ID I3TDH8_THEC1 Unreviewed; 425 AA.
AC I3TDH8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=tRNA-t(6)A37 methylthiotransferase {ECO:0000256|RuleBase:RU368081};
DE EC=2.8.4.5 {ECO:0000256|RuleBase:RU368081};
GN OrderedLocusNames=TCELL_0391 {ECO:0000313|EMBL:AFK50816.1};
OS Thermogladius calderae (strain DSM 22663 / VKM B-2946 / 1633).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Thermogladius.
OX NCBI_TaxID=1184251 {ECO:0000313|EMBL:AFK50816.1, ECO:0000313|Proteomes:UP000005270};
RN [1] {ECO:0000313|EMBL:AFK50816.1, ECO:0000313|Proteomes:UP000005270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22663 / VKM B-2946 / 1633
RC {ECO:0000313|Proteomes:UP000005270};
RX PubMed=22843584; DOI=10.1128/JB.00894-12;
RA Mardanov A.V., Kochetkova T.V., Beletsky A.V., Bonch-Osmolovskaya E.A.,
RA Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the hyperthermophilic cellulolytic
RT Crenarchaeon 'Thermogladius cellulolyticus' 1633.";
RL J. Bacteriol. 194:4446-4447(2012).
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|RuleBase:RU368081}.
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|RuleBase:RU368081};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|RuleBase:RU368081};
CC Note=Binds 1 or 2 [4Fe-4S] cluster. One cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000256|RuleBase:RU368081};
CC -!- SIMILARITY: Belongs to the methylthiotransferase family. CDKAL1
CC subfamily. {ECO:0000256|RuleBase:RU368081}.
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DR EMBL; CP003531; AFK50816.1; -; Genomic_DNA.
DR RefSeq; WP_014737066.1; NC_017954.1.
DR AlphaFoldDB; I3TDH8; -.
DR STRING; 1184251.TCELL_0391; -.
DR GeneID; 13012681; -.
DR KEGG; thg:TCELL_0391; -.
DR eggNOG; arCOG01358; Archaea.
DR HOGENOM; CLU_018697_4_2_2; -.
DR InParanoid; I3TDH8; -.
DR OrthoDB; 372134at2157; -.
DR Proteomes; UP000005270; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0035598; F:N6-threonylcarbomyladenosine methylthiotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0061712; F:tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase; 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 InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR005839; Methylthiotransferase.
DR InterPro; IPR013848; Methylthiotransferase_N.
DR InterPro; IPR038135; Methylthiotransferase_N_sf.
DR InterPro; IPR006466; MiaB-like_arc_euk.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR NCBIfam; TIGR01578; MiaB-like-B; 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 SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51449; MTTASE_N; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU368081};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU368081};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU368081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU368081};
KW Reference proteome {ECO:0000313|Proteomes:UP000005270};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU368081};
KW Transferase {ECO:0000256|RuleBase:RU368081};
KW tRNA processing {ECO:0000256|RuleBase:RU368081}.
FT DOMAIN 1..115
FT /note="MTTase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51449"
FT DOMAIN 131..362
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 425 AA; 47877 MW; BEE6AC53FF92F6E9 CRC64;
MKVYLETYGC ALNKSDEALM KRVLTDRGHG IVDDPTSADA LVINTCTVRL DTEYRMARRI
AELYRLAKES GKKLVVAGCL AKAQPYKVAK LAPDASIVSP QNADKIYLAV ESNSRVVLLT
GLRSRGSIGV FLTGRIAPIP AQEGCLGNCT FCIVKHARRV LVSHPIEDVK KAVEEAVRLG
AVEIELTGMD LGTYGIDLYK TRKLPELIES VAEVEGDFMV RVGMLNPEHL SYILDDLVEA
LQHRKVYKFL HIPLQSGSNR ILKLMGRKYT VEEYIDYVEE LKSKIPGISI ATDILVGFPH
ETDEDFQDTV EVIKKLRFER VHLAAYSIRP RTLATSLPQI PTQTKKSRVL QALRVIEQVG
LEDKQRYVNT VQNCFTTEKE KGWVCRLENY IPVVLRSEED LDYGRWVKVA ISEATFFDLR
GYVIN
//
