(data stored in SCRATCH zone)

SWISSPROT: B8I9M6_METNO

ID   B8I9M6_METNO            Unreviewed;       447 AA.
AC   B8I9M6;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 68.
DE   RecName: Full=tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase {ECO:0000256|HAMAP-Rule:MF_01864, ECO:0000256|SAAS:SAAS00763205};
DE            EC=2.8.4.3 {ECO:0000256|HAMAP-Rule:MF_01864, ECO:0000256|SAAS:SAAS00763213};
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   OrderedLocusNames=Mnod_0235 {ECO:0000313|EMBL:ACL55279.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55279.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55279.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) 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:0000256|HAMAP-Rule:MF_01864, ECO:0000256|SAAS:SAAS00763283}.
CC   -!- CATALYTIC ACTIVITY: N(6)-dimethylallyladenine(37) in tRNA +
CC       sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced
CC       electron acceptor = 2-methylthio-N(6)-dimethylallyladenine(37) in
CC       tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine
CC       + 5'-deoxyadenosine + electron acceptor. {ECO:0000256|HAMAP-
CC       Rule:MF_01864, ECO:0000256|SAAS:SAAS00763238}.
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:SAAS00763304}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01864,
CC       ECO:0000256|SAAS:SAAS00763209}.
CC   -!- SIMILARITY: Belongs to the methylthiotransferase family. MiaB
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01864,
CC       ECO:0000256|SAAS:SAAS00763254}.
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DR   EMBL; CP001349; ACL55279.1; -; Genomic_DNA.
DR   RefSeq; WP_015926992.1; NC_011894.1.
DR   ProteinModelPortal; B8I9M6; -.
DR   STRING; 460265.Mnod_0235; -.
DR   EnsemblBacteria; ACL55279; ACL55279; Mnod_0235.
DR   KEGG; mno:Mnod_0235; -.
DR   eggNOG; ENOG4105CIW; Bacteria.
DR   eggNOG; COG0621; LUCA.
DR   HOGENOM; HOG000224767; -.
DR   KO; K06168; -.
DR   OMA; KVCEHFH; -.
DR   OrthoDB; POG091H00LG; -.
DR   Proteomes; UP000008207; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 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   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   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; B8I9M6.
DR   SWISS-2DPAGE; B8I9M6.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00077934};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00763228};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01864, ECO:0000256|SAAS:SAAS00077904};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00455342};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00077869};
KW   Oxidoreductase {ECO:0000313|EMBL:ACL55279.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00455284};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00763201};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01864,
KW   ECO:0000256|SAAS:SAAS00763263}.
FT   DOMAIN        2    122       MTTase N-terminal. {ECO:0000259|PROSITE:
FT                                PS51449}.
FT   DOMAIN      378    440       TRAM. {ECO:0000259|PROSITE:PS50926}.
FT   METAL        11     11       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL        47     47       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_01864}.
FT   METAL        85     85       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   447 AA;  48706 MW;  078B890AC620D71D CRC64;
     MKKAFVKSYG CQMNVYDAAR MVDLLGREGF TETAVIEEAD VVVLNTCHIR EKAAEKVYSE
     LGRVRDLKGE RAEAGRETTI VVAGCVAQAE GREIIHRAPA VDVVVGPQSY HRLPDLLRRA
     RAEKVVDTEF PIDDKFDHLP PRRIAGVSSF LTVQEGCDKF CAFCVVPYTR GAEVSRPVAK
     VLAEAERLAA GGARELTLIG QNVNAYHGEG PDGATWSLGR LLRRLAEVPG IARLRYTTSH
     PRDMDDDLIA AHRDCPALMP YLHLPVQSGS DRVLAAMNRK HDAETYLRLI DRIRTARPDI
     ALSSDFIVGF PGETDADHAA TMRLVAEVGF ASAFSFKYSP RPGTPAAESA DAVPEAVKRE
     RLAELQALLE EQNRAFNRAT IGRTVEVLFE KPGRHPGQVA GKSPYLQAVQ IEADPAVIGT
     VLPVRLTRPG SNSLFGERAE AAPAAAA
//

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