ID A0A510E3B7_9CREN Unreviewed; 331 AA. AC A0A510E3B7; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 13-NOV-2019, entry version 2. 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=IC007_1503 {ECO:0000313|EMBL:BBG26976.1}; OS Sulfolobus sp. JCM 16834. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus; unclassified Sulfolobus. OX NCBI_TaxID=2173830 {ECO:0000313|EMBL:BBG26976.1}; RN [1] {ECO:0000313|EMBL:BBG26976.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IC-007 {ECO:0000313|EMBL:BBG26976.1}; 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. CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group CC on adenosine at position 37 (t(6)A37) in tRNAs that read codons CC beginning with adenine. Is probably involved in the transfer of CC the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to CC the N6 group of A37. {ECO:0000256|HAMAP-Rule:MF_01446}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = CC AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA; CC Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA- CC COMP:10163, ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; CC EC=2.3.1.234; Evidence={ECO:0000256|HAMAP-Rule:MF_01446, CC ECO:0000256|SAAS:SAAS01118488}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01446}; CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01446}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01446, CC ECO:0000256|SAAS:SAAS00346542}. 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 CC of 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; AP018930; BBG26976.1; -; Genomic_DNA. DR HAMAP; MF_01446; Kae1; 1. DR InterPro; IPR000905; Gcp-like_dom. DR InterPro; IPR034680; Kae1/OSGEP. DR InterPro; IPR017861; KAE1/TsaD. DR InterPro; IPR022449; Kae1_arc. DR InterPro; IPR017860; Peptidase_M22_CS. DR PANTHER; PTHR11735; PTHR11735; 1. DR PANTHER; PTHR11735:SF14; PTHR11735:SF14; 1. DR Pfam; PF00814; Peptidase_M22; 1. DR PRINTS; PR00789; OSIALOPTASE. 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|HAMAP-Rule:MF_01446, KW ECO:0000256|SAAS:SAAS00195274}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01446, KW ECO:0000256|SAAS:SAAS00195276}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01446, ECO:0000256|SAAS:SAAS00195263}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01446, KW ECO:0000256|SAAS:SAAS00195272}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01446, KW ECO:0000256|SAAS:SAAS00195271, ECO:0000313|EMBL:BBG26976.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01446, KW ECO:0000256|SAAS:SAAS00195265}. FT DOMAIN 28 297 Peptidase_M22. {ECO:0000259|Pfam: FT PF00814}. FT REGION 130 134 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01446}. FT METAL 109 109 Iron. {ECO:0000256|HAMAP-Rule:MF_01446}. FT METAL 113 113 Iron. {ECO:0000256|HAMAP-Rule:MF_01446}. FT METAL 130 130 Iron. {ECO:0000256|HAMAP-Rule:MF_01446}. FT METAL 290 290 Iron. {ECO:0000256|HAMAP-Rule:MF_01446}. FT BINDING 162 162 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01446}. FT BINDING 183 183 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01446}. FT BINDING 262 262 Substrate. {ECO:0000256|HAMAP-Rule: FT 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 //