ID MIAA_MARMS Reviewed; 310 AA. AC A6VYL7; DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 24-JAN-2024, entry version 90. DE RecName: Full=tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE EC=2.5.1.75 {ECO:0000255|HAMAP-Rule:MF_00185}; DE AltName: Full=Dimethylallyl diphosphate:tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=DMAPP:tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=DMATase {ECO:0000255|HAMAP-Rule:MF_00185}; DE AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=IPP transferase {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=IPPT {ECO:0000255|HAMAP-Rule:MF_00185}; DE Short=IPTase {ECO:0000255|HAMAP-Rule:MF_00185}; GN Name=miaA {ECO:0000255|HAMAP-Rule:MF_00185}; OrderedLocusNames=Mmwyl1_2633; OS Marinomonas sp. (strain MWYL1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales; OC Oceanospirillaceae; Marinomonas. OX NCBI_TaxID=400668; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MWYL1; 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., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y., RA Richardson P.; RT "Complete sequence of Marinomonas sp. MWYL1."; RL Submitted (JUN-2007) 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:0000255|HAMAP-Rule:MF_00185}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00185}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00185}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00185}. CC -!- SIMILARITY: Belongs to the IPP transferase family. {ECO:0000255|HAMAP- CC 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; CP000749; ABR71546.1; -; Genomic_DNA. DR AlphaFoldDB; A6VYL7; -. DR SMR; A6VYL7; -. DR STRING; 400668.Mmwyl1_2633; -. DR KEGG; mmw:Mmwyl1_2633; -. DR eggNOG; COG0324; Bacteria. DR HOGENOM; CLU_032616_0_0_6; -. DR OMA; YAKRQYT; -. DR OrthoDB; 9776390at2; -. 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; 1.10.20.140; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00185; IPP_trans; 1. DR InterPro; IPR039657; Dimethylallyltransferase. DR InterPro; IPR018022; IPT. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR00174; miaA; 1. DR PANTHER; PTHR11088; TRNA DIMETHYLALLYLTRANSFERASE; 1. DR PANTHER; PTHR11088:SF60; TRNA DIMETHYLALLYLTRANSFERASE 9; 1. DR Pfam; PF01715; IPPT; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. PE 3: Inferred from homology; KW ATP-binding; Magnesium; Nucleotide-binding; Transferase; tRNA processing. FT CHAIN 1..310 FT /note="tRNA dimethylallyltransferase" FT /id="PRO_0000377215" FT REGION 36..39 FT /note="Interaction with substrate tRNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185" FT REGION 160..164 FT /note="Interaction with substrate tRNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185" FT REGION 242..247 FT /note="Interaction with substrate tRNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185" FT BINDING 11..18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185" FT BINDING 13..18 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185" FT SITE 102 FT /note="Interaction with substrate tRNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185" FT SITE 124 FT /note="Interaction with substrate tRNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185" SQ SEQUENCE 310 AA; 35239 MW; 013911EA1DEDA547 CRC64; MTKPYVVCLM GPTASGKTGL AVELAEHHNF EIISVDSALV YKGMDIGTAK PSAELLARAP HRLIDIIDPL EFYSAADFVL DAVEQSQEIL AKGKTPLLVG GTMMYFNALQ KGLAEMPQAD AELRVIIEAE AAEKGWAALH EELQRFDPEA ASRIHPNDPQ RLQRAIEVYR LTGKTMTHFW RQQEAVSLPF EMINMAVMPK ERSVLHERIE QRFYDMMDQG FLAEVEGFYR RGDLTIDMPS MRCVGYRQLW QYLDGVDLLE DAIFKGVVAS RQLAKRQLTW LRGWEDLMIF DSLSKDLVPE ALNYIESRII //