ID MIAB_PROM0 Reviewed; 464 AA. AC A3PED9; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 02-SEP-2026, entry version 103. DE RecName: Full=tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase {ECO:0000255|HAMAP-Rule:MF_01864}; DE EC=2.8.4.3 {ECO:0000255|HAMAP-Rule:MF_01864}; DE AltName: Full=(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB {ECO:0000255|HAMAP-Rule:MF_01864}; DE AltName: Full=tRNA-i(6)A37 methylthiotransferase {ECO:0000255|HAMAP-Rule:MF_01864}; GN Name=miaB {ECO:0000255|HAMAP-Rule:MF_01864}; GN OrderedLocusNames=P9301_14911; OS Prochlorococcus marinus (strain MIT 9301). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; Prochlorococcus. OX NCBI_TaxID=167546; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9301; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., RA Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). 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:0000255|HAMAP-Rule:MF_01864}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6)-dimethylallyladenosine(37) in tRNA + (sulfur carrier)-SH CC + AH2 + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)- CC dimethylallyladenosine(37) in tRNA + (sulfur carrier)-H + 5'- CC deoxyadenosine + L-methionine + A + S-adenosyl-L-homocysteine + 2 CC H(+); Xref=Rhea:RHEA:37067, Rhea:RHEA-COMP:10375, Rhea:RHEA- CC COMP:10376, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, CC ChEBI:CHEBI:17499, ChEBI:CHEBI:29917, ChEBI:CHEBI:57844, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64428, CC ChEBI:CHEBI:74415, ChEBI:CHEBI:74417; EC=2.8.4.3; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01864}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01864}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01864}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01864}. CC -!- SIMILARITY: Belongs to the methylthiotransferase family. MiaB CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01864}. 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; CP000576; ABO18114.1; -; Genomic_DNA. DR RefSeq; WP_011863421.1; NC_009091.1. DR AlphaFoldDB; A3PED9; -. DR SMR; A3PED9; -. DR STRING; 167546.P9301_14911; -. DR KEGG; pmg:P9301_14911; -. DR eggNOG; COG0621; Bacteria. DR HOGENOM; CLU_018697_2_2_3; -. DR OrthoDB; 9805215at2; -. DR Proteomes; UP000001430; Chromosome. 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:0035597; F:tRNA-2-methylthio-N(6)-dimethylallyladenosine(37) synthase activity; IEA:UniProtKB-EC. DR CDD; cd01335; Radical_SAM; 1. DR FunFam; 3.40.50.12160:FF:000006; tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase; 1. DR FunFam; 3.80.30.20:FF:000001; tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase 2; 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; IPR058240; rSAM_sf. 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; PF01938; TRAM; 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 SFLD; SFLDS00029; Radical_SAM; 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; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1..464 FT /note="tRNA-2-methylthio-N(6)-dimethylallyladenosine FT synthase" FT /id="PRO_0000374447" FT DOMAIN 19..135 FT /note="MTTase N-terminal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01864" FT DOMAIN 156..394 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT DOMAIN 396..464 FT /note="TRAM" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01864" FT BINDING 28 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01864" FT BINDING 64 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01864" FT BINDING 98 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01864" FT BINDING 170 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:0000255|HAMAP-Rule:MF_01864" FT BINDING 174 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:0000255|HAMAP-Rule:MF_01864" FT BINDING 177 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:0000255|HAMAP-Rule:MF_01864" SQ SEQUENCE 464 AA; 52724 MW; A71367685D741370 CRC64; MLTKTKSDEI KTQKDSTTGS YWITTFGCQM NKADSERMAG TLEKMGYTRA DNELNADLVL YNTCTIRDNA EQKVYSFLGR QAKRKHKTPR LKLVVAGCLA QQEGESLLRR VPELDLVMGP QHVNNLENLL GKVDLGNQVV ATEETFISED ITSARRESSI CGWVNIIYGC NERCSYCVVP SVRGKEQSRY PNAIKSEIQK LADDNFKEIT LLGQNIDAYG RDLPGTTKEG RKENTLTDLL YYIHDVKGIR RIRFATSHPR YFSKRLIQAC YELDKVCEHF HIPFQSGNDE ILKQMSRGYS IKKYKNIIEN IRSLMPDASI TADAIVAFPG ETEKQYQDTL KLISEIGFDQ VNTAAYSARP NTPAAVWTNQ LSEEVKKARL QEINDLVEKT ARSRNQRYID NIESVLIEGL NPKNSSQIMG RTRTNRLTFV EIPKNINFNF SLGDEINVRI NEARPFSLTG ELSL //