ID A0A1Q8XDV6_9ACTO Unreviewed; 553 AA. AC A0A1Q8XDV6; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 27-MAR-2024, entry version 29. DE RecName: Full=tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase {ECO:0000256|ARBA:ARBA00033765, ECO:0000256|HAMAP-Rule:MF_01864}; DE EC=2.8.4.3 {ECO:0000256|ARBA:ARBA00033765, ECO:0000256|HAMAP-Rule:MF_01864}; 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; Actinomycetota; Actinomycetes; 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., Beighton D.; RT "Genomic comparison of strains in the 'Actinomyces naeslundii' group."; RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine CC (i(6)A), leading to the formation of 2-methylthio-N6- CC (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read CC codons beginning with uridine. {ECO:0000256|ARBA:ARBA00003234, CC ECO:0000256|HAMAP-Rule:MF_01864}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in CC tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)- CC dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur CC carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:37067, Rhea:RHEA-COMP:10375, Rhea:RHEA-COMP:10376, CC Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, ChEBI:CHEBI:13193, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:29917, ChEBI:CHEBI:57844, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64428, ChEBI:CHEBI:74415, CC ChEBI:CHEBI:74417; EC=2.8.4.3; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01864}; 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01864}. CC -!- SIMILARITY: Belongs to the methylthiotransferase family. MiaB CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01864}. 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: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 AlphaFoldDB; A0A1Q8XDV6; -. 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:0035596; F:methylthiotransferase activity; IEA:InterPro. DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule. DR CDD; cd01335; Radical_SAM; 1. DR Gene3D; 3.40.50.12160; Methylthiotransferase, N-terminal domain; 1. DR Gene3D; 3.80.30.20; tm_1862 like domain; 1. DR HAMAP; MF_01864; tRNA_metthiotr_MiaB; 1. DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM. 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 NCBIfam; TIGR01574; miaB-methiolase; 1. DR NCBIfam; TIGR00089; MiaB/RimO family radical SAM methylthiotransferase; 1. DR PANTHER; PTHR43020; CDK5 REGULATORY SUBUNIT-ASSOCIATED PROTEIN 1; 1. DR PANTHER; PTHR43020:SF2; MITOCHONDRIAL TRNA METHYLTHIOTRANSFERASE CDK5RAP1; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF00919; UPF0004; 1. DR SFLD; SFLDF00273; (dimethylallyl)adenosine_tRNA; 1. DR SFLD; SFLDG01082; B12-binding_domain_containing; 1. DR SFLD; SFLDG01061; methylthiotransferase; 1. DR SMART; SM00729; Elp3; 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 1. DR PROSITE; PS51449; MTTASE_N; 1. DR PROSITE; PS01278; MTTASE_RADICAL; 1. DR PROSITE; PS51918; RADICAL_SAM; 1. DR PROSITE; PS50926; TRAM; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01864}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01864}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01864}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_01864}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01864}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_01864}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01864}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_01864}. FT DOMAIN 19..147 FT /note="MTTase N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51449" FT DOMAIN 170..400 FT /note="Radical SAM core" FT /evidence="ECO:0000259|PROSITE:PS51918" FT DOMAIN 403..480 FT /note="TRAM" FT /evidence="ECO:0000259|PROSITE:PS50926" FT REGION 533..553 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 28 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01864" FT BINDING 76 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01864" FT BINDING 110 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01864" FT BINDING 184 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01864" FT BINDING 188 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01864" FT BINDING 191 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="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 //