ID   MIAA2_SYNC1             Reviewed;         298 AA.
AC   Q39ZX2;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2013, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=tRNA dimethylallyltransferase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=DMAPP:tRNA dimethylallyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=DMATase 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE   AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=IPP transferase 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=IPPT 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=IPTase 2 {ECO:0000255|HAMAP-Rule:MF_00185};
GN   Name=miaA2 {ECO:0000255|HAMAP-Rule:MF_00185}; OrderedLocusNames=Pcar_3100;
OS   Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS   (Pelobacter carbinolicus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Syntrophotaleaceae; Syntrophotalea.
OX   NCBI_TaxID=338963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL   Submitted (OCT-2005) 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; CP000142; ABA90335.2; -; Genomic_DNA.
DR   RefSeq; WP_011342895.1; NC_007498.2.
DR   AlphaFoldDB; Q39ZX2; -.
DR   SMR; Q39ZX2; -.
DR   STRING; 338963.Pcar_3100; -.
DR   EnsemblBacteria; ABA90335; ABA90335; Pcar_3100.
DR   KEGG; pca:Pcar_3100; -.
DR   eggNOG; COG0324; Bacteria.
DR   HOGENOM; CLU_032616_0_1_7; -.
DR   OrthoDB; 1069591at2; -.
DR   Proteomes; UP000002534; 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..298
FT                   /note="tRNA dimethylallyltransferase 2"
FT                   /id="PRO_0000377256"
FT   REGION          35..38
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   BINDING         10..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   BINDING         12..17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   SITE            100
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ   SEQUENCE   298 AA;  33655 MW;  41F7C35EFAA9AFA3 CRC64;
     MTCNLLVILG PTASGKTRLG VAAARALDGE IISADSRQVF RGMDIGTGKD LSEYGDVPYH
     LIDICEAGSE FSVFDFQERF CTAYADIRKR GRLPVLVGGT GLYLDCVLRN YRLVKVPENP
     VLRAELDPLS MDQLAERLRA LKPEQHNTTD LGHRERLLRA IEIAEGEKAC GETGPVLPGL
     RPLVFGVRWE RAVLRRRITA RLKERLDAGL IDEVQALLDA GVAHRMLEHY GLEYRLVSQH
     LRGELNRNDM FQKLNSAIHQ FAKRQDTWFR RMERQGVQIH WLDGAGDPLQ GLLRVFMS