MIAA_TREPA
ID MIAA_TREPA Reviewed; 316 AA.
AC O83644;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=TP_0637;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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; AE000520; AAC65611.1; -; Genomic_DNA.
DR PIR; B71301; B71301.
DR RefSeq; WP_010882082.1; NC_021490.2.
DR AlphaFoldDB; O83644; -.
DR SMR; O83644; -.
DR IntAct; O83644; 4.
DR STRING; 243276.TPANIC_0637; -.
DR PRIDE; O83644; -.
DR EnsemblBacteria; AAC65611; AAC65611; TP_0637.
DR GeneID; 57879159; -.
DR KEGG; tpa:TP_0637; -.
DR eggNOG; COG0324; Bacteria.
DR HOGENOM; CLU_032616_0_1_12; -.
DR OMA; LEIAIHQ; -.
DR OrthoDB; 1069591at2; -.
DR Proteomes; UP000000811; 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; Reference proteome;
KW Transferase; tRNA processing.
FT CHAIN 1..316
FT /note="tRNA dimethylallyltransferase"
FT /id="PRO_0000164001"
FT REGION 52..55
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT BINDING 29..34
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
FT SITE 117
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00185"
SQ SEQUENCE 316 AA; 36174 MW; E4BE144EE6ED5208 CRC64;
MRLETQALVP YPVRFDRSHH DALVVLGATA TGKTALAVAL AQKYQGEIIS ADSRQVYRGL
DVGTGKDLAL YGSVPYHLID VCDPYEEYNV FRFQQAVYGI VPSILRAHKV PIIVGGTGLY
LDAVLRQYAL VPVERNQALR ASLRGASLSH MRAVYFSLKD SHAVHNKTDL EDPARLMRAI
EIAVFHATHP ELLQQARETR PMMRAKVYGI QYPRSMLRAR IRARLEQRIR GGLIEEVAAL
HKGGVSWQRL EYFGLEYRFT AQYLQGIIAT RDEYVDLLFR AISRFAKRQE TWFRRMQRLG
VKIHWLVHTE NGFVLR
