ID   MIAA_PSYCK              Reviewed;         414 AA.
AC   Q1QAN0;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=tRNA dimethylallyltransferase {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 {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=DMAPP:tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=DMATase {ECO:0000255|HAMAP-Rule:MF_00185};
DE   AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=IPP transferase {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=IPPT {ECO:0000255|HAMAP-Rule:MF_00185};
DE            Short=IPTase {ECO:0000255|HAMAP-Rule:MF_00185};
GN   Name=miaA {ECO:0000255|HAMAP-Rule:MF_00185}; OrderedLocusNames=Pcryo_1494;
OS   Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS   / K5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=335284;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL   Submitted (MAR-2006) 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: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; CP000323; ABE75273.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1QAN0; -.
DR   SMR; Q1QAN0; -.
DR   STRING; 335284.Pcryo_1494; -.
DR   KEGG; pcr:Pcryo_1494; -.
DR   eggNOG; COG0324; Bacteria.
DR   HOGENOM; CLU_032616_1_0_6; -.
DR   OMA; HHLVDII; -.
DR   Proteomes; UP000002425; 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; 1.
DR   TIGRFAMs; TIGR00174; miaA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Magnesium; Nucleotide-binding; Transferase; tRNA processing.
FT   CHAIN           1..414
FT                   /note="tRNA dimethylallyltransferase"
FT                   /id="PRO_0000377274"
FT   REGION          58..61
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   REGION          182..186
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   REGION          266..271
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   BINDING         35..40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   SITE            124
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT   SITE            146
FT                   /note="Interaction with substrate tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ   SEQUENCE   414 AA;  46624 MW;  5FFC7A95348F525A CRC64;
     MTIKGKYMRL SSDSLSSYLS PNLADNSVVC LMAPTASGKT ALAYELYNSG RYELISVDSA
     LVYRDMTVGT AKPNAAELAR YPHHLVDIID PMQSYSVAEF VNDVARLIDS CHQNGKIPLL
     VGGTMMYYMA LLDGLSPVPD SDDSVRARVE QWRQDEGISA LYDYLGKVDA ISHERLNATD
     TQRITRAVEV YLQTDIPISD WQRQPKQALA YNPNQQWHAL AVMPDRPWLH TRIEQRLDIM
     WREGLVAEVI SLLEHYPLTP GLPSMRCVGY RQVLEYLVQT NHPVFEQPHL DKAQFYDAFA
     QSEPSSNESK EQDTTIQSSI TQTHLPMATA QTEALACQQM QNKALYATRQ LAKRQYTWLR
     KVMQLSNTAA VPTTESITAS STSTVGSDDV TDFQKNKLIL HSFSTMEQAR AYLV