ID MIAA_BURCM Reviewed; 324 AA. AC Q0BI05; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 22. 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=Bamb_0659; OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia OS cepacia (strain AMMD)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=339670; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., RA Konstantinidis K., Ramette A., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."; RL Submitted (AUG-2006) 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: 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 http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000440; ABI86218.1; -; Genomic_DNA. DR RefSeq; YP_772552.1; -. DR GeneID; 4311312; -. DR GenomeReviews; CP000440_GR; Bamb_0659. DR KEGG; bam:Bamb_0659; -. DR NMPDR; fig|339670.3.peg.3149; -. DR OMA; Q0BI05; VNADSMQ. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. 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; -; 1. DR InterPro; IPR002627; IPPT. DR InterPro; IPR018022; tRNA_delta_PyrP_Trfase. DR PANTHER; PTHR11088; IPPT; 1. DR Pfam; PF01715; IPPT; 1. DR ProDom; PD004674; IPPT; 1. DR ProDom; PD005388; IPPtrans_like; 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 1 324 tRNA Delta(2)-isopentenylpyrophosphate FT transferase. FT /FTId=PRO_1000020572. FT NP_BIND 17 24 ATP (Potential). FT REGION 19 24 Substrate binding (By similarity). FT REGION 42 45 Interaction with substrate tRNA (By FT similarity). FT REGION 166 170 Interaction with substrate tRNA (By FT similarity). FT REGION 251 256 Interaction with substrate tRNA (By FT similarity). FT REGION 284 291 Interaction with substrate tRNA (By FT similarity). FT SITE 108 108 Interaction with substrate tRNA (By FT similarity). FT SITE 130 130 Interaction with substrate tRNA (By FT similarity). SQ SEQUENCE 324 AA; 35584 MW; 2654BB1163F3E3C5 CRC64; MSASPQSRPT TITCLLGPTA SGKTAAALAL AARRPIEIVS VDSALVYRDM DIGTAKPTRD ERARVPHHLI DIIDPADAYS AAEFRADALR LIGEIAARGR TPLLAGGTML YYKALTQGLN DLPTADPAVR AELDADAARD GWPALHARLA QVDPATAARL APNDSQRIQR ALEVFLLSGQ PMSVLLAAPR RADDEAAAYR FVPVALEPSD RAVLHARIAQ RFDAMLDAGF IDEVERLRRR EDLHLGLPSM RCVGYRQAWE FLDGDTDYRT MRDKGIFATR QLCKRQITWL RAMPERIVVD CVAPDATALA LDTLERVLDD RLPT //