ID   MIAA_ANAVT              Reviewed;         294 AA.
AC   Q3MA53;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, 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=Ava_2518;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) 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.
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DR   EMBL; CP000117; ABA22133.1; -; Genomic_DNA.
DR   RefSeq; YP_323028.1; -.
DR   GeneID; 3682616; -.
DR   GenomeReviews; CP000117_GR; Ava_2518.
DR   KEGG; ava:Ava_2518; -.
DR   NMPDR; fig|240292.3.peg.2000; -.
DR   HOGENOM; Q3MA53; -.
DR   OMA; Q3MA53; VNADSMQ.
DR   BioCyc; AVAR240292:AVA_2518-MON; -.
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    294       tRNA Delta(2)-isopentenylpyrophosphate
FT                                transferase.
FT                                /FTId=PRO_1000020560.
FT   NP_BIND       9     16       ATP (Potential).
FT   REGION       11     16       Substrate binding (By similarity).
FT   REGION       34     37       Interaction with substrate tRNA (By
FT                                similarity).
FT   SITE         98     98       Interaction with substrate tRNA (By
FT                                similarity).
SQ   SEQUENCE   294 AA;  32947 MW;  CB930651D840B17A CRC64;
     MTKLIVICGA TATGKSGLAL NLAMRLGSVI LSADSRQVYR EFDIGTAKPT LAEQKAVPHY
     LIDICTPRET MTVADYQEQA QALINSLPVS PLLLVGGTGL YIRSIVQGMK IPRVAPNYEL
     RSQLESLGQT TLYGILQQVD PVAAQKIHPH DPVRTLRAVE VFYVTGIPIS AQQGENPPDY
     PILQIGLDCE MERLSERIHK RTEQMIADGL VGEVEYLCQK YGADLPLLNT LGYQEIKQYL
     AGEISLEAAK ELIVLHTRQF AKRQRTWFRA YPQIEWFNAD DADLLDIVWQ RIQQ
//