ID A7NP77_ROSCS Unreviewed; 362 AA. AC A7NP77; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 02-SEP-2026, entry version 100. DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_01445}; DE EC=2.3.1.234 {ECO:0000256|HAMAP-Rule:MF_01445}; DE AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000256|HAMAP-Rule:MF_01445}; DE Short=t(6)A synthase {ECO:0000256|HAMAP-Rule:MF_01445}; DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000256|HAMAP-Rule:MF_01445}; DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000256|HAMAP-Rule:MF_01445}; GN Name=tsaD {ECO:0000256|HAMAP-Rule:MF_01445}; GN OrderedLocusNames=Rcas_3323 {ECO:0000313|EMBL:ABU59373.1}; OS Roseiflexus castenholzii (strain DSM 13941 / HLO8). OC Bacteria; Bacillati; Chloroflexota; Chloroflexia; Chloroflexales; OC Roseiflexineae; Roseiflexaceae; Roseiflexus. OX NCBI_TaxID=383372 {ECO:0000313|EMBL:ABU59373.1, ECO:0000313|Proteomes:UP000000263}; RN [1] {ECO:0000313|EMBL:ABU59373.1, ECO:0000313|Proteomes:UP000000263} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13941 / HLO8 {ECO:0000313|Proteomes:UP000000263}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C., RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.; RT "Complete sequence of Roseiflexus castenholzii DSM 13941."; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_01445}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonylcarbamoyladenylate + adenosine(37) in tRNA = N(6)-L- CC threonylcarbamoyladenosine(37) in tRNA + AMP + H(+); 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:0000256|ARBA:ARBA00048117, ECO:0000256|HAMAP- CC Rule:MF_01445}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01445}; CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01445}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01445}. CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000256|HAMAP- CC Rule:MF_01445}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-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; CP000804; ABU59373.1; -; Genomic_DNA. DR RefSeq; WP_012121797.1; NC_009767.1. DR AlphaFoldDB; A7NP77; -. DR STRING; 383372.Rcas_3323; -. DR KEGG; rca:Rcas_3323; -. DR eggNOG; COG0533; Bacteria. DR HOGENOM; CLU_023208_0_2_0; -. DR OrthoDB; 9806197at2; -. DR Proteomes; UP000000263; 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:tRNA N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule. DR CDD; cd24133; ASKHA_NBD_TsaD_bac; 1. DR FunFam; 3.30.420.40:FF:000012; tRNA N6-adenosine threonylcarbamoyltransferase; 1. DR FunFam; 3.30.420.40:FF:000040; tRNA N6-adenosine threonylcarbamoyltransferase; 1. 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; 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. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP- KW Rule:MF_01445}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01445}; KW Hydrolase {ECO:0000313|EMBL:ABU59373.1}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01445}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01445}; Protease {ECO:0000313|EMBL:ABU59373.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000263}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01445}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_01445}. FT DOMAIN 28..334 FT /note="Gcp-like" FT /evidence="ECO:0000259|Pfam:PF00814" FT BINDING 115 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01445" FT BINDING 119 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01445" FT BINDING 144..148 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01445" FT BINDING 177 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01445" FT BINDING 190 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01445" FT BINDING 303 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01445" FT BINDING 328 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01445" SQ SEQUENCE 362 AA; 38324 MW; DD063B333F2F7B66 CRC64; MDTNFTILAI ETSCDETAAA VIRGGRMIVS NVVASQIEEH RRYGGVVPEV ASRQHILTID AVVRDALHPL PGGWNDIHAV AATYGPGLAG ALMTGLNVAK AIAWMRELPF IGVNHIEAHI YANWLLTDAQ PDAPEPQFPV VALVVSGGHT LLALLEGHGR YRMLGQTRDD AAGEAFDKVA RLLGLGFPGG PAIQTAAENA PGGVTLPRAW LRDSYDFSFS GLKTAVLHQI REYRAREAAL QPGAGKRGAS AATEPPPLPP AIVARLARAF QESVVDVLVT KTVEAARAFG AAEVVLAGGV AANLRLREEL CRRSPVPVHI PPVALCTDNA AMIGAAAFYR LNAGKQDGWD LDVQPNLPLH AG //