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MNMA_MYCAP
ID   MNMA_MYCAP              Reviewed;         374 AA.
AC   A5IYK6;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=MAG4170;
OS   Mycoplasmopsis agalactiae (strain NCTC 10123 / CIP 59.7 / PG2) (Mycoplasma
OS   agalactiae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=347257;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10123 / CIP 59.7 / PG2;
RX   PubMed=17511520; DOI=10.1371/journal.pgen.0030075;
RA   Sirand-Pugnet P., Lartigue C., Marenda M., Jacob D., Barre A., Barbe V.,
RA   Schenowitz C., Mangenot S., Couloux A., Segurens B., de Daruvar A.,
RA   Blanchard A., Citti C.;
RT   "Being pathogenic, plastic, and sexual while living with a nearly minimal
RT   bacterial genome.";
RL   PLoS Genet. 3:744-758(2007).
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; CU179680; CAL59115.1; -; Genomic_DNA.
DR   RefSeq; WP_011949589.1; NC_009497.1.
DR   AlphaFoldDB; A5IYK6; -.
DR   SMR; A5IYK6; -.
DR   STRING; 347257.MAG4170; -.
DR   PRIDE; A5IYK6; -.
DR   EnsemblBacteria; CAL59115; CAL59115; MAG4170.
DR   KEGG; maa:MAG4170; -.
DR   HOGENOM; CLU_035188_1_0_14; -.
DR   OMA; AVCTGHY; -.
DR   Proteomes; UP000007065; 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_0000349705"
FT   REGION          106..108
FT                   /note="Interaction with target base in tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   REGION          154..156
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   REGION          312..313
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   ACT_SITE        111
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   ACT_SITE        205
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   BINDING         10..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   BINDING         36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   BINDING         136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   SITE            137
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   SITE            345
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   DISULFID        111..205
FT                   /note="Alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
SQ   SEQUENCE   374 AA;  42594 MW;  20D1EA75022F3E87 CRC64;
     MSNKKKVILG MSGGVDSSVC AYLLLKQGYE VEGLFMRNWD SMLNNDFLGN ENISQDICPQ
     EQDYQDALEV ANKLGIKLHR VDFVNEYWND VFKTFISEYE AGRTPNPDIL CNKYIKFKAF
     SDYAFNNLGA DYIAMGHYAK VTDGRLYRAK DQNKDQTYFL AQLSHEQLKR VLMPLAEFSS
     KEEVRKIAQE QDLITASKKD STGICFIGER KFTKFLQNYI PMQPGDIVDI RTNKKLGKHE
     GCFYYTIGQR KGLNLGGQAE PYYVCGHDVK KNILYVAPSS DLSYLTSDAL LATGLTLNHD
     DFDHNNLSAK FRYRQQDIPV TIELLPNNTI KVYYPSESQA VTPGQQVVLY EGQKCLGGAV
     IEKIYYKGSE KTYL
 
 
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