ID F6IPA9_9SPHN Unreviewed; 328 AA.
AC F6IPA9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=PP1Y_AT24692 {ECO:0000313|EMBL:CCA93261.1};
OS Novosphingobium sp. PP1Y.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=702113 {ECO:0000313|EMBL:CCA93261.1, ECO:0000313|Proteomes:UP000009242};
RN [1] {ECO:0000313|EMBL:CCA93261.1, ECO:0000313|Proteomes:UP000009242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=sp. PP1Y {ECO:0000313|Proteomes:UP000009242};
RX PubMed=21685292; DOI=10.1128/JB.05349-11;
RA D'Argenio V., Petrillo M., Cantiello P., Naso B., Cozzuto L., Notomista E.,
RA Paolella G., Di Donato A., Salvatore F.;
RT "De novo sequencing and assembly of the whole genome of Novosphingobium sp.
RT strain PP1Y.";
RL J. Bacteriol. 193:4296-4296(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|ARBA:ARBA00001946,
CC 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; FR856862; CCA93261.1; -; Genomic_DNA.
DR RefSeq; WP_013833546.1; NC_015580.1.
DR AlphaFoldDB; F6IPA9; -.
DR KEGG; npp:PP1Y_AT24692; -.
DR eggNOG; COG0324; Bacteria.
DR HOGENOM; CLU_032616_0_1_5; -.
DR OrthoDB; 9776390at2; -.
DR Proteomes; UP000009242; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000009242};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00185};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00185}.
FT REGION 56..59
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00185"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00185"
FT BINDING 28..33
FT /ligand="substrate"
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"
FT SITE 144
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00185"
SQ SEQUENCE 328 AA; 35770 MW; 0D6FE2FD58E7E5A3 CRC64;
MSTANILDAS LNIAAADRPP LALIAGPTAS GKSDCAVMLA RELERLGRRC VVVNADSSQV
YADLQVLSAR PTFEEMGGIE HRLFGDWDGS RSCSAADWAQ AARQTISAIH AEGALPILVG
GTGLYIKTLL EGIAPVPAID PAIRDSVRAL PVDEAFAALR QEDPERASRL APADTARIAR
ALEVVRSSGK TLAQWHAETS GGIANAVTVF PAILLPERQA LYRRCDLRFE RMIERGALAE
VETLLTRDLD PALPVMRAIG VPELAGVVRG DWPLVDAIAR GSQATRNYAK RQFTWLRHQP
PEDWPRLSFE NFDSNAIHEI LFRIFHLT
//