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Database: UniProt
Entry: F6IPA9_9SPHN
LinkDB: F6IPA9_9SPHN
Original site: F6IPA9_9SPHN 
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
//
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