ID   G0M011_LACPE            Unreviewed;       311 AA.
AC   G0M011;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   09-JAN-2013, entry version 5.
DE   RecName: Full=tRNA dimethylallyltransferase;
DE            EC=2.5.1.75;
DE   AltName: Full=Dimethylallyl diphosphate:tRNA dimethylallyltransferase;
DE   AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase;
GN   Name=miaA; ORFNames=LPENT_00400;
OS   Lactobacillus pentosus IG1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1042160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IG1;
RA   Maldonado-Barragan A., Caballero-Guerrero B., Lucena-Padros H.,
RA   Ruiz-Barba J.L.;
RT   "Genome Sequence of Lactobacillus pentosus IG1, a Strain Isolated from
RT   Spanish-Style Green Olive Fermentations.";
RL   J. Bacteriol. 193:5605-5605(2011).
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: Dimethylallyl diphosphate + tRNA = diphosphate
CC       + tRNA containing 6-dimethylallyladenosine.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the IPP transferase family.
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DR   EMBL; FR874854; CCC15704.1; -; Genomic_DNA.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IEA:HAMAP.
DR   GO; GO:0008033; P:tRNA processing; IEA:HAMAP.
DR   HAMAP; MF_00185; IPP_trans; 1; -.
DR   InterPro; IPR002627; IPPT.
DR   InterPro; IPR018022; tRNA_delta_PyrP_Trfase.
DR   PANTHER; PTHR11088; PTHR11088; 1.
DR   Pfam; PF01715; IPPT; 1.
DR   TIGRFAMs; TIGR00174; miaA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Magnesium; Nucleotide-binding; Transferase;
KW   tRNA processing.
FT   NP_BIND      14     21       ATP (By similarity).
FT   REGION       16     21       Substrate binding (By similarity).
FT   REGION       39     42       Interaction with substrate tRNA (By
FT                                similarity).
FT   SITE        105    105       Interaction with substrate tRNA (By
FT                                similarity).
FT   SITE        130    130       Interaction with substrate tRNA (By
FT                                similarity).
SQ   SEQUENCE   311 AA;  34492 MW;  160BC0F2955D0C99 CRC64;
     MATIPKHKVL LIAGPTAVGK TALSLALAKQ LNGEIISGDS MQVYRHLDIG TAKIMPDERA
     GIPHYLIDIK TVDQRFTVAE FVSRATALIN DITARGKLPI IVGGTGFYLQ SLLAGYQFGP
     NDNAPDMAYR QQWFDRAANA GNQAVWDALN QRDPQAAAAI APANLVRVVR ALEYLHTTGQ
     LFSAQADTAT ETLDAYTLCL TAERSLLYDR INQRVDLMLN VGLEAEARWL YDQGGADLPA
     GKGIGYHEWF PYFAGTQSRD ATIAAIKQDS RRYAKRQLTW FRNKMTVDWV DLLEHPELRA
     SIDQRLASWL S
//