ID   MIAA2_PORG3             Reviewed;         300 AA.
AC   B2RLA0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=tRNA dimethylallyltransferase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=DMAPP:tRNA dimethylallyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=DMATase 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE   AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=IPP transferase 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=IPPT 2 {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=IPTase 2 {ECO:0000255|HAMAP-Rule:MF_00185};
GN   Name=miaA2 {ECO:0000255|HAMAP-Rule:MF_00185}; OrderedLocusNames=PGN_1626;
OS   Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS   12257 / NCTC 11834 / 2561).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=431947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX   PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA   Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA   Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA   Nakayama K.;
RT   "Determination of the genome sequence of Porphyromonas gingivalis strain
RT   ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT   rearrangements in P. gingivalis.";
RL   DNA Res. 15:215-225(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; AP009380; BAG34145.1; -; Genomic_DNA.
DR   RefSeq; WP_012458417.1; NZ_CP025930.1.
DR   AlphaFoldDB; B2RLA0; -.
DR   SMR; B2RLA0; -.
DR   STRING; 431947.PGN_1626; -.
DR   EnsemblBacteria; BAG34145; BAG34145; PGN_1626.
DR   GeneID; 29256794; -.
DR   KEGG; pgn:PGN_1626; -.
DR   eggNOG; COG0324; Bacteria.
DR   HOGENOM; CLU_032616_0_1_10; -.
DR   OMA; YAKRQYT; -.
DR   BioCyc; PGIN431947:G1G2V-1828-MON; -.
DR   Proteomes; UP000008842; 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; -; 1.
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; 2.
DR   TIGRFAMs; TIGR00174; miaA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Magnesium; Nucleotide-binding; Transferase; tRNA processing.
FT   CHAIN           1..300
FT                   /note="tRNA dimethylallyltransferase 2"
FT                   /id="PRO_1000098676"
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            104
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   SITE            126
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ   SEQUENCE   300 AA;  34722 MW;  FD3EE1DA7B315D4A CRC64;
     METQDHTLYV LLGPTGVGKT DLSLDIAERL GSPIISADSR QIFRELPIGT AAPTPEQRAR
     VPHLFVGTHS VRDYYSAGMY EVEVLEALKE LFRKYRGVLL TGGSMMYIDA VCRGIDDIPD
     PFPEVREELY ARYAAEGLDG ILAQLRLLDP DYYAKVDRRN YKRVIHGLEI CLSTGRPFSS
     FHRHEAKERP FRIVKIGLYR EREELCKRID ARVLEMMEQG LEEEARAVYP LRHLNALNTV
     GYKEMFEYFD GSIDRAEAVR RIQRNSRVYA RKQMTWFRRD STIRWFHPEA DKGTVLTLVT