TTUA_METJA
ID TTUA_METJA Reviewed; 303 AA.
AC Q58873;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=tRNA-5-methyluridine(54) 2-sulfurtransferase {ECO:0000250|UniProtKB:O58038};
DE EC=2.8.1.- {ECO:0000250|UniProtKB:O58038};
DE AltName: Full=tRNA thiouridine synthetase TtuA {ECO:0000250|UniProtKB:O58038};
GN OrderedLocusNames=MJ1478;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: Catalyzes the ATP-dependent 2-thiolation of 5-methyluridine
CC residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-
CC thiouridine (m(5)s(2)U or s(2)T) (By similarity). This modification
CC allows thermal stabilization of tRNAs in thermophilic microorganisms,
CC and is required for cell growth at high temperatures (By similarity).
CC {ECO:0000250|UniProtKB:O58038, ECO:0000250|UniProtKB:Q72LF3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methyluridine(54) in tRNA + ATP + hydrogen sulfide = 5-
CC methyl-2-thiouridine(54) in tRNA + AMP + diphosphate;
CC Xref=Rhea:RHEA:55188, Rhea:RHEA-COMP:10167, Rhea:RHEA-COMP:13344,
CC ChEBI:CHEBI:29919, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:74447, ChEBI:CHEBI:136799, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:O58038};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:O58038};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by
CC three Cys residues, the fourth Fe with a free coordination site may
CC bind a small ligand, such as exogenous sulfide, thus acting as a sulfur
CC carrier. {ECO:0000250|UniProtKB:O58038};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O58038};
CC -!- PATHWAY: tRNA modification. {ECO:0000250|UniProtKB:O58038}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O58038}.
CC -!- MISCELLANEOUS: In TtuA from T.thermophilus, the sulfur inserted into
CC the nucleoside comes from the C-terminal thiocarboxylate of TtuB, but
CC there is no TtuB ortholog in M.jannaschii. {ECO:0000305}.
CC -!- MISCELLANEOUS: The thiolation reaction likely consists of two steps: a
CC first activation step by ATP to form an adenylated intermediate of the
CC target base of tRNA, and a second nucleophilic substitution step of the
CC sulfur (S) atom supplied by the hydrosulfide attached to the Fe-S
CC cluster. {ECO:0000250|UniProtKB:O58038}.
CC -!- SIMILARITY: Belongs to the TtcA family. TtuA subfamily. {ECO:0000305}.
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DR EMBL; L77117; AAB99482.1; -; Genomic_DNA.
DR PIR; E64484; E64484.
DR AlphaFoldDB; Q58873; -.
DR SMR; Q58873; -.
DR STRING; 243232.MJ_1478; -.
DR EnsemblBacteria; AAB99482; AAB99482; MJ_1478.
DR KEGG; mja:MJ_1478; -.
DR eggNOG; arCOG00042; Archaea.
DR HOGENOM; CLU_026481_1_1_2; -.
DR InParanoid; Q58873; -.
DR OMA; CLHINLG; -.
DR PhylomeDB; Q58873; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0002144; C:cytosolic tRNA wobble base thiouridylase complex; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR000541; Ncs6/Tuc1/Ctu1.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR011063; TilS/TtcA_N.
DR InterPro; IPR035107; tRNA_thiolation_TtcA_Ctu1.
DR InterPro; IPR020554; UPF0021_CS.
DR Pfam; PF01171; ATP_bind_3; 1.
DR PIRSF; PIRSF004976; ATPase_YdaO; 1.
DR TIGRFAMs; TIGR00269; TIGR00269; 1.
DR PROSITE; PS01263; UPF0021; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; Iron; Iron-sulfur; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; RNA-binding; Transferase;
KW tRNA processing; tRNA-binding; Zinc.
FT CHAIN 1..303
FT /note="tRNA-5-methyluridine(54) 2-sulfurtransferase"
FT /id="PRO_0000219892"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 130
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 133
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 222
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58038"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58038"
SQ SEQUENCE 303 AA; 35543 MW; D62272DDA060A40D CRC64;
MVKTMKCKFC DKKSYIKLKS PKMYLCKEHF VEYFENKVKK SIDKYKMLSK DEKILVAVSG
GKDGHAAAWV LKKLGYNIEL FHINLGIEGF SEESLKAVKE LAEKLEVPLH VVNLKDITGK
TMEDIRGKKC SICGTTKRYL MNKFGYENGF DVIVTGHNLD DEVSFILNNL FNWNIRYLAK
HEPVLPAHDK FLKKVKIFFE IEEELILKYA EAEEIPYTTV ECKYAERAIT LKHRAYLNEL
EKERPGIKYQ FLSGYMKNRH LFKVEEEDFQ FRECEVCGMT SAGKICSFCR VWKLYKKKKE
NRN
