ID   MNMA_THIDA              Reviewed;         358 AA.
AC   Q3SKH7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=tRNA-specific 2-thiouridylase MnmA {ECO:0000255|HAMAP-Rule:MF_00144};
DE            EC=2.8.1.13 {ECO:0000255|HAMAP-Rule:MF_00144};
GN   Name=mnmA {ECO:0000255|HAMAP-Rule:MF_00144}; OrderedLocusNames=Tbd_0851;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259;
RX   PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT   anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
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:0000255|HAMAP-
CC       Rule:MF_00144}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00144};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00144}.
CC   -!- SIMILARITY: Belongs to the MnmA/TRMU family. {ECO:0000255|HAMAP-
CC       Rule:MF_00144}.
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DR   EMBL; CP000116; AAZ96804.1; -; Genomic_DNA.
DR   RefSeq; WP_011311363.1; NC_007404.1.
DR   AlphaFoldDB; Q3SKH7; -.
DR   SMR; Q3SKH7; -.
DR   STRING; 292415.Tbd_0851; -.
DR   PRIDE; Q3SKH7; -.
DR   EnsemblBacteria; AAZ96804; AAZ96804; Tbd_0851.
DR   KEGG; tbd:Tbd_0851; -.
DR   eggNOG; COG0482; Bacteria.
DR   HOGENOM; CLU_035188_1_0_4; -.
DR   OMA; AVCTGHY; -.
DR   OrthoDB; 1054741at2; -.
DR   Proteomes; UP000008291; 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;
KW   Reference proteome; RNA-binding; Transferase; tRNA processing;
KW   tRNA-binding.
FT   CHAIN           1..358
FT                   /note="tRNA-specific 2-thiouridylase MnmA"
FT                   /id="PRO_0000349848"
FT   REGION          94..96
FT                   /note="Interaction with target base in tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   REGION          146..148
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   REGION          308..309
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   ACT_SITE        99
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   ACT_SITE        196
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   BINDING         34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   BINDING         123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   SITE            124
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   SITE            341
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   DISULFID        99..196
FT                   /note="Alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
SQ   SEQUENCE   358 AA;  39292 MW;  1AE27C3FB00E5CCF CRC64;
     MSTRVVVGLS GGVDSAVAAY LLKQQGYDVL GVFMKNWDDD DNTEHCTARQ DFLDVLAVAD
     VLGIEVEAVN FAAEYKERVF SYFLAEYQAG RTPNPDVLCN AEIKFKAFLD DAIARGADYI
     ATGHYVGKGH DTFGRAALLR ARDANKDQSY FLYRLNQAQL SPALFPLARL PKPEVREIAR
     RIGLPNAAKK DSTGICFIGE RNFREFLERY LPRDPGDMTT PEGRVVGQHQ GLMYYTLGQR
     QGLGIGGQKG GSDAPWFVAA KDMATNTLVV VQGHDHPLLQ RFGVGAGQLS WIAGVAPDPE
     RPYTAKTRYR QTDAACHITT LYDDTLELVF DAPQWAVTPG QSVVLYDGDV CLGGGIIC