Full=Lipoate synthase {ECO:0000256|HAMAP-Rule:MF_00206}; DE AltName: Full=Lipoic acid synthase {ECO:0000256|HAMAP-Rule:MF_00206}; DE AltName: Full=Sulfur insertion protein LipA {ECO:0000256|HAMAP-Rule:MF_00206}; DE Short=LS {ECO:0000256|HAMAP-Rule:MF_00206}; GN Name=lipA {ECO:0000256|HAMAP-Rule:MF_00206}; GN Synonyms=lipB {ECO:0000256|HAMAP-Rule:MF_00013}; GN ORFNames=CL511_00020 {ECO:0000313|EMBL:MBS92057.1}; OS Actinobacteria bacterium. OC Bacteria; Actinobacteria. OX NCBI_TaxID=1883427 {ECO:0000313|EMBL:MBS92057.1}; RN [1] {ECO:0000313|EMBL:MBS92057.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RS471 {ECO:0000313|EMBL:MBS92057.1}; RA Tully B.J., Graham E.D., Heidelberg J.F.; RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from RT the Global Oceans."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the radical-mediated insertion of two sulfur CC atoms into the C-6 and C-8 positions of the octanoyl moiety bound CC to the lipoyl domains of lipoate-dependent enzymes, thereby CC converting the octanoylated domains into lipoylated derivatives. CC {ECO:0000256|HAMAP-Rule:MF_00206}. 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|SAAS:SAAS00848413}. 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|SAAS:SAAS01056741}. CC -!- CATALYTIC ACTIVITY: Protein N(6)-(octanoyl)lysine + an [Fe-S] CC cluster scaffold protein carrying a [4Fe-4S](2+) cluster + 2 S- CC adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H(+) = CC protein N(6)-(dihydrolipoyl)lysine + an [Fe-S] cluster scaffold CC protein + 2 sulfide + 4 Fe(3+) + 2 L-methionine + 2 5'- CC deoxyadenosine + 2 reduced [2Fe-2S] ferredoxin. CC {ECO:0000256|HAMAP-Rule:MF_00206}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00206}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. One cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine. {ECO:0000256|HAMAP-Rule:MF_00206}; CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier- CC protein]: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00206}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00013, CC ECO:0000256|SAAS:SAAS00848401}. 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|SAAS:SAAS00848418}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl CC synthase family. {ECO:0000256|HAMAP-Rule:MF_00206}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00206}. 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:MBS92057.1}. 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; PBXU01000001; MBS92057.1; -; Genomic_DNA. DR UniPathway; UPA00538; UER00593. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule. DR GO; GO:0016992; F:lipoate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0102555; F:octanoyl transferase activity (acting on glycine-cleavage complex H protein); IEA:UniProtKB-EC. DR GO; GO:0009249; P:protein lipoylation; IEA:UniProtKB-UniRule. DR CDD; cd16444; LipB; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00013; LipB; 1. DR HAMAP; MF_00206; Lipoyl_synth; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004143; BPL_LPL_catalytic. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR031691; LIAS_N. DR InterPro; IPR003698; Lipoyl_synth. DR InterPro; IPR000544; Octanoyltransferase. DR InterPro; IPR020605; Octanoyltransferase_CS. DR InterPro; IPR007197; rSAM. DR Pfam; PF16881; LIAS_N; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00510; lipA; 1. DR TIGRFAMs; TIGR00214; lipB; 1. DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1. DR PROSITE; PS01313; LIPB; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00206}; KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00013, KW ECO:0000256|SAAS:SAAS00853398}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00013, KW ECO:0000256|SAAS:SAAS00848411}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00206}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00206}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00206}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00206}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00013, KW ECO:0000256|SAAS:SAAS00853388}. FT DOMAIN 32 212 BPL/LPL catalytic. {ECO:0000259|PROSITE: FT PS51733}. FT REGION 77 84 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00013}. FT REGION 143 145 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00013}. FT REGION 156 158 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00013}. FT ACT_SITE 174 174 Acyl-thioester intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00013}. FT METAL 293 293 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_00206}. FT METAL 298 298 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_00206}. FT METAL 304 304 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000256|HAMAP-Rule:MF_00206}. FT METAL 323 323 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_00206}. FT METAL 326 326 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_00206}. FT SITE 140 140 Lowers pKa of active site Cys. FT {ECO:0000256|HAMAP-Rule:MF_00013}. SQ SEQUENCE 542 AA; 60946 MW; 0D2E5CA28B5F1C8D CRC64; MRDLNIRWLG KLPYSEAYDL QLGLHRSVSQ EDSKDDYLLL LEHNNVITSG RSSKENNLLV SKGQLHELGI EYFETDRGGD ITYHGDGQLI GYPIIRLSDP KKVIPFVRNL ENVIIDSLRK FKIDSFTKED DTGVWTAKGK IASVGIKVSK WTTYHGFSLN IFDSLDGYQL INPCGNQSEQ ITSIHQFNPD ISFEEVASEI SDNFVKVFGY ANTDRQFSQF TPRQLKRTKE FNIDQMVKDG VFKINQNKIP VTVRGVLPSE PKRPEWMKVK ANLGSDYVSL KNLLSEKKLN TVCEEASCPN IYECWSMGTA TFMIMGDVXT RACGFCDVKT GRPGELDLGE PLRVAESVXA MNLTHAVITS VNRDDLEDGG SMFFADTIRA VKDKNSHCDV EVLVPDFKGL RSAIQNIIDA SPEVFNHNLE TVPRLQREIR TAASYGRSLS LLEYVKKQGF MGKTKTGLIV GMGETKEEVI SVLKDLSKIE VDIVTIGQYL RPTAKHRPID RYATIEEFED YKIIGESYGI PHVESGPLVR SSYHAKDSFA SA //