MIAA_BURCC
ID MIAA_BURCC Reviewed; 324 AA.
AC B1JW31;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Bcenmc03_0733;
OS Burkholderia cenocepacia (strain MC0-3).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=406425;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC0-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3.";
RL Submitted (FEB-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; CP000958; ACA89911.1; -; Genomic_DNA.
DR RefSeq; WP_006476825.1; NC_010508.1.
DR AlphaFoldDB; B1JW31; -.
DR SMR; B1JW31; -.
DR EnsemblBacteria; ACA89911; ACA89911; Bcenmc03_0733.
DR KEGG; bcm:Bcenmc03_0733; -.
DR HOGENOM; CLU_032616_0_0_4; -.
DR OMA; YAKRQYT; -.
DR Proteomes; UP000002169; 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; 1.
DR TIGRFAMs; TIGR00174; miaA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Magnesium; Nucleotide-binding; Transferase; tRNA processing.
FT CHAIN 1..324
FT /note="tRNA dimethylallyltransferase"
FT /id="PRO_1000098648"
FT REGION 42..45
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT REGION 166..170
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT REGION 251..256
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT REGION 284..291
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT BINDING 17..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT BINDING 19..24
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT SITE 108
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT SITE 130
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ SEQUENCE 324 AA; 35509 MW; 3CAD563E24CFCBFD CRC64;
MSASSQSRPT TIACLLGPTA SGKTAAALAL AARRPIEIVS VDSALVYRDM DIGTAKPSRD
ERASVPHHLI DIIDPADAYS AAEFRADTLR LIGEIVARGR TPLLAGGTML YYKALTQGLN
DLPGADPEVR AALDADAARD GWPALHARLA QVDPDTAARL APNDSQRIQR ALEIFMLSGQ
PMSALLAAPR RTDDAAAAYR FVPVALEPSD RAVLHARIAQ RFDAMLDAGF IDEVERLRRR
DDLHPDLPSM RCVGYRQAWE FLDGDTDYRT MRDKGIFATR QLCKRQITWL RAMPERIVVD
CIAPDSTARA LDALERVLDG RTPD
