ID   MIAA_RHIRD              Reviewed;         298 AA.
AC   P0A3Q6; P38436;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 66.
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};
OS   Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS   radiobacter).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1735704; DOI=10.1128/jb.174.4.1086-1098.1992;
RA   Gray J., Wang J., Gelvin S.B.;
RT   "Mutation of the miaA gene of Agrobacterium tumefaciens results in reduced
RT   vir gene expression.";
RL   J. Bacteriol. 174:1086-1098(1992).
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   -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC       {ECO:0000305}.
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; M83532; AAA22091.1; -; Genomic_DNA.
DR   PIR; B42643; B42643.
DR   RefSeq; WP_010972016.1; NZ_JZLL01000041.1.
DR   AlphaFoldDB; P0A3Q6; -.
DR   SMR; P0A3Q6; -.
DR   STRING; 1082932.ATCR1_17252; -.
DR   DNASU; 1134077; -.
DR   eggNOG; COG0324; Bacteria.
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; 2.
DR   TIGRFAMs; TIGR00174; miaA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Magnesium; Nucleotide-binding; Transferase; tRNA processing;
KW   Virulence.
FT   CHAIN           1..298
FT                   /note="tRNA dimethylallyltransferase"
FT                   /id="PRO_0000163865"
FT   REGION          41..44
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   REGION          165..169
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   BINDING         16..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   BINDING         18..23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   SITE            107
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   SITE            129
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ   SEQUENCE   298 AA;  32660 MW;  B3F7D30AE2133097 CRC64;
     MMKNLDQNFD AILITGPTAS GKSALALRLA RERNGVVINA DSMQVYDTLR VLTARPSDHE
     MEGVPHRLYG HVPAGSAYST GEWLRDISGL LSDLRGEGRF PVIVGGTGLY FKALTGGLSD
     MPAIPDDLRE GLRARLIEEG AAKLHAELVS RDPSMAQMLQ PGDGQRIVRA LEVLEATGKS
     IRDFQRASGP MIIDPERAQK FIVLPERPVL HDRINRRFEA MMDSGAVEEV QALLALNLAP
     DATAMKAIGV AQIADMLTGR MGAAEVIEKS AAATRQYAKR QMTWFRNQMG DDWTRIQP