ID MIAB_PROA2 Reviewed; 441 AA.
AC B4S564;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 01-MAY-2013, entry version 34.
DE RecName: Full=(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB;
DE EC=2.-.-.-;
DE AltName: Full=tRNA-i(6)A37 methylthiotransferase;
GN Name=miaB; OrderedLocusNames=Paes_1999;
OS Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=290512;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 271 / SK 413;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Prosthecochloris aestuarii DSM
RT 271.";
RL Submitted (JUN-2008) 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; CP001108; ACF47010.1; -; Genomic_DNA.
DR RefSeq; YP_002016657.1; NC_011059.1.
DR ProteinModelPortal; B4S564; -.
DR STRING; 290512.Paes_1999; -.
DR EnsemblBacteria; ACF47010; ACF47010; Paes_1999.
DR GeneID; 6459858; -.
DR KEGG; paa:Paes_1999; -.
DR PATRIC; 23043926; VBIProAes37017_2128.
DR eggNOG; COG0621; -.
DR HOGENOM; HOG000224767; -.
DR KO; K06168; -.
DR OMA; GIDRIRY; -.
DR ProtClustDB; PRK14340; -.
DR BioCyc; PAES290512:GHUT-2114-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 1 441 (Dimethylallyl)adenosine tRNA
FT methylthiotransferase MiaB.
FT /FTId=PRO_0000374456.
FT DOMAIN 3 119 MTTase N-terminal.
FT DOMAIN 374 437 TRAM.
FT METAL 12 12 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 155 155 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 159 159 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 162 162 Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT similarity).
SQ SEQUENCE 441 AA; 49395 MW; A6601F13B0D39CE3 CRC64;
MTKKVSIRTF GCQMNQADTE IISSLLTAEG YCLVAEEDDA DLVMLNTCAV RENAVEKIMH
HLDSLKGLRR RRRGLVVGVI GCVPQYYREE MFQKSGVIDF IAGPDSYRKL PGLIRNAFQG
IRGAELFLTQ SETYGDIEPM RSGSISAFIP VMRGCNNMCA FCVVPFTRGR ERSRSLQSVL
DEVRRLEGQG YRELTLLGQN VNSYRDDEAG ADFALLLDEV SKAAGEMRVR FTTSHPKDIS
EDLVNVVAQR ENVCNAIHLP VQSGSSRMLE VMHRGHTRRE YLDKIAMIRS AVPGVALSTD
LIAGFCGETE EDHLQTLSLM EEVRFDYAYM FYYSVRPGTY AARHLTDDVA LEEKKRRLQE
IIDLQSGISG EIFGNDVGSV QEVLAESESR RSSDMLMGRS DTNRVVVFDR QHYQPGDLVR
VVIESSTQAT LIGRCQDPGE G
//
