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-MAY-2013, entry version 48.
DE RecName: Full=(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB;
DE EC=2.-.-.-;
DE AltName: Full=tRNA-i(6)A37 methylthiotransferase;
GN Name=miaB; 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 (By similarity).
CC -!- COFACTOR: Binds 2 4Fe-4S clusters. One cluster is coordinated with
CC 3 cysteines and an exchangeable S-adenosyl-L-methionine (By
CC similarity).
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- SIMILARITY: Belongs to the methylthiotransferase family. MiaB
CC subfamily.
CC -!- SIMILARITY: Contains 1 MTTase N-terminal domain.
CC -!- SIMILARITY: Contains 1 TRAM domain.
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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; GIDRIRY; -.
DR ProtClustDB; PRK14330; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:HAMAP.
DR GO; GO:0005506; F:iron ion binding; IEA:HAMAP.
DR GO; GO:0016740; F:transferase activity; IEA:HAMAP.
DR GO; GO:0006400; P:tRNA modification; IEA: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; TIGR01574; miaB-methiolase; 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 (Dimethylallyl)adenosine tRNA
FT methylthiotransferase MiaB.
FT /FTId=PRO_0000374615.
FT DOMAIN 1 114 MTTase N-terminal.
FT DOMAIN 370 431 TRAM.
FT METAL 10 10 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 46 46 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 79 79 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 150 150 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 154 154 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 157 157 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
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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