ID   MIAA1_PARD8             Reviewed;         307 AA.
AC   A6L8Q7;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-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=BDI_0286;
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(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; CP000140; ABR42071.1; -; Genomic_DNA.
DR   RefSeq; WP_005861832.1; NC_009615.1.
DR   AlphaFoldDB; A6L8Q7; -.
DR   SMR; A6L8Q7; -.
DR   STRING; 435591.BDI_0286; -.
DR   EnsemblBacteria; ABR42071; ABR42071; BDI_0286.
DR   GeneID; 57237313; -.
DR   KEGG; pdi:BDI_0286; -.
DR   eggNOG; COG0324; Bacteria.
DR   HOGENOM; CLU_032616_0_1_10; -.
DR   OMA; LEIAIHQ; -.
DR   OrthoDB; 1069591at2; -.
DR   BioCyc; PDIS435591:G1G5A-293-MON; -.
DR   Proteomes; UP000000566; 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; 2.
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..307
FT                   /note="tRNA dimethylallyltransferase 1"
FT                   /id="PRO_0000377250"
FT   REGION          36..39
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   REGION          159..163
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            105
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ   SEQUENCE   307 AA;  35576 MW;  85E4FFDBD64D49C4 CRC64;
     MKSYELITIL GPTASGKTTF AAALAAQLDT EIISADSRQI YRSMDIGTGK DLADYNVNGK
     QIPYHLIDIC EPGYKYNVFE YQHDFFRVYE DMKRRGKLPI LCGGTGMYIE AVLKGYKLLD
     VPQNPELRES LRNKTLEELE TILASYKILH NKTDVDTAQR AIRAIEIEEY YKTQAPDVNE
     YNPINSLIIG IHIDRELRRE KISRRLRTRL DEGMVDEVRT ILATGVKPED LIYYGLEYKF
     LTLYIIGELS FEEMVSQLEI AIHQFAKRQM TWFRGMERRG CEIHWIDATL PTEEKIATTM
     RILNNQL