ID MIAB_DEHSB Reviewed; 418 AA.
AC A5FPV2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 01-MAY-2013, entry version 49.
DE RecName: Full=(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB;
DE EC=2.-.-.-;
DE AltName: Full=tRNA-i(6)A37 methylthiotransferase;
GN Name=miaB; OrderedLocusNames=DehaBAV1_1195;
OS Dehalococcoides sp. (strain BAV1).
OC Bacteria; Chloroflexi; Dehalococcoidetes; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=216389;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAV1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Lowry S.,
RA Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Ritalahti K.M., Loeffler F., Richardson P.;
RT "Complete sequence of Dehalococcoides sp. BAV1.";
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; CP000688; ABQ17774.1; -; Genomic_DNA.
DR RefSeq; YP_001214652.1; NC_009455.1.
DR ProteinModelPortal; A5FPV2; -.
DR STRING; 216389.DehaBAV1_1195; -.
DR EnsemblBacteria; ABQ17774; ABQ17774; DehaBAV1_1195.
DR GeneID; 5131513; -.
DR KEGG; deb:DehaBAV1_1195; -.
DR eggNOG; COG0621; -.
DR HOGENOM; HOG000224767; -.
DR KO; K06168; -.
DR OMA; RDSEHII; -.
DR ProtClustDB; PRK14336; -.
DR BioCyc; DSP216389:GH6D-1246-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; 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 1 418 (Dimethylallyl)adenosine tRNA
FT methylthiotransferase MiaB.
FT /FTId=PRO_0000374256.
FT DOMAIN 2 118 MTTase N-terminal.
FT DOMAIN 346 414 TRAM.
FT METAL 11 11 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 47 47 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 81 81 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 134 134 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 138 138 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 141 141 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
SQ SEQUENCE 418 AA; 46970 MW; A8A1ABB0A189424A CRC64;
MPGYYLWTIG CQMNQAESDR LGRLFELWGY SLADKAEDAE LVLVNSCVVR EHAENKVVNR
LHLLRSLKNE NPKLKIALTG CLVGQDISLI KKKFPFVDYI FGPGSMPDWR EIPEGFILPL
RPPVSANVTI MQGCNNFCTY CVVPYRRGRE KSRSIAEIGC EVAELVRRGS REVVLLGQNV
DSYGHDLPEK PCLADLLSAL HDITGLLRIR FLTSHPKDIS QKLIDAMAHL PKVCRSLSLP
VQSGDDTILA SMRRGYTNQQ YRELVERIKT AMPDISLQTD LIVGFPSENE EQFNQSYKLM
ADIGYDAIHV AAYSPRPQTV AAHDMADDVP VIEKKRRLKL IEDLQKETVG KANAALMDTF
AEVLVEGLQK NKWQGRTLGG KLVFLESDLP LEGCLVKVKI FKTSPWSLQA KLVNIMES
//
