ID   MIAA_METPB              Reviewed;         317 AA.
AC   B1ZDL3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=Mpop_2776;
OS   Methylorubrum populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
OS   (Methylobacterium populi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=441620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-705 / NCIMB 13946 / BJ001;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Marx C., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium populi BJ001.";
RL   Submitted (APR-2008) 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; CP001029; ACB80931.1; -; Genomic_DNA.
DR   RefSeq; WP_012454653.1; NC_010725.1.
DR   AlphaFoldDB; B1ZDL3; -.
DR   SMR; B1ZDL3; -.
DR   STRING; 441620.Mpop_2776; -.
DR   EnsemblBacteria; ACB80931; ACB80931; Mpop_2776.
DR   KEGG; mpo:Mpop_2776; -.
DR   eggNOG; COG0324; Bacteria.
DR   HOGENOM; CLU_032616_0_1_5; -.
DR   OMA; YAKRQYT; -.
DR   Proteomes; UP000007136; 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; 2.
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..317
FT                   /note="tRNA dimethylallyltransferase"
FT                   /id="PRO_1000191858"
FT   REGION          44..47
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   BINDING         19..26
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   BINDING         21..26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   SITE            109
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   SITE            131
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ   SEQUENCE   317 AA;  34798 MW;  62FF3700AE127FB2 CRC64;
     MRSSDGQEAG RPAAILIAGP TASGKSALGL RIARAFGGTV INTDSMQVYA DLRVLSARPT
     ADEEAEAPHR LYGSVDGAVN FSVGHFQRQA AVILSEMAPD QLPVFVGGTG LYFRSLEDGI
     SDLPEVPEPI RQQIRAEAEG RPTEALHATL TLRDPKTAQR LRPSDRMRVM RALEIFAATG
     RSIGSFQETR LPGPLAGRPL LKVFLSPERE ILRRRIDARF VTMMENGALD EVAALRDRRL
     DPLLPVMRAH GVPGLIAHLD GALSREEAVQ RGQGDTRRYA KRQFTWFRHQ MGEAWHWTTP
     EAAWSLAEAL LSAPVGQ