(data stored in ACNUC29543 zone)

SWISSPROT: MIAB_SYNR3

ID   MIAB_SYNR3              Reviewed;         453 AA.
AC   A5GRJ8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 74.
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=SynRCC307_0604;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) 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.
CC       {ECO:0000255|HAMAP-Rule:MF_01864}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-SH + AH2 + N(6)-
CC         dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine =
CC         2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-
CC         deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine
CC         + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:37067, Rhea:RHEA-
CC         COMP:10375, Rhea:RHEA-COMP:10376, Rhea:RHEA-COMP:14737,
CC         Rhea:RHEA-COMP:14739, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17319, ChEBI:CHEBI:17499, ChEBI:CHEBI:29917,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:64428, ChEBI:CHEBI:74415, ChEBI:CHEBI:74417;
CC         EC=2.8.4.3; Evidence={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}.
DR   EMBL; CT978603; CAK27507.1; -; Genomic_DNA.
DR   RefSeq; WP_011935022.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0604; -.
DR   PRIDE; A5GRJ8; -.
DR   EnsemblBacteria; CAK27507; CAK27507; SynRCC307_0604.
DR   KEGG; syr:SynRCC307_0604; -.
DR   eggNOG; ENOG4105CIW; Bacteria.
DR   eggNOG; COG0621; LUCA.
DR   HOGENOM; HOG000224767; -.
DR   KO; K06168; -.
DR   OMA; FGCQMNK; -.
DR   OrthoDB; 397139at2; -.
DR   BioCyc; SSP316278:G1GJL-591-MONOMER; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.12160; -; 1.
DR   Gene3D; 3.80.30.20; -; 1.
DR   HAMAP; MF_01864; tRNA_metthiotr_MiaB; 1.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR005839; Methylthiotransferase.
DR   InterPro; IPR020612; Methylthiotransferase_CS.
DR   InterPro; IPR013848; Methylthiotransferase_N.
DR   InterPro; IPR038135; Methylthiotransferase_N_sf.
DR   InterPro; IPR006463; MiaB_methiolase.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   InterPro; IPR002792; TRAM_dom.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF01938; TRAM; 1.
DR   Pfam; PF00919; UPF0004; 1.
DR   SFLD; SFLDF00273; (dimethylallyl)adenosine_tRNA_; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 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;
DR   PRODOM; A5GRJ8.
DR   SWISS-2DPAGE; A5GRJ8.
KW   4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
KW   Metal-binding; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN         1    453       tRNA-2-methylthio-N(6)-
FT                                dimethylallyladenosine synthase.
FT                                /FTId=PRO_0000374600.
FT   DOMAIN        7    123       MTTase N-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01864}.
FT   DOMAIN      384    447       TRAM. {ECO:0000255|HAMAP-Rule:MF_01864}.
FT   METAL        16     16       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL        52     52       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL        86     86       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL       158    158       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01864}.
FT   METAL       162    162       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01864}.
FT   METAL       165    165       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01864}.
SQ   SEQUENCE   453 AA;  50615 MW;  A72844FF02209532 CRC64;
     MADSSRGTYW ITTFGCQMNK ADSERMAGIL ESMGYCAGSG EDQADLVLYN TCTIRDNAEQ
     KVYSYLGRQA RRKRDNPALT LVVAGCVAQQ EGESLLRRVP ELDLVMGPQH ANRLDTLLSQ
     VEAGQQVVAT DDHHILEDIT TARRDSSLCA WVNVIYGCNE RCTYCVVPSV RGQEQSRLPQ
     AIRLEMEGLA ASGYKEITLL GQNIDAYGRD LPGITPEGRR QNTLTDLLHH VHDVKGIERI
     RFATSHPRYF TERLIEACAE LPKVCEHFHV PFQSGDDELL KAMARGYTTA RYRRIVEQIR
     KLMPDAAISA DAIVGFPGET DAQFRRTLEL VDEIGFDLLN TAAYSPRPNT PAADWPDQVE
     EHVKVERLKE LNALVERKAK ACSQRYLGRV EEVLAEGINP KDNTQLMGRT RTNRLTFFPA
     GSHRVGDTVP VRIEQVRAFS LSGSAQAQPA LVR
//

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