ID   MNMA_ENDTX              Reviewed;         360 AA.
AC   B1GZY9;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=tRNA-specific 2-thiouridylase MnmA;
DE            EC=2.8.1.13;
GN   Name=mnmA; OrderedLocusNames=TGRD_338;
OS   Endomicrobium trichonymphae.
OC   Bacteria; Elusimicrobia; Endomicrobia; Endomicrobiales; Endomicrobiaceae;
OC   Endomicrobium.
OX   NCBI_TaxID=1408204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18391199; DOI=10.1073/pnas.0801389105;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Complete genome of the uncultured termite group 1 bacteria in a single
RT   host protist cell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(2008).
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}.
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DR   EMBL; AP009510; BAG13821.1; -; Genomic_DNA.
DR   RefSeq; YP_001956282.1; NC_020419.1.
DR   AlphaFoldDB; B1GZY9; -.
DR   SMR; B1GZY9; -.
DR   STRING; 471821.TGRD_338; -.
DR   EnsemblBacteria; BAG13821; BAG13821; TGRD_338.
DR   KEGG; rsd:TGRD_338; -.
DR   PATRIC; fig|471821.5.peg.544; -.
DR   HOGENOM; CLU_035188_0_0_0; -.
DR   OMA; AVCTGHY; -.
DR   OrthoDB; 1054741at2; -.
DR   Proteomes; UP000001691; 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:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Disulfide bond; Nucleotide-binding; RNA-binding;
KW   Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..360
FT                   /note="tRNA-specific 2-thiouridylase MnmA"
FT                   /id="PRO_0000349852"
FT   REGION          159..161
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        109
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        210
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         135
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            136
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000250"
FT   SITE            343
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000250"
FT   DISULFID        109..210
FT                   /note="Alternate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   360 AA;  39935 MW;  F341B504A9B62218 CRC64;
     METEMKILIG LSGGVDSAVA AYLLKKQGYE VTGTTMSIWD NFLPAPKTKV NDSCLGPENE
     NIETAHKIAD FLTIPLYVTD CSGEYKKVVL ENFRNEYKEG RTPNPCIRCN AYIKFGILPA
     AVKKTGLSFD KFATGHYANI GFDSSTNMYK LYKAADLNKD QTYFLYRLTQ KTLSETIFPL
     GIYTKEQVRN IAKKIGLPSA EKPDSQDFYC GDYNDILQFP ANPGNIVDKN GRVLGKHNGI
     WNYTIGKRKG LGLLGGTKDP LYVINISAKQ NMVTIGTKED LYSSSLTAKK VSWCSILPPK
     KTIEATAKIR RQHKPEKAFI IPQEDSSVKV EFAQPQMSVT AGQSIVFYKD DTVLGGGVII