ID   MIAA_HELAH              Reviewed;         266 AA.
AC   Q17ZN6;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=tRNA dimethylallyltransferase;
DE            EC=2.5.1.75;
DE   AltName: Full=Dimethylallyl diphosphate:tRNA dimethylallyltransferase;
DE            Short=DMAPP:tRNA dimethylallyltransferase;
DE            Short=DMATase;
DE   AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase;
DE            Short=IPP transferase;
DE            Short=IPPT;
DE            Short=IPTase;
GN   Name=miaA; OrderedLocusNames=Hac_0022;
OS   Helicobacter acinonychis (strain Sheeba).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=382638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheeba;
RX   PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA   Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA   Gressmann H., Achtman M., Schuster S.C.;
RT   "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT   host jump from early humans to large felines.";
RL   PLoS Genet. 2:1097-1110(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). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA + dimethylallyl diphosphate =
CC         diphosphate + N(6)-dimethylallyladenosine(37) in tRNA;
CC         Xref=Rhea:RHEA:26482, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10375,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:74411,
CC         ChEBI:CHEBI:74415; EC=2.5.1.75;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the IPP transferase family. {ECO:0000305}.
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DR   EMBL; AM260522; CAJ98890.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q17ZN6; -.
DR   SMR; Q17ZN6; -.
DR   STRING; 382638.Hac_0022; -.
DR   PRIDE; Q17ZN6; -.
DR   EnsemblBacteria; CAJ98890; CAJ98890; Hac_0022.
DR   KEGG; hac:Hac_0022; -.
DR   eggNOG; COG0324; Bacteria.
DR   HOGENOM; CLU_032616_0_1_7; -.
DR   OMA; YAKRQYT; -.
DR   Proteomes; UP000000775; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR039657; Dimethylallyltransferase.
DR   InterPro; IPR018022; IPT.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11088; PTHR11088; 1.
DR   TIGRFAMs; TIGR00174; miaA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Magnesium; Nucleotide-binding; Transferase; tRNA processing.
FT   CHAIN           1..266
FT                   /note="tRNA dimethylallyltransferase"
FT                   /id="PRO_0000377183"
FT   SITE            63
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   266 AA;  30580 MW;  9333E3E06E1F4323 CRC64;
     MSIYKDINIA SAKPSLKERK NIKHYALDCL NIDEKNNAPL FKTLLEDAMK VSQKEILLIV
     GGSSFYLKSI LEGLSSMPKL NNDQILKIER EIATLTNPYA FLKSIDPNMA FKIHSNDTYR
     IHKALEIFYA THTPPSEYFK KNPKKPFEHA ITLFALCIEK TVLHNRIKQR TKNMLDCGLI
     EEIKALYTQY PKDSQPFKAI GVKESILYLE KQLTLKELEE AIVSNTIKLA KRQNTFNKTQ
     FNNLYVGSVE EVRHAILKRS KSGIKE