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Database: UniProt
Entry: B2AHA4
LinkDB: B2AHA4
Original site: B2AHA4 
ID   MIAB_CUPTR              Reviewed;         450 AA.
AC   B2AHA4;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   14-MAY-2014, entry version 45.
DE   RecName: Full=tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase;
DE            EC=2.8.4.3;
DE   AltName: Full=(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB;
DE   AltName: Full=tRNA-i(6)A37 methylthiotransferase;
GN   Name=miaB; OrderedLocusNames=RALTA_A0485;
OS   Cupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis
OS   (strain LMG 19424)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=164546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R1 / LMG 19424;
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M.,
RA   Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V.,
RA   Batut J., Medigue C., Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
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   -!- 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.
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; CU633749; CAP63153.1; -; Genomic_DNA.
DR   RefSeq; YP_001795873.1; NC_010528.1.
DR   ProteinModelPortal; B2AHA4; -.
DR   STRING; 164546.RALTA_A0485; -.
DR   EnsemblBacteria; CAP63153; CAP63153; RALTA_A0485.
DR   GeneID; 6301293; -.
DR   KEGG; cti:RALTA_A0485; -.
DR   PATRIC; 21527616; VBICupTai42494_0492.
DR   eggNOG; COG0621; -.
DR   HOGENOM; HOG000224767; -.
DR   KO; K06168; -.
DR   OMA; FAFLLEC; -.
DR   OrthoDB; EOG6P5ZD8; -.
DR   BioCyc; CTAI164546:GJNE-484-MONOMER; -.
DR   BioCyc; CTAI977880:GLC7-484-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    450       tRNA-2-methylthio-N(6)-
FT                                dimethylallyladenosine synthase.
FT                                /FTId=PRO_0000374249.
FT   DOMAIN        2    119       MTTase N-terminal.
FT   DOMAIN      378    448       TRAM.
FT   METAL        11     11       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        48     48       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        82     82       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       156    156       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL       160    160       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL       163    163       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
SQ   SEQUENCE   450 AA;  50166 MW;  E656AAB93C91F42B CRC64;
     MKKVFVKTYG CQMNEYDSDK MVDVLNASQG LEATDNVEDA DVILFNTCSV REKAQEKVFS
     ELGRMKALKA VKPDLVIGVG GCVASQEGAS IVSRAPYVDV VFGPQTLHRL PDLIARRQRT
     GQSQVDISFP EIEKFDHLPP ARVEGPSAFV SIMEGCSKYC SYCVVPYTRG EEVSRPFEDV
     LAEVAGLAEQ GVREVTLLGQ NVNAYRGKMG DTSEIADFAL LIEYVAEIPG IERIRYTTSH
     PKEFTSRLVE LYGRCDKLVN HLHLPVQHAS DRILMAMKRG YSVLEYKSII RRLRALRPDM
     SMSSDFIVGF PGETDADFDK LMAMIEEIGY DTSFSFIFSP RPGTPAANLH DDTPREVKLQ
     RLQRLQATIE ENVQRISQGM VGTVQRILVE GPARKDPTEL HGRTENNRVV NFALPGVPQA
     GRDRLVGQLV DVSITQAFPH SLRGEIVVRQ
//
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