ID   G0M011_LACPE            Unreviewed;       311 AA.
AC   G0M011;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   13-SEP-2023, entry version 44.
DE   RecName: Full=tRNA dimethylallyltransferase {ECO:0000256|HAMAP-Rule:MF_00185};
DE            EC=2.5.1.75 {ECO:0000256|HAMAP-Rule:MF_00185};
DE   AltName: Full=Dimethylallyl diphosphate:tRNA dimethylallyltransferase {ECO:0000256|HAMAP-Rule:MF_00185};
DE            Short=DMAPP:tRNA dimethylallyltransferase {ECO:0000256|HAMAP-Rule:MF_00185};
DE            Short=DMATase {ECO:0000256|HAMAP-Rule:MF_00185};
DE   AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase {ECO:0000256|HAMAP-Rule:MF_00185};
DE            Short=IPP transferase {ECO:0000256|HAMAP-Rule:MF_00185};
DE            Short=IPPT {ECO:0000256|HAMAP-Rule:MF_00185};
DE            Short=IPTase {ECO:0000256|HAMAP-Rule:MF_00185};
GN   Name=miaA {ECO:0000256|HAMAP-Rule:MF_00185};
GN   ORFNames=LPENT_00400 {ECO:0000313|EMBL:CCC15704.1};
OS   Lactiplantibacillus pentosus IG1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1042160 {ECO:0000313|EMBL:CCC15704.1};
RN   [1] {ECO:0000313|EMBL:CCC15704.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IG1 {ECO:0000313|EMBL:CCC15704.1};
RA   Maldonado-Barragan A., Caballero-Guerrero B., Lucena-Padros H.,
RA   Ruiz-Barba J.L.;
RT   "Genome Sequence of Lactobacillus pentosus IG1, a Strain Isolated from
RT   Spanish-Style Green Olive Fermentations.";
RL   J. Bacteriol. 193:5605-5605(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:0000256|ARBA:ARBA00003213, ECO:0000256|HAMAP-
CC       Rule:MF_00185, ECO:0000256|RuleBase:RU003784}.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001549, ECO:0000256|HAMAP-
CC         Rule:MF_00185, ECO:0000256|RuleBase:RU003783};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00185};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00185}.
CC   -!- SIMILARITY: Belongs to the IPP transferase family.
CC       {ECO:0000256|ARBA:ARBA00005842, ECO:0000256|HAMAP-Rule:MF_00185,
CC       ECO:0000256|RuleBase:RU003785}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00185}.
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DR   EMBL; FR874854; CCC15704.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0M011; -.
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; 1.10.20.140; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00185; IPP_trans; 1.
DR   InterPro; IPR039657; Dimethylallyltransferase.
DR   InterPro; IPR018022; IPT.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00174; miaA; 1.
DR   PANTHER; PTHR11088; TRNA DIMETHYLALLYLTRANSFERASE; 1.
DR   PANTHER; PTHR11088:SF60; TRNA DIMETHYLALLYLTRANSFERASE 9; 1.
DR   Pfam; PF01715; IPPT; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00185,
KW   ECO:0000256|RuleBase:RU003785};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00185};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00185,
KW   ECO:0000256|RuleBase:RU003785};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00185};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00185,
KW   ECO:0000256|RuleBase:RU003783}.
FT   REGION          39..42
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00185"
FT   BINDING         14..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00185"
FT   BINDING         16..21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00185"
FT   SITE            105
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00185"
FT   SITE            130
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00185"
SQ   SEQUENCE   311 AA;  34492 MW;  160BC0F2955D0C99 CRC64;
     MATIPKHKVL LIAGPTAVGK TALSLALAKQ LNGEIISGDS MQVYRHLDIG TAKIMPDERA
     GIPHYLIDIK TVDQRFTVAE FVSRATALIN DITARGKLPI IVGGTGFYLQ SLLAGYQFGP
     NDNAPDMAYR QQWFDRAANA GNQAVWDALN QRDPQAAAAI APANLVRVVR ALEYLHTTGQ
     LFSAQADTAT ETLDAYTLCL TAERSLLYDR INQRVDLMLN VGLEAEARWL YDQGGADLPA
     GKGIGYHEWF PYFAGTQSRD ATIAAIKQDS RRYAKRQLTW FRNKMTVDWV DLLEHPELRA
     SIDQRLASWL S
//