ID MIAA_CLOPS Reviewed; 310 AA. AC Q0STR2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-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=CPR_1173; OS Clostridium perfringens (strain SM101 / Type A). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=289380; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16825665; DOI=10.1101/gr.5238106; RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., RA DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., RA Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., RA Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., RA Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., RA Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I., RA Melville S.B., Paulsen I.T.; RT "Skewed genomic variability in strains of the toxigenic bacterial RT pathogen, Clostridium perfringens."; RL Genome Res. 16:1031-1040(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; CP000312; ABG87314.1; -; Genomic_DNA. DR RefSeq; YP_698495.1; -. DR GeneID; 4206507; -. DR GenomeReviews; CP000312_GR; CPR_1173. DR KEGG; cpr:CPR_1173; -. DR TIGR; CPR_1173; -. DR HOGENOM; Q0STR2; -. DR OMA; Q0STR2; 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 1 310 tRNA Delta(2)-isopentenylpyrophosphate FT transferase. FT /FTId=PRO_1000020589. FT NP_BIND 10 17 ATP (Potential). FT REGION 12 17 Substrate binding (By similarity). FT REGION 35 38 Interaction with substrate tRNA (By FT similarity). FT SITE 101 101 Interaction with substrate tRNA (By FT similarity). FT SITE 124 124 Interaction with substrate tRNA (By FT similarity). SQ SEQUENCE 310 AA; 35730 MW; 3DAA96DC872ADDEE CRC64; MNNNLLIIAG PTAVGKSDLS VDLAKKLNGE IISVDSMQIY KYMDIGSAKI SKEEMGGIPH YLIDFVDPSK EFSVAEFKEL ATEKIKDIQS RGKLPILVGG TGLYINSIIC NMNFAESDKD EEYREELEKI ANEHGNEYLH EMLKDIDLES YNSIHFNNRK RVIRALETYK LTGKPFSSFK AKNSIYETPY NIYYYVLNMD RAKLYERINK RVDIMFEKGL LEEVKNLKAM GLTDDMQSMK GIGYKEVLYY LDGKISLEQC IEMIKQGSRN YAKRQLTWFR KDPRAIFIDK DTFSSEEDIS SKIINDIINS //