ID A3DBR2_ACET2 Unreviewed; 434 AA. AC A3DBR2; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 24-JAN-2024, entry version 95. DE RecName: Full=tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase {ECO:0000256|ARBA:ARBA00013273}; DE EC=2.8.4.5 {ECO:0000256|ARBA:ARBA00013273}; DE AltName: Full=tRNA-t(6)A37 methylthiotransferase {ECO:0000256|ARBA:ARBA00031213}; GN OrderedLocusNames=Cthe_0150 {ECO:0000313|EMBL:ABN51391.1}; OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae; OC Acetivibrio. OX NCBI_TaxID=203119 {ECO:0000313|EMBL:ABN51391.1, ECO:0000313|Proteomes:UP000002145}; RN [1] {ECO:0000313|Proteomes:UP000002145} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / RC NRRL B-4536 / VPI 7372 {ECO:0000313|Proteomes:UP000002145}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., RA Newcomb M., Richardson P.; RT "Complete sequence of Clostridium thermocellum ATCC 27405."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABN51391.1, ECO:0000313|Proteomes:UP000002145} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / RC NRRL B-4536 / VPI 7372 {ECO:0000313|Proteomes:UP000002145}; RX PubMed=24295562; DOI=10.1186/1754-6834-6-179; RA Wilson C.M., Rodriguez M.Jr., Johnson C.M., Martin S.L., Chu T.M., RA Wolfinger R.D., Hauser L.J., Land M.L., Klingeman D.M., Syed M.H., RA Ragauskas A.J., Tschaplinski T.J., Mielenz J.R., Brown S.D.; RT "Global transcriptome analysis of Clostridium thermocellum ATCC 27405 RT during growth on dilute acid pretreated Populus and switchgrass."; RL Biotechnol. Biofuels 6:179-179(2013). CC -!- FUNCTION: Catalyzes the methylthiolation of N6- CC threonylcarbamoyladenosine (t(6)A), leading to the formation of 2- CC methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in CC tRNAs that read codons beginning with adenine. CC {ECO:0000256|ARBA:ARBA00002399}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[sulfur carrier]-SH + AH2 + N(6)-L- CC threonylcarbamoyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = CC 2-methylsulfanyl-N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 5'- CC deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S- CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:37075, Rhea:RHEA-COMP:10163, CC Rhea:RHEA-COMP:11092, 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:74418, ChEBI:CHEBI:74420; EC=2.8.4.5; CC Evidence={ECO:0000256|ARBA:ARBA00000730}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|ARBA:ARBA00001966}; 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; CP000568; ABN51391.1; -; Genomic_DNA. DR RefSeq; WP_003518029.1; NC_009012.1. DR AlphaFoldDB; A3DBR2; -. DR STRING; 203119.Cthe_0150; -. DR GeneID; 57419527; -. DR KEGG; cth:Cthe_0150; -. DR eggNOG; COG0621; Bacteria. DR HOGENOM; CLU_018697_1_0_9; -. DR OMA; HFHIPLQ; -. DR OrthoDB; 9805215at2; -. DR Proteomes; UP000002145; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0035598; F:N6-threonylcarbomyladenosine methylthiotransferase activity; IEA:InterPro. 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 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; IPR006467; MiaB-like_bact. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR InterPro; IPR034557; ThrcA_tRNA_MEthiotransferase. DR InterPro; IPR002792; TRAM_dom. DR NCBIfam; TIGR01579; MiaB-like-C; 1. DR NCBIfam; TIGR00089; MiaB/RimO family radical SAM methylthiotransferase; 1. DR PANTHER; PTHR11918; RADICAL SAM PROTEINS; 1. DR PANTHER; PTHR11918:SF45; THREONYLCARBAMOYLADENOSINE TRNA METHYLTHIOTRANSFERASE; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF00919; UPF0004; 1. DR SFLD; SFLDG01082; B12-binding_domain_containing; 1. DR SFLD; SFLDS00029; Radical_SAM; 1. DR SFLD; SFLDF00295; threonylcarbamoyladenosine_tRN; 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 4: Predicted; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485}; KW Iron {ECO:0000256|ARBA:ARBA00023004}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Reference proteome {ECO:0000313|Proteomes:UP000002145}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 2..114 FT /note="MTTase N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51449" FT DOMAIN 139..368 FT /note="Radical SAM core" FT /evidence="ECO:0000259|PROSITE:PS51918" FT DOMAIN 371..434 FT /note="TRAM" FT /evidence="ECO:0000259|PROSITE:PS50926" SQ SEQUENCE 434 AA; 49691 MW; FB7F868991CD2383 CRC64; MKRAAFYTLG CKVNQYETEA ISEMFEKAGY KIVDFEDEAD VYVINTCTVT NLSDRKSRQM IRRAKRNNEN SIVIVIGCYA QTAPEEVSKI EGVNLVVGTK DRSRILEYLK ELETSGGRRN YVGDIMKTRE FEELGVNVYK ERTRAFIKIQ EGCNQFCTYC IIPYARGPVR SRSEENILKE VSGLAHSGYK EVVLTGIHVA SYGKDIKNTS LIDIIRKVHE IEGIERIRLG SIEPTTVTEE FVRAIKGMEK LCPQFHISLQ SGCDSTLKRM NRKYTTKEYL RSVELLRENL KDVAVTTDVM VGFPGETDEE FNETCRFVEK VLFARMHVFK YSRRKGTPAA SYPDQVAPQK KEERSRILIE LASRMTLEYN KSFTGRVLPV LFEQEVKGKE GFMEGLTPNY IRVECKGDKD IEGQILNVLL REAKDDYIVG EIVN //