ID MIAA_BORA1 Reviewed; 312 AA. AC Q2KX23; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 23. 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=BAV0724; OS Bordetella avium (strain 197N). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=360910; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16885469; DOI=10.1128/JB.01927-05; RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., RA King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., RA Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., RA Squares S., Woodward J., Parkhill J., Temple L.M.; RT "Comparison of the genome sequence of the poultry pathogen Bordetella RT avium with those of B. bronchiseptica, B. pertussis, and B. RT parapertussis reveals extensive diversity in surface structures RT associated with host interaction."; RL J. Bacteriol. 188:6002-6015(2006). 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; AM167904; CAJ48335.1; -; Genomic_DNA. DR RefSeq; YP_785257.1; -. DR GeneID; 6267599; -. DR GenomeReviews; AM167904_GR; BAV0724. DR KEGG; bav:BAV0724; -. DR NMPDR; fig|521.1.peg.899; -. DR HOGENOM; Q2KX23; -. DR OMA; Q2KX23; 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 1 312 tRNA Delta(2)-isopentenylpyrophosphate FT transferase. FT /FTId=PRO_1000020565. 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 243 248 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 312 AA; 33927 MW; 1CC8244E91D49FAF CRC64; MNTPPLICLA GPTAAGKSAA TLALAERWPL EIINVDSATI YRGMDIGTAK PSAAEQAQVA QHLLDIRDPS QAYSAADFRT DTLALIEDIQ ARGRIPLLAG GTMLYYKALR EGLDDLPQAD PVLRAELEAR AANEGWPALH AELARHDPIT AARLSPNDSQ RIQRALEVCL LSGRAMSALL TGTRRPAPSD LRFVTISLEP SDRAGLHARI AQRFDAMLQA GLEAEVRSLK QRTDLHPGLP SVRCVGYRQM WAYLDGEVSF DEAREQGIAA TRQLAKRQLT WLRAQPERVI VDCLAAGTAA RVVDIAARYL PG //