MIAA_SALTY
ID MIAA_SALTY Reviewed; 316 AA.
AC P37724;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=tRNA dimethylallyltransferase {ECO:0000255|HAMAP-Rule:MF_00185};
DE EC=2.5.1.75 {ECO:0000255|HAMAP-Rule:MF_00185, ECO:0000269|PubMed:25453905};
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, ECO:0000303|PubMed:25453905};
GN OrderedLocusNames=STM4360;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95.
RX PubMed=2676972; DOI=10.1128/jb.171.10.5325-5331.1989;
RA Mankovich J.A., McIntyre C.A., Walker G.C.;
RT "Nucleotide sequence of the Salmonella typhimurium mutL gene required for
RT mismatch repair: homology of MutL to HexB of Streptococcus pneumoniae and
RT to PMS1 of the yeast Saccharomyces cerevisiae.";
RL J. Bacteriol. 171:5325-5331(1989).
RN [3]
RP IDENTIFICATION.
RX PubMed=7920643; DOI=10.1038/ng0694-205;
RA Robison K., Gilbert W., Church G.M.;
RT "Large scale bacterial gene discovery by similarity search.";
RL Nat. Genet. 7:205-214(1994).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=25453905; DOI=10.1021/bi5012207;
RA Subedi B.P., Corder A.L., Zhang S., Foss F.W. Jr., Pierce B.S.;
RT "Steady-state kinetics and spectroscopic characterization of enzyme-tRNA
RT interactions for the non-heme diiron tRNA-monooxygenase, MiaE.";
RL Biochemistry 54:363-376(2015).
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 ECO:0000269|PubMed:25453905}.
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, ECO:0000269|PubMed:25453905};
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; AE006468; AAL23180.1; -; Genomic_DNA.
DR EMBL; M29687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_463221.1; NC_003197.2.
DR RefSeq; WP_001000734.1; NC_003197.2.
DR AlphaFoldDB; P37724; -.
DR SMR; P37724; -.
DR STRING; 99287.STM4360; -.
DR PaxDb; P37724; -.
DR EnsemblBacteria; AAL23180; AAL23180; STM4360.
DR GeneID; 1255886; -.
DR KEGG; stm:STM4360; -.
DR PATRIC; fig|99287.12.peg.4584; -.
DR HOGENOM; CLU_032616_0_0_6; -.
DR OMA; YAKRQYT; -.
DR PhylomeDB; P37724; -.
DR BioCyc; SENT99287:STM4360-MON; -.
DR BRENDA; 2.5.1.75; 2169.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IBA:GO_Central.
DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Magnesium; Nucleotide-binding; Reference proteome;
KW Transferase; tRNA processing.
FT CHAIN 1..316
FT /note="tRNA dimethylallyltransferase"
FT /id="PRO_0000163969"
FT REGION 42..45
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT REGION 166..170
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT REGION 247..252
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT BINDING 17..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT BINDING 19..24
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT SITE 108
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT SITE 130
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ SEQUENCE 316 AA; 35170 MW; DADE1981E30E8CBA CRC64;
MNDVSKASLP KAIFLMGPTA SGKTALAIEL RKVLPVELIS VDSALIYRGM DIGTAKPNAD
ELKAAPHRLL DIRDPSQAYS AADFRRDALA QMAEITAAGR IPLLVGGTML YFKALLEGLS
PLPSADPEVR SRIEQQAAEL GWEALHQQLQ EIDPVAAARI HPNDPQRLSR ALEVFFISGK
TLTELTQTSG DALPYQVHQF AIAPASRELL HQRIELRFHQ MLASGFEAEV RALFARGDLH
TDLPSIRCVG YRQMWSYIEG EISYDEMVYR GVCATRQLAK RQMTWLRGWE GVRWLDSENP
DRARKEVLQV VGAIAD
