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Database: UniProt
Entry: A3MNX8
LinkDB: A3MNX8
Original site: A3MNX8 
ID   MIAB_BURM7              Reviewed;         457 AA.
AC   A3MNX8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   26-NOV-2014, entry version 57.
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=BMA10247_2438;
OS   Burkholderia mallei (strain NCTC 10247).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320389;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10247;
RA   DeShazer D., Woods D.E., Nierman W.C.;
RL   Submitted (JAN-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:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01864};
CC       Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3
CC       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; CP000548; ABO04043.1; -; Genomic_DNA.
DR   RefSeq; YP_001081964.1; NC_009080.1.
DR   ProteinModelPortal; A3MNX8; -.
DR   STRING; 320389.BMA10247_2438; -.
DR   EnsemblBacteria; ABO04043; ABO04043; BMA10247_2438.
DR   GeneID; 4891932; -.
DR   KEGG; bmn:BMA10247_2438; -.
DR   PATRIC; 19147239; VBIBurMal96640_4653.
DR   eggNOG; COG0621; -.
DR   HOGENOM; HOG000224767; -.
DR   KO; K06168; -.
DR   OMA; FAFLLEC; -.
DR   OrthoDB; EOG6P5ZD8; -.
DR   BioCyc; BMAL320389:GH97-2429-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
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    457       tRNA-2-methylthio-N(6)-
FT                                dimethylallyladenosine synthase.
FT                                /FTId=PRO_0000374180.
FT   DOMAIN        3    120       MTTase N-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01864}.
FT   DOMAIN      380    447       TRAM. {ECO:0000255|HAMAP-Rule:MF_01864}.
FT   METAL        12     12       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL        49     49       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL        83     83       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL       157    157       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01864}.
FT   METAL       161    161       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}.
SQ   SEQUENCE   457 AA;  50512 MW;  F68BEB06D39F043B CRC64;
     MTKKVYVKTF GCQMNEYDSD KMVDVLNAAE GLEKTDTPED ADIILFNTCS VREKAQEKVF
     SDLGRVRELK EAKPDLLIGV GGCVASQEGA SIVARAPYVD LVFGPQTLHR LPQMIDARRE
     SGRAQVDITF PEIEKFDHLP PARVEGPSAF VSIMEGCSKY CSYCVVPYTR GDEVSRPLDD
     VLTEVAGLAD QGVREVTLLG QNVNAYRGAI AAGSAEIADF ATLIEYVADI PGIERIRYTT
     SHPKEFTQRL LDVYAKVPKL VDHLHLPVQH GSDRILMAMK RGYTVLEYKS VIRKLRAIRP
     NLSLSTDIIV GFPGETDADF DKTMALVHEM SYDTSFSFIY SPRPGTPAAN LADDTPRELK
     LKRLQHLQAT IEENVARISQ SMLGKVERIL VEGPSRKDPN ELAGRTENNR VVNFPAPSAA
     HPRLIGQMID VKINHAYPHS LRGELVLAHG DASAATH
//
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