(data stored in SCRATCH zone)

SWISSPROT: B7UKU4_ECO27

ID   B7UKU4_ECO27            Unreviewed;       474 AA.
AC   B7UKU4;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase {ECO:0000256|HAMAP-Rule:MF_01864, ECO:0000256|SAAS:SAAS00623688};
DE            EC=2.8.4.3 {ECO:0000256|HAMAP-Rule:MF_01864, ECO:0000256|SAAS:SAAS00623691};
DE   AltName: Full=(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB {ECO:0000256|HAMAP-Rule:MF_01864};
DE   AltName: Full=tRNA-i(6)A37 methylthiotransferase {ECO:0000256|HAMAP-Rule:MF_01864};
GN   Name=miaB {ECO:0000256|HAMAP-Rule:MF_01864,
GN   ECO:0000313|EMBL:CAS08102.1};
GN   OrderedLocusNames=E2348C_0554 {ECO:0000313|EMBL:CAS08102.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08102.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08102.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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:0000256|HAMAP-Rule:MF_01864, ECO:0000256|SAAS:SAAS00623708}.
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:0000256|HAMAP-Rule:MF_01864,
CC         ECO:0000256|SAAS:SAAS01123679};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_01864};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01864,
CC       ECO:0000256|SAAS:SAAS00623714}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01864,
CC       ECO:0000256|SAAS:SAAS00623711}.
CC   -!- SIMILARITY: Belongs to the methylthiotransferase family. MiaB
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01864,
CC       ECO:0000256|SAAS:SAAS00623705}.
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DR   EMBL; FM180568; CAS08102.1; -; Genomic_DNA.
DR   RefSeq; WP_000162747.1; NC_011601.1.
DR   EnsemblBacteria; CAS08102; CAS08102; E2348C_0554.
DR   KEGG; ecg:E2348C_0554; -.
DR   HOGENOM; HOG000224767; -.
DR   KO; K06168; -.
DR   OMA; FGCQMNK; -.
DR   BioCyc; ECOL574521:E2348C_RS02910-MONOMER; -.
DR   Proteomes; UP000008205; 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; SFLDG01061; methylthiotransferase; 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; B7UKU4.
DR   SWISS-2DPAGE; B7UKU4.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00455264};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00623717};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01864, ECO:0000256|SAAS:SAAS00455234};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00078019};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00455354};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00077875};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00623694};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00623699}.
FT   DOMAIN        3    120       MTTase N-terminal. {ECO:0000259|PROSITE:
FT                                PS51449}.
FT   DOMAIN      378    441       TRAM. {ECO:0000259|PROSITE:PS50926}.
FT   METAL        12     12       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL        49     49       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL        83     83       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL       157    157       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01864}.
FT   METAL       161    161       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01864}.
FT   METAL       164    164       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01864}.
SQ   SEQUENCE   474 AA;  53663 MW;  47C4C1738926AE96 CRC64;
     MTKKLHIKTW GCQMNEYDSS KMADLLDATH GYQLTDVAEE ADVLLLNTCS IREKAQEKVF
     HQLGRWKLLK EKNPDLIIGV GGCVASQEGE HIRQRAHYVD IIFGPQTLHR LPEMINSVRG
     DRSPVVDISF PEIEKFDRLP EPRAEGPTAF VSIMEGCNKY CTYCVVPYTR GEEVSRPSDD
     ILFEIAQLAA QGVREVNLLG QNVNAWRGEN YDGTTGTFAD LLRLVAAIDG IDRIRFTTSH
     PIEFTDDIIE VYRDTPELVS FLHLPVQSGS DRILNLMGRT HTALEYKAII RKLRAARPDI
     QISSDFIVGF PGETTDDFEK TMKLIADVNF DMSYSFIFSA RPGTPAADMV DDVPEEEKKQ
     RLYILQERIN QQAMAWSRRM LGTTQRILVE GTSRKSIMEL SGRTENNRVV NFEGTPDMIG
     KFVDVEITDV YPNSLRGKVV RTEDEMGLRV AETPESVIAR TRKENDLGVG YYQP
//

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