ID   MNMA_THEM4              Reviewed;         339 AA.
AC   A6LNA3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=tRNA-specific 2-thiouridylase MnmA;
DE            EC=2.8.1.13;
GN   Name=mnmA; OrderedLocusNames=Tmel_1559;
OS   Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC   Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX   NCBI_TaxID=391009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12029 / CIP 104789 / BI429;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT   "Complete sequence of Thermosipho melanesiensis BI429.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position
CC       (U34) of tRNA, leading to the formation of s(2)U34. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in
CC         tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-
CC         cysteinyl-[protein]; Xref=Rhea:RHEA:47032, Rhea:RHEA-COMP:10131,
CC         Rhea:RHEA-COMP:11726, Rhea:RHEA-COMP:11727, Rhea:RHEA-COMP:11728,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61963, ChEBI:CHEBI:65315, ChEBI:CHEBI:87170,
CC         ChEBI:CHEBI:456215; EC=2.8.1.13;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MnmA/TRMU family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000716; ABR31404.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6LNA3; -.
DR   SMR; A6LNA3; -.
DR   STRING; 391009.Tmel_1559; -.
DR   EnsemblBacteria; ABR31404; ABR31404; Tmel_1559.
DR   KEGG; tme:Tmel_1559; -.
DR   eggNOG; COG0482; Bacteria.
DR   HOGENOM; CLU_035188_0_0_0; -.
DR   OMA; AVCTGHY; -.
DR   Proteomes; UP000001110; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
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   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; Cytoplasm; Disulfide bond; Nucleotide-binding; RNA-binding;
KW   Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..339
FT                   /note="tRNA-specific 2-thiouridylase MnmA"
FT                   /id="PRO_0000349843"
FT   REGION          126..128
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        84
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        176
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            109
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000250"
FT   SITE            310
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000250"
FT   DISULFID        84..176
FT                   /note="Alternate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   339 AA;  39110 MW;  4007CCD284BB3A1C CRC64;
     MKKKGYAVTA YHLKTVPDSL YLTKQIKHKV CCSPSDTFDA KKVAQKFGVE LKIIHVENVF
     RETIIKYFIN EYKRGRTPNP CFFCNDWIKF GVLLERIIQD GNDYVASGHY ALLRDGKLYK
     AKNKEKDQSY FLASIKREKL GYLVFPNGEY NKDEIRNIAK DLNIHIHSKE DSQDLCFIPD
     NNIYGFLKEN GVGFKEGLII DTKGNILGTH KGLSNYTIGQ RKIGIAVRER MYVLRKDFEK
     NLLVVGKKGE VFNNKFTVSK LNFLQDVYKK IEGYVKVRKK FKEVKCRVYV DNDNLYVETR
     EPIFAITPGQ IAVIYDEDGA VIVSGVIEKE GWNGFESFN