MIAA_BORPE
ID MIAA_BORPE Reviewed; 313 AA.
AC Q7U366;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=BP0243;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX640411; CAE40623.1; -; Genomic_DNA.
DR RefSeq; NP_879128.1; NC_002929.2.
DR RefSeq; WP_003814337.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7U366; -.
DR SMR; Q7U366; -.
DR STRING; 257313.BP0243; -.
DR GeneID; 56477441; -.
DR GeneID; 66437380; -.
DR KEGG; bpe:BP0243; -.
DR PATRIC; fig|257313.5.peg.264; -.
DR eggNOG; COG0324; Bacteria.
DR HOGENOM; CLU_032616_0_0_4; -.
DR OMA; YAKRQYT; -.
DR Proteomes; UP000002676; 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..313
FT /note="tRNA dimethylallyltransferase"
FT /id="PRO_0000163886"
FT REGION 36..39
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT REGION 160..164
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT REGION 244..249
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT BINDING 13..18
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT SITE 102
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT SITE 124
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ SEQUENCE 313 AA; 34049 MW; 42BC4A6183DDE13B CRC64;
MTPRAIICLA GPTAAGKSAS TLALAQRWPL EIINVDSATI YRGMDIGTAK PSAAERAQVP
QHLLDIRDPA QSYSAAEFRA DALRLIAEIH ARGRIPLLAG GTMLYYKALR EGLDDLPQAD
PALRAELEAR AARLGWPALH AELALLDPAT AARLSPNDSQ RIQRALEICR LAGQPMSALL
QGERRGDAPS PYRYVTLSLE PSERAALHAR IAQRFDAMLA AGLVEEVRGL HARPDLHPGL
PSVRCVGYRQ MWSYLDGDID LDTAREQGVA ATRQLAKRQL TWLRAQPERV IIDCLAGDAV
ARTVDAMARA LPD
