MTU1_PONAB
ID MTU1_PONAB Reviewed; 422 AA.
AC Q5RB73;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Mitochondrial tRNA-specific 2-thiouridylase 1;
DE EC=2.8.1.14 {ECO:0000250|UniProtKB:Q12093};
GN Name=TRMU; Synonyms=MTU1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:O75648}.
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; CR858781; CAH90987.1; -; mRNA.
DR RefSeq; NP_001125570.1; NM_001132098.1.
DR AlphaFoldDB; Q5RB73; -.
DR SMR; Q5RB73; -.
DR STRING; 9601.ENSPPYP00000013334; -.
DR GeneID; 100172484; -.
DR KEGG; pon:100172484; -.
DR CTD; 55687; -.
DR eggNOG; KOG2805; Eukaryota.
DR InParanoid; Q5RB73; -.
DR OrthoDB; 697006at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd01998; tRNA_Me_trans; 1.
DR Gene3D; 2.30.30.280; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 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 2: Evidence at transcript level;
KW ATP-binding; Disulfide bond; Mitochondrion; Nucleotide-binding;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..422
FT /note="Mitochondrial tRNA-specific 2-thiouridylase 1"
FT /id="PRO_0000248302"
FT REGION 96..98
FT /note="Interaction with target base in tRNA"
FT /evidence="ECO:0000250"
FT REGION 171..173
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT REGION 335..336
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT REGION 402..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 223
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 127
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 268
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 368
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT DISULFID 101..223
FT /note="Alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 422 AA; 47764 MW; 128CC2169B2F4E9A CRC64;
MQAVRHVVCA LSGGVDSAVA ALLLRRRGYQ VTGVFMKNWD SLDEHGVCTA DKDCEDAYRV
CQILDIPFHQ VSYVKEYWND VFSDFLNEYE KGRTPNPDIV CNKHIKFSCF FHYAVDNLGA
DAIATGHYAR TSLEDEEVFE QKHIKKPEGL FRNRFEVRNA VKLLQAADSF KGQTFFLSQV
FSQDALRRTI FPLGGLTKEF VKKIAAENRL HHVLQKKESM GMCFIGKRNF EHFLLQYLQP
RPGHFISIED NKVLGTHKGW FLYTLGQRAN IGGLREPWYV VEKDSVKGDV FVAPRTDHPA
LYRDLLRTSR VHWIAEEPPA VLVRDKMMEC HFRFRHQMAL VPCVLTLNQD GTVWVTAVQA
VRALATGQFA VFYKGDECLG SGKILRLGPS AYTLQKGQCG AEVATESPTD SPEDGPGLSP
LL
