ID A0A139DAI0_9FIRM Unreviewed; 436 AA.
AC A0A139DAI0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 ORFNames=AWL62_19 {ECO:0000313|EMBL:KXS50527.1};
OS Halanaerobium sp. T82-1.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=1794808 {ECO:0000313|EMBL:KXS50527.1, ECO:0000313|Proteomes:UP000070487};
RN [1] {ECO:0000313|EMBL:KXS50527.1, ECO:0000313|Proteomes:UP000070487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T82-1 {ECO:0000313|EMBL:KXS50527.1};
RA Wolfe R., Daly R., Wrighton K.;
RT "Halanaerobium-1 T82 Annotated.";
RL Submitted (JAN-2016) 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:KXS50527.1}.
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DR EMBL; LSBN01000001; KXS50527.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139DAI0; -.
DR PATRIC; fig|1794808.3.peg.1225; -.
DR Proteomes; UP000070487; 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; PF01938; TRAM; 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 S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..115
FT /note="MTTase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51449"
FT DOMAIN 140..378
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 372..436
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
SQ SEQUENCE 436 AA; 49420 MW; 1729F2067CD81F0D CRC64;
MIKRAAFYTL GCKVNQYETE AVIDIFIDNG YQIVNFSEKA DVYIVNSCTV TNEAARKTRQ
IARRAKRRSE DSIVAIVGCY TQAFPDEVRD IEEIDFVMGS NNKADILDKA EEMLAGKSIE
NDVKEYKELK EYEELELKRL TNTTRANVKI EDGCNQFCSY CIIPYARGPV RSRKKEDVAA
EIKRLAEQGV KEIILTGTHL GAYGSENGNN KELTKLMADL TEIENLNRVR LSSIEGTEID
KGMMDLIAEE DIFCPHLHLP LQSGSNKILE AMNRPYTLEE FKKTVAELRN RIPDLAVTTD
VIVGFPGETE ETFAETLEAV KEIGFSKVHV FPYSAREGTP AAEMEQLNGN LVKEYSKKLR
LVNEALMLDY QKEFIGREKE VLIEEVRDHT TGLLTGYTDN YLKILVDGSD DLKNELVKVK
LKKSVDPYHL KGEIIK
//
