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 01-MAY-2013, entry version 39.
DE RecName: Full=(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB;
DE EC=2.-.-.-;
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 -!- 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; GIDRIRY; -.
DR ProtClustDB; PRK14325; -.
DR BioCyc; CTAI164546:GJNE-484-MONOMER; -.
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 1 450 (Dimethylallyl)adenosine tRNA
FT methylthiotransferase MiaB.
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
//
