ID   MIAA_HELPG              Reviewed;         276 AA.
AC   B5Z937;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=HPG27_1338;
OS   Helicobacter pylori (strain G27).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=563041;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G27;
RX   PubMed=18952803; DOI=10.1128/jb.01416-08;
RA   Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA   Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT   "The complete genome sequence of Helicobacter pylori strain G27.";
RL   J. Bacteriol. 191:447-448(2009).
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; CP001173; ACI28086.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5Z937; -.
DR   SMR; B5Z937; -.
DR   EnsemblBacteria; ACI28086; ACI28086; HPG27_1338.
DR   KEGG; hpg:HPG27_1338; -.
DR   HOGENOM; CLU_032616_0_1_7; -.
DR   OMA; YAKRQYT; -.
DR   Proteomes; UP000001735; 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..276
FT                   /note="tRNA dimethylallyltransferase"
FT                   /id="PRO_0000377185"
FT   REGION          9..12
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000250"
FT   SITE            73
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   276 AA;  31421 MW;  296B603441AA962D CRC64;
     MDAEIFSLDS LSIYKDINIA SAKPSLKERK NIKHYALDYL NIDEKNNAQL FKTLLEDAMR
     VSSKEILLIV GGSSFYLKSI LEGLSDTPKI SGEEVVKIER EIATLSNPYI FLKSIDPNMA
     FKIHSNDTYR IHKALEIFYA THTPPSEYFK ANPKKPFAHA ISLFALSVEK NALHNNIKQR
     TKNMLHSGLI EEIKALYTQY PKDSQPFKAI GVKESILFLE KRLTLKELEE TITSNTIKLA
     KRQNTFNKTQ FNNLYTGSVK EVRHAILKHS KSGIKG