ID   MIAA_BORAP              Reviewed;         300 AA.
AC   Q0SM30;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-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=BAPKO_0874;
OS   Borrelia afzelii (strain PKo).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M.,
RA   Suehnel J., Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(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; CP000395; ABH02098.1; -; Genomic_DNA.
DR   RefSeq; YP_710274.1; -.
DR   GeneID; 4227151; -.
DR   GenomeReviews; CP000395_GR; BAPKO_0874.
DR   KEGG; baf:BAPKO_0874; -.
DR   NMPDR; fig|390236.5.peg.876; -.
DR   HOGENOM; Q0SM30; -.
DR   OMA; Q0SM30; VNADSMQ.
DR   BioCyc; BAFZ390236:BAPKO_0874-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    300       tRNA Delta(2)-isopentenylpyrophosphate
FT                                transferase.
FT                                /FTId=PRO_1000020566.
FT   NP_BIND      11     18       ATP (Potential).
FT   REGION       13     18       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        123    123       Interaction with substrate tRNA (By
FT                                similarity).
SQ   SEQUENCE   300 AA;  35076 MW;  2B3181ABC60C3128 CRC64;
     MKEDRIVFIF GPTAVGKSNI LFHFPRNKAE IINVDSIQVY KEFNIASSKP GKSLMKHIKH
     HLVDFLEPEK EYTLGIFYEQ ALKIVKEIRQ KKKIPIFVGG TAFYFKHLKD GFPSTPLVTS
     KIRIYVNNLL DLKGKSHLLK ELKNVDPIRF NMLNKNDIYR IKRSLEVYYQ TGIPISQFQK
     KQNSEFKNIL IVGLKRSFED LKTRISIRIN EMLNSGLLSE IKGLFSKGYN ENTPAFKGIG
     YNEFLLWKSR PWYSLNDIIS LINKNSVLYA KRQMTFFAKM PDVLWFHPED DLDDILNLIF
//