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Database: UniProt
Entry: A5EXA7
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ID   MIAB_DICNV              Reviewed;         456 AA.
AC   A5EXA7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   01-OCT-2014, entry version 54.
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=DNO_1245;
OS   Dichelobacter nodosus (strain VCS1703A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cardiobacteriales;
OC   Cardiobacteriaceae; Dichelobacter.
OX   NCBI_TaxID=246195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VCS1703A;
RX   PubMed=17468768; DOI=10.1038/nbt1302;
RA   Myers G.S.A., Parker D., Al-Hasani K., Kennan R.M., Seemann T.,
RA   Ren Q., Badger J.H., Selengut J.D., Deboy R.T., Tettelin H.,
RA   Boyce J.D., McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y.,
RA   Holley T., Fedorova N., Khouri H., Bottomley S.P., Whittington R.J.,
RA   Adler B., Songer J.G., Rood J.I., Paulsen I.T.;
RT   "Genome sequence and identification of candidate vaccine antigens from
RT   the animal pathogen Dichelobacter nodosus.";
RL   Nat. Biotechnol. 25:569-575(2007).
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; CP000513; ABQ14300.1; -; Genomic_DNA.
DR   RefSeq; YP_001210121.1; NC_009446.1.
DR   ProteinModelPortal; A5EXA7; -.
DR   STRING; 246195.DNO_1245; -.
DR   EnsemblBacteria; ABQ14300; ABQ14300; DNO_1245.
DR   GeneID; 5122130; -.
DR   KEGG; dno:DNO_1245; -.
DR   PATRIC; 21786844; VBIDicNod48475_1238.
DR   eggNOG; COG0621; -.
DR   HOGENOM; HOG000224767; -.
DR   KO; K06168; -.
DR   OMA; IEVYKDT; -.
DR   OrthoDB; EOG6P5ZD8; -.
DR   BioCyc; DNOD246195:GHHS-1242-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; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN         1    456       tRNA-2-methylthio-N(6)-
FT                                dimethylallyladenosine synthase.
FT                                /FTId=PRO_0000374269.
FT   DOMAIN        6    123       MTTase N-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01864}.
FT   DOMAIN      381    444       TRAM. {ECO:0000255|HAMAP-Rule:MF_01864}.
FT   METAL        15     15       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL        52     52       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL        86     86       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL       160    160       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01864}.
FT   METAL       164    164       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01864}.
FT   METAL       167    167       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01864}.
SQ   SEQUENCE   456 AA;  51013 MW;  B20D924B8494970D CRC64;
     MQTVLKHVYI ETYGCQMNEY DSSKMLAVLK NSHGITPVAT PEEADVLLLN TCSVREKAQE
     KVFSQLGRWK SLKERKPHLI IGVGGCVASQ EGEMIRRRAP EVDVVFGPQT LHRLPNLIEE
     AQRSRGGVVD VSFPEIEKFD HLPEPRAEGP TAYVSVMEGC SKYCTYCVVP YTRGAEISRP
     FDDVLAECAT LAAQGVREIN LLGQNVNAYR GAMHDGTIAD LALLIEYVAA IPNIGRIRFT
     TSHPSEFSDA LIETYRRVPK LVSHLHLPVQ SGSNRILALM KRDYKVAEYQ EKLAKIRAIR
     PDISFSSDFI VGFPGEEEED FQATMDLIEA VFFDTSYSFI YSQRPGTPAS TMPDRVPLTV
     KKERLARLQA RILEMAASIS EAMVGTEQWV LVDRLSRKSE REVSGRTENN RVVNFSAPAS
     LIGRFAKVQI TAAYKNSLRG RLIEAELLPD PVVYTR
//
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