MTU1_SCHPO
ID MTU1_SCHPO Reviewed; 415 AA.
AC O13947;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Mitochondrial tRNA-specific 2-thiouridylase 1;
DE EC=2.8.1.14 {ECO:0000250|UniProtKB:Q12093};
GN ORFNames=SPAC23H4.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; CU329670; CAB11659.1; -; Genomic_DNA.
DR PIR; T38324; T38324.
DR RefSeq; NP_593402.1; NM_001018834.2.
DR AlphaFoldDB; O13947; -.
DR SMR; O13947; -.
DR STRING; 4896.SPAC23H4.04.1; -.
DR MaxQB; O13947; -.
DR PaxDb; O13947; -.
DR EnsemblFungi; SPAC23H4.04.1; SPAC23H4.04.1:pep; SPAC23H4.04.
DR GeneID; 2541868; -.
DR KEGG; spo:SPAC23H4.04; -.
DR PomBase; SPAC23H4.04; -.
DR VEuPathDB; FungiDB:SPAC23H4.04; -.
DR eggNOG; KOG2805; Eukaryota.
DR HOGENOM; CLU_035188_1_2_1; -.
DR InParanoid; O13947; -.
DR OMA; AVCTGHY; -.
DR PhylomeDB; O13947; -.
DR PRO; PR:O13947; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0106054; F:tRNA U34 sulfurtransferase activity; NAS:PomBase.
DR GO; GO:0061708; F:tRNA-5-taurinomethyluridine 2-sulfurtransferase; ISO:PomBase.
DR GO; GO:1990799; P:mitochondrial tRNA wobble position uridine thiolation; ISO:PomBase.
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..415
FT /note="Mitochondrial tRNA-specific 2-thiouridylase 1"
FT /id="PRO_0000121710"
FT REGION 124..126
FT /note="Interaction with target base in tRNA"
FT /evidence="ECO:0000250"
FT REGION 183..185
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT REGION 356..357
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT ACT_SITE 129
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 234
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 160
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 285
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 389
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT DISULFID 129..234
FT /note="Alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 415 AA; 47627 MW; D2B604335B7A935F CRC64;
MRVSLFLQKQ IIECSKAFQP HSTRLQWPKS QDKVFVAMSG GVDSSFSAYL LKSQGYNVEG
VFMRNWLDED SAPSGCPAER DWATVQKVCK KLNISCRRFN FEKEYWNLVF EPSLDLYENG
LTPNPDVSCN RQVKFGALFD ALKKHCENNV KGDWWLASGH YAKSVVNIET NESHMCIPTD
KRKDQTLFLC TIRKEALEKT IFPLHNWTKE NVKKQASSAG FKEIAEKQES QGLCFVSPNV
GRKFRKFLQR YLNFSDRPIK VIAGKNVVGE FSGNHGIWSL TVGERCGLSL PQAQSEYFGR
WYVWKKDIKN NALYICRGTN NELLMSKCIY LKDWKWCGTK LQNLEKSALS CFVRVRHQQP
LQPAKVTWRN PESVKIHFQD KQRAVTPGQV IAVYVNDVCL GGGMVDTVEP EKDFD
