ID MIAA_KOCRD Reviewed; 313 AA. AC B2GKG9; DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 1. DT 09-FEB-2010, entry version 18. DE RecName: Full=tRNA Delta(2)-isopentenylpyrophosphate transferase; DE Short=IPP transferase; DE EC=2.5.1.8; DE AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase; DE Short=IPTase; DE Short=IPPT; DE AltName: Full=Dimethylallyl diphosphate:tRNA dimethylallyltransferase; DE Short=DMAPP:tRNA dimethylallyltransferase; DE Short=DMATase; GN Name=miaA; OrderedLocusNames=KRH_15810; OS Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / OS DC2201). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Kocuria. OX NCBI_TaxID=378753; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=18408034; DOI=10.1128/JB.01853-07; RA Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S., RA Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., RA Harayama S.; RT "Complete genome sequence of the soil actinomycete Kocuria RT rhizophila."; RL J. Bacteriol. 190:4139-4146(2008). 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: Isopentenyl diphosphate + tRNA = diphosphate + CC tRNA containing 6-isopentenyladenosine. 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; AP009152; BAG29928.1; -; Genomic_DNA. DR RefSeq; YP_001855434.1; -. DR GeneID; 6239346; -. DR GenomeReviews; AP009152_GR; KRH_15810. DR KEGG; krh:KRH_15810; -. DR HOGENOM; HBG559459; -. DR OMA; VNADSMQ; -. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0004811; F:tRNA isopentenyltransferase activity; IEA:HAMAP. DR GO; GO:0008033; P:tRNA processing; IEA:HAMAP. DR HAMAP; MF_00185; IPP_trans; 1; -. DR InterPro; IPR002627; IPPT. DR InterPro; IPR018022; tRNA_delta_PyrP_Trfase. DR PANTHER; PTHR11088; IPPT; 1. DR Pfam; PF01715; IPPT; 1. DR TIGRFAMs; TIGR00174; miaA; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Magnesium; Nucleotide-binding; KW Nucleotidyltransferase; Transferase; tRNA processing. FT CHAIN 1 313 tRNA Delta(2)-isopentenylpyrophosphate FT transferase. FT /FTId=PRO_0000377195. FT NP_BIND 20 27 ATP (Potential). FT REGION 22 27 Substrate binding (By similarity). FT SITE 111 111 Interaction with substrate tRNA (By FT similarity). FT SITE 132 132 Interaction with substrate tRNA (By FT similarity). SQ SEQUENCE 313 AA; 34331 MW; F39C134E5CE81678 CRC64; MSAPDAGRED TRIPLVAVVG PTGTGKSELA IALARELDGE VVNADALQLY RGMDVGTAKL TPEERQGVPH HLLDVLEIHE EASVAAFQRD ARRAVDEIRG RGRVPVLVGG SGLYVRAALD AIEFPGTDAT VRARREEQLR ERGRAALLRE LAAVDPGSAE RVKDDRRLVR ALEVHDLTGR PFTSFMPERR YVQPTVQIGL AMDREVLNRR LAHRVDLMLE RGWLEEVKAL EARGLRESPT AGRALGYPQL LAVLDGSATL DEAREDTVAA TRRFTKRQRT WFGADPRVHW LDAGDPNGID GLTAGAVRLV AAQ //