ID   MIAA_AYWBP              Reviewed;         291 AA.
AC   Q2NJ30;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=AYWB_446;
OS   Aster yellows witches'-broom phytoplasma (strain AYWB).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Candidatus Phytoplasma;
OC   Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=322098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16672622; DOI=10.1128/JB.188.10.3682-3696.2006;
RA   Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A.,
RA   Shevchenko D.V., Tsukerman K., Walunas T., Lapidus A., Campbell J.W.,
RA   Hogenhout S.A.;
RT   "Living with genome instability: the adaptation of phytoplasmas to
RT   diverse environments of their insect and plant hosts.";
RL   J. Bacteriol. 188:3682-3696(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.
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DR   EMBL; CP000061; ABC65563.1; -; Genomic_DNA.
DR   RefSeq; YP_456642.1; -.
DR   GeneID; 3865779; -.
DR   GenomeReviews; CP000061_GR; AYWB_446.
DR   KEGG; ayw:AYWB_446; -.
DR   HOGENOM; Q2NJ30; -.
DR   OMA; Q2NJ30; QLPYTVA.
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    291       tRNA Delta(2)-isopentenylpyrophosphate
FT                                transferase.
FT                                /FTId=PRO_1000020561.
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         96     96       Interaction with substrate tRNA (By
FT                                similarity).
SQ   SEQUENCE   291 AA;  33524 MW;  4DCC40BC1C2582D5 CRC64;
     MKKVIAITGP TASGKTSLSI KIAKKFNLEI INCDSLQMYQ KYDIGTAKIT IEEAQGIKHH
     LLDFLTPGTN YNIYYFQKDA RKKIEEMPLP LFVGGSGLYL KSVLFDYELT PKSLFLPPIS
     LTAIENMVDF IKKKDPQLIA NLDLKNPRRI LSAYQDLLSG TLRSQKNKKH NPLYSSLIFY
     LDIDRQILKK RVILRLEQML KKGFIEEVNQ IQTFFPNANF NIIGYREIKV LLEGKITLDQ
     AKTLIIQKTM QYAKRQKTWF KNQIKPMILD ALSPDLEKTT IGLINNFLKT D
//