MTU1_YEAST
ID MTU1_YEAST Reviewed; 417 AA.
AC Q12093; D6VRW0; Q6IUF4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Mitochondrial tRNA-specific 2-thiouridylase 1;
DE EC=2.8.1.14 {ECO:0000269|PubMed:15509579, ECO:0000269|PubMed:17706197};
DE AltName: Full=Mitochondrial translation optimization protein 2;
DE AltName: Full=Synthetic lethal with MSS4 3;
GN Name=SLM3; Synonyms=MTO2, MTU1; OrderedLocusNames=YDL033C; ORFNames=D2761;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 201238 / W303-1B;
RX PubMed=15944150; DOI=10.1074/jbc.m504247200;
RA Yan Q., Li X., Faye G., Guan M.-X.;
RT "Mutations in MTO2 related to tRNA modification impair mitochondrial gene
RT expression and protein synthesis in the presence of a paromomycin
RT resistance mutation in mitochondrial 15 S rRNA.";
RL J. Biol. Chem. 280:29151-29157(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-38.
RX PubMed=15509579; DOI=10.1074/jbc.m409306200;
RA Umeda N., Suzuki T., Yukawa M., Ohya Y., Shindo H., Watanabe K., Suzuki T.;
RT "Mitochondria-specific RNA-modifying enzymes responsible for the
RT biosynthesis of the wobble base in mitochondrial tRNAs. Implications for
RT the molecular pathogenesis of human mitochondrial diseases.";
RL J. Biol. Chem. 280:1613-1624(2005).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17706197; DOI=10.1016/j.febslet.2007.07.067;
RA Wang X., Yan Q., Guan M.X.;
RT "Deletion of the MTO2 gene related to tRNA modification causes a failure in
RT mitochondrial RNA metabolism in the yeast Saccharomyces cerevisiae.";
RL FEBS Lett. 581:4228-4234(2007).
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:0000269|PubMed:15509579, ECO:0000269|PubMed:15944150,
CC ECO:0000269|PubMed:17706197}.
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:0000269|PubMed:15509579,
CC ECO:0000269|PubMed:17706197};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15509579,
CC ECO:0000269|PubMed:15944150}.
CC -!- MISCELLANEOUS: Present with 1510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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}.
CC -!- CAUTION: Was originally thought to be a 5-methylaminomethyl-2-
CC methyltransferase involved in tRNA modification. {ECO:0000305}.
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DR EMBL; AY624369; AAT44736.1; -; Genomic_DNA.
DR EMBL; Z71781; CAA96456.1; -; Genomic_DNA.
DR EMBL; Z74081; CAA98591.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11820.1; -; Genomic_DNA.
DR PIR; S67566; S67566.
DR RefSeq; NP_010251.1; NM_001180092.1.
DR AlphaFoldDB; Q12093; -.
DR SMR; Q12093; -.
DR BioGRID; 32024; 539.
DR IntAct; Q12093; 2.
DR STRING; 4932.YDL033C; -.
DR iPTMnet; Q12093; -.
DR MaxQB; Q12093; -.
DR PaxDb; Q12093; -.
DR PRIDE; Q12093; -.
DR EnsemblFungi; YDL033C_mRNA; YDL033C; YDL033C.
DR GeneID; 851529; -.
DR KEGG; sce:YDL033C; -.
DR SGD; S000002191; SLM3.
DR VEuPathDB; FungiDB:YDL033C; -.
DR eggNOG; KOG2805; Eukaryota.
DR GeneTree; ENSGT00390000014323; -.
DR HOGENOM; CLU_035188_1_0_1; -.
DR InParanoid; Q12093; -.
DR OMA; AVCTGHY; -.
DR BioCyc; MetaCyc:G3O-29458-MON; -.
DR BioCyc; YEAST:G3O-29458-MON; -.
DR PRO; PR:Q12093; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12093; protein.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016783; F:sulfurtransferase activity; TAS:Reactome.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0061708; F:tRNA-5-taurinomethyluridine 2-sulfurtransferase; IMP:SGD.
DR GO; GO:1990799; P:mitochondrial tRNA wobble position uridine thiolation; IMP:SGD.
DR GO; GO:0006400; P:tRNA modification; TAS:Reactome.
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 1: Evidence at protein level;
KW ATP-binding; Disulfide bond; Mitochondrion; Nucleotide-binding;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..417
FT /note="Mitochondrial tRNA-specific 2-thiouridylase 1"
FT /id="PRO_0000121711"
FT REGION 122..124
FT /note="Interaction with target base in tRNA"
FT /evidence="ECO:0000250"
FT REGION 179..181
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT REGION 354..355
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT ACT_SITE 127
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 229
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 155
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 281
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 391
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT DISULFID 127..229
FT /note="Alternate"
FT /evidence="ECO:0000250"
FT MUTAGEN 38
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15509579"
SQ SEQUENCE 417 AA; 47049 MW; 15BF63FD9A094890 CRC64;
MLARYLNLIG RRSASPYRPQ RLPAKFDNVI VAMSSGVDSS VAAALFAGEF PNTRGVYMQN
WSESQSLDDP GKEPCYERDW RDVNRVAKHL NIRVDKVNFE QDYWIDVFEP MLRGYSEGST
PNPDIGCNKF VKFGKLREWL DEKYGTGNYW LVTGHYARVM QEMNGKGLFH LLRSIYRPKD
QSYYLSQINS TVLSSLLLPI GHLTKPEVRD LAKYAGLPTA EKPDSQGICF VNNSQHGKFK
NFLKHYLPSS PGDIITVDPQ SGAKTTWGRH DGLWSYTIGQ KVGISMPQAD PNYQGTWFVS
EKLRDTNEIL IVRGRDNPAL YSDTMRIENF SSLGPREDTI NAFQNTGALT LQFRSLQVPV
QIKSCKLNRS ADNLDITIHL ASKQRAITPG QSCCLYIDDR VLGSGPISHV NNNDTHA
