ID MNMA_BRUSU Reviewed; 398 AA. AC Q8CY38; G0K6C8; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 99. 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}; Synonyms=trmU; GN OrderedLocusNames=BR1591, BS1330_I1585; OS Brucella suis biovar 1 (strain 1330). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=204722; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330; RX PubMed=12271122; DOI=10.1073/pnas.192319099; RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E., RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.; RT "The Brucella suis genome reveals fundamental similarities between animal RT and plant pathogens and symbionts."; RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330; RX PubMed=22038969; DOI=10.1128/jb.06181-11; RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.; RT "Revised genome sequence of Brucella suis 1330."; RL J. Bacteriol. 193:6410-6410(2011). 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}. 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; AE014291; AAN30496.1; -; Genomic_DNA. DR EMBL; CP002997; AEM18912.1; -; Genomic_DNA. DR AlphaFoldDB; Q8CY38; -. DR SMR; Q8CY38; -. DR KEGG; bms:BR1591; -. DR KEGG; bsi:BS1330_I1585; -. DR PATRIC; fig|204722.21.peg.3233; -. DR HOGENOM; CLU_035188_0_1_5; -. DR PhylomeDB; Q8CY38; -. DR Proteomes; UP000007104; Chromosome I. 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; Adenine nucleotide alpha hydrolases-like domains; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1. DR InterPro; IPR046885; MnmA-like_C. DR InterPro; IPR046884; MnmA-like_central. DR InterPro; IPR023382; MnmA-like_central_sf. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR004506; tRNA-specific_2-thiouridylase. DR NCBIfam; TIGR00420; trmU; 1. DR PANTHER; PTHR11933:SF5; MITOCHONDRIAL TRNA-SPECIFIC 2-THIOURIDYLASE 1; 1. DR PANTHER; PTHR11933; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDYLATE -METHYLTRANSFERASE; 1. DR Pfam; PF03054; tRNA_Me_trans; 1. DR Pfam; PF20258; tRNA_Me_trans_C; 1. DR Pfam; PF20259; tRNA_Me_trans_M; 1. DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 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..398 FT /note="tRNA-specific 2-thiouridylase MnmA" FT /id="PRO_0000121614" FT REGION 160..162 FT /note="Interaction with tRNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144" FT ACT_SITE 114 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144" FT ACT_SITE 210 FT /note="Cysteine persulfide intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144" FT BINDING 20..27 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144" FT BINDING 46 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144" FT BINDING 138 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144" FT SITE 139 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 114..210 FT /note="Alternate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144" SQ SEQUENCE 398 AA; 43229 MW; 937367AC3BAB9ED3 CRC64; MSLNSLDLPG KPEDTRVVVA MSGGVDSSVV AGILKREGYD VVGVTLQLYD HGAAVHRAGS CCAGQDIEDA RRVSESLGIP HYVLDYEARF REAVIDPFAN SYVSGETPIP CVSCNQTVKF ADLLQTARDL GADALATGHY IRSRANGAHR ALYRPVDTDR DQSYFLFATT QEQIDYLRFP LGHLPKAQVR EIAEELGLTV AKKQDSQDIC FVPQGKYSDI ISRLKPEAAN PGDIVHIDGR TLGRHDGIVH YTVGQRRGIG VATGEALYVV HLDAANARVI VGPREALETH KVFLRDVNWL GDTPIADLPK SGMEVFAKVR STRPPRPAVL RHADGQTWVE LVDGESGIAP GQACVLYSDD SNAARVFGGG FIGRSEREPQ AEEMLRRLMA NADKASAA //