ID TSAD_MYCGE Reviewed; 315 AA. AC P47292; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 134. DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01445}; DE EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_01445}; DE AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000255|HAMAP-Rule:MF_01445}; DE Short=t(6)A synthase {ECO:0000255|HAMAP-Rule:MF_01445}; DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000255|HAMAP-Rule:MF_01445}; DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000255|HAMAP-Rule:MF_01445}; GN Name=tsaD {ECO:0000255|HAMAP-Rule:MF_01445}; Synonyms=gcp; GN OrderedLocusNames=MG046; OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37) OS (Mycoplasmoides genitalium). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on CC adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning CC with adenine. Is involved in the transfer of the threonylcarbamoyl CC moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, CC together with TsaE and TsaB. TsaD likely plays a direct catalytic role CC in this reaction. {ECO:0000255|HAMAP-Rule:MF_01445}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + CC H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA; CC Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411, CC ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01445}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01445}; CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01445}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01445}. CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP- CC Rule:MF_01445}. 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; L43967; AAC71262.1; -; Genomic_DNA. DR PIR; A64205; A64205. DR RefSeq; WP_009885708.1; NZ_AAGX01000003.1. DR AlphaFoldDB; P47292; -. DR SMR; P47292; -. DR STRING; 243273.MG_046; -. DR KEGG; mge:MG_046; -. DR eggNOG; COG0533; Bacteria. DR HOGENOM; CLU_023208_0_1_14; -. DR InParanoid; P47292; -. DR OrthoDB; 9806197at2; -. DR BioCyc; MGEN243273:G1GJ2-46-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.420.40; -; 2. DR HAMAP; MF_01445; TsaD; 1. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR000905; Gcp-like_dom. DR InterPro; IPR017861; KAE1/TsaD. DR InterPro; IPR017860; Peptidase_M22_CS. DR InterPro; IPR022450; TsaD. DR NCBIfam; TIGR00329; gcp_kae1; 1. DR NCBIfam; TIGR03723; T6A_TsaD_YgjD; 1. DR PANTHER; PTHR11735; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE; 1. DR PANTHER; PTHR11735:SF6; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1. DR Pfam; PF00814; TsaD; 1. DR PRINTS; PR00789; OSIALOPTASE. DR SUPFAM; SSF53067; Actin-like ATPase domain; 1. DR PROSITE; PS01016; GLYCOPROTEASE; 1. PE 3: Inferred from homology; KW Acyltransferase; Cytoplasm; Iron; Metal-binding; Reference proteome; KW Transferase; tRNA processing. FT CHAIN 1..315 FT /note="tRNA N6-adenosine threonylcarbamoyltransferase" FT /id="PRO_0000096967" FT BINDING 110 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445" FT BINDING 114 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445" FT BINDING 135..139 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445" FT BINDING 168 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445" FT BINDING 181 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445" FT BINDING 185 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445" FT BINDING 273 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445" FT BINDING 297 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445" SQ SEQUENCE 315 AA; 34708 MW; D186ECD176C4E574 CRC64; MEQPLCVLGI ETTCDDTGLS IVIDQKIKSN IVISSANLHV KTGGVVPEIA ARCHEQNLFK AIRDLNFEIR DLSHIAYACN PGLAGCLHVG ATFARSLSFL LDKPLLPINH LYAHIFSCLI DQDLNKLQLP ALGLVISGGH TAIYLVKSFY ELELIAETSD DAIGEVYDKI GRAMGFDYPA GSKIDSLFNK ELVKPHYFFK PSTKWTKFSY SGLKSQCLNK IKQISANKTR IDWSELASNF QATIIDHYID HVKNAIKKFA PKMLLVGGGV SANSYLSNRI STLNLPFLIA DSKYTSDNGA MIGFYASLLI NGDKN //