ID B1V741_CLOPF Unreviewed; 434 AA.
AC B1V741;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=CJD_2612 {ECO:0000313|EMBL:EDT70368.1};
OS Clostridium perfringens D str. JGS1721.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=488537 {ECO:0000313|EMBL:EDT70368.1, ECO:0000313|Proteomes:UP000003188};
RN [1] {ECO:0000313|EMBL:EDT70368.1, ECO:0000313|Proteomes:UP000003188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D str. JGS1721 {ECO:0000313|Proteomes:UP000003188};
RA Paulsen I., Sebastian Y.;
RL Submitted (MAR-2008) 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:EDT70368.1}.
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DR EMBL; ABOO01000055; EDT70368.1; -; Genomic_DNA.
DR RefSeq; WP_004460760.1; NZ_ABOO01000055.1.
DR AlphaFoldDB; B1V741; -.
DR Proteomes; UP000003188; 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; SFLDG01061; methylthiotransferase; 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 1..113
FT /note="MTTase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51449"
FT DOMAIN 138..368
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT DOMAIN 371..434
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
SQ SEQUENCE 434 AA; 49126 MW; 8475456031973390 CRC64;
MKVAFATLGC RVNTYESEAM TEKFVREGYE VVDFNEMADV YVVNTCSVTN MGDKKSRQII
GRARRQNPEA IIAVVGCYAQ IAPTEVSGIE GVDVVLGSRN KGEIVYYVNK ARDEGKQQVK
VGAVLKNKVF EDLKIEEYNN KTRAFLKIQD GCNRFCAYCL IPYTRGSVCS KDPKKVLDEI
RSLAEHGFKE IILSGIHTAS YGVDLDEKVT LVDLLEEIEK IDGIERVRIG SIDPTFFTED
VVRRILALKK LCPHFHLSLQ SGCDSTLKRM NRRYTAKEYE DIVNLLRDKI EDVSITTDVI
VGFPGETDEE FEETYEFLKR IALSKTHIFK YSPRKGTRAE NMENQVDGNK KDERSKKLIE
LNRINEKAFA EKYIGEVIDV LFEEEVELGS GVYTGYTRNY IKVNAKADCN VSGKILNVKI
NSFEGEVAKG EIVL
//
