ID   MIAA_SHESR              Reviewed;         296 AA.
AC   Q0HR41;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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};
GN   OrderedLocusNames=Shewmr7_3433;
OS   Shewanella sp. (strain MR-7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-7;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA   Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL   Submitted (AUG-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}.
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DR   EMBL; CP000444; ABI44414.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0HR41; -.
DR   SMR; Q0HR41; -.
DR   EnsemblBacteria; ABI44414; ABI44414; Shewmr7_3433.
DR   KEGG; shm:Shewmr7_3433; -.
DR   HOGENOM; CLU_032616_0_0_6; -.
DR   OMA; YAKRQYT; -.
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; Transferase; tRNA processing.
FT   CHAIN           1..296
FT                   /note="tRNA dimethylallyltransferase"
FT                   /id="PRO_0000377320"
FT   REGION          27..30
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   REGION          151..155
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   REGION          232..237
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   BINDING         2..9
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   BINDING         4..9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   SITE            93
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   SITE            115
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ   SEQUENCE   296 AA;  33143 MW;  BC553A5C0BF3FDD2 CRC64;
     MGPTASGKTA LALELAEKHN CEIISVDSAL IYRGMDIGSA KPSAEELARG PHRLIDIRDP
     AESYSAADFR ADALREIEQI ISMGKTPVLV GGTMMYFKAL LEGLSPLPSA DEAIRAEIQA
     EADANGWEAL HAQLREIDPV SAERIHPNDP QRLSRAIEVY RISGKSLTEL TQTKSAPLPY
     DVVQFAIAPR ERKVLHELIG QRFRIMLEQG FIDEVAQLKA RGDLHLDLPS MRCVGYRQCW
     QYLDGEFDYD TMVEKAVAAT RQLAKRQLTW LRSWPELNWL ESGAEGNLVT LMRQCR