MTU1_DICDI
ID MTU1_DICDI Reviewed; 451 AA.
AC Q54I63;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Mitochondrial tRNA-specific 2-thiouridylase 1;
DE EC=2.8.1.14 {ECO:0000250|UniProtKB:Q12093};
GN Name=trmu; ORFNames=DDB_G0288979;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position
CC (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for
CC the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of
CC mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble
CC position. ATP is required to activate the C2 atom of the wobble base.
CC {ECO:0000250|UniProtKB:Q12093}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-
CC cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A +
CC AMP + diphosphate + H(+) + L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:47040, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11726,
CC Rhea:RHEA-COMP:11732, Rhea:RHEA-COMP:11733, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:61963,
CC ChEBI:CHEBI:87171, ChEBI:CHEBI:87172, ChEBI:CHEBI:456215;
CC EC=2.8.1.14; Evidence={ECO:0000250|UniProtKB:Q12093};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- MISCELLANEOUS: During the reaction, ATP is used to activate the C2 atom
CC of U34 by adenylation. After this, the persulfide sulfur on the
CC catalytic cysteine is transferred to the C2 atom of the wobble base
CC (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). The reaction
CC probably involves hydrogen sulfide that is generated from the
CC persulfide intermediate and that acts as nucleophile towards the
CC activated C2 atom on U34. Subsequently, a transient disulfide bond is
CC formed between the two active site cysteine residues (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MnmA/TRMU family. {ECO:0000305}.
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DR EMBL; AAFI02000129; EAL62944.1; -; Genomic_DNA.
DR RefSeq; XP_636447.1; XM_631355.1.
DR AlphaFoldDB; Q54I63; -.
DR SMR; Q54I63; -.
DR STRING; 44689.DDB0238286; -.
DR PaxDb; Q54I63; -.
DR EnsemblProtists; EAL62944; EAL62944; DDB_G0288979.
DR GeneID; 8626899; -.
DR KEGG; ddi:DDB_G0288979; -.
DR dictyBase; DDB_G0288979; trmu.
DR eggNOG; KOG2805; Eukaryota.
DR HOGENOM; CLU_035188_1_1_1; -.
DR InParanoid; Q54I63; -.
DR OMA; VHLLCEQ; -.
DR PhylomeDB; Q54I63; -.
DR PRO; PR:Q54I63; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0061708; F:tRNA-5-taurinomethyluridine 2-sulfurtransferase; IEA:RHEA.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IBA:GO_Central.
DR CDD; cd01998; tRNA_Me_trans; 1.
DR Gene3D; 2.30.30.280; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR023382; Adenine_a_hdrlase_dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004506; tRNA-specific_2-thiouridylase.
DR TIGRFAMs; TIGR00420; trmU; 1.
PE 3: Inferred from homology;
KW ATP-binding; Disulfide bond; Mitochondrion; Nucleotide-binding;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..451
FT /note="Mitochondrial tRNA-specific 2-thiouridylase 1"
FT /id="PRO_0000349876"
FT REGION 156..158
FT /note="Interaction with target base in tRNA"
FT /evidence="ECO:0000250"
FT REGION 216..218
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT REGION 386..387
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT ACT_SITE 161
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 268
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT BINDING 70..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 187
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 422
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT DISULFID 161..268
FT /note="Alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 451 AA; 51498 MW; DFF8281DCB00D343 CRC64;
MINNINRIKK TYNTFLNVNK LRYSTSIISS NILENDNNNI DDFEQVLKST KVRMPTSALL
LPKKPKVCIG MSGGVDSTIT AKLLKLQGFD VTGVFIKSWD EVEDTGRCQG ERDWKDALEA
SNFLDIPMYK ADFVKDYWNR VFVDFLKDYK NGLTPNPDVW CNREIKFDLF FDFAKENFGV
DYIATGHYSN LYYGEENVGD NNNNNLQLHR AIDKNKDQTF FLCMTKGERL KQAIFPIGGF
TKENIVSFAK TIPNFSKITS KKSSRGICFI GKRPLPDFLS QYMTLKPGDF FDISTNSFIK
GKKHKGSVCY TMGQKANIDS LSERYFIVRS DIERNIVYVC PESQFDQFSL YYEFNTHSFN
WINEIPTEVK SEQGFKGRGI CRHRGDVVNL TIKDTGKTSP IDGSVIYSVN LDQPLRSVAS
GQILCLFDRN TDRCFGGGVI NSSPLYNPTQ F
