MIAA_BURCJ
ID MIAA_BURCJ Reviewed; 326 AA.
AC B4EDH3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=BceJ2315_31980; ORFNames=BCAL3257;
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX PubMed=18931103; DOI=10.1128/jb.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
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; AM747720; CAR53581.1; -; Genomic_DNA.
DR RefSeq; WP_006484937.1; NC_011000.1.
DR AlphaFoldDB; B4EDH3; -.
DR SMR; B4EDH3; -.
DR STRING; 216591.BCAL3257; -.
DR PRIDE; B4EDH3; -.
DR EnsemblBacteria; CAR53581; CAR53581; BCAL3257.
DR KEGG; bcj:BCAL3257; -.
DR eggNOG; COG0324; Bacteria.
DR HOGENOM; CLU_032616_0_0_4; -.
DR OMA; YAKRQYT; -.
DR OrthoDB; 1069591at2; -.
DR BioCyc; BCEN216591:G1G1V-3628-MON; -.
DR Proteomes; UP000001035; Chromosome 1.
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.
FT CHAIN 1..326
FT /note="tRNA dimethylallyltransferase"
FT /id="PRO_1000098649"
FT REGION 44..47
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT REGION 168..172
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT REGION 253..258
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT REGION 286..293
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 110
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT SITE 132
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ SEQUENCE 326 AA; 35699 MW; CC1944B7ACA4B01D CRC64;
MSAVPHATPS PTTIACLLGP TASGKTAAAL ALAARRPIEI VSVDSALVYR DMDIGTAKPS
RDERASVPHH LIDIIDPADA YSAASFRADT LRLIGEIAAR GRTPLLAGGT MLYYKALTQG
LNDLPGADPD VRATLDAEAE RDGWPALHAR LAQVDPDTAA RLAPNDSQRI QRALEVFMLS
GQPMSVLLAA PRRTDDAAAA YRFVPVALEP SDRAVLHKRI AQRFDAMLDA GFIDEVERLR
RREDLHPDLP SMRCVGYRQA WEFLDGDTDY RTMRDKGIFA TRQLCKRQIT WLRAMPERIV
VDCIAPDSTA RALDALERVL DGRTPG
