ID TSAD_RICCN Reviewed; 344 AA. AC Q92JK6; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 114. 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=RC0061; OS Rickettsia conorii (strain ATCC VR-613 / Malish 7). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=272944; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-613 / Malish 7; RX PubMed=11557893; DOI=10.1126/science.1061471; RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.; RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii."; RL Science 293:2093-2098(2001). 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; AE006914; AAL02599.1; -; Genomic_DNA. DR PIR; E97707; E97707. DR RefSeq; WP_010976747.1; NC_003103.1. DR AlphaFoldDB; Q92JK6; -. DR SMR; Q92JK6; -. DR GeneID; 928604; -. DR KEGG; rco:RC0061; -. DR PATRIC; fig|272944.4.peg.72; -. DR HOGENOM; CLU_023208_0_2_5; -. DR Proteomes; UP000000816; 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; 2. DR PROSITE; PS01016; GLYCOPROTEASE; 1. PE 3: Inferred from homology; KW Acyltransferase; Cytoplasm; Iron; Metal-binding; Transferase; KW tRNA processing. FT CHAIN 1..344 FT /note="tRNA N6-adenosine threonylcarbamoyltransferase" FT /id="PRO_0000303523" FT BINDING 112 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445" FT BINDING 116 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445" FT BINDING 134..138 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445" FT BINDING 167 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445" FT BINDING 180 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445" FT BINDING 280 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445" FT BINDING 308 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445" SQ SEQUENCE 344 AA; 37302 MW; 72B082999B0B7408 CRC64; MIKILGIESS CDDTAVSIIT ENREILSNII ISQNTEHAVF GGVVPEIAAR SHLSHLDKAL KNVLKESNTK LTDISTIAAT SGPGLIGGVI VGSMFARSLS SALKKPFIAI NHLEGHALTA RLTDNIPYPY LLLLASGGHC QFVAVLGLGK YKILGSTIDD AVGEAFDKVA KMLNLAFPGG PEIEKRAKLG DPHKYKFPKP IINSGNCNMS FSGLKTAVRT LIMTLKEIND TVINDIAASF QFTIGEILSS KVQDAIRAYE QITNNFDKKN IVIAGGVAAN KYLQKILSSC AKTYGYRLIY PPIHLCTDNA AMIAYAGLER YNNKLFTPLN FCPKARWSLE DISN //