ID   MNMA_COXB2              Reviewed;         371 AA.
AC   B6IZW5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=CbuG_0861;
OS   Coxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=434923;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CbuG_Q212;
RX   PubMed=19047403; DOI=10.1128/iai.01141-08;
RA   Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA   Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA   Heinzen R.A.;
RT   "Comparative genomics reveal extensive transposon-mediated genomic
RT   plasticity and diversity among potential effector proteins within the genus
RT   Coxiella.";
RL   Infect. Immun. 77:642-656(2009).
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; CP001019; ACJ18243.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6IZW5; -.
DR   SMR; B6IZW5; -.
DR   KEGG; cbg:CbuG_0861; -.
DR   HOGENOM; CLU_035188_1_0_6; -.
DR   OMA; AVCTGHY; -.
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..371
FT                   /note="tRNA-specific 2-thiouridylase MnmA"
FT                   /id="PRO_1000203304"
FT   REGION          108..110
FT                   /note="Interaction with target base in tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   REGION          159..161
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   ACT_SITE        113
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   ACT_SITE        209
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   BINDING         22..29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   BINDING         48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   BINDING         137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   SITE            138
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   SITE            354
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   DISULFID        113..209
FT                   /note="Alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
SQ   SEQUENCE   371 AA;  41916 MW;  E38B231E1BA18DA0 CRC64;
     MGIIFYTTQM PNFEQNQVIA VGLSGGVDSS VAALVLKEKG YEVIGLFMQN WETDSKDPFC
     TAEQDLSDAK AIADHIGIPL YVVNFSKAYW NHVFQHCLDE FAQGRTPNPD VWCNREIKFK
     SLLDHAKKLG ATHLATGHYA CIQNENNEYR LLKSNDSHKD QSYFLHLLNQ YQLANSVFPI
     GGYQKSEVRA IAKKRGFINH AKKDSTGICF IGERKFKDFL NEFLLAQPGN IETSEGKIIG
     KHDGIMFYTV GQRKGLHIGG RPDAGEAPWY VVDKDVKRNV LIVVQGYEHP LLYSQELTCT
     NLHWIRDTEP SFPLTCKAKT RCRQADQTCV VTRLDNDHCH VQFEHPQRAI TRGQSVVFYL
     GNECLGGGII N