ID MNMA_SHIF8 Reviewed; 368 AA.
AC Q0T5N9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 01-MAY-2013, entry version 54.
DE RecName: Full=tRNA-specific 2-thiouridylase MnmA;
DE EC=2.8.1.-;
GN Name=mnmA; OrderedLocusNames=SFV_1168;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z.,
RA Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y.,
RA Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
CC -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble
CC position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to
CC the formation of s(2)U34, the first step of tRNA-mnm(5)s(2)U34
CC synthesis. Sulfur is provided by IscS, via a sulfur-relay system.
CC Binds ATP and its substrate tRNAs (By similarity).
CC -!- SUBUNIT: Interacts with TusE (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the MnmA/TRMU family.
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DR EMBL; CP000266; ABF03376.1; -; Genomic_DNA.
DR RefSeq; YP_688681.1; NC_008258.1.
DR ProteinModelPortal; Q0T5N9; -.
DR SMR; Q0T5N9; 4-368.
DR STRING; 373384.SFV_1168; -.
DR EnsemblBacteria; ABF03376; ABF03376; SFV_1168.
DR GeneID; 4209110; -.
DR KEGG; sfv:SFV_1168; -.
DR PATRIC; 18725638; VBIShiFle33408_1343.
DR eggNOG; COG0482; -.
DR HOGENOM; HOG000218046; -.
DR KO; K00566; -.
DR OMA; QPGNIET; -.
DR ProtClustDB; PRK00143; -.
DR BioCyc; SFLE373384:GHZM-1261-MONOMER; -.
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:HAMAP.
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 PANTHER; PTHR11933; PTHR11933; 1.
DR Pfam; PF03054; tRNA_Me_trans; 1.
DR TIGRFAMs; TIGR00420; trmU; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; Disulfide bond;
KW Nucleotide-binding; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1 368 tRNA-specific 2-thiouridylase MnmA.
FT /FTId=PRO_0000349799.
FT NP_BIND 11 18 ATP (By similarity).
FT REGION 97 99 Interaction with target base in tRNA (By
FT similarity).
FT REGION 149 151 Interaction with tRNA (By similarity).
FT REGION 311 312 Interaction with tRNA (By similarity).
FT ACT_SITE 102 102 Nucleophile (By similarity).
FT ACT_SITE 199 199 Cysteine persulfide intermediate (By
FT similarity).
FT BINDING 37 37 ATP; via amide nitrogen and carbonyl
FT oxygen (By similarity).
FT BINDING 127 127 ATP; via amide nitrogen (By similarity).
FT SITE 128 128 Interaction with tRNA (By similarity).
FT SITE 344 344 Interaction with tRNA (By similarity).
FT DISULFID 102 199 Alternate (By similarity).
SQ SEQUENCE 368 AA; 40958 MW; F41C92676D080D6E CRC64;
MSETAKKVIV GMSGGVDSSV SAWLLQQQGY QVEGLFMKNW EEDDGEEYCT AAADLADAQA
VCDKLGIELH TVNFAAEYWD NVFELFLAEY KAGRTPNPDI LCNKEIKFKA FLEFAAEDLG
ADYIATGHYV RRADVDGKSR LLRGLDSNKD QSYFLYTLSH EQIAQSLFPV GELEKPQVRK
IAEDLGLVTA KKKDSTGICF IGERKFREFL GRYLPAQPGK IITVDGDEIG EHQGLMYHTL
GQRKGLGIGG TKEGTEEPWY VVDKDVENNI LVVAQGHEHP RLMSVGLIAQ QLHWVDREPF
TGTMRCTVKT RYRQTDIPCT VKALDDDRIK VIFDEPVAAV TPGQSAVFYN GEVCLGGGII
EQRLPLPV
//
