ID   MIAA_ALBFT              Reviewed;         350 AA.
AC   Q21Y86;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185};
DE            EC=2.5.1.75 {ECO:0000255|HAMAP-Rule:MF_00185};
DE   AltName: Full=Dimethylallyl diphosphate:tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=DMAPP:tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=DMATase {ECO:0000255|HAMAP-Rule:MF_00185};
DE   AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=IPP transferase {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=IPPT {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=IPTase {ECO:0000255|HAMAP-Rule:MF_00185};
GN   Name=miaA {ECO:0000255|HAMAP-Rule:MF_00185}; OrderedLocusNames=Rfer_1535;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_00185}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00185};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00185};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00185}.
CC   -!- SIMILARITY: Belongs to the IPP transferase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00185}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000267; ABD69267.1; -; Genomic_DNA.
DR   RefSeq; WP_011463835.1; NC_007908.1.
DR   AlphaFoldDB; Q21Y86; -.
DR   SMR; Q21Y86; -.
DR   STRING; 338969.Rfer_1535; -.
DR   EnsemblBacteria; ABD69267; ABD69267; Rfer_1535.
DR   KEGG; rfr:Rfer_1535; -.
DR   eggNOG; COG0324; Bacteria.
DR   HOGENOM; CLU_032616_0_0_4; -.
DR   OMA; YAKRQYT; -.
DR   OrthoDB; 1069591at2; -.
DR   Proteomes; UP000008332; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00185; IPP_trans; 1.
DR   InterPro; IPR039657; Dimethylallyltransferase.
DR   InterPro; IPR018022; IPT.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11088; PTHR11088; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00174; miaA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Magnesium; Nucleotide-binding; Reference proteome;
KW   Transferase; tRNA processing.
FT   CHAIN           1..350
FT                   /note="tRNA dimethylallyltransferase"
FT                   /id="PRO_0000377287"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..55
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   REGION          176..180
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   REGION          273..278
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   BINDING         27..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   BINDING         29..34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   SITE            118
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   SITE            140
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ   SEQUENCE   350 AA;  37927 MW;  7481BBDF720E5F0F CRC64;
     MMNTERPAGP LRPPHPPHPP RYLALAGPTA SGKTAAALAI ARVHEVEIIS VDSALVYRGM
     DIGTAKPSAA ELAAVPHHLI DIRDPLQAYS AAEFVADAQA LIAAITARGR LPLLVGGTML
     YFKALLEGLD PMPKADPATR ALIATEAAEQ GWPALHAALA EVDPVSAKRL HPADSQRIAR
     ALEVYRLSGQ PLSSFQTTKL IATNEGVTGA RGQKCLNIPE NDRCLISLEP QNRAWLHQRI
     AERFDAMLAA GFIDEVRALR ARGDLQADLP AMRCVGYRQA WQALDGLWPM SELRDKGICA
     TRQLAKRQLT WLRSMPERRV VACDAPDALD QVLALARDFV NAGNKLQGQP