ID A0A510E3B7_9CREN Unreviewed; 331 AA. AC A0A510E3B7; A0A510DVL7; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 12-OCT-2022, entry version 13. DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_01446}; DE EC=2.3.1.234 {ECO:0000256|HAMAP-Rule:MF_01446}; DE AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000256|HAMAP-Rule:MF_01446}; DE Short=t(6)A synthase {ECO:0000256|HAMAP-Rule:MF_01446}; DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000256|HAMAP-Rule:MF_01446}; DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000256|HAMAP-Rule:MF_01446}; GN Name=kae1 {ECO:0000256|HAMAP-Rule:MF_01446}; GN ORFNames=IC006_1526 {ECO:0000313|EMBL:BBG24219.1}, IC007_1503 GN {ECO:0000313|EMBL:BBG26976.1}; OS Sulfuracidifex tepidarius. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfuracidifex. OX NCBI_TaxID=1294262 {ECO:0000313|EMBL:BBG26976.1, ECO:0000313|Proteomes:UP000325030}; RN [1] {ECO:0000313|Proteomes:UP000322983} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IC-006 {ECO:0000313|Proteomes:UP000322983}; RA Kato S., Itoh T., Ohkuma M.; RT "Complete Genome Sequencing of Sulfolobus sp. JCM 16833."; RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000325030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IC-007 {ECO:0000313|Proteomes:UP000325030}; RA Kato S., Itoh T., Ohkuma M.; RT "Complete Genome Sequencing of Sulfolobus sp. JCM 16834."; RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:BBG26976.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IC-006 {ECO:0000313|EMBL:BBG24219.1}, and IC-007 RC {ECO:0000313|EMBL:BBG26976.1}; RA Itoh T., Miura T., Sakai H.D., Kato S., Ohkuma M., Takashina T.; RT "Sulfuracidifex tepidarius gen. nov., sp. nov. and transfer of Sulfolobus RT metallicus Huber and Stetter 1992 to the genus Sulfuracidifex as RT Sulfuracidifex metallicus comb. nov."; RL Int. J. Syst. Evol. Microbiol. 0:0-0(2020). 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 probably involved in the transfer of the CC threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 CC group of A37. {ECO:0000256|HAMAP-Rule:MF_01446}. 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:0000256|ARBA:ARBA00001866, ECO:0000256|HAMAP- CC Rule:MF_01446}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01446}; CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01446}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01446}. CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000256|HAMAP- CC Rule:MF_01446}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01446}. 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; AP018929; BBG24219.1; -; Genomic_DNA. DR EMBL; AP018930; BBG26976.1; -; Genomic_DNA. DR RefSeq; WP_054845101.1; NZ_AP018930.1. DR STRING; 1294262.GCA_001316085_00518; -. DR GeneID; 41717841; -. DR KEGG; step:IC006_1526; -. DR Proteomes; UP000322983; Chromosome. DR Proteomes; UP000325030; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000408; C:EKC/KEOPS complex; IEA:InterPro. 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 HAMAP; MF_01446; Kae1; 1. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR000905; Gcp-like_dom. DR InterPro; IPR017861; KAE1/TsaD. DR InterPro; IPR022449; Kae1_arc. DR InterPro; IPR034680; Kae1_archaea_euk. DR InterPro; IPR017860; Peptidase_M22_CS. DR PANTHER; PTHR11735; PTHR11735; 1. DR PANTHER; PTHR11735:SF14; PTHR11735:SF14; 1. DR Pfam; PF00814; TsaD; 1. DR PRINTS; PR00789; OSIALOPTASE. DR SUPFAM; SSF53067; SSF53067; 1. DR TIGRFAMs; TIGR03722; arch_KAE1; 1. DR TIGRFAMs; TIGR00329; gcp_kae1; 1. DR PROSITE; PS01016; GLYCOPROTEASE; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP- KW Rule:MF_01446}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01446}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01446}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01446}; Reference proteome {ECO:0000313|Proteomes:UP000322983}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01446}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_01446}. FT DOMAIN 28..297 FT /note="TsaD" FT /evidence="ECO:0000259|Pfam:PF00814" FT BINDING 109 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01446" FT BINDING 113 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01446" FT BINDING 130..134 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01446" FT BINDING 130 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01446" FT BINDING 162 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01446" FT BINDING 183 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01446" FT BINDING 262 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01446" FT BINDING 290 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01446" SQ SEQUENCE 331 AA; 35763 MW; D4517FAEA0D0C4E5 CRC64; MLVLGIESTA HTFGVGIVRD EDPYILANER DTYVPKEGGM KPTDLLSHHA SVAPSVMRSA LRKASISMND VDYIAFSMGP GIGPALRVGA TVARALSLRY GKPLVPVNHG IGHIEIGFLT TKVKDPLVLY LSGGNTQIIT LYKGRFRVFG ETLDIALGNL MDTFSRDAGL APPYIINGRH VIDLCAEKGN KIIDFPYVVK GQDMSYSGLL TAAENALKNN DIGDVCLTLR EVAFDMLLEA TERALALSGK REILIVGGVA ASGSLRNKFE ALGKDWGVEI KVVPSEFSGD NGAMIAYAGM LEAKAGITVD VDKSQVRPRW RVDEVEAKWR S //