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Database: UniProt
Entry: A5IJD4
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ID   MIAB_THEP1              Reviewed;         443 AA.
AC   A5IJD4;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   01-OCT-2014, entry version 55.
DE   RecName: Full=tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase {ECO:0000255|HAMAP-Rule:MF_01864};
DE            EC=2.8.4.3 {ECO:0000255|HAMAP-Rule:MF_01864};
DE   AltName: Full=(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB {ECO:0000255|HAMAP-Rule:MF_01864};
DE   AltName: Full=tRNA-i(6)A37 methylthiotransferase {ECO:0000255|HAMAP-Rule:MF_01864};
GN   Name=miaB {ECO:0000255|HAMAP-Rule:MF_01864};
GN   OrderedLocusNames=Tpet_0278;
OS   Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=390874;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKU-1 / ATCC BAA-488 / DSM 13995;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P.,
RA   Noll K., Richardson P.;
RT   "Complete sequence of Thermotoga petrophila RKU-1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the methylthiolation of N6-
CC       (dimethylallyl)adenosine (i(6)A), leading to the formation of 2-
CC       methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37
CC       in tRNAs that read codons beginning with uridine.
CC       {ECO:0000255|HAMAP-Rule:MF_01864}.
CC   -!- CATALYTIC ACTIVITY: N(6)-dimethylallyladenine(37) in tRNA +
CC       sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = 2-
CC       methylthio-N(6)-dimethylallyladenine(37) in tRNA + S-adenosyl-L-
CC       homocysteine + (sulfur carrier) + L-methionine + 5'-
CC       deoxyadenosine. {ECO:0000255|HAMAP-Rule:MF_01864}.
CC   -!- COFACTOR: Binds 2 4Fe-4S clusters. One cluster is coordinated with
CC       3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000255|HAMAP-Rule:MF_01864}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01864}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01864}.
CC   -!- SIMILARITY: Belongs to the methylthiotransferase family. MiaB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01864}.
CC   -!- SIMILARITY: Contains 1 MTTase N-terminal domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01864}.
CC   -!- SIMILARITY: Contains 1 TRAM domain. {ECO:0000255|HAMAP-
CC       Rule:MF_01864}.
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DR   EMBL; CP000702; ABQ46307.1; -; Genomic_DNA.
DR   RefSeq; YP_001243883.1; NC_009486.1.
DR   ProteinModelPortal; A5IJD4; -.
DR   STRING; 390874.Tpet_0278; -.
DR   EnsemblBacteria; ABQ46307; ABQ46307; Tpet_0278.
DR   GeneID; 5171186; -.
DR   KEGG; tpt:Tpet_0278; -.
DR   PATRIC; 23943281; VBIThePet65348_0278.
DR   eggNOG; COG0621; -.
DR   HOGENOM; HOG000224767; -.
DR   KO; K06168; -.
DR   OMA; IEVYKDT; -.
DR   OrthoDB; EOG6P5ZD8; -.
DR   BioCyc; TPET390874:GHJI-283-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.80.30.20; -; 1.
DR   HAMAP; MF_01864; tRNA_metthiotr_MiaB; 1.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR023970; MeThioTfrase/rSAM.
DR   InterPro; IPR005839; Methylthiotransferase.
DR   InterPro; IPR020612; Methylthiotransferase_CS.
DR   InterPro; IPR013848; Methylthiotransferase_N.
DR   InterPro; IPR006463; MiaB_methiolase.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   InterPro; IPR002792; TRAM_dom.
DR   PANTHER; PTHR11918; PTHR11918; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF01938; TRAM; 1.
DR   Pfam; PF00919; UPF0004; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00089; TIGR00089; 1.
DR   PROSITE; PS51449; MTTASE_N; 1.
DR   PROSITE; PS01278; MTTASE_RADICAL; 1.
DR   PROSITE; PS50926; TRAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
KW   Metal-binding; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN         1    443       tRNA-2-methylthio-N(6)-
FT                                dimethylallyladenosine synthase.
FT                                /FTId=PRO_0000374615.
FT   DOMAIN        1    114       MTTase N-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01864}.
FT   DOMAIN      370    431       TRAM. {ECO:0000255|HAMAP-Rule:MF_01864}.
FT   METAL        10     10       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL        46     46       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL        79     79       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL       150    150       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01864}.
FT   METAL       154    154       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01864}.
FT   METAL       157    157       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01864}.
SQ   SEQUENCE   443 AA;  50928 MW;  141AE95E9233ACCE CRC64;
     MRFYIKTFGC QMNENDSETM AGLLMKEGFT PASAPEEADV VIINTCAVRR KSEEKAYSEL
     GQMLKIKRKR KLVVGVAGCV AEKEREKLLE RGADFVLGTR AVLKVTEAVK RALQGEKVAL
     FEDHLDEYTH ELPRIRSSKH HAWVTIIFGC DRFCTYCIVP YTRGREKSRP MEDILEEVRE
     LAKQGYREVT FLGQNVDAYG KDLKDGSSLA KLLEEASKIE GIERIWFLTS YPTDFSDELI
     EVIARNPKVA KSVHLPVQSG SNRILKLMNR SYTKEEYLAL LERIRSKVPD VAISSDIIVG
     FPTETEEDFM ETIDLVEKAQ FERLNLAIYS PRKGTVAWKH YKDEVPYEEK VRRMQFLMNL
     QKRINRKLNE RYKGKTVRVI VEAQAKNGLF YGRDIRNKII AFEGEEWMIG RFADVKIEKI
     TAGPLYGKVV WIEETPSPVS TDK
//
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