ID A0A6G6W845_9ACTN Unreviewed; 312 AA. AC A0A6G6W845; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 07-OCT-2020, entry version 2. DE RecName: Full=tRNA dimethylallyltransferase {ECO:0000256|HAMAP-Rule:MF_00185}; DE EC=2.5.1.75 {ECO:0000256|HAMAP-Rule:MF_00185}; DE AltName: Full=Dimethylallyl diphosphate:tRNA dimethylallyltransferase {ECO:0000256|HAMAP-Rule:MF_00185}; DE Short=DMAPP:tRNA dimethylallyltransferase {ECO:0000256|HAMAP-Rule:MF_00185}; DE Short=DMATase {ECO:0000256|HAMAP-Rule:MF_00185}; DE AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase {ECO:0000256|HAMAP-Rule:MF_00185}; DE Short=IPP transferase {ECO:0000256|HAMAP-Rule:MF_00185}; DE Short=IPPT {ECO:0000256|HAMAP-Rule:MF_00185}; DE Short=IPTase {ECO:0000256|HAMAP-Rule:MF_00185}; GN Name=miaA {ECO:0000256|HAMAP-Rule:MF_00185, GN ECO:0000313|EMBL:QIG41508.1}; GN ORFNames=G5V58_00840 {ECO:0000313|EMBL:QIG41508.1}; OS Nocardioides sp. R-3366. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Nocardioides. OX NCBI_TaxID=2712223 {ECO:0000313|EMBL:QIG41508.1}; RN [1] {ECO:0000313|EMBL:QIG41508.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=R-3366 {ECO:0000313|EMBL:QIG41508.1}; RA Im W.-T.; RT "Full genome sequence of Nocardioides sp. R-3366."; RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the CC adenine at position 37 in tRNAs that read codons beginning with CC uridine, leading to the formation of N6-(dimethylallyl)adenosine CC (i(6)A). {ECO:0000256|ARBA:ARBA00003213, ECO:0000256|HAMAP- CC Rule:MF_00185, ECO:0000256|RuleBase:RU003784}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(37) in tRNA + dimethylallyl diphosphate = CC diphosphate + N(6)-dimethylallyladenosine(37) in tRNA; CC Xref=Rhea:RHEA:26482, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10375, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:74411, CC ChEBI:CHEBI:74415; EC=2.5.1.75; CC Evidence={ECO:0000256|ARBA:ARBA00001549, ECO:0000256|HAMAP- CC Rule:MF_00185, ECO:0000256|RuleBase:RU003783}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00185}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00185}. CC -!- SIMILARITY: Belongs to the IPP transferase family. CC {ECO:0000256|ARBA:ARBA00005842, ECO:0000256|HAMAP-Rule:MF_00185, CC ECO:0000256|RuleBase:RU003785}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00185}. 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; CP049257; QIG41508.1; -; Genomic_DNA. DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IEA:UniProtKB-EC. DR HAMAP; MF_00185; IPP_trans; 1. DR InterPro; IPR039657; Dimethylallyltransferase. DR InterPro; IPR018022; IPT. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11088; PTHR11088; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR00174; miaA; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00185, ECO:0000256|RuleBase:RU003785}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00185}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00185, ECO:0000256|RuleBase:RU003785}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00185, ECO:0000256|RuleBase:RU003785, ECO:0000313|EMBL:QIG41508.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00185, KW ECO:0000256|RuleBase:RU003783}. FT NP_BIND 9..16 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00185" FT REGION 11..16 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00185" FT SITE 100 FT /note="Interaction with substrate tRNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00185" FT SITE 121 FT /note="Interaction with substrate tRNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00185" SQ SEQUENCE 312 AA; 34807 MW; 94C5759D6FFF69A0 CRC64; MVPIVAVVGA TASGKTTLSL DLAERLRGEV VNTDAMQVYR GMDVGTAKLP AHERRGIPHH LLDTLTVTEP ATVAEFQRWA REVIDRLRAR EVTPVLVGGS ALYTRSVLDR FEFPGTDQEV RARWEAELAA RGPHALHALL AERDPEAAAG ILPENGRRTV RALEVIELTG ERFSASLPVL EYADPATVQI GVDIDRETLD RRIAERVDAM FASGFVDEVR HLLDHGLEQG RTASRAIGYR EVIALLRGEL DETEARERTA RATRRFARRQ DSWFRKDPRI VWVRYDDPDR VERAVEAVGK IGRVEPGATT PD //