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Database: UniProt
Entry: Q0AF59
LinkDB: Q0AF59
Original site: Q0AF59 
ID   MIAB_NITEC              Reviewed;         443 AA.
AC   Q0AF59;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   26-NOV-2014, entry version 61.
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=Neut_1789;
OS   Nitrosomonas eutropha (strain C91).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=335283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C91;
RX   PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA   Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA   Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M.,
RA   Wei X.;
RT   "Whole-genome analysis of the ammonia-oxidizing bacterium,
RT   Nitrosomonas eutropha C91: implications for niche adaptation.";
RL   Environ. Microbiol. 9:2993-3007(2007).
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; CP000450; ABI60023.1; -; Genomic_DNA.
DR   RefSeq; WP_011634829.1; NC_008344.1.
DR   RefSeq; YP_747988.1; NC_008344.1.
DR   ProteinModelPortal; Q0AF59; -.
DR   STRING; 335283.Neut_1789; -.
DR   EnsemblBacteria; ABI60023; ABI60023; Neut_1789.
DR   GeneID; 4272267; -.
DR   KEGG; net:Neut_1789; -.
DR   PATRIC; 22721062; VBINitEut7577_2181.
DR   eggNOG; COG0621; -.
DR   HOGENOM; HOG000224767; -.
DR   KO; K06168; -.
DR   OMA; FAFLLEC; -.
DR   OrthoDB; EOG6P5ZD8; -.
DR   BioCyc; NEUT335283:GHT6-1824-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    443       tRNA-2-methylthio-N(6)-
FT                                dimethylallyladenosine synthase.
FT                                /FTId=PRO_0000374412.
FT   DOMAIN        3    120       MTTase N-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01864}.
FT   DOMAIN      378    441       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   443 AA;  49757 MW;  B24AEB28A94A5EEB CRC64;
     MSSKLYIKTF GCQMNEYDSA KMADILLSEK NMELTEVPEE ADLILFNTCS VREKAQEKVF
     HDLGRVRHLK NSKPDLLIGV GGCVASQEGS EIVRRAPFVD LVFGPQTLHR LPELIDARRR
     TGQSQVDITF PEIEKFDRLP PARTTGATAF VSIMEGCSKY CSFCVVPYTR GEEVSRPLDD
     VLTEVAGLVI QGVKEVTLLG QNVNAYYDKT SGEGDIDFAT LLDYIHEIPG LVRIRYTTSH
     PREFTARLIE TYQRLPKLVG HVHLPIQSGS DRILAAMKRG YTIIEYKSII RKLRTIRPNI
     SISSDFIVGF PGETDTDFEE TMKLIDDVKF DESFSFIYSP RPGTPASDLP DDTPYRIKLA
     RLHQLQEKIQ RNAQMISQSM VDTIQRVLVE GPSKKDPNEF CGRTDNNRVV NFAGHAGLVG
     SFVDIKITAV SSHTLRGEIS DMQ
//
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