ID   MIAA1_AZOPC             Reviewed;         306 AA.
AC   B6YQT8;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=CFPG_297;
OS   Azobacteroides pseudotrichonymphae genomovar. CFP2.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Candidatus Azobacteroides.
OX   NCBI_TaxID=511995;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19008447; DOI=10.1126/science.1165578;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT
RT   protist cells in termite gut.";
RL   Science 322:1108-1109(2008).
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; AP010656; BAG83560.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6YQT8; -.
DR   SMR; B6YQT8; -.
DR   STRING; 511995.CFPG_297; -.
DR   EnsemblBacteria; BAG83560; BAG83560; CFPG_297.
DR   KEGG; aps:CFPG_297; -.
DR   eggNOG; COG0324; Bacteria.
DR   HOGENOM; CLU_032616_0_1_10; -.
DR   OMA; LEIAIHQ; -.
DR   Proteomes; UP000000723; 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; -; 2.
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..306
FT                   /note="tRNA dimethylallyltransferase 1"
FT                   /id="PRO_0000377072"
FT   REGION          38..41
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   BINDING         13..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   BINDING         15..20
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   SITE            107
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ   SEQUENCE   306 AA;  35962 MW;  B4CD58A4847DF783 CRC64;
     MELQEYELIT VLGPTASGKT AFATRLANEL NSEIISADSR QVYRNMTIGT GKDLDNYIIE
     GKFIPYHLID ICQAGEKYNV FRFQHDFHEI FTKIKKKGKL PILCGGTGLY IESVLKGYKL
     LDVPENLILR SNLKDKSVDE LKKILKSYKN LHNQTDTDSV RKIIRAIEIE TCYPTQKNNP
     INSYSSIKSL IIGVNIDREL RRNRISLRLK KRLEEGMIEE VKNLLETELS PDQLIYYGLE
     YKYITLYLIG QLSYSEMYQQ LEIAIHQYAK RQMTWFRGME RRGFKIHWID VYEMNHLNEI
     FNRIHF