ID A0A1E3SZ16_MYCSH Unreviewed; 303 AA.
AC A0A1E3SZ16;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=MSP7336_04036 {ECO:0000313|EMBL:SRX95763.1};
OS Mycobacterium shimoidei.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=29313 {ECO:0000313|EMBL:SRX95763.1, ECO:0000313|Proteomes:UP000252015};
RN [1] {ECO:0000313|EMBL:SRX95763.1, ECO:0000313|Proteomes:UP000252015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P7336 {ECO:0000313|EMBL:SRX95763.1,
RC ECO:0000313|Proteomes:UP000252015};
RG IHU Genomes;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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; UEGW01000001; SRX95763.1; -; Genomic_DNA.
DR RefSeq; WP_069398076.1; NZ_UEGW01000001.1.
DR AlphaFoldDB; A0A1E3SZ16; -.
DR STRING; 29313.BHQ16_21280; -.
DR OrthoDB; 9776390at2; -.
DR Proteomes; UP000252015; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR011704; ATPase_dyneun-rel_AAA.
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:SF95; TRNA DIMETHYLALLYLTRANSFERASE; 1.
DR Pfam; PF07728; AAA_5; 1.
DR Pfam; PF01715; IPPT; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00185}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00185};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00185};
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 DOMAIN 4..35
FT /note="ATPase dynein-related AAA"
FT /evidence="ECO:0000259|Pfam:PF07728"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00185"
FT BINDING 10..15
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00185"
FT SITE 101
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00185"
FT SITE 122
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00185"
SQ SEQUENCE 303 AA; 32796 MW; 87A4292EAF1A4AE5 CRC64;
MRPLAIVGPT GTGKSQLALE IAERLGRNVE IVNADAMQLY RGMDIGTAKL PVAQRRGIPH
HQLDVLDVTE TASVARYQQA AAADIEAIMT RGAVPIVVGG SMLYIQSLLD DWSFPATDPA
VRAKWERRLA VEGAAALHAE LARQDPAAAA SILASDGRRI VRALEVVELT GQPFAASAPS
IGAPRWDTVI IGLDCATELL DDRLARRTDT MFDSGLVQEV ITLLGQGLRD GVTASRALGY
AQVIADLDAG GTGEGAREPT FTGTRRYVRR QRSWFRRDHR IQWFDATAAG LAQDVVRAWR
HVS
//
