ID   MIAA2_SYNAS             Reviewed;         311 AA.
AC   Q2LUR0;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
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};
GN   OrderedLocusNames=SYNAS_19450; ORFNames=SYN_02888;
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC   Syntrophus.
OX   NCBI_TaxID=56780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB;
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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; CP000252; ABC77824.1; -; Genomic_DNA.
DR   RefSeq; WP_011417845.1; NC_007759.1.
DR   AlphaFoldDB; Q2LUR0; -.
DR   SMR; Q2LUR0; -.
DR   STRING; 56780.SYN_02888; -.
DR   EnsemblBacteria; ABC77824; ABC77824; SYN_02888.
DR   KEGG; sat:SYN_02888; -.
DR   eggNOG; COG0324; Bacteria.
DR   HOGENOM; CLU_032616_0_1_7; -.
DR   OMA; YAKRQYT; -.
DR   OrthoDB; 1069591at2; -.
DR   Proteomes; UP000001933; 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; Reference proteome;
KW   Transferase; tRNA processing.
FT   CHAIN           1..311
FT                   /note="tRNA dimethylallyltransferase 2"
FT                   /id="PRO_0000377352"
FT   REGION          40..43
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   BINDING         15..22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   BINDING         17..22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   SITE            106
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   SITE            128
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ   SEQUENCE   311 AA;  35314 MW;  A3180B9C0000EE6B CRC64;
     MTGSIEKPRL IVVMGPTAVG KTAAAIRLAK QWGGEIISAD SMQVYRHMDI GTAKPTPDQQ
     CRVPHHLIDI VNPDESFNAA CFMERARAVI AELHKRGKKI IVVGGTGLYI RAVLGGLFDG
     PAADEALRRH YFTILEREGK AGLYGMLKAR DRRAAAIIHP NDTTRMIRAL EVLDLTGVSI
     VEQQQEHRFA QRPYRVLKIG LRCSRSVLYE RIEARTEEML AQGFLDEVRQ LLDMGFHEGL
     RPMQALGYRQ MVGFLKGELD LDEAVDQLKR ETRRYAKRQL TWFGADPEIR WFEPGNEEEI
     LRYAGRFLRG E