ID A0A1Q8XDV6_9ACTO Unreviewed; 553 AA. AC A0A1Q8XDV6; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 08-MAY-2019, entry version 10. DE RecName: Full=tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase {ECO:0000256|HAMAP-Rule:MF_01864, ECO:0000256|SAAS:SAAS00623688}; DE EC=2.8.4.3 {ECO:0000256|HAMAP-Rule:MF_01864, ECO:0000256|SAAS:SAAS00623691}; DE AltName: Full=(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB {ECO:0000256|HAMAP-Rule:MF_01864}; DE AltName: Full=tRNA-i(6)A37 methylthiotransferase {ECO:0000256|HAMAP-Rule:MF_01864}; GN Name=miaB {ECO:0000256|HAMAP-Rule:MF_01864}; GN ORFNames=BKH18_04750 {ECO:0000313|EMBL:OLO78522.1}; OS Actinomyces oris. OC Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; OC Actinomyces. OX NCBI_TaxID=544580 {ECO:0000313|EMBL:OLO78522.1, ECO:0000313|Proteomes:UP000186219}; RN [1] {ECO:0000313|EMBL:OLO78522.1, ECO:0000313|Proteomes:UP000186219} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R23275 {ECO:0000313|EMBL:OLO78522.1, RC ECO:0000313|Proteomes:UP000186219}; RA Mughal S.R., Do T., Gilbert S.C., Witherden E.A., Didelot X., RA Beighton D.; RT "Genomic comparison of strains in the 'Actinomyces naeslundii' RT group."; RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the methylthiolation of N6- CC (dimethylallyl)adenosine (i(6)A), leading to the formation of 2- CC methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 CC in tRNAs that read codons beginning with uridine. CC {ECO:0000256|HAMAP-Rule:MF_01864, ECO:0000256|SAAS:SAAS00623708}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[sulfur carrier]-SH + AH2 + N(6)- CC dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = CC 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'- CC deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:37067, Rhea:RHEA- CC COMP:10375, Rhea:RHEA-COMP:10376, Rhea:RHEA-COMP:14737, CC Rhea:RHEA-COMP:14739, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17319, ChEBI:CHEBI:17499, ChEBI:CHEBI:29917, CC ChEBI:CHEBI:57844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:64428, ChEBI:CHEBI:74415, ChEBI:CHEBI:74417; CC EC=2.8.4.3; Evidence={ECO:0000256|HAMAP-Rule:MF_01864, CC ECO:0000256|SAAS:SAAS01123679}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01864}; CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000256|HAMAP-Rule:MF_01864}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01864, CC ECO:0000256|SAAS:SAAS00623714}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01864, CC ECO:0000256|SAAS:SAAS00623711}. CC -!- SIMILARITY: Belongs to the methylthiotransferase family. MiaB CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01864, CC ECO:0000256|SAAS:SAAS00623705}. 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:OLO78522.1}. 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; MSKU01000019; OLO78522.1; -; Genomic_DNA. DR RefSeq; WP_075374447.1; NZ_MSKU01000019.1. DR Proteomes; UP000186219; Unassembled WGS sequence. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.12160; -; 1. DR Gene3D; 3.80.30.20; -; 1. DR HAMAP; MF_01864; tRNA_metthiotr_MiaB; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR005839; Methylthiotransferase. DR InterPro; IPR020612; Methylthiotransferase_CS. DR InterPro; IPR013848; Methylthiotransferase_N. DR InterPro; IPR038135; Methylthiotransferase_N_sf. DR InterPro; IPR006463; MiaB_methiolase. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR InterPro; IPR002792; TRAM_dom. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF00919; UPF0004; 1. DR SFLD; SFLDF00273; (dimethylallyl)adenosine_tRNA_; 1. DR SFLD; SFLDG01061; methylthiotransferase; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00089; TIGR00089; 1. DR PROSITE; PS51449; MTTASE_N; 1. DR PROSITE; PS01278; MTTASE_RADICAL; 1. DR PROSITE; PS50926; TRAM; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01864, KW ECO:0000256|SAAS:SAAS00455264}; KW Complete proteome {ECO:0000313|Proteomes:UP000186219}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01864, KW ECO:0000256|SAAS:SAAS00623717}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01864, ECO:0000256|SAAS:SAAS00455234}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01864, KW ECO:0000256|SAAS:SAAS00078019}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01864, KW ECO:0000256|SAAS:SAAS00455354}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01864, KW ECO:0000256|SAAS:SAAS00077875}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01864, KW ECO:0000256|SAAS:SAAS00623694, ECO:0000313|EMBL:OLO78522.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01864, KW ECO:0000256|SAAS:SAAS00623699}. FT DOMAIN 19 147 MTTase N-terminal. {ECO:0000259|PROSITE: FT PS51449}. FT DOMAIN 403 480 TRAM. {ECO:0000259|PROSITE:PS50926}. FT METAL 28 28 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01864}. FT METAL 76 76 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01864}. FT METAL 110 110 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01864}. FT METAL 184 184 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01864}. FT METAL 188 188 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01864}. FT METAL 191 191 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000256|HAMAP-Rule:MF_01864}. SQ SEQUENCE 553 AA; 59672 MW; 286E2680EF2D6DA7 CRC64; MTTLTTSAPV LDARGGLPRT YHVRTLGCQM NVHDSEHMAG LLERAGYLRV EDVPEAAARA TDAGDGGADV VIINTCSVRE NAATRLFGNL GQLAAVKRER PGMQIAVAGC LAQQMGEGIV ERAPWVDVVF GTHNLDVLPA LLERARHNSA AAVELEESLK VFPSTLPTRR ESSYAAWVSI AVGCNNTCTF CIVPSLRGKQ RDRRPGDVLA EVEAVAAQGA IEVTLLGQNV NSYGVGFGDR GAFAKLLRAT GSVEGIERVR FTSPHPAAFT DDVIEAMATT EAVMPSLHMP LQSGSDRVLR AMRRSYRTQR FLGILDKVRA VMPEAAITTD IIVGFPGETE EDFQATLDVV EQARFASAYT FEYSPRPGTP AADRDDQVPT EVVKDRYRRL DALVRRIAHE ENERQEGRVV EVLVAEGEGR RDTVTARISG RAADNRLVHV ALPEGLAEND YAGGAPRPGD MVTVRVTHGA PHNLIADSAR CGHELDPRAA AANEALKPGD RLWLDDGPAL FQVRRTHAGD AWERRQAEAC ATPEPDTAPV NLGLPTLRVG APA //