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Database: UniProt
Entry: E8R6G7_ISOPI
LinkDB: E8R6G7_ISOPI
Original site: E8R6G7_ISOPI 
ID   E8R6G7_ISOPI            Unreviewed;       633 AA.
AC   E8R6G7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 72.
DE   RecName: Full=tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase {ECO:0000256|ARBA:ARBA00033765, ECO:0000256|HAMAP-Rule:MF_01864};
DE            EC=2.8.4.3 {ECO:0000256|ARBA:ARBA00033765, ECO:0000256|HAMAP-Rule:MF_01864};
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=Isop_2300 {ECO:0000313|EMBL:ADV62878.1};
OS   Isosphaera pallida (strain ATCC 43644 / DSM 9630 / IS1B).
OC   Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC   Isosphaera.
OX   NCBI_TaxID=575540 {ECO:0000313|EMBL:ADV62878.1, ECO:0000313|Proteomes:UP000008631};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 43644;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Eisen J.A.;
RT   "The complete sequence of chromosome of Isophaera pallida ATCC 43644.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADV62878.1, ECO:0000313|Proteomes:UP000008631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43644 / DSM 9630 / IS1B
RC   {ECO:0000313|Proteomes:UP000008631};
RX   PubMed=21475588; DOI=10.4056/sigs.1533840;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Goker M., Cleland D., Saunders E., Lapidus A., Nolan M., Lucas S.,
RA   Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA   Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Detter J.C., Beck B., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Isosphaera pallida type strain (IS1B).";
RL   Stand. Genomic Sci. 4:63-71(2011).
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:0000256|ARBA:ARBA00003234,
CC       ECO:0000256|HAMAP-Rule:MF_01864}.
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:0000256|HAMAP-
CC         Rule:MF_01864};
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01864}.
CC   -!- SIMILARITY: Belongs to the methylthiotransferase family. MiaB
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01864}.
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DR   EMBL; CP002353; ADV62878.1; -; Genomic_DNA.
DR   AlphaFoldDB; E8R6G7; -.
DR   STRING; 575540.Isop_2300; -.
DR   KEGG; ipa:Isop_2300; -.
DR   eggNOG; COG0621; Bacteria.
DR   HOGENOM; CLU_018697_2_2_0; -.
DR   InParanoid; E8R6G7; -.
DR   Proteomes; UP000008631; 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:0035596; F:methylthiotransferase activity; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.40.50.12160; Methylthiotransferase, N-terminal domain; 1.
DR   Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR   HAMAP; MF_01864; tRNA_metthiotr_MiaB; 1.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
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   NCBIfam; TIGR01574; miaB-methiolase; 1.
DR   NCBIfam; TIGR00089; MiaB/RimO family radical SAM methylthiotransferase; 1.
DR   PANTHER; PTHR43020; CDK5 REGULATORY SUBUNIT-ASSOCIATED PROTEIN 1; 1.
DR   PANTHER; PTHR43020:SF2; MITOCHONDRIAL TRNA METHYLTHIOTRANSFERASE CDK5RAP1; 1.
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; SFLDG01082; B12-binding_domain_containing; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51449; MTTASE_N; 1.
DR   PROSITE; PS01278; MTTASE_RADICAL; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01864};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01864};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01864};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_01864};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01864}; Reference proteome {ECO:0000313|Proteomes:UP000008631};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01864};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01864}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_01864}.
FT   DOMAIN          45..161
FT                   /note="MTTase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51449"
FT   DOMAIN          197..430
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          503..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          609..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..633
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         54
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01864"
FT   BINDING         90
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01864"
FT   BINDING         124
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01864"
FT   BINDING         211
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:0000256|HAMAP-Rule:MF_01864"
FT   BINDING         215
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:0000256|HAMAP-Rule:MF_01864"
FT   BINDING         218
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:0000256|HAMAP-Rule:MF_01864"
SQ   SEQUENCE   633 AA;  69325 MW;  A8DC4F91BD8CE722 CRC64;
     MASPNPDCDD DRPTPLIPSQ GTACAAPQPI DPERSAPGSD APPPRRLFIE TVGCQMNVLD
     SELVVERLRR DGYELTSDPQ QADTILFNTC SVRQHAEDKV YSALGRLRGL KAEHPEVTIG
     VLGCMAQKDQ KRILQRAPHV DLMVGPGQLE VVPELIARAK NGERKLTAFS LPRTAGSRDR
     VAASFNEFDP ARRKEARKVP FQAFVRIMMG CDKFCTYCIV PSVRGPEQSR HPDEIVEEVR
     NLVDQGTREV TLLGQTVNSY RHKTPDGRIT SFADLLAKLH DIDGLRRIKF VTNYPNDMTD
     ELLAAIRDLP RISRYLHVPA QSGCDQVLKR MKRGYTVGLY NDMMARIRET LPEAAVTSDF
     IVGFCGETEA SFQKTVDLVR RWRFKNSFIF KYSPREGTKA YNLFPDDVPE AVKRRRNNEL
     LAVQNAIALE DQQAFVGRTV EILVEGPSKA HLKAAGGPGA VFNGSASPAI VFRSIPSSAS
     SHGSGIPDPD FGAEPAQDVA SPTLLTEPHS PIPIVSGAKD EGGSSRPSAL VSLAPPPRPH
     LVALPTPPDR ESEEDRPLQL TGRTACDRIV VFEGHPRLIG SFLPVTIQAA SAVTLFGQAV
     TRESVVAQAG AWEPESAESN DRSSRSKELG RLA
//
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