MNMA2_BACFR
ID MNMA2_BACFR Reviewed; 353 AA.
AC Q64WG8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=tRNA-specific 2-thiouridylase MnmA 2 {ECO:0000255|HAMAP-Rule:MF_00144};
DE EC=2.8.1.13 {ECO:0000255|HAMAP-Rule:MF_00144};
GN Name=mnmA2 {ECO:0000255|HAMAP-Rule:MF_00144}; OrderedLocusNames=BF1407;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD48158.1; -; Genomic_DNA.
DR RefSeq; WP_011202407.1; NC_006347.1.
DR RefSeq; YP_098692.1; NC_006347.1.
DR AlphaFoldDB; Q64WG8; -.
DR SMR; Q64WG8; -.
DR STRING; 295405.BF1407; -.
DR EnsemblBacteria; BAD48158; BAD48158; BF1407.
DR KEGG; bfr:BF1407; -.
DR PATRIC; fig|295405.11.peg.1374; -.
DR HOGENOM; CLU_035188_1_0_10; -.
DR OMA; VHLLCEQ; -.
DR Proteomes; UP000002197; 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..353
FT /note="tRNA-specific 2-thiouridylase MnmA 2"
FT /id="PRO_0000349522"
FT REGION 92..94
FT /note="Interaction with target base in tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT REGION 142..144
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 97
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 192
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 6..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT SITE 121
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT SITE 334
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT DISULFID 97..192
FT /note="Alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
SQ SEQUENCE 353 AA; 39657 MW; F0559249FA1F150D CRC64;
MDIAALLSGG VDSSVVVHLL CEQGYKPTLF YIKIGMDGAE YMDCSAEEDI ELSTAIARRY
GLALEVVDLH REYWDNVAAY AIEKIRKGQT PNPDVMCNKL IKFGCFEQQV GKDFDLTATG
HYATTLQLGG KTWLGTAKDP IKDQTDFLAQ IDYLQVSKLL FPIGGLMKHE VREIALRAGL
PSARRKDSQG ICFLGKINYN DFVRRFLGEK EGAVIEFETG KKIGTHRGYW FHTIGQRKGL
GLGGGPWFVV KKDIQDNIIY VSHGYDAEQQ YGYEFRMKDF NFITDNPWEG STGEEEVTFK
IRHTPEFIKG RLLHDEEGYR IISSEKLQGI APGQFGVIYD AESRVCFGSG EIG
