MNMA_WOLWR
ID MNMA_WOLWR Reviewed; 370 AA.
AC C0R4S5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=WRi_012330;
OS Wolbachia sp. subsp. Drosophila simulans (strain wRi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=66084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wRi;
RX PubMed=19307581; DOI=10.1073/pnas.0810753106;
RA Klasson L., Westberg J., Sapountzis P., Naeslund K., Lutnaes Y.,
RA Darby A.C., Veneti Z., Chen L., Braig H.R., Garrett R., Bourtzis K.,
RA Andersson S.G.;
RT "The mosaic genome structure of the Wolbachia wRi strain infecting
RT Drosophila simulans.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5725-5730(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; CP001391; ACN95917.1; -; Genomic_DNA.
DR RefSeq; WP_007548792.1; NC_012416.1.
DR AlphaFoldDB; C0R4S5; -.
DR SMR; C0R4S5; -.
DR STRING; 66084.WRi_012330; -.
DR EnsemblBacteria; ACN95917; ACN95917; WRi_012330.
DR KEGG; wri:WRi_012330; -.
DR HOGENOM; CLU_035188_0_1_5; -.
DR OMA; AVCTGHY; -.
DR Proteomes; UP000001293; 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..370
FT /note="tRNA-specific 2-thiouridylase MnmA"
FT /id="PRO_1000198636"
FT REGION 165..167
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 215
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 24..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT SITE 144
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT SITE 352
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT DISULFID 119..215
FT /note="Alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
SQ SEQUENCE 370 AA; 40938 MW; F1B6E09873A7DF32 CRC64;
MLKEFEIEPL LKDKAPHQIK AIVAMSGGVD SSVAAALLHN LGYQVIGVTL QLYGTDGNAN
ARKGACCAGQ DIYDAKRVAE SVGFPHYILN YEEIFKKEVI EDFASTYMRG ETPIPCVRCN
QTVKFRDLLQ VTKNLGADVL VTGHYVRRLE KNGEVKLCRS IDKSKDQSYF LFATTQEQLK
LLRFPLGGFY KSDIRKLAKY FSLQISEKPD SQDICFVSES YSKTIAKLAP QSVQKGKIVD
VNGKVLGEHS GIVNFTVGQR KGLGIAHNEP LYVIKINTEN NEVIVGPINV LMQKKILIKE
LNWLEQPKEG MEVTVKLRSS HAGSLATIHS TDEKNKACVI LNDDYFGISP GQACVAYKGE
QVIGGGWICS
