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Database: UniProt
Entry: F5LN47_9BACL
LinkDB: F5LN47_9BACL
Original site: F5LN47_9BACL 
ID   F5LN47_9BACL            Unreviewed;       453 AA.
AC   F5LN47;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase {ECO:0000256|ARBA:ARBA00013273};
DE            EC=2.8.4.5 {ECO:0000256|ARBA:ARBA00013273};
DE   AltName: Full=tRNA-t(6)A37 methylthiotransferase {ECO:0000256|ARBA:ARBA00031213};
GN   Name=yqeV {ECO:0000313|EMBL:EGL16227.1};
GN   ORFNames=HMPREF9413_2094 {ECO:0000313|EMBL:EGL16227.1};
OS   Paenibacillus sp. HGF7.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=944559 {ECO:0000313|EMBL:EGL16227.1, ECO:0000313|Proteomes:UP000003445};
RN   [1] {ECO:0000313|EMBL:EGL16227.1, ECO:0000313|Proteomes:UP000003445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGF7 {ECO:0000313|EMBL:EGL16227.1,
RC   ECO:0000313|Proteomes:UP000003445};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the methylthiolation of N6-
CC       threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-
CC       methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in
CC       tRNAs that read codons beginning with adenine.
CC       {ECO:0000256|ARBA:ARBA00002399}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-SH + AH2 + N(6)-L-
CC         threonylcarbamoyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine =
CC         2-methylsulfanyl-N(6)-L-threonylcarbamoyladenosine(37) in tRNA + 5'-
CC         deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:37075, Rhea:RHEA-COMP:10163,
CC         Rhea:RHEA-COMP:11092, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:29917, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64428,
CC         ChEBI:CHEBI:74418, ChEBI:CHEBI:74420; EC=2.8.4.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00000730};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGL16227.1}.
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DR   EMBL; AFDH01000106; EGL16227.1; -; Genomic_DNA.
DR   RefSeq; WP_009675423.1; NZ_AFDH01000106.1.
DR   AlphaFoldDB; F5LN47; -.
DR   OrthoDB; 9805215at2; -.
DR   Proteomes; UP000003445; Unassembled WGS sequence.
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:0035598; F:N6-threonylcarbomyladenosine methylthiotransferase activity; IEA:InterPro.
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   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; IPR006467; MiaB-like_bact.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   InterPro; IPR034557; ThrcA_tRNA_MEthiotransferase.
DR   InterPro; IPR002792; TRAM_dom.
DR   NCBIfam; TIGR01579; MiaB-like-C; 1.
DR   NCBIfam; TIGR00089; MiaB/RimO family radical SAM methylthiotransferase; 1.
DR   PANTHER; PTHR11918; RADICAL SAM PROTEINS; 1.
DR   PANTHER; PTHR11918:SF45; THREONYLCARBAMOYLADENOSINE TRNA METHYLTHIOTRANSFERASE; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF00919; UPF0004; 1.
DR   SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SFLD; SFLDF00295; threonylcarbamoyladenosine_tRN; 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.
DR   PROSITE; PS50926; TRAM; 1.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003445};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGL16227.1}.
FT   DOMAIN          2..114
FT                   /note="MTTase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51449"
FT   DOMAIN          139..368
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   DOMAIN          371..437
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
SQ   SEQUENCE   453 AA;  51273 MW;  A81AA475D92BAC31 CRC64;
     MSTVAFHTLG CKVNFYDTEA IWQMFKGEGY EQVDFEQTAD VYVINTCTVT NTGDKKSRQM
     IRRAVRRNPE AIVAVTGCYA QTSPAEIMAI PGVDLVIGTQ DRDKIISLVK QFQQERQPIN
     AVRNIMKTRQ FEELDVPDFA DRTRAFLKIQ EGCNNFCTFC IIPWSRGLMR SREPESVVKQ
     AHMLVDAGYK EIVLTGIHTG GYGEDMENYS LARLLWDLDK VDGLNRIRIS SIEASQITDE
     VLEVLGASDK MCRHLHIPLQ AGNDQVLARM RRKYTTAEYG RKIELIHKAL PGAAITTDII
     VGFPGETDEM FREGYAFMEQ MKFAEMHVFP YSKRTGTPAA RMLDQIDEEI KNARVHELID
     LSENMQLEYA KQYVGKQLEV IPERAYKGAA EDSGLLMGYS DNYMQMVFEA PEEMIGRVCT
     VEVQEAGVNE SKGKLIRVAE EQSAPANRIK AIV
//
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