MNMA_MESFL
ID MNMA_MESFL Reviewed; 374 AA.
AC Q6F152;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Mfl412;
OS Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS (Acholeplasma florum).
OC Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Entomoplasmataceae;
OC Mesoplasma.
OX NCBI_TaxID=265311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1;
RA Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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; AE017263; AAT75771.1; -; Genomic_DNA.
DR RefSeq; WP_011183311.1; NC_006055.1.
DR RefSeq; YP_053655.1; NC_006055.1.
DR AlphaFoldDB; Q6F152; -.
DR SMR; Q6F152; -.
DR STRING; 265311.Mfl412; -.
DR EnsemblBacteria; AAT75771; AAT75771; Mfl412.
DR GeneID; 2898225; -.
DR KEGG; mfl:Mfl412; -.
DR PATRIC; fig|265311.5.peg.413; -.
DR eggNOG; COG0482; Bacteria.
DR HOGENOM; CLU_035188_1_0_14; -.
DR OMA; AVCTGHY; -.
DR Proteomes; UP000006647; 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;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..374
FT /note="tRNA-specific 2-thiouridylase MnmA"
FT /id="PRO_0000349694"
FT REGION 104..106
FT /note="Interaction with target base in tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT REGION 158..160
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT REGION 321..322
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 109
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 208
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT SITE 135
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 109..208
FT /note="Alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
SQ SEQUENCE 374 AA; 42889 MW; 8C09C4C9223B489C CRC64;
MKKKVIVGLS GGVDSSVAAY LLIQQGYEVE GLFMRNWDSS ANNDILGNQE IDNDVCPQEQ
DYLDALEVAN KLGIKLHRID FVQEYWEYVF EYFIKEYKKG RTPNPDILCN KYIKFDKFLN
HAINELKADY IAMGHYAGVR FNEKTKQYEM IRAVDTNKDQ TYFLCQLTQN QLSKTLFPLQ
SLEKPEIRKI AAEQGLITAD KKDSTGICFI GEREFTKFLQ NYISNQPGDI VDIKTNEVLG
KHIGAMYYTI GQRKGLNLGG MKEPYYVAAK DIDKKIIYVC PASDESYLLS NNAIVTEINW
SLDLKQYIDN VEEFECTAKF RYRQPDVKVR LNKIKDNEYK VSYDAIVKAV TPGQEAVFYL
NDICLGGGII DIVE
