MIAB_BUCCC
ID MIAB_BUCCC Reviewed; 435 AA.
AC Q057G5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase;
DE EC=2.8.4.3;
DE AltName: Full=(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB;
DE AltName: Full=tRNA-i(6)A37 methylthiotransferase;
GN Name=miaB; OrderedLocusNames=BCc_272;
OS Buchnera aphidicola subsp. Cinara cedri (strain Cc).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=372461;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cc;
RX PubMed=17038625; DOI=10.1126/science.1130441;
RA Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M.,
RA Silva F.J., Moya A., Latorre A.;
RT "A small microbial genome: the end of a long symbiotic relationship?";
RL Science 314:312-313(2006).
CC -!- FUNCTION: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine
CC (i(6)A), leading to the formation of 2-methylthio-N6-
CC (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read
CC codons beginning with uridine. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in
CC tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-
CC dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur
CC carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:37067, Rhea:RHEA-COMP:10375, Rhea:RHEA-COMP:10376,
CC Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29917, ChEBI:CHEBI:57844, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64428, ChEBI:CHEBI:74415,
CC ChEBI:CHEBI:74417; EC=2.8.4.3;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster, which is coordinated with 3 cysteines
CC and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00780}.
CC -!- SIMILARITY: Belongs to the methylthiotransferase family. MiaB
CC subfamily. {ECO:0000305}.
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DR EMBL; CP000263; ABJ90734.1; -; Genomic_DNA.
DR RefSeq; WP_011672653.1; NC_008513.1.
DR AlphaFoldDB; Q057G5; -.
DR SMR; Q057G5; -.
DR STRING; 372461.BCc_272; -.
DR PRIDE; Q057G5; -.
DR EnsemblBacteria; ABJ90734; ABJ90734; BCc_272.
DR KEGG; bcc:BCc_272; -.
DR eggNOG; COG0621; Bacteria.
DR HOGENOM; CLU_018697_2_0_6; -.
DR OMA; CEHFHIP; -.
DR OrthoDB; 397139at2; -.
DR Proteomes; UP000000669; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035596; F:methylthiotransferase activity; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR Gene3D; 3.40.50.12160; -; 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; IPR007197; rSAM.
DR InterPro; IPR002792; TRAM_dom.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF01938; TRAM; 1.
DR Pfam; PF00919; UPF0004; 1.
DR SFLD; SFLDG01061; methylthiotransferase; 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; PS51918; RADICAL_SAM; 1.
DR PROSITE; PS50926; TRAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..435
FT /note="tRNA-2-methylthio-N(6)-dimethylallyladenosine
FT synthase"
FT /id="PRO_0000374171"
FT DOMAIN 1..107
FT /note="MTTase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT DOMAIN 133..366
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 367..431
FT /note="TRAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT BINDING 147
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 151
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
FT BINDING 154
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00780"
SQ SEQUENCE 435 AA; 50960 MW; 6AA6AA1924EB2062 CRC64;
MNEHDSSIIE NILKKTNLYI ITKKPEISDI LILNTCSIRE KAQEKLFHQL GRWKKLKQKN
SKILIAVGGC VAVQEGKKIY KRAKFIDIIF GPQTLHKLPK LLIESNKKKS LIINIKKKSL
KKFNYTINKN TNIKKKFSSF VTIMEGCNKY CSFCIVPYTR GKEVSRNNKK IISEIIELSK
KGVREITLLG QNVNAYKFSD TFNKKNYSFS DLLYSISEIP RIDRIRFITS HPVEFNNNII
EAYKKIPKLT NFLHLPVQSG SNKILKLMKR GYTIEKYENI VNKIKKIRPK INISSDFIIG
FPGETKEDFQ KTIYFISKIN FDTSYSFIYS KRPRTRASKL EDNVTMEEKK KRLYKVQQKI
NQQAFQWKRR STEQIVLVEG ISKNNIQELY GRTENNRTVF FEGNPKFIGN FIKLKIISIK
YNTFLKGKII SNNYF
