MIAB_ECOLI
ID MIAB_ECOLI Reviewed; 474 AA.
AC P0AEI1; P77645; Q2MBJ9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
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, ECO:0000305|PubMed:10572129};
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, ECO:0000303|PubMed:10572129};
GN Synonyms=yleA; OrderedLocusNames=b0661, JW0658;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION.
RX PubMed=10572129; DOI=10.1128/jb.181.23.7256-7265.1999;
RA Esberg B., Leung H.-C.E., Tsui H.-C.T., Bjoerk G.R., Winkler M.E.;
RT "Identification of the miaB gene, involved in methylthiolation of
RT isopentenylated A37 derivatives in the tRNA of Salmonella typhimurium and
RT Escherichia coli.";
RL J. Bacteriol. 181:7256-7265(1999).
RN [5]
RP COFACTOR, SUBUNIT, AND MUTAGENESIS OF CYS-157; CYS-161 AND CYS-164.
RX PubMed=11882645; DOI=10.1074/jbc.c100609200;
RA Pierrel F., Bjoerk G.R., Fontecave M., Atta M.;
RT "Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein.";
RL J. Biol. Chem. 277:13367-13370(2002).
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:0000255|HAMAP-Rule:MF_01864,
CC ECO:0000269|PubMed:10572129}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01864, ECO:0000305|PubMed:10572129};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37068;
CC Evidence={ECO:0000305|PubMed:10572129};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in
CC tRNA + S-adenosyl-L-methionine = 2-thio-N(6)-
CC dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur
CC carrier]-H + A + H(+) + L-methionine; Xref=Rhea:RHEA:36339,
CC Rhea:RHEA-COMP:10375, Rhea:RHEA-COMP:10377, 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:59789, ChEBI:CHEBI:64428,
CC ChEBI:CHEBI:74415, ChEBI:CHEBI:74416;
CC Evidence={ECO:0000250|UniProtKB:Q9WZC1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36340;
CC Evidence={ECO:0000250|UniProtKB:Q9WZC1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-thio-N(6)-dimethylallyladenosine(37) in tRNA + S-adenosyl-L-
CC methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA
CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:37063, Rhea:RHEA-
CC COMP:10376, Rhea:RHEA-COMP:10377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74416,
CC ChEBI:CHEBI:74417; Evidence={ECO:0000250|UniProtKB:Q9WZC1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37064;
CC Evidence={ECO:0000250|UniProtKB:Q9WZC1};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000305|PubMed:11882645};
CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000305|PubMed:11882645};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01864,
CC ECO:0000269|PubMed:11882645}.
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}.
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DR EMBL; U82598; AAB40863.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73762.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76357.1; -; Genomic_DNA.
DR PIR; C64801; C64801.
DR RefSeq; NP_415194.1; NC_000913.3.
DR RefSeq; WP_000162740.1; NZ_STEB01000031.1.
DR AlphaFoldDB; P0AEI1; -.
DR SMR; P0AEI1; -.
DR BioGRID; 4261232; 46.
DR DIP; DIP-48018N; -.
DR IntAct; P0AEI1; 15.
DR STRING; 511145.b0661; -.
DR jPOST; P0AEI1; -.
DR PaxDb; P0AEI1; -.
DR PRIDE; P0AEI1; -.
DR DNASU; 945260; -.
DR EnsemblBacteria; AAC73762; AAC73762; b0661.
DR EnsemblBacteria; BAE76357; BAE76357; BAE76357.
DR GeneID; 66671065; -.
DR GeneID; 945260; -.
DR KEGG; ecj:JW0658; -.
DR KEGG; eco:b0661; -.
DR PATRIC; fig|1411691.4.peg.1607; -.
DR EchoBASE; EB3421; -.
DR eggNOG; COG0621; Bacteria.
DR HOGENOM; CLU_018697_2_0_6; -.
DR InParanoid; P0AEI1; -.
DR OMA; CEHFHIP; -.
DR PhylomeDB; P0AEI1; -.
DR BioCyc; EcoCyc:G6364-MON; -.
DR BioCyc; MetaCyc:G6364-MON; -.
DR BRENDA; 2.8.4.3; 2026.
DR PRO; PR:P0AEI1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035596; F:methylthiotransferase activity; IBA:GO_Central.
DR GO; GO:0035597; F:N6-isopentenyladenosine methylthiotransferase activity; IDA:EcoCyc.
DR GO; GO:0030488; P:tRNA methylation; IMP:EcoCyc.
DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GO_Central.
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; PS51918; RADICAL_SAM; 1.
DR PROSITE; PS50926; TRAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..474
FT /note="tRNA-2-methylthio-N(6)-dimethylallyladenosine
FT synthase"
FT /id="PRO_0000141734"
FT DOMAIN 3..120
FT /note="MTTase N-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01864"
FT DOMAIN 143..375
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 378..441
FT /note="TRAM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01864"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01864"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01864"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01864"
FT BINDING 157
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000305"
FT BINDING 161
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000305"
FT BINDING 164
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000305"
FT MUTAGEN 157
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11882645"
FT MUTAGEN 161
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11882645"
FT MUTAGEN 164
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11882645"
SQ SEQUENCE 474 AA; 53663 MW; 49CBCB93888F7F9D CRC64;
MTKKLHIKTW GCQMNEYDSS KMADLLDATH GYQLTDVAEE ADVLLLNTCS IREKAQEKVF
HQLGRWKLLK EKNPDLIIGV GGCVASQEGE HIRQRAHYVD IIFGPQTLHR LPEMINSVRG
DRSPVVDISF PEIEKFDRLP EPRAEGPTAF VSIMEGCNKY CTYCVVPYTR GEEVSRPSDD
ILFEIAQLAA QGVREVNLLG QNVNAWRGEN YDGTTGSFAD LLRLVAAIDG IDRIRFTTSH
PIEFTDDIIE VYRDTPELVS FLHLPVQSGS DRILNLMGRT HTALEYKAII RKLRAARPDI
QISSDFIVGF PGETTEDFEK TMKLIADVNF DMSYSFIFSA RPGTPAADMV DDVPEEEKKQ
RLYILQERIN QQAMAWSRRM LGTTQRILVE GTSRKSIMEL SGRTENNRVV NFEGTPDMIG
KFVDVEITDV YPNSLRGKVV RTEDEMGLRV AETPESVIAR TRKENDLGVG YYQP
