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 14-MAY-2014, entry version 51. DE RecName: Full=tRNA dimethylallyltransferase; DE EC=2.5.1.75; DE AltName: Full=Dimethylallyl diphosphate:tRNA dimethylallyltransferase; DE Short=DMAPP:tRNA dimethylallyltransferase; DE Short=DMATase; DE AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase; DE Short=IPP transferase; DE Short=IPPT; DE Short=IPTase; GN Name=miaA; OrderedLocusNames=Mmwyl1_2633; OS Marinomonas sp. (strain MWYL1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC 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., RA Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Johnston A.W.B., Todd J.D., Rogers R., Wexler M., RA Bond P.L., Li Y., 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) (By similarity). CC -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + adenine(37) in CC tRNA = diphosphate + N(6)-dimethylallyladenine(37) in tRNA. CC -!- COFACTOR: Magnesium (By similarity). CC -!- SUBUNIT: Monomer (By similarity). CC -!- SIMILARITY: Belongs to the IPP transferase family. 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 RefSeq; YP_001341481.1; NC_009654.1. DR ProteinModelPortal; A6VYL7; -. DR STRING; 400668.Mmwyl1_2633; -. DR EnsemblBacteria; ABR71546; ABR71546; Mmwyl1_2633. DR GeneID; 5365666; -. DR KEGG; mmw:Mmwyl1_2633; -. DR PATRIC; 22468733; VBIMarSp124341_2719. DR eggNOG; COG0324; -. DR HOGENOM; HOG000039996; -. DR KO; K00791; -. DR OMA; INCDSKQ; -. DR OrthoDB; EOG661HB3; -. DR BioCyc; MSP400668:GHKD-2694-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00185; IPP_trans; 1. DR InterPro; IPR002627; IPPT. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR018022; tRNA_delta_PyrP_Trfase. DR PANTHER; PTHR11088; PTHR11088; 1. DR Pfam; PF01715; IPPT; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR TIGRFAMs; TIGR00174; miaA; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Magnesium; Nucleotide-binding; KW Transferase; tRNA processing. FT CHAIN 1 310 tRNA dimethylallyltransferase. FT /FTId=PRO_0000377215. FT NP_BIND 11 18 ATP (Potential). FT REGION 13 18 Substrate binding (By similarity). FT REGION 36 39 Interaction with substrate tRNA (By FT similarity). FT REGION 160 164 Interaction with substrate tRNA (By FT similarity). FT REGION 242 247 Interaction with substrate tRNA (By FT similarity). FT SITE 102 102 Interaction with substrate tRNA (By FT similarity). FT SITE 124 124 Interaction with substrate tRNA (By FT similarity). 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 //