MIAA1_MYCUA
ID MIAA1_MYCUA Reviewed; 314 AA.
AC A0PT81;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=tRNA dimethylallyltransferase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00185};
DE Short=DMAPP:tRNA dimethylallyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00185};
DE Short=DMATase 1 {ECO:0000255|HAMAP-Rule:MF_00185};
DE AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00185};
DE Short=IPP transferase 1 {ECO:0000255|HAMAP-Rule:MF_00185};
DE Short=IPPT 1 {ECO:0000255|HAMAP-Rule:MF_00185};
DE Short=IPTase 1 {ECO:0000255|HAMAP-Rule:MF_00185};
GN Name=miaA1 {ECO:0000255|HAMAP-Rule:MF_00185}; OrderedLocusNames=MUL_3370;
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=362242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99;
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
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; CP000325; ABL05550.1; -; Genomic_DNA.
DR RefSeq; WP_011741158.1; NC_008611.1.
DR AlphaFoldDB; A0PT81; -.
DR SMR; A0PT81; -.
DR STRING; 362242.MUL_3370; -.
DR EnsemblBacteria; ABL05550; ABL05550; MUL_3370.
DR KEGG; mul:MUL_3370; -.
DR eggNOG; COG0324; Bacteria.
DR HOGENOM; CLU_032616_0_1_11; -.
DR OMA; YAKRQYT; -.
DR Proteomes; UP000000765; 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..314
FT /note="tRNA dimethylallyltransferase 1"
FT /id="PRO_0000377232"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT BINDING 10..15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT SITE 103
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 314 AA; 33967 MW; 713B3568F4A3DFC8 CRC64;
MRPLAIIGPT GSGKSQLALD VAERLAGEVP AEIVNADAMQ LYRGMDIGTA KLSVAARRGI
PHHQLDVLNV AETATVARYQ QAAAADIEAI IARGHVPIVV GGSMLHVQSL LDNWSFPATD
PAVRARWEEC LAELGVGELH AELARRDPAA AATILPTDGR RIVRALEVIE LTGQPFAASA
PRIGAAQWGT AIIGLDCDTP ILDDRLAVRT DSMFERGLVE EVRVLLRAGL RDGVTAARAL
GYAQVLAALD AGGGAELLDD AREQTYFGTR RYVRRQRSWF RRDHRVHWCD AGATGPSDRV
AMVDEALRVW RHVT