ID A0A6G6W845_9ACTN Unreviewed; 312 AA. AC A0A6G6W845; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 12-OCT-2022, entry version 9. 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 anomalus. OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae; OC Nocardioides. OX NCBI_TaxID=2712223 {ECO:0000313|EMBL:QIG41508.1, ECO:0000313|Proteomes:UP000502996}; RN [1] {ECO:0000313|EMBL:QIG41508.1, ECO:0000313|Proteomes:UP000502996} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R-3366 {ECO:0000313|EMBL:QIG41508.1, RC ECO:0000313|Proteomes:UP000502996}; 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 KEGG; nano:G5V58_00840; -. DR Proteomes; UP000502996; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.300; -; 1. 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|HAMAP-Rule:MF_00185, KW ECO:0000256|RuleBase:RU003785}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00185}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00185, KW ECO:0000256|RuleBase:RU003785}; KW Reference proteome {ECO:0000313|Proteomes:UP000502996}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00185}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00185, KW ECO:0000256|RuleBase:RU003783}. FT BINDING 9..16 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00185" FT BINDING 11..16 FT /ligand="substrate" 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 //