ID A0A6H2BUD5_DOLFA Unreviewed; 453 AA. AC A0A6H2BUD5; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 22-FEB-2023, entry version 10. 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 ECO:0000313|EMBL:QJB43195.1}; GN ORFNames=HGD76_02060 {ECO:0000313|EMBL:QJB43195.1}; OS Dolichospermum flos-aquae CCAP 1403/13F. OC Bacteria; Cyanobacteria; Nostocales; Aphanizomenonaceae; Dolichospermum. OX NCBI_TaxID=315271 {ECO:0000313|EMBL:QJB43195.1, ECO:0000313|Proteomes:UP000502433}; RN [1] {ECO:0000313|EMBL:QJB43195.1, ECO:0000313|Proteomes:UP000502433} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCAP 1403/13f {ECO:0000313|EMBL:QJB43195.1, RC ECO:0000313|Proteomes:UP000502433}; RA Wu V.; RT "Genome-Wide Identification of 5-Methylcytosine Sites in Bacterial Genomes RT By High-Throughput Sequencing of MspJI Restriction Fragments."; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QJB43195.1, ECO:0000313|Proteomes:UP000502433} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCAP 1403/13f {ECO:0000313|EMBL:QJB43195.1, RC ECO:0000313|Proteomes:UP000502433}; RA Fomenkov A., Anton B.P., Roberts R.J.; RL Submitted (APR-2020) 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 --------------------------------------------------------------------------- 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; CP051206; QJB43195.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6H2BUD5; -. DR KEGG; dfs:HGD76_02060; -. DR Proteomes; UP000502433; 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: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 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; SFLDS00029; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 1. DR TIGRFAMs; TIGR01574; miaB-methiolase; 1. DR TIGRFAMs; TIGR00089; radical SAM methylthiotransferase, MiaB/RimO family; 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|ARBA:ARBA00022490, 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 5..121 FT /note="MTTase N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51449" FT DOMAIN 142..379 FT /note="Radical SAM core" FT /evidence="ECO:0000259|PROSITE:PS51918" FT DOMAIN 382..446 FT /note="TRAM" FT /evidence="ECO:0000259|PROSITE:PS50926" FT BINDING 14 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 50 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 84 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 156 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 160 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 163 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 453 AA; 51324 MW; 3A7A6830F27EA127 CRC64; MTTKRNYHII TFGCQMNKAD SERMAGILED MGFEWSEDPN QADLILYNTC TIRDNAEQKV YSYLGRQAKR KQEEPDLTLI VAGCVAQQEG AALLRRVPEL DLVMGPQHAN RLKDLLESVF AGNQVVATEE VHIFEDITQP RRDSQVTAWV NIIYGCNERC TYCVVPNVRG VEQSRTPEAV RSEIEQLARQ GYKEITLLGQ NIDAYGRDLP GSTPEGRHLH TLTDLLYYVH DVPGIERIRF ATSHPRYFTE RLIKACADLP KVCEHFHIPF QSGDNELLKA MSRGYTHEKY RRIIDTIRGY MPDASISADA IVGFPGETET QFENTLKLVE DIGFDLVNTA AYSPRPGTPA ALWDNQLSEE VKSDRLQRLN HLVNIKAAER SQRYFGRIEE VLVEAQNTKD TNQVMGRTGG NRLTFFTGDI NELKGQIVKV KITEVRAFSL TGEVVEVRQP VTV //