MIAA_BORBZ
ID MIAA_BORBZ Reviewed; 306 AA.
AC B7J0R6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=BbuZS7_0851;
OS Borreliella burgdorferi (strain ZS7) (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=445985;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS7;
RX PubMed=20935092; DOI=10.1128/jb.01158-10;
RA Schutzer S.E., Fraser-Liggett C.M., Casjens S.R., Qiu W.G., Dunn J.J.,
RA Mongodin E.F., Luft B.J.;
RT "Whole-genome sequences of thirteen isolates of Borrelia burgdorferi.";
RL J. Bacteriol. 193:1018-1020(2011).
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; CP001205; ACK75052.1; -; Genomic_DNA.
DR RefSeq; WP_002657257.1; NC_011728.1.
DR AlphaFoldDB; B7J0R6; -.
DR SMR; B7J0R6; -.
DR EnsemblBacteria; ACK75052; ACK75052; BbuZS7_0851.
DR GeneID; 56567399; -.
DR KEGG; bbz:BbuZS7_0851; -.
DR HOGENOM; CLU_032616_0_2_12; -.
DR OMA; YAKRQYT; -.
DR OrthoDB; 1069591at2; -.
DR Proteomes; UP000006901; 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; Transferase; tRNA processing.
FT CHAIN 1..306
FT /note="tRNA dimethylallyltransferase"
FT /id="PRO_1000118520"
FT REGION 35..38
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 101
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT SITE 123
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ SEQUENCE 306 AA; 35658 MW; 2D2E54B842323C93 CRC64;
MKEDRVVFIF GPTAVGKSNI LFHFPKNKAE IINVDSIQVY KEFNIASSKP SKNLMKHIKH
HLVDFLDPEK DYTIGIFYEQ ALKIVKEIRQ KKKIPIFVGG TAFYFKHLKD GFPSTPLVTS
KIRIYVNNLL ELKGKSYLLK ELKNVDPIRF NMLNKNDIYR IKRSLEVYYQ TGIPISQFQK
KQNSEFKNIV IIGLKRSFED LKTRISIRIN EMLNSGLLSE IKGLFSKGYN ENTPAFKGIG
YNEFLLWKSR PCYGLNDIIG LINKNSFLYA KRQMTFFAKI SDVLWLHPED DLDNILNLIF
KVDKEI